|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
855-1935 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1464.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 855 TRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEM 934
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 935 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEER 1014
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1015 ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1094
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1095 KEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQE 1174
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1175 LRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAK 1254
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1255 QEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEE 1334
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1335 TRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1415 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1494
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1495 LARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEV 1574
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1575 NMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQL 1654
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1655 RKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNAL 1734
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1735 QDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGA 1814
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1815 VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLE 1894
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 92091586 1895 EAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKL 1935
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-778 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1319.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKG------TLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYT-FLSNGFVPIPAAQDDEMFQETV 337
Cdd:cd01377 155 STGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd01377 235 EAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKThRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd01377 315 GQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnpPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK-FQKPKQL 576
Cdd:cd01377 394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 577 KDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSASKTKKGM 656
Cdd:cd01377 472 KSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKKGGS 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 657 FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 736
Cdd:cd01377 541 FRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYS 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 92091586 737 ILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01377 621 ILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1317.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSItqgpsfaYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI-------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14921 154 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14921 234 AMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14921 314 QTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd14921 394 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFR 658
Cdd:cd14921 474 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14921 554 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14921 634 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1296.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSItqgpsfaYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI-------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14920 154 VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETME 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14920 234 AMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14920 314 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFR 658
Cdd:cd14920 474 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14920 634 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1211.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSitqGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS---SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14932 158 VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEsSLPSASKTKKGMFR 658
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14932 637 TPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1155.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitqgpsfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14919 151 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14919 231 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14919 311 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd14919 391 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFR 658
Cdd:cd14919 471 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14919 631 TPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-778 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1145.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSitqGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN---SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd15896 158 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd15896 318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd15896 398 FILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEssLPSASKTKKGMFR 658
Cdd:cd15896 478 EADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKGMFR 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd15896 556 TVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 635
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd15896 636 TPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1133.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASShKGKKDTSI---TQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 256 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 335
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 496 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpKQ 575
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 576 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLDQMAkMTESSLpsASKTKKG 655
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GARTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 656 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 92091586 736 EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-778 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1123.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 87 VEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 167 QDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdtsitqgpsfaYGELEKQLLQANPILEAFGNAKTVKNDNS 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN-----------VGRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 247 SRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIP 325
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 326 AAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILT 405
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 406 PRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINY 485
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 486 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQG 565
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 566 SHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqMAKMTESS 645
Cdd:pfam00063 467 KHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAE----SAAANESG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 646 LPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNR 725
Cdd:pfam00063 542 KSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 726 IVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:pfam00063 622 ITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1073.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITqgpsfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAaQDDEMFQETVE 338
Cdd:cd14930 154 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKD 578
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESslPSASKTKKGMFR 658
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDG--PPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14930 631 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-790 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1003.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 80 NPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIAD 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 160 TAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKkdtsitqgpsfayGELEKQLLQANPILEAFGNAK 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV-------------GSVEDQILESNPILEAFGNAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 240 TVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN 319
Cdd:smart00242 148 TLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 320 GFVPIPAAQDD-EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNT-AAQKVCHLMGINVT 397
Cdd:smart00242 228 GGCLTVDGIDDaEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 398 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNS 477
Cdd:smart00242 308 ELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 478 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFV 557
Cdd:smart00242 387 FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 558 EKLCTEQGSHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldq 637
Cdd:smart00242 464 EKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSG-------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 638 makmtesslpSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 717
Cdd:smart00242 535 ----------VSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRI 604
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 718 CRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERD 790
Cdd:smart00242 605 RRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1198 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 882.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 36 VWVPSEKQGFEAASIKEEKGDEVVVEL---VENGKKVTVGKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLRERYF 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEegkKEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 111 SGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 191 VIQYLAVVASSHkgkkdtsitqgpSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIET 270
Cdd:COG5022 172 IMQYLASVTSSS------------TVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 271 YLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETVEAMAIMGFSEEE 349
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 350 QLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVE 429
Cdd:COG5022 320 QDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 430 ALAKATYERLFRWILTRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQRE 509
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 510 GIEWNFIDFgLDLQPCIELIERpNNPPGVLALLDEECWFPKATDKSFVEKLCT--EQGSHPKFQKPKQLKDKteFSIIHY 587
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVVKHY 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 588 AGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVgldqmakmtesslpsasktKKGMFRTVGQLYKEQ 667
Cdd:COG5022 554 AGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRFKES 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 668 LGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANA----I 743
Cdd:COG5022 615 LNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgE 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 744 PKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLTAM 823
Cdd:COG5022 695 YTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKI 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 824 KVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKED---ELQKTKERQQKAeNELKELEQKHsqltEEKNLLQ 900
Cdd:COG5022 775 QVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLAciiKLQKTIKREKKL-RETEEVEFSL----KAEVLIQ 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 901 EqlqaetelYAEAEEMRVRLAAKKQelEEILHEMEARLEEEEDRGQQLQAERKKMAQqmldleeqleeeeAARQKLQLEK 980
Cdd:COG5022 850 K--------FGRSLKAKKRFSLLKK--ETIYLQSAQRVELAERQLQELKIDVKSISS-------------LKLVNLELES 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 981 VTAEAKIKKLEDEILVMDDQNNKLSKERKLLEER--ISDLTTNLAEEEEKAKNLTKLKNKHESmISELEVRLKKEE---- 1054
Cdd:COG5022 907 EIIELKKSLSSDLIENLEFKTELIARLKKLLNNIdlEEGPSIEYVKLPELNKLHEVESKLKET-SEEYEDLLKKSTilvr 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1055 ---KSRQELEKLKRKLEGdasdFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNaLKKIRELEghisdlq 1131
Cdd:COG5022 986 egnKANSELKNFKKELAE----LSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELSI-LKPLQKLK------- 1052
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1132 edldseraarNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHE 1198
Cdd:COG5022 1053 ----------GLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLV 1109
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-778 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 878.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDTSITqgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS--------SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL-----SNGFVPIPAAQDDEM 332
Cdd:cd00124 153 DPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 333 FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNT--DQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKV 410
Cdd:cd00124 233 FQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 411 GRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ-GASFLGILDIAGFEIFEVNSFEQLCINYTNEK 489
Cdd:cd00124 313 GGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 490 LQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK 569
Cdd:cd00124 393 LQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 570 FQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivgldqmakmtesslpsa 649
Cdd:cd00124 470 FFSKKR-KAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------ 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 650 sktkkgmfrtvgqlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 729
Cdd:cd00124 519 --------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFD 584
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 92091586 730 EFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd00124 585 EFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 786.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsiTQGPSFAYG-ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKK--AQFLATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQE 335
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEELMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd14927 238 TDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 494
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 495 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKP 573
Cdd:cd14927 396 NHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 574 ---KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtESSLPSAS 650
Cdd:cd14927 473 rpdKKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDSTED--PKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 651 KTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd14927 548 RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 92091586 731 FRQRYEILAANAIPK-GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14927 628 FKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 763.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSH--KGKKDTSITqgpsfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGdlAKKKDSKMK-------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQE 335
Cdd:cd14913 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDV 414
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 493
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 494 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQK 572
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 573 PKQLKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmakmtESSLPSAS 650
Cdd:cd14913 468 PKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVA 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 651 KTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd14913 540 KKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGD 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 92091586 731 FRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14913 620 FKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 751.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSitqgpsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAK-------SKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14909 154 PTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd14909 234 QAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14909 314 GRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQL 576
Cdd:cd14909 393 MFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 577 K---DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpSASKTK 653
Cdd:cd14909 470 KpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSGGGEQAK-------GGRGKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 654 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14909 543 GGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKM 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 734 RYEILAANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14909 623 RYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 740.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDtsitqgpsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD---------GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAK-EKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14934 152 TTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd14934 232 VAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14934 312 GQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQL 576
Cdd:cd14934 391 MFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 577 KDK---TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdriVGLDQMAKMTESSLPSASKTK 653
Cdd:cd14934 468 KGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS--------------LGLLALLFKEEEAPAGSKKQK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 654 KGM-FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd14934 534 RGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFK 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 733 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14934 614 QRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-778 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 710.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSG-LIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKkdTSItqgpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGE--TQV-----------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAAQDDEMFQETV 337
Cdd:cd01380 149 KNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 497 TMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK--FQKPK 574
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 575 QlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNassdkfvadlwkdvdrivgldqmakmtesslpsASKTKK 654
Cdd:cd01380 465 F--SNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLK---------------------------------ASKNRK 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 655 gmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd01380 510 ---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSR 586
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 92091586 735 YEILaanaIPKGF---MDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01380 587 YRVL----LPSKEwlrDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-778 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 709.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTsitqgpsfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL----------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmRSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQET 336
Cdd:cd14929 151 ARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 337 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 416
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 417 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQgaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14929 309 RSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 496 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPK 574
Cdd:cd14929 387 QHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPK 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 575 QLKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLW-KDVdrivgldqmakMTESSLPSASK 651
Cdd:cd14929 464 PDKKKFEahFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFeNYI-----------STDSAIQFGEK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 T-KKGM-FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 729
Cdd:cd14929 533 KrKKGAsFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYA 612
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 92091586 730 EFRQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14929 613 DFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 696.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKDtsitQGPsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD----QTP--GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRsDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQET 336
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELL-DMLLITNNpyDYAFISQGETTVASIDDAEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 337 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd14917 235 DNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14917 314 TKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 496 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPK 574
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 575 QLKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdriVGLDQMAKmtesslPSASKT 652
Cdd:cd14917 470 NIKGKPEahFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPIE------KGKGKA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 653 KKG-MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14917 541 KKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 92091586 732 RQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14917 621 RQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-778 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 693.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 181 GAGKTENTKKVIQYLAVVASSHKGKKDTSitqgpSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES-----GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 261 GYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVEA 339
Cdd:cd14918 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 340 MAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd14918 317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQLK 577
Cdd:cd14918 396 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVVK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 578 DKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqMAKMTESSLPSASKTKKG 655
Cdd:cd14918 473 GKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKKGS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 656 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14918 545 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 92091586 736 EILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14918 625 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 690.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKGKKDtsitQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKE----QQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFN--NYTFLSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 416
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 417 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14923 316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 497 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQ 575
Cdd:cd14923 395 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 576 LKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslPSASKTK 653
Cdd:cd14923 472 AKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGS------KKGGKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 654 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14923 546 GSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 734 RYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14923 626 RYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 686.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKGKKDtSITQGPsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-EATSGK--MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14910 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14910 318 GQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQL 576
Cdd:cd14910 397 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 577 KDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASKTKK 654
Cdd:cd14910 474 KGKVEahFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA-------AAAEAEEGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 655 GMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd14910 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 735 YEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14910 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 682.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKGKKDtSITQGPsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKE-EITSGK--MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLSNGFVPIPAAQDDEMFQETVE 338
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14912 318 GQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQL 576
Cdd:cd14912 397 MFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVV 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 577 KDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGldqmaKMTESSLPSASKTKK 654
Cdd:cd14912 474 KGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG-----ASAGGGAKKGGKKKG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 655 GMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd14912 549 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 735 YEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14912 629 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 682.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVAS-SHKGKKDTSitqgpSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENP-----NANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEgfNN---YTFLSNGFVPIPAAQDDEMFQE 335
Cdd:cd14916 157 ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNTA-AQKVCHLMGINVTDFTRSILTPRIKVGRDV 414
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 494
Cdd:cd14916 314 VTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 495 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKP 573
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 574 KQLKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldQMAKMTESSLPSASK 651
Cdd:cd14916 470 RNVKGKQEahFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 TKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14916 543 KKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 92091586 732 RQRYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14916 623 RQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-778 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 674.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKGKKDTSiTQGPsfAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEA-ASGK--MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMrSDLLLEGFNNYTF--LSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmPDNT-AAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQ 416
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 417 KAQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNH 496
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 497 TMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQ-GSHPKFQKPKQ 575
Cdd:cd14915 396 HMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKP 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 576 LKDKTE--FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMAKMTESSLPSASKTK 653
Cdd:cd14915 473 AKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-------GQTAEAEGGGGKKGGKKK 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 654 KGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14915 546 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 734 RYEILAANAIPKG-FMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14915 626 RYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-778 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 657.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKgkkdtsitqgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQET 336
Cdd:cd14883 146 SGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 337 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKK-ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDK---THRqgasFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 492
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPgqkNSR----FIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 493 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 572
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 573 PKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVD--RIVGLDQMAKMTESSlpsaS 650
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDllALTGLSISLGGDTTS----R 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 651 KTKKGMfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd14883 535 GTSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKE 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 92091586 731 FRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14883 614 FVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-778 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 648.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHKGkkdtsitqgpsfaygeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEMFQETVE 338
Cdd:cd01383 144 AGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 418
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 419 QTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 498
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 499 FILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKpkqlKD 578
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 579 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdRIVGLDQMAKMTESSLPSASKTKKgmfR 658
Cdd:cd01383 457 GGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLF-----ASKMLDASRKALPLTKASGSDSQK---Q 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 659 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 738
Cdd:cd01383 529 SVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL 608
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 739 AANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01383 609 LPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-778 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 642.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVASSHkgkkDTSITQGpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGS----ESEVERV--------KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEM-FQETVE 338
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAAdFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG---RDVV 415
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 495
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 496 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFP-KATDKSFVEKLCTEQGSHPKFQKPK 574
Cdd:cd01378 389 ELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 575 QLKD--KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakmtesslpsaSKT 652
Cdd:cd01378 466 GHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGV-------------------DLD 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 653 KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd01378 527 SKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFL 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 733 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01378 607 ERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-778 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 610.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAvvassHKGKKDTsiTQGPSfaygeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLA-----YMGGRAV--TEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFvPIPAAQDDEMFQE 335
Cdd:cd01384 149 DDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPD---NTAAQKVCHLMGINVTDFTRSiLTPRIKVGR 412
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 413 D-VVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 491
Cdd:cd01384 307 DgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 492 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQ 571
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 572 KPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtesslpsaSK 651
Cdd:cd01384 463 KPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------------EG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 TKKGM-FRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd01384 523 TSSSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEE 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 92091586 731 FRQRYEILAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd01384 603 FLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-778 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 601.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHkgkkdTSItqgpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQH-----SWI-----------EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETV 337
Cdd:cd01381 145 KNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKK--ERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQL 493
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSRTsiGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 494 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELI-ERPNNppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQK 572
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 573 PKQLKDkTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkDVDRIVGLDqmakmtesslpSASKT 652
Cdd:cd01381 461 PKSDLN-TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TRKKS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 653 KkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFR 732
Cdd:cd01381 528 P-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFV 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 733 QRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01381 603 ERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-778 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 589.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVVASSHKGkkdtsitqgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG---------------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLegfnnytflsngfvpIPAAQDDEMFQETV 337
Cdd:cd01382 146 NEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLK---------------DPLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNT-------DQASMPDNTAAQKvchLMGINVTDF-----TRSILT 405
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRVMQT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 406 PRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdkTHRQGASFLGILDIAGFEIFEVNSFEQLCINY 485
Cdd:cd01382 288 TRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYFEVNSFEQFCINY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 486 TNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQG 565
Cdd:cd01382 366 CNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 566 SHPKFQKP--------KQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldq 637
Cdd:cd01382 443 NHFRLSIPrksklkihRNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF----------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 638 mAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRI 717
Cdd:cd01382 512 -ESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDL 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 718 CRQGFPNRIVFQEFRQRYEILAANAIPKgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01382 591 MQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-778 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 567.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGkkdtsitqgpsfaygeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSnGFVPIPAAQDDEMFQETVE 338
Cdd:cd14872 145 NRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLS-GCIEVEGVDDVADFEEVVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 339 AMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS---MPDNTAAQKVCHLMGINVTDFTRSILTPRIKV-GRDV 414
Cdd:cd14872 224 AMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDP 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLF 494
Cdd:cd14872 304 TRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 495 NHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPK 574
Cdd:cd14872 384 NQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIE--KKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 575 QLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqMAKMTESSLPSaSKTKK 654
Cdd:cd14872 461 VRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL----------------IAVLFPPSEGD-QKTSK 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 655 GmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 734
Cdd:cd14872 524 V---TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 735 YEILAAnAIPKGFM-DGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14872 601 YRFLVK-TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-778 |
6.63e-179 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 558.62 E-value: 6.63e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 174 ILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSF---AYGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAieqTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 251 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 330
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASmpDNTAAQ---KVCHLMGINVTDFTRSILTPR 407
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 408 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTN 487
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 488 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIE-RPNNPPGVLALLDeECWFPKAT--DKSFVEKL---- 560
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 561 ---------CTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkdvdr 631
Cdd:cd14890 476 grksgsggtRRGSSQHPHFVHPKFDADK-QFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 632 ivgldqmakmteSSLPSASktkkgmfrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGV 711
Cdd:cd14890 542 ------------RSIREVS---------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 712 LEGIRICRQGFPNRIVFQEFRQRYEILAANAipkgfMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-778 |
2.01e-173 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 543.58 E-value: 2.01e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASShkgkKDTSITQgpsfaygelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQR----RNNLVTE-----------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 vTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDEMFQETV 337
Cdd:cd01387 146 -GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ---ASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDV 414
Cdd:cd01387 225 AAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVN----KALDKTHRqgasfLGILDIAGFEIFEVNSFEQLCINYTNEKL 490
Cdd:cd01387 305 IFTPLTIDQALDARDAIAKALYALLFSWLVTRVNaivySGTQDTLS-----IAILDIFGFEDLSENSFEQLCINYANENL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 491 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF 570
Cdd:cd01387 380 QYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 571 QKPKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldQMAKMTESSLPSAS 650
Cdd:cd01387 457 SKPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFS---------SHRAQTDKAPPRLG 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 651 K----TKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd01387 526 KgrfvTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRL 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 727 VFQEFRQRYEILAANAIPKGfMDGKQACILMIKALELDP-NLYRIGQSKIFFR 778
Cdd:cd01387 606 PFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-778 |
3.42e-170 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 535.80 E-value: 3.42e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLavVASSHKGkkdtsitqgpsFAYGeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG-----------YGSG-VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLsNGFVPIPAAQDDEM--FQET 336
Cdd:cd01385 147 ENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYL-NQSDCYTLEGEDEKyeFERL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 337 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKER-NTDQASMPDNTAAQK-VCHLMGINVTDFTRSILTPRIKVGRDV 414
Cdd:cd01385 226 KQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASfLGILDIAGFEIFEVNSFEQLCINYTNEKL 490
Cdd:cd01385 306 LILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 491 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF 570
Cdd:cd01385 385 QYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 571 QKPkQLKDkTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLwkdvdriVGLD-------------- 636
Cdd:cd01385 462 EKP-QVME-PAFIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDpvavfrwavlraff 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 637 -QMAKMTESSLPSASKT-------------------KKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGK 696
Cdd:cd01385 533 rAMAAFREAGRRRAQRTaghsltlhdrttksllhlhKKKKPPSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLR 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 697 LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 776
Cdd:cd01385 613 FDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVF 688
|
..
gi 92091586 777 FR 778
Cdd:cd01385 689 LK 690
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-778 |
2.50e-169 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 531.57 E-value: 2.50e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKK-RHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLavvasSHKGKKDTSitqgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHL-----MKLSPSDDS----------DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDE------ 331
Cdd:cd14897 146 TENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEeleyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 332 -MFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKV 410
Cdd:cd14897 226 qMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 411 GRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYT 486
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 487 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGS 566
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 567 HPKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtessl 646
Cdd:cd14897 463 SPRYVASP--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 647 psasktkkgmfrtvgQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd14897 522 ---------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRI 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 727 VFQEFRQRYEILAANAiPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd14897 587 KYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-776 |
4.58e-169 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 531.67 E-value: 4.58e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY------KGKKRHEMPPHIYAIADTAYRSMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 171 --DQSILCTGESGAGKTENTKKVIQYLAVVASSHkgkkdtsiTQGPSFAYGE-LEKQLLQANPILEAFGNAKTVKNDNSS 247
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSAT--------THGQNATEREnVRDRVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 248 RFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIP 325
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 326 AAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-KKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSIL 404
Cdd:cd14901 233 GVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 405 TPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAS-FLGILDIAGFEIFEVNSFEQLCI 483
Cdd:cd14901 313 TREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 484 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIELIERpnNPPGVLALLDEECWFPKATDKSFVEK 559
Cdd:cd14901 393 NFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEA--RPTGLFSLLDEQCLLPRGNDEKLANK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 560 LCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqma 639
Cdd:cd14901 466 YYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS--------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 640 kmtesslpsasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICR 719
Cdd:cd14901 531 -------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 720 QGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKA------LELDPNLYrIGQSKIF 776
Cdd:cd14901 592 SGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-778 |
6.06e-168 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 528.58 E-value: 6.06e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVVASshkGKKDTSItqgpsfaygeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFlSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM--PDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 415
Cdd:cd14903 225 EALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 416 QKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQgASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 495
Cdd:cd14903 305 TVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 496 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLcteQGSHPKFQK--- 572
Cdd:cd14903 384 QDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKL---SSIHKDEQDvie 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 573 -PKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrIVGLDQMAKMTESSLPSASK 651
Cdd:cd14903 457 fPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGARRRR 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 TKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14903 532 GGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEF 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 92091586 732 RQRYEILAANAiPKGFMDGKQACILMIKALELD-PNLYRIGQSKIFFR 778
Cdd:cd14903 612 LDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-739 |
8.51e-168 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 528.49 E-value: 8.51e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKgKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVVASSHKGKKDTsitqgpsfaygeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL------------VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVT---------GYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP----- 323
Cdd:cd14888 148 SKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPisidm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 324 -------------------IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTA 384
Cdd:cd14888 228 ssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 385 AQ---KVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASF 461
Cdd:cd14888 308 TDdleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 462 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLAL 541
Cdd:cd14888 388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 542 LDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKF 621
Cdd:cd14888 465 LDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 622 VADLWKD-VDRIVGldqmakmtesslpsaSKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAF 700
Cdd:cd14888 543 ISNLFSAyLRRGTD---------------GNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRI 607
|
650 660 670
....*....|....*....|....*....|....*....
gi 92091586 701 LVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 739
Cdd:cd14888 608 SVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILL 646
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-778 |
1.14e-166 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 524.15 E-value: 1.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVasshkGKKDTsitqgpsfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-----GKANN----------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSD---LLLEGFNNYTFLSNGFVPIPAAQDD--EMFQ 334
Cdd:cd01379 147 TGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGnrEKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 335 ETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFK---KERNTDQASM-PDNTAAQKVCHLMGINVTDFtRSILTPRIKV 410
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRiSNPEALNNVAKLLGIEADEL-QEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 411 GR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL--DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTN 487
Cdd:cd01379 306 TRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 488 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIE-LIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGS 566
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 567 HPkFQKPKqlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSl 646
Cdd:cd01379 462 KY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-----------------RQTVAT- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 647 psasktkkgMFRtvgqlY--KEQLGKLMTtlrnTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPN 724
Cdd:cd01379 521 ---------YFR-----YslMDLLSKMVV----GQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSH 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 725 RIVFQEFRQRYEILA--ANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd01379 583 RILFADFLKRYYFLAfkWNEEVVA---NRENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-778 |
6.73e-164 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 517.43 E-value: 6.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVV----ASSHKGKKDTSItqgpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 253
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIsqqsLELSLKEKTSCV-----------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 254 RINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPAAQDDEM 332
Cdd:cd14873 150 QLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQES 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 333 FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKkerNTDQASMPDNTAAQKVCHLMGINVTDFTrSILTPRIKVGR 412
Cdd:cd14873 230 FREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLT-DALTQRSMFLR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 413 -DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKthRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 491
Cdd:cd14873 306 gEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRIKG--KEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 492 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQ 571
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 572 KPKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmAKMTESSLPSASK 651
Cdd:cd14873 460 KPRV--AVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVS--------SRNNQDTLKCGSK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 TKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14873 530 HRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDF 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 92091586 732 RQRYEILAANAIPKGFMDGKqaCILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14873 607 YKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-778 |
3.36e-162 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 512.77 E-value: 3.36e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEM---PPHIYAIADTAYRSMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 172 QSILCTGESGAGKTENTKKVIQYLAVvASSHKgkKDTSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAT-ASKLA--KGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 252 FIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDD 330
Cdd:cd14892 158 YIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGVDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQ----ASMPDNTAAQKVCHLMGINVTDFTRSILTP 406
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKLVTQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 407 RIKVGR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQ---------GASFLGILDIAGFEIFEVN 476
Cdd:cd14892 316 TTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 477 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATDKS 555
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 556 FVEKL-CTEQGSHPKFQKPKQLKDktEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkdvdrivg 634
Cdd:cd14892 473 LLTIYhQTHLDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK--------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 635 ldqmakmtesslpsasktkkgmFRTvgqlykeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEG 714
Cdd:cd14892 536 ----------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEV 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 715 IRICRQGFPNRIVFQEFRQRYEILAAN-AIPKGFMDGKQACILMIKALE-----LDPNLYRIGQSKIFFR 778
Cdd:cd14892 587 VRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-778 |
2.17e-151 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 483.25 E-value: 2.17e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 101 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 177 TGESGAGKTENTKKVIQYLavvasshkgkkdTSITQGPSfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQI------------MELCRGNS----QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 257 FDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRSDLLLEGFnnYTFLSNGFvpipaAQDDEM-- 332
Cdd:cd14889 147 FR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA-----GCKREVqy 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 333 ----FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkkERNTDQASMPDNTA---AQKVCHLMGINVTDFTRSiLT 405
Cdd:cd14889 219 wkkkYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSngwLKAAAGQFGVSEEDLLKT-LT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 406 PRIKVGR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQG--ASFLGILDIAGFEIFEVNSFEQLC 482
Cdd:cd14889 296 CTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 483 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIerPNNPPGVLALLDEECWFPKATDKSFVEKLCT 562
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 563 EQGSHPKFQKPKQLKDKteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKM 641
Cdd:cd14889 453 HFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTaTRSRTGTLMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 642 TESSLPSASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQG 721
Cdd:cd14889 531 PQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 722 FPNRIVFQEFRQRYEILAANAIPKGfmdGKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd14889 608 FSWRPSFAEFAERYKILLCEPALPG---TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-741 |
1.06e-146 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 470.67 E-value: 1.06e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRH--------EMPPHIYAIADTAYRSMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 170 EDQSILCTGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITQGPSFAYG-----ELEKQLLQANPILEAFGNAKTVKND 244
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFL-TQLSQQEQNSEEVLTLTSSIRATskstkSIEQKILSCNPILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 245 NSSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG---FNNYTFLS-N 319
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLKkS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 320 GFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQA--SMPDNTAAQKVCHLMGINVT 397
Cdd:cd14907 240 NCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 398 DFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL------DKTHRQGASF-LGILDIAGF 470
Cdd:cd14907 320 ELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 471 EIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIELIErpNNPPGVLALLDEECWF 548
Cdd:cd14907 400 EVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLD--KPPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 549 PKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTeFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkd 628
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF-- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 629 vdriVGLDQMAKMTESSLPSASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRC 708
Cdd:cd14907 554 ----SGEDGSQQQNQSKQKKSQKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670
....*....|....*....|....*....|...
gi 92091586 709 NGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 741
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-778 |
3.24e-143 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 460.28 E-value: 3.24e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERyfSGLI----YTYSGLFCVVVNPYKHLPiysEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 172 QSILCTGESGAGKTENTKKVIQYLAV--VASSHKGKKDTSITQGPSFAYG-ELEKQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTraVGGKKASGQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 249 FGKFIRINFDVTGY-IVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLS-NGFVPIPA 326
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 327 AQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKK----ERNTDQASMPDNTAAQKVCHLMGINVTDFTRS 402
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 403 ILTPRIkVGRDVVQKAQ-TKEQADFAVEALAKATYERLFRWILTRVNKALDKtHRQGASFLGILDIAGFEIFE-VNSFEQ 480
Cdd:cd14891 316 ITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFEtKNDFEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 481 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI-ERPNnppGVLALLDEECWFPKATDKSFVEK 559
Cdd:cd14891 394 LLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPN---GILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 560 LCTEQGSHPKFQKPKQlKDKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLnASSDKFvadlwkdvdrivgLDQM 638
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLL-ASSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 639 AkmtesslpsasktkkgmfrtvgqlykeqlgKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIC 718
Cdd:cd14891 535 Q------------------------------ELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 719 RQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIK-ALELDPNLYRIGQSKIFFR 778
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTLTQAILwAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-744 |
4.72e-139 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 447.83 E-value: 4.72e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMY-----------KGKKRHEMPPHIYAIADTAYRSM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAvvassHKGKKDTSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKN 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLA-----QAGDNNLAASVSMGKSTSGIAAKVLQTNILLESFGNARTLRN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 244 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEkmrsdlllegfnnytflsngfvp 323
Cdd:cd14900 157 DNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE----------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 324 ipAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTD-QASMPDNTAAQKV------CHLMGINV 396
Cdd:cd14900 214 --AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 397 TDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD----KTHRQGASFLGILDIAGFEI 472
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKmddsSKSHGGLHFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 473 FEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERpnNPPGVLALLDEECWFPKAT 552
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQ--RPTGILSLIDEECVMPKGS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 553 DKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVtsllnassdkfvadlwkdVDri 632
Cdd:cd14900 449 DTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEA------------------VD-- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 633 vgldqmakmtesslpsasktkkgMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVL 712
Cdd:cd14900 509 -----------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVM 564
|
650 660 670
....*....|....*....|....*....|..
gi 92091586 713 EGIRICRQGFPNRIVFQEFRQRYEILAANAIP 744
Cdd:cd14900 565 EAVRVARAGFPIRLLHDEFVARYFSLARAKNR 596
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-735 |
2.82e-137 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 446.26 E-value: 2.82e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYK--------GKKRHEMPPHIYAIADTAYRSMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 169 REDQSILCTGESGAGKTENTKKVIQYLAVVASshkgkkDTSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR------DQSSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 249 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN---GFVPIP 325
Cdd:cd14902 155 FGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSygpSFARKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 326 AAQDD--EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQ--KVCHLMGINVTDFT 400
Cdd:cd14902 235 AVADKyaQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAEnGQEDATAVTAASRFHlaKCAELMGVDVDKLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 401 RSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD--------KTHRQGASFLGILDIAGFEI 472
Cdd:cd14902 315 TLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFES 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 473 FEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKAT 552
Cdd:cd14902 395 LNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFD--DKSNGLFSLLDQECLMPKGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 553 DKSFVEKLCTEQGShpkfqkpkqlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDkfvadlwkDVDRI 632
Cdd:cd14902 472 NQALSTKFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------EVVVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 633 VGLDQMAKMTESSLPSASKTKKGMFRT--VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNG 710
Cdd:cd14902 532 IGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660
....*....|....*....|....*
gi 92091586 711 VLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFIELF 636
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-778 |
8.04e-137 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 444.40 E-value: 8.04e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPiyseKIVDMYKgkKRHEMP------PHIYAIADTAYRSMLQ------ 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP----GLYDLHK--YREEMPgwtalpPHVFSIAEGAYRSLRRrlhepg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 168 -DREDQSILCTGESGAGKTENTKKVIQYLAVVAsshkgkKDTSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNS 246
Cdd:cd14895 76 aSKKNQTILVSGESGAGKTETTKFIMNYLAESS------KHTTATSSSKRRRAISGSELLSANPILESFGNARTLRNDNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 247 SRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTF--LSN 319
Cdd:cd14895 150 SRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFqyISG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 320 G--FVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERntDQASMPDNTAAQKVCHLMGINVT 397
Cdd:cd14895 230 GqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASS--EDEGEEDNGAASAPCRLASASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 398 DFT-------------------RSILTPR-IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL------ 451
Cdd:cd14895 308 SLTvqqhldivsklfavdqdelVSALTTRkISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 452 ----DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIE 527
Cdd:cd14895 388 lnpnKAANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 528 LIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLN 607
Cdd:cd14895 467 MLEQ--RPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPN 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 608 DNVTSLLNASSDKFVADLWKDVDRIVGldqmAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCII 687
Cdd:cd14895 545 AELFSVLGKTSDAHLRELFEFFKASES----AELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 688 PNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELdpnl 767
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL---- 696
|
730
....*....|.
gi 92091586 768 yriGQSKIFFR 778
Cdd:cd14895 697 ---GKTRVFLR 704
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-778 |
4.26e-135 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 437.84 E-value: 4.26e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAVVASshkGKKDTSITQgpsfaygelekqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIAK------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGFVPIPAAQDDEMFQE 335
Cdd:cd14904 146 DGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDF-----TRSILT--PRI 408
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIeealcNRSVVTrnESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 409 KVGRDVVQKAQTKeqadfavEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNE 488
Cdd:cd14904 305 TVPLAPVEAEENR-------DALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 489 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpnNPPGVLALLDEECWFPKATDKSFVEKLCT---EQG 565
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIRTnhqTKK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 566 SHPKFQKPKQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESS 645
Cdd:cd14904 454 DNESIDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----------APSET 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 646 LPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNR 725
Cdd:cd14904 522 KEGKSGKGTKAPKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSR 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 726 IVFQEFRQRYEILAANAIPKGfmDGKQACILMIKAL-ELDPNLYRIGQSKIFFR 778
Cdd:cd14904 602 LTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-778 |
2.72e-134 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 435.36 E-value: 2.72e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLavvasshkgkkdTSITQGPSfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL------------SSLYQDQT---EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 vTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFV-PIPAAQDDEMFQETV 337
Cdd:cd14896 146 -HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQ--ASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKV-GRDV 414
Cdd:cd14896 225 KALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 415 VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQL 493
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 494 FNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKP 573
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 574 KQlkDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKmtesslpsasktk 653
Cdd:cd14896 461 QL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 654 kgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 733
Cdd:cd14896 526 -----TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 734 RYEILAANAIPkGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14896 601 RFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
64-821 |
2.70e-133 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 438.69 E-value: 2.70e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 64 ENGKKVTVGKDDIQKMNPP-KFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY 142
Cdd:PTZ00014 74 PTNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 143 KGKKRHE-MPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItqgpsfaygel 221
Cdd:PTZ00014 154 RDAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI----------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 222 EKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEK 301
Cdd:PTZ00014 220 QNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDE 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 302 MRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASM 379
Cdd:PTZ00014 300 MKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 380 --PDNTAA-QKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKThr 456
Cdd:PTZ00014 380 isDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPP-- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 457 QG-ASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNp 535
Cdd:PTZ00014 458 GGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 536 pGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKtEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLN 615
Cdd:PTZ00014 536 -SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVK 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 616 ASSDKFVADLWKDVdrivgldqmaKMTEsslpsaSKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSG 695
Cdd:PTZ00014 614 ASPNPLVRDLFEGV----------EVEK------GKLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPL 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 696 KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKI 775
Cdd:PTZ00014 676 DWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMV 755
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 92091586 776 FF-RTGV--LAHLEEERDLKITDVIMAFQAMCRGYLARKAFAKRQQQLT 821
Cdd:PTZ00014 756 FLkKDAAkeLTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKNIKSLV 804
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-778 |
7.09e-133 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 432.89 E-value: 7.09e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKkdtsITqgpsfaygeLEKqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LS---------VEK--LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNytflSNGFVPIPAAQDDEM----- 332
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQKPEDKqkaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 333 -FQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSI-------- 403
Cdd:cd01386 222 aFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsgg 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 404 ----LTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEifevN--- 476
Cdd:cd01386 302 pqqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGFQ----Npah 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 477 -------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPN------------NPPG 537
Cdd:cd01386 377 sgsqrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPqqalvrsdlrdeDRRG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 538 VLALLDEECWFPKATDKSFVEKLCTEQG--SHPKFQKPKQLKDKT-EFSIIHYAGK--VDYNASAWLTK-NMDPLNDNVT 611
Cdd:cd01386 457 LLWLLDEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNAT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 612 SLLNASSDKFVAdlwkdvdrivgldqmakmtesslpsasKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCIIPNH- 690
Cdd:cd01386 537 QLLQESQKETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHn 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 691 -EKRSGK----------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGF-----MDGKQAC 754
Cdd:cd01386 586 aGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAV 665
|
730 740
....*....|....*....|....
gi 92091586 755 ILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-764 |
2.86e-132 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 430.87 E-value: 2.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYK--GKKRHE-------MPPHIYAIADTAYRSMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 169 REDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGkkdtSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSR 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEG----APNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 249 FGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRS--------DLLLEGFNNYTFLSNG 320
Cdd:cd14908 157 FGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 321 FVP-IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQK----VCHLMGIN 395
Cdd:cd14908 237 GAPdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 396 VTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA-SFLGILDIAGFEIFE 474
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 475 VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPnnPPGVLALLDEECWFP-KATD 553
Cdd:cd14908 396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 554 KSFVEKL--------CTEQGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNA-SAWLTKNMDPLndnvtsllnassdkfvad 624
Cdd:cd14908 473 ANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVeTTFCEKNKDEI------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 625 lwkdvdrivgldqmakmtesslpsaSKTKKGMFRTvGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 704
Cdd:cd14908 535 -------------------------PLTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTE 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 705 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnAIPK----GFMDGKQACILMIKALELD 764
Cdd:cd14908 589 QLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKD 651
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-776 |
7.79e-128 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 417.08 E-value: 7.79e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRH-EMPPHIYAIADTAYRSMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTSItqgpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI-----------QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETV 337
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKErntDQASMPDntAA----------QKVCHLMGINVTDFTRSILTPR 407
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 408 IKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsFLGILDIAGFEIFEVNSFEQLCINYTN 487
Cdd:cd14876 302 TKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 488 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSH 567
Cdd:cd14876 381 EMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 568 PKFqKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVdrivgldqmaKMTesslp 647
Cdd:cd14876 458 GKF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV----------VVE----- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 648 sASKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 727
Cdd:cd14876 522 -KGKIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRP 598
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 92091586 728 FQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIF 776
Cdd:cd14876 599 FEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-774 |
7.59e-119 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 393.96 E-value: 7.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 177 TGESGAGKTENTKKVIQYLaVVASSHKGKKDTSITQGPSfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYL-INTSSSNQQQNNNNNNNNN----SIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 257 FDVTGYIV-GANIETYLLEKSR-AIRQARDERTFHIFYYMIAGAKEKMRSDLLLEG-FNNYTFL--------------SN 319
Cdd:cd14906 156 FRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqsSN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 320 GFVPIPAAQD-DEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQAS--MPDNTAA-QKVCHLMGIN 395
Cdd:cd14906 236 KNSNHNNKTEsIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 396 VTDFTRSILTPRIKVG---------RDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKALDK----------THR 456
Cdd:cd14906 316 ESVFKQALLNRNLKAGgrgsvycrpMEVAQSEQTRD-------ALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 457 QGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNNpp 536
Cdd:cd14906 389 KNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD-- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 537 GVLALLDEECWFPKATDKSFVEKlCTEQgSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNA 616
Cdd:cd14906 466 GILSLLDDECIMPKGSEQSLLEK-YNKQ-YHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 617 SSDKFVADLWkdvdrivgldqmaKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGK 696
Cdd:cd14906 544 SSNFLKKSLF-------------QQQITSTTNTTKKQTQSNTVSGQ-FLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNN 609
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 697 LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSK 774
Cdd:cd14906 610 FNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-739 |
6.41e-118 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 389.21 E-value: 6.41e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKR-HEMPPHIYAIADTAYRSMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAE-------RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 255 INFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGfvpiPAAQDDEMFQ 334
Cdd:cd14880 154 LQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEEDCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 335 ETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKV---CHLMGINVTDFTRSILTPRIKVG 411
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVrtsALLLKLPEDHLLETLQIRTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 412 RD--VVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEK 489
Cdd:cd14880 310 KQqqVFKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 490 LQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPK 569
Cdd:cd14880 390 LQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALAGNP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 570 FQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRivgldqmakmtESSLPSA 649
Cdd:cd14880 467 CLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPE-----------EKTQEEP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 650 SKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQ 729
Cdd:cd14880 536 SGQSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
|
650
....*....|
gi 92091586 730 EFRQRYEILA 739
Cdd:cd14880 616 NFVERYKLLR 625
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-778 |
1.42e-110 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 368.37 E-value: 1.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERyFSGLIYTYS--GLFCVVVNPYKHLPIYSEKIVDMY-KGKKRHEMPPHIYAIADTAYRSM-LQDREDQSI 174
Cdd:cd14875 1 ATLLHCIKER-FEKLHQQYSlmGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 175 LCTGESGAGKTENTKKVIQYLAVVASSHKGKkdtsiTQGPSFAyGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 254
Cdd:cd14875 80 VISGESGSGKTENAKMLIAYLGQLSYMHSSN-----TSQRSIA-DKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 255 INFD-VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDL----------LLEGFNnyTFLSNGfVP 323
Cdd:cd14875 154 LYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgglktaqdykCLNGGN--TFVRRG-VD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 324 IPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtDQASMPDNTAAQKVCHLMGINVTDFTRSI 403
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 404 LtprIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALD-KTHRQGASFLGILDIAGFEIFEVNSFEQLC 482
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 483 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKLCT 562
Cdd:cd14875 387 INYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKRT--GIFSMLDEECNFKGGTTERFTTNLWD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 563 E-QGSHPKFQKPKQLKdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWkdvdrivgldqmakm 641
Cdd:cd14875 464 QwANKSPYFVLPKSTI-PNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLL--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 642 teSSLPSASKTKKgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQG 721
Cdd:cd14875 528 --STEKGLARRKQ----TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQG 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 722 FPNRIVFQEF-RQRYEILAANAIpKGFMDGK--QACILMIKALE-----LDPNlYRIGQSKIFFR 778
Cdd:cd14875 602 YPVRRPIEQFcRYFYLIMPRSTA-SLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-735 |
1.49e-110 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 370.19 E-value: 1.49e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMY----------KGKKRHEMPPHIYAIADTAYRSMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 168 DREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGP--SFAYGELEKQLLQANPILEAFGNAKTVKNDN 245
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPpaSPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 246 SSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-----AKEKMRSDLLLEGFNNYTFLSN 319
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 320 GFVPI--PAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-----KKERNT--DQASMPDNTAA----- 385
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 386 QKVCHLMGINvTDFTRSILTPR--------IKVGRDVVQKAQTKEqadfaveALAKATYERLFRWILTRVNKAL------ 451
Cdd:cd14899 321 TKAAELLGVS-TEALDHALTKRwlhasnetLVVGVDVAHARNTRN-------ALTMECYRLLFEWLVARVNNKLqrqasa 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 452 --------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQ 523
Cdd:cd14899 393 pwgadesdVDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNR 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 524 PCIELIErpNNPPGVLALLDEECWFPKATDKSFVEKLCTE---QGSHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLT 600
Cdd:cd14899 472 ACLELFE--HRPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLA 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 601 KNMDPLNDNVTSLLNASSDKFVADLWK-DVDRIVGLDQMAKMTESSLPSASKTKKGMFrTVGQLYKEQLGKLMTTLRNTT 679
Cdd:cd14899 550 KNKDSFCESAAQLLAGSSNPLIQALAAgSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATT 628
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 680 PNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 735
Cdd:cd14899 629 PRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-778 |
2.08e-109 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 364.59 E-value: 2.08e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRH-----EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 173 SILCTGESGAGKTENTKKVIQYLAVvasshkgkkdtsitqGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY---------------GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 253 IRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNG-FVPIPAAQDDE 331
Cdd:cd14886 146 IKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASkCYDAPGIDDQK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 332 MFQETVEAMAIMgFSEEEQLSILKVVSSVLQLGNIVFKKERN--TDQASMPDNTAA-QKVCHLMGINVTDFTRSILTPRI 408
Cdd:cd14886 226 EFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 409 KVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALdKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNE 488
Cdd:cd14886 305 VINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 489 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELIERPNNppGVLALLDEECWFPKATDKSFVEKlCTEQGSHP 568
Cdd:cd14886 384 RLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSS-CKSKIKNN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 569 KF--QKPKQLKdkteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVadlwkdvdrivgldqmaKMTESSL 646
Cdd:cd14886 460 SFipGKGSQCN----FTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-----------------NKAFSDI 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 647 PSASKTKKGMFrtVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRI 726
Cdd:cd14886 519 PNEDGNMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYND 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 727 VFQEFRQRYEILA--ANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14886 597 TFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-778 |
7.22e-97 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 330.46 E-value: 7.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFS--------GLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 171 DQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKdtsiTQGpsfaygeLEKQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGAD----SQG-------LEARLLQSGPVLEAFGNAHTVLNANSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 251 KFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLL-EGFNNYTFLsngfvpipaaqd 329
Cdd:cd14887 150 KMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAgEGDPESTDL------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 330 demfQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTA--------AQKVCHLM-------GI 394
Cdd:cd14887 218 ----RRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 395 NVTDFTRSILTPRIK------------------VGRDV--VQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKT 454
Cdd:cd14887 294 KVTEASRKHLKTVARllglppgvegeemlrlalVSRSVreTRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 455 HR-------------QGASFLGILDIAGFEIFE---VNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI-- 516
Cdd:cd14887 374 AKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDcs 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 517 DFGLDLQPCIELIERPNN----------------------PPGVLALLDEECWFPKATDKSFVEKLCTEQGSHP------ 568
Cdd:cd14887 454 AFPFSFPLASTLTSSPSStspfsptpsfrsssafatspslPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNiinsak 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 569 -KFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSdkfvadlwkDVDRIVGLDQmakmteSSLP 647
Cdd:cd14887 534 yKNITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS---------TYTRLVGSKK------NSGV 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 648 SASKTKKgmfRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIV 727
Cdd:cd14887 599 RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLP 675
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 728 FQEFRQRYEILAANAIpKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 778
Cdd:cd14887 676 YVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-777 |
3.51e-96 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 326.04 E-value: 3.51e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 96 LNEASVLHNLRERYFSGLIYTY---SGLfcVVVNPYKHLPI--------YSEKIVDMYKGKKRHEMPpHIYAIADTAYRS 164
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 165 MLQDREDQSILCTGESGAGKTENTKKVI-QYLAVVASSHKGKKdtsitqgpsfaygeLEKQLLQANPILEAFGNAKTVKN 243
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK--------------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 244 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFL--SNGF 321
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 322 --VPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF--KKERNTDQASMpDNTAA-QKVCHLMGINV 396
Cdd:cd14879 224 plPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 397 TDFtRSILTPRIK-VGRDVV----QKAQTKEQADfaveALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFE 471
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKELCtvflDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 472 IF---EVNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIELIERPnnPPGVLALLD 543
Cdd:cd14879 378 NRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGILD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 544 EEC-WFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE---FSIIHYAGKVDYNASAWLTKNMDPLndnvtsllnaSSD 619
Cdd:cd14879 450 DQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 620 kFVAdlwkdvdrivgldqmakmtesslpsasktkkgMFRTVGQLyKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDA 699
Cdd:cd14879 520 -FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDK 565
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 700 FLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgFMDGKQACILMIKALELDPNLYRIGQSKIFF 777
Cdd:cd14879 566 RRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-778 |
1.36e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 318.68 E-value: 1.36e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMY---KGKKRHEMPPHIYAIADTAYRSMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 176 CTGESGAGKTENTKKVIQYLAVVASShkgkkdtsitQGPSFaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----------SRTTF-----DSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 256 NF-DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVP-IPAA---QDD 330
Cdd:cd14878 146 QFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMREdVSTAersLNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINvTDFTRSILTPRIKV 410
Cdd:cd14878 226 EKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVS-TDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 411 GR-DVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKAL---DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYT 486
Cdd:cd14878 305 FKgDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 487 NEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIELIERPNN-----------PPGVLALLDEECWFPKATDKS 555
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVEPN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 556 FVEKLCT--EQGSHPKFQKPKQ-------LKDK-TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADL 625
Cdd:cd14878 452 LPKKLQSllESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHL 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 626 WKdvdrivgldqmAKMTesslpsasktkkgmfrTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQ 705
Cdd:cd14878 532 FQ-----------SKLV----------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQ 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 706 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI-PKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd14878 585 LQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-742 |
7.45e-93 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 314.14 E-value: 7.45e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHempPHIYAIADTAYRSMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLKNYSHVE---PHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAvvassHKGKKDTSItqgpsfaygelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDv 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLV-----ERTASTTSI-----------EKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 tGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLlegfNNYTFLSNGFVPIPAAQDDEMFQETVEA 339
Cdd:cd14898 141 -GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI----DTSSTAGNKESIVQLSEKYKMTCSAMKS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 340 MAIMGFSEEEQLSIlkvvsSVLQLGNIVFKKERNTDQASmpdNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQ 419
Cdd:cd14898 216 LGIANFKSIEDCLL-----GILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 420 TKEQADFAVEALAKATYERLFRWILTRVNKALDKThrqGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 499
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 500 ILEQEEYQREGIEWNFIDFgLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLcteqgsHPKFQKPKQLKDK 579
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI------KKYLNGFINTKAR 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 580 TEFSIIHYAGKVDYNASAWLTKNMDplndnvtsllnassdkfvadlwKDVDRIVGLDQMAkmTESSLPSASKtkkgmfrt 659
Cdd:cd14898 435 DKIKVSHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLIN--DEGSKEDLVK-------- 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 660 vgqLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILA 739
Cdd:cd14898 483 ---YFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
...
gi 92091586 740 ANA 742
Cdd:cd14898 560 ITL 562
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-778 |
5.89e-87 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 298.85 E-value: 5.89e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPiysekiVDM--YKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILC 176
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVID------VDIneYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIII 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 177 TGESGAGKTENTKKVIQ-YLAVVasshkgKKDTSITqgpsfaygeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 255
Cdd:cd14937 75 SGESGSGKTEASKLVIKyYLSGV------KEDNEIS-----------NTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 256 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 335
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 336 TVEAMAIMGFSEEEQlSILKVVSSVLQLGNIVFK---KERNTDQASMPDNT--AAQKVCHLMGINVTDFTRSILTPRIKV 410
Cdd:cd14937 218 LMISFDKMNMHDMKD-DLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 411 GRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDkTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKL 490
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 491 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIELIeRPNNppGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF 570
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLL-RGKT--SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 571 QKPKqlKDKTE-FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrivgldqmakMTESslpsa 649
Cdd:cd14937 452 ASTK--KDINKnFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSES----- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 650 sktkKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRIcRQGFPNRIVFQ 729
Cdd:cd14937 515 ----LGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFD 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 92091586 730 EFRQRYEILAANAIPKGFMDGKQACILMIKAlELDPNLYRIGQSKIFFR 778
Cdd:cd14937 590 VFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-765 |
2.41e-78 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 273.53 E-value: 2.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYkhlpiysekivdMYKGKKRH-------EMPPHIYAIADTAYRSMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 173 SILCTGESGAGKTENTKKVIQYLAVVASShkgkkdtsitqGPSfayGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-----------GPE---TDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHF 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 253 IRINFdVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFN--NYTFLSNGFVPIPAAQDD 330
Cdd:cd14881 136 IEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 EMFQETVEAMAIMG--FseeeqLSILKVVSSVLQLGNIVFkKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSiLTPRI 408
Cdd:cd14881 215 ARFQAWKACLGILGipF-----LDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRG-LTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 409 K-VGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVN--KALDKTHRQGAS--FLGILDIAGFEIFEVNSFEQLCI 483
Cdd:cd14881 288 HnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANslKRLGSTLGTHATdgFIGILDMFGFEDPKPSQLEHLCI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 484 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIELIErpNNPPGVLALLDEECwFPKATDKSFVEKLCT 562
Cdd:cd14881 368 NLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 563 EQGSHPKFQKPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFvadlwkdvdrivgldqmakmt 642
Cdd:cd14881 444 QHRQNPRLFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF--------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 643 esslpsasktkkgMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGF 722
Cdd:cd14881 502 -------------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGY 568
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 92091586 723 PNRIVFQEFRQRYEILAANAIPKGFMDGKQAC--ILMIKALELDP 765
Cdd:cd14881 569 PHRMRFKAFNARYRLLAPFRLLRRVEEKALEDcaLILQFLEAQPP 613
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-730 |
1.04e-77 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 273.32 E-value: 1.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHE-------MPPHIYAIADTAYRSMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 171 DQSILCTGESGAGKTENTKKVIQYLavvassHKGKKDTSITqgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYF------HYIQTDSQMT--------ERIDKLIYINNILESMSNATTIKNNNSSRCG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 251 KFIRINFD---------VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG-AKEKMRSDLLLEGFNNYTFL--- 317
Cdd:cd14884 147 RINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 318 -----------------SNGFVPIPAAQDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerntdqasmp 380
Cdd:cd14884 227 eshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA---------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 381 dntaaqkVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGA- 459
Cdd:cd14884 297 -------AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEs 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 460 ----------SFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIELI 529
Cdd:cd14884 370 dnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 530 ERpnnppgVLALLDE-----ECWFPKATDKSF-----------VEKLCTEQGSHPKFQK---PKQLKDKTEFSIIHYAGK 590
Cdd:cd14884 449 AK------IFRRLDDitklkNQGQKKTDDHFFryllnnerqqqLEGKVSYGFVLNHDADgtaKKQNIKKNIFFIRHYAGL 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 591 VDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADlwkdvdrivgldqmakmtesslpSASKTKKGMFRTVGQLYKEQLGK 670
Cdd:cd14884 523 VTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKELDN 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 671 LMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQE 730
Cdd:cd14884 580 LFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-738 |
2.64e-72 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 255.57 E-value: 2.64e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 99 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYkgkkrhemppHIYAIADTAYRSMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 178 GESGAGKTENTKKVIQYLAvvaSSHKGKKDTsitqgpsfaygeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVTT--------------KHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 258 DvTGYIVGANIE-TYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQET 336
Cdd:cd14874 134 K-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 337 VEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTD---QASMPDNTAAQK-VCHLMGINVTDFTrSILTPRIKVGR 412
Cdd:cd14874 213 EDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKwVAFLLEVDFDQLV-NFLLPKSEDGT 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 413 DVvqkaqTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHRQGAsfLGILDIAGFEIFEVNSFEQLCINYTNEKLQQ 492
Cdd:cd14874 292 TI-----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIEN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 493 LFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQ 571
Cdd:cd14874 365 LFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 572 KPKQlKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslpSASK 651
Cdd:cd14874 443 KARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFE--------------------SYSS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 652 TKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 731
Cdd:cd14874 502 NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
....*..
gi 92091586 732 RQRYEIL 738
Cdd:cd14874 582 ARQYRCL 588
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-778 |
7.00e-72 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 254.67 E-value: 7.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 180 SGAGKTENTKKVIQYLAVVAsshKGKKDTSitqgpsfaygeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG---DGNRGAT-------------GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 260 TGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAG--AKEKMRsDLLLEGFNNYTFL----SNGFVPIPAAQDD--- 330
Cdd:cd14882 146 TGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLrippEVPPSKLKYRRDDpeg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 --EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKerNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRI 408
Cdd:cd14882 225 nvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 409 KVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHrqgaSFLG------ILDIAGFEIFEVNSFEQLC 482
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR----AVFGdkysisIHDMFGFECFHRNRLEQLM 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 483 INYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQpciELIERPNnppGVLALLDEECwfPKATDKSFVek 559
Cdd:cd14882 379 VNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYI-- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 560 LCTEQGSHPKFQKPKQlkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDvdrivglDQMA 639
Cdd:cd14882 449 MDRIKEKHSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVR 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 640 KMtesslpsasktkkgmfRTVGQLYKEQLGKLMTTLRNTTPN----FVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGI 715
Cdd:cd14882 519 NM----------------RTLAATFRATSLELLKMLSIGANSggthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTA 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 716 RICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDgKQACILMIKALELDPnlYRIGQSKIFFR 778
Cdd:cd14882 583 KARQKGFSYRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-731 |
2.50e-71 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 253.86 E-value: 2.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKgkKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVasshkgkkDTSITQgpsfaygELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 258
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTT--------DLSRSK-------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 259 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSN-GFVPIPAAQDDEMFQETV 337
Cdd:cd14905 145 LYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 338 EAMAIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNtdQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 417
Cdd:cd14905 225 MSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVEN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 418 AqtkeqadfavEALAKATYERLFRWILTRVNKALDKThrQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 497
Cdd:cd14905 303 R----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 498 MFILEQEEYQREGIEW-NFIDFGlDLQPCIELIERpnnppgVLALLDEECWFPKATDKSFVEKLCTEQGSHPKF-QKPKQ 575
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 576 lkdkteFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDK--FVADLWKDVDRIVG-LDQMAKMTESSLPSASKT 652
Cdd:cd14905 444 ------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKylFSRDGVFNINATVAeLNQMFDAKNTAKKSPLSI 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 653 KKGMFrTVGQLYKEQL-----------------------GKLMTTLRNTTP---------NFVRCIIPNHEKRSGKLDAF 700
Cdd:cd14905 518 VKVLL-SCGSNNPNNVnnpnnnsgggggggnsgggsgsgGSTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVK 596
|
650 660 670
....*....|....*....|....*....|....*
gi 92091586 701 LVLEQLRCNGVLEGIRICRQGFP----NRIVFQEF 731
Cdd:cd14905 597 SVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-736 |
2.32e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 249.89 E-value: 2.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 102 LHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIY----------SEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYtpdhmqaynkSREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 172 QSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTsitQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDS---EGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 252 FIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKE--KMRSDLLL-EGFNNYTFLSNGFVPIPA-A 327
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHdpTLRDSLEMnKCVNEFVMLKQADPLATNfA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 328 QDDEMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNIVF-------KKERNTDQASMPDNTA------AQ--KVCHLM 392
Cdd:cd14893 241 LDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQScalkdpAQilLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 393 GIN--VTD---FTRSILTpriKVGRDVVQ--KAQTKEQADFAVEALAKATYERLFRWILTRVNKAL----DKTHRQG--- 458
Cdd:cd14893 321 EVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivi 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 459 -ASFLGILDIAGFEIFE--VNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCIEL 528
Cdd:cd14893 398 nSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 529 IERPnnPPGVLALLDEECWFPKATDKSFVEKLCTEQGSHPKFQKPKQLKDKTE------------FSIIHYAGKVDYNAS 596
Cdd:cd14893 478 FEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 597 AWLTKNMDPLNDNVTSLLNASSDKfvadlwkdVDRIVGLDQM--------AKMTESSLPSASKTKKGMFR---------- 658
Cdd:cd14893 556 GLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMaaassekaAKQTEERGSTSSKFRKSASSaresknitds 627
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 659 TVGQLYKeQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 736
Cdd:cd14893 628 AATDVYN-QADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-262 |
1.78e-65 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 219.52 E-value: 1.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 121 FCVVVNPYKHLPIYSEKIVD-MYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIvFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 200 SSHKGKKDTSITQGPSFAYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGY 262
Cdd:cd01363 81 FNGINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-776 |
1.05e-55 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 208.15 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 100 SVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYK-GKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 179 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFAYGE--------LEKQLLQANPILEAFGNAKTVKNDNSSRFG 250
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNEentdyqfnMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 251 KFIRINFDvTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYMIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDD 330
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 331 EMFQETVEAMAIMGFSEEEQLSILKVVSSVLQLGNI-----VFKKE---------------------RNTDQASMPDNTA 384
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkaFRKKSllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 385 AQKV-CHLMGINVTDFTRSILTPRIkVGRDVVQKAQTKEQADFAVEALAKATYERLFRWILTRVNKALDKTHR--QGASF 461
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 462 LGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNppGVLAL 541
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 542 LDEECWFPKATDKSFVEKLCTEQGSH-PKFQKPKQLK-DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSD 619
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRnSKYIKKDDITgNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 620 KFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQ----LYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRS- 694
Cdd:cd14938 558 EYMRQFCMFYNYDNSGNIVEEKRRYSIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 695 GKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAnaipkgfmDGKQACILMIKALELDPNLYRIGQSK 774
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 92091586 775 IF 776
Cdd:cd14938 710 IF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
870-1684 |
2.56e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 144.43 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 870 KTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMrVRLAAKKQELEEI-LHEMEARLEEEEDRGQQL 948
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLK---SLERQAEKA-ERYKELKAELRELeLALLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 949 QAERKKMAQQmldleeqleeeeaaRQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1028
Cdd:TIGR02168 245 QEELKEAEEE--------------LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1029 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD 1108
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1109 EIAQKNNALKKIRELEGHISDLQ---EDLDSERAARNKA--EKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1183
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEdrrERLQQEIEELLKKleEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1184 TVLKKALDEEtrshEAQVQEMRQKHAqAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRV-----------LGQ 1252
Cdd:TIGR02168 471 EEAEQALDAA----ERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVdegyeaaieaaLGG 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1253 AKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHK--------LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQ- 1323
Cdd:TIGR02168 546 RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTeiqgndreILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1324 -----LQDTQELLQEETRQKLNVS---------------------------TKLRQLEEERNSLQDQLDEEMEAKQNLER 1371
Cdd:TIGR02168 626 lvvddLDNALELAKKLRPGYRIVTldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1372 HISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS 1451
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1452 NLEKKQRKF-DQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKM------LKAEMEDLV 1524
Cdd:TIGR02168 786 ELEAQIEQLkEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELsediesLAAEIEELE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1525 SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQ 1604
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA-QLELRLEGLEVRIDNLQER 944
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1605 LHE-YETELEDERKQRALAAAAKKKLEGDLKDLELQADS-------AIKGREEAIKQLRKLQAQMKDFQRELEDARASRD 1676
Cdd:TIGR02168 945 LSEeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIE 1024
|
....*...
gi 92091586 1677 EIFATAKE 1684
Cdd:TIGR02168 1025 EIDREARE 1032
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1111-1920 |
9.38e-33 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 139.42 E-value: 9.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1111 AQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTATQQELRAKREQEvtvlkkal 1190
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREELE-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1191 deETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQE 1270
Cdd:TIGR02168 243 --ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1271 LQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1350
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1351 ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKL--QDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYDKL 1425
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELEELQEELerlEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1426 EKTKNRLQQELDDLVVDLDNQRQL---VSNLEKKQRKFDQ---LLAEEKNISSKY-----ADERDRAEAEAREKETKAL- 1493
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFsegVKALLKNQSGLSGilgVLSELISVDEGYeaaieAALGGRLQAVVVENLNAAKk 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1494 ---SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKL 1570
Cdd:TIGR02168 561 aiaFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1571 ------------------------RLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAA 1625
Cdd:TIGR02168 641 lrpgyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1626 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA 1705
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1706 AERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERS 1785
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1786 TAQKNESARQQLERQNKELRSKLHEMEGAVKskfkstiaALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKE--ILL 1863
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRS--------ELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEeySLT 952
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1864 QVEDERKMAEQyKEQAEKGNARVKQLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1920
Cdd:TIGR02168 953 LEEAEALENKI-EDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQKEDLTEA 1015
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-719 |
7.68e-30 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 129.48 E-value: 7.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 105 LRERYFSGLIYTYSGLFCV-VVNPYKHL------PIYSEKIVDMYKGKKRHE--MPPHIYAIAD---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 160 ----TAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAVVASS--HKGKKDTSITQGPS------------------ 215
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPalSKGSEETCKVSGSTrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 216 ----------------------------------------------------------FAYGELEKQL------------ 225
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 226 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAIRQA------RDERTFHI 290
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 291 FYYMIAGAK-----EKMRSDLLLEGFN--NYTFLSN------GFVPIPAA--QDDEMFQETVEAMAIMGFSEEEQLSILK 355
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDGIDcsALTYLGRsdhklaGFVSKEDTwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 356 VVSSVLQLGNIVFKKERNTDQASMPDN---TAAQKVCHLMGI-NVTDFTRSILTPRIKV--GRDVVQKAQTKEQADFAVE 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 430 ALAKATYERLFRWILTRVNKAL----------------DKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLqql 493
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL--- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 494 fnhtmfileqeeYQREGiewNFIDFGLDLQPciELIERPN---------NPPGVLALLDEECWFPKAT----------DK 554
Cdd:cd14894 563 ------------YAREE---QVIAVAYSSRP--HLTARDSekdvlfiyeHPLGVFASLEELTILHQSEnmnaqqeekrNK 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 555 SFVEKLCTEQGSHPKfQKPKQLKDKTE----------FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVAD 624
Cdd:cd14894 626 LFVRNIYDRNSSRLP-EPPRVLSNAKRhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCR 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 625 LWKDVDRivgLDQMAKMTESSLPSASKTKKGMFRTVGQlYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLE 704
Cdd:cd14894 705 MLNESSQ---LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQ 780
|
810
....*....|....*
gi 92091586 705 QLRCNGVLEGIRICR 719
Cdd:cd14894 781 QCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1059-1889 |
2.12e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.64 E-value: 2.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1059 ELEKLKRKLEGDASDfHEQIADLQAQIAELKMQLAKKE-EELQAALARLDDEIAQKNnalKKIRELEGHISDLQEDLDSE 1137
Cdd:TIGR02168 197 ELERQLKSLERQAEK-AERYKELKAELRELELALLVLRlEELREELEELQEELKEAE---EELEELTAELQELEEKLEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1138 RAARNKAEKQKRDLGEELEALKTELEDTldsTATQQELRAKREQEVTVLKKAldeetrshEAQVQEMRQKHAQAVEELTE 1217
Cdd:TIGR02168 273 RLEVSELEEEIEELQKELYALANEISRL---EQQKQILRERLANLERQLEEL--------EAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1218 QLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1297
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1298 SVTGMLNEAEGKAIK-LAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDE---EMEAKQNLERHI 1373
Cdd:TIGR02168 422 EIEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQlqaRLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1374 STLN---IQLSDSKKKLQDFASTVEALEEGKKRFQKEIENL-----------TQQYEEKAAAYDKLEKTKNRLQQELDDL 1439
Cdd:TIGR02168 502 EGFSegvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1440 VVDLDN------------QRQLVSNLEKKQRKFDQLLAeekNISSKYADERDRAEAEAREKETKALSLA------RALEE 1501
Cdd:TIGR02168 582 KGTEIQgndreilkniegFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGYRIvtldgdLVRPG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1502 ALEAKEELERTNKML--KAEMEDLVsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL 1579
Cdd:TIGR02168 659 GVITGGSAKTNSSILerRREIEELE-------EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1580 KGQFERdLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQA 1659
Cdd:TIGR02168 732 RKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1660 QMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAeelasslSGRNALQDEKR 1739
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE-------SELEALLNERA 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1740 RLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKF 1819
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKI 963
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1820 KSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQL 1889
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1005-1833 |
2.30e-28 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 125.18 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1005 SKERKLLEERISdlttNLAE-EEEKAKNLTKLK------NKHESMISELEVRLKKEEKSRQELEK----LKRKLEGDASD 1073
Cdd:TIGR02169 152 PVERRKIIDEIA----GVAEfDRKKEKALEELEeveeniERLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1074 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEdldsERAARNKAEKqkrdlgE 1153
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE----EEQLRVKEKI------G 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1154 ELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEElteqleqFKRAKANLDKNK 1233
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE-------YAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDkvhkLQNEVESVTGMLNEAEGKAIKL 1313
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1314 AKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST 1393
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1394 VEALEEGKKRFQKEIE--------NLTQQYEEKAAAYDKLEKTK----------NRLQQELDDL--------------VV 1441
Cdd:TIGR02169 527 VAQLGSVGERYATAIEvaagnrlnNVVVEDDAVAKEAIELLKRRkagratflplNKMRDERRDLsilsedgvigfavdLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1442 DLDNQRQ-----------LVSNLEKKQRKFDQL--------LAEEKNISSKYADERDRAEAEAREKETKALSLARALEEA 1502
Cdd:TIGR02169 607 EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1503 LEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL--- 1579
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELear 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1580 KGQFERDLQA-RDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQ 1658
Cdd:TIGR02169 767 IEELEEDLHKlEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1659 AQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQED-------LAAAERARKQADLEKEELAEELASSLSGR 1731
Cdd:TIGR02169 847 EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKErdeleaqLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1732 NALQDEKRRLEARIAQLEEELEEEQ--GNMEAMSDRVRKATQQAEQLSNELATERSTAQKN----ESARQQLERQNKELR 1805
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRldelKEKRAKLEEERKAIL 1006
|
890 900
....*....|....*....|....*...
gi 92091586 1806 SKLHEMEGAVKSKFKSTIAALEAKIAQL 1833
Cdd:TIGR02169 1007 ERIEEYEKKKREVFMEAFEAINENFNEI 1034
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
836-1613 |
3.10e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.78 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 836 LRNWQWWRLftkvkpLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQ-AETELYAeae 914
Cdd:TIGR02168 222 LRELELALL------VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEeLQKELYA--- 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 915 emrvrLAAKKQELEEilhemearleeeedRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEI 994
Cdd:TIGR02168 293 -----LANEISRLEQ--------------QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 995 LVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDf 1074
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1075 hEQIADLQAQIAELKMQLAKKEEEL---QAALARLDDEIAQKNNALKKIRELEGHIS-------DLQEDLDSERAARNKA 1144
Cdd:TIGR02168 433 -AELKELQAELEELEEELEELQEELerlEEALEELREELEEAEQALDAAERELAQLQarldsleRLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1145 EKQKRDLG-------------EELE-ALKTELEDTLDSTATQQELRAKREQEVtvLKKAldEETRSHEAQVQEMRQKHAQ 1210
Cdd:TIGR02168 512 LKNQSGLSgilgvlselisvdEGYEaAIEAALGGRLQAVVVENLNAAKKAIAF--LKQN--ELGRVTFLPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1211 AVE-ELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVL--GQAKQEVEHKKKKLEAQVQ---ELQSKCSDGERARAE 1284
Cdd:TIGR02168 588 GNDrEILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVddLDNALELAKKLRPGYRIVTldgDLVRPGGVITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1285 LNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDtqelLQEETRQKLnvsTKLRQLEEERNSLQDQLDEEME 1364
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEE----LEEELEQLR---KELEELSRQISALRKDLARLEA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1365 AKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLD 1444
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1445 NQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLV 1524
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1525 SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDaKLRLEVNMQAlkgqfeRDLQARDEQNEEKRRQLQRQ 1604
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE-RLSEEYSLTL------EEAEALENKIEDDEEEARRR 973
|
....*....
gi 92091586 1605 LHEYETELE 1613
Cdd:TIGR02168 974 LKRLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
858-1573 |
6.44e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.55 E-value: 6.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 937
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISD 1017
Cdd:TIGR02168 346 LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEE---------EKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFH------EQIADLQ 1082
Cdd:TIGR02168 426 LLKKLEEAElkelqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDslerlqENLEGFS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1083 AQIAELKM-------------QLAKKEEELQAAL-----ARLDDEI------------AQKNNALKKIRELEGHISDLQE 1132
Cdd:TIGR02168 506 EGVKALLKnqsglsgilgvlsELISVDEGYEAAIeaalgGRLQAVVvenlnaakkaiaFLKQNELGRVTFLPLDSIKGTE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1133 dLDSERAARNKAEKQKRDLGEELEALKTELEDTL----------DSTATQQELRAKREQEVTVLKKALDEETRS-----H 1197
Cdd:TIGR02168 586 -IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitgG 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1198 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSD 1277
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1278 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQd 1357
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR- 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1358 qldeemEAKQNLERhistlniQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELD 1437
Cdd:TIGR02168 824 ------ERLESLER-------RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1438 DLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARaleealeakeeleRTNKMLK 1517
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS-------------LTLEEAE 957
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1518 AEMEDLVSSKDDVGKNVHELEKSKRAL-------ETQMEEMKTQLEELEDELQATEDAKLRLE 1573
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1120-1929 |
4.01e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.86 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1120 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEA 1199
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1200 QVQEMRQKhaqaVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAK-QEVEHKKKKLEAQVQELQSKCSDG 1278
Cdd:TIGR02169 245 QLASLEEE----LEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1279 ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQE------ETRQKL-NVSTKLRQLEEE 1351
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkefaETRDELkDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALeegkkrfQKEIENLTQQYEEKAAAYDKLEKTKNR 1431
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK-------ALEIKKQEWKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1432 LQQELDdlvvdldnqrQLVSNLEKKQRKFDQLLAeEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELER 1511
Cdd:TIGR02169 474 LKEEYD----------RVEKELSKLQRELAEAEA-QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1512 TnkMLKAEMEDLVSSKDDVGKNVHELEKSK---RALETQMEEMKTQLEELEdelQATEDAKLRLEVNMQALKGQFE---- 1584
Cdd:TIGR02169 543 V--AAGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1585 ---RDLQARDEQNEEKRRQLQRQLHEYETELEDE--------RKQRALAAAAKKKLE------GDLKDLELQADSAIKGR 1647
Cdd:TIGR02169 618 yvfGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsRAPRGGILFSRSEPAelqrlrERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1648 EEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELass 1727
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL--- 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1728 lsgrNALQDEKRRLEARIAQLEEELEEEQGN-MEAMSDRVRKATQQAEQLSNELATERSTAqknESARQQLERQNKELRS 1806
Cdd:TIGR02169 775 ----HKLEEALNDLEARLSHSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYL---EKEIQELQEQRIDLKE 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1807 KLHEMEGAV------KSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAE 1880
Cdd:TIGR02169 848 QIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 92091586 1881 KGNARVKQLKRQLEEAEEESQRInANRRKLQRELDEATESNEAMGrEVN 1929
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEE-LSLEDVQAELQRVEEEIRALE-PVN 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1713 |
4.24e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 114.38 E-value: 4.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 978 LEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSR 1057
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1058 QELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSE 1137
Cdd:TIGR02168 312 ANLERQLEELE-------AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1138 RAARNKAEKQKRDLGEELEALKTELEDTLDSTA-TQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELT 1216
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRErLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1217 EQLEQFKRAKANLDKNKQTLEKENADLAG------ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK-- 1288
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSlerlqeNLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAAlg 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1289 -------VHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQ----- 1356
Cdd:TIGR02168 545 grlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllgg 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1357 ----DQLDEEMEAKQNLERHistLNIQLSDSKKKLQDFASTVEALEEGKKRF--QKEIENLTQQYEEKAAAYDKLEKTKN 1430
Cdd:TIGR02168 625 vlvvDDLDNALELAKKLRPG---YRIVTLDGDLVRPGGVITGGSAKTNSSILerRREIEELEEKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1431 RLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARAleealeakeele 1510
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER------------ 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1511 rtnkmlkaemedlvsskddvgknVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErdlqar 1590
Cdd:TIGR02168 770 -----------------------LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA------ 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1591 deQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqreled 1670
Cdd:TIGR02168 821 --NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA-------- 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 92091586 1671 arASRDEIF---ATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1713
Cdd:TIGR02168 891 --LLRSELEelsEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
872-1489 |
6.78e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 872 KERQQKAENELKELEQKhsqLTEEKNLLQE---QLQaetELYAEAEemrvrLAAKKQELEEILHEMEARLEEEEDRGQQL 948
Cdd:COG1196 171 KERKEEAERKLEATEEN---LERLEDILGElerQLE---PLERQAE-----KAERYRELKEELKELEAELLLLKLRELEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 949 QAERKKMAQQmldleeqleEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1028
Cdd:COG1196 240 ELEELEAELE---------ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1029 AKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD 1108
Cdd:COG1196 311 RREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1109 EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKreqevtvlkk 1188
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE---------- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1189 aLDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQV 1268
Cdd:COG1196 454 -LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1269 QELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLnVSTKLRQL 1348
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL-VASDLREA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1349 EEERNSLQDQLDEE-------MEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1421
Cdd:COG1196 612 DARYYVLGDTLLGRtlvaarlEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1422 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKE 1489
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
814-1439 |
1.79e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 814 AKRQQQLTAMKVIQRNCAAYLKLRNWQwwrlftkvkplLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLT 893
Cdd:COG1196 212 AERYRELKEELKELEAELLLLKLRELE-----------AELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 894 EEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgQQLQAERKKMAQQMLDLEEQLEEEEAAR 973
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERL--------------EELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 974 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKE 1053
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1054 EKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQED 1133
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1134 LDSERAARNKAEKQK----------------RDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSH 1197
Cdd:COG1196 507 LEGVKAALLLAGLRGlagavavligveaayeAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1198 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLgqAKQEVEHKKKKLEAQVQELQSKCSD 1277
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1278 GERARAELNDKVHKLQNEVESvtgmlNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD 1357
Cdd:COG1196 665 GSRRELLAALLEAEAELEELA-----ERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1358 QLDEEMEAKQNLERHISTLNIQLSDSKKKLqdfastvealeegkKRFQKEIENL-------TQQYEEKAAAYDKLEKTKN 1430
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELEREL--------------ERLEREIEALgpvnllaIEEYEELEERYDFLSEQRE 805
|
....*....
gi 92091586 1431 RLQQELDDL 1439
Cdd:COG1196 806 DLEEARETL 814
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1333-1929 |
1.82e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1333 EETRQKLN-VSTKLRQLEEERNSLQDQ---------LDEEMEAKQ---------NLERHISTLNIQLSDSKKKLQDFAST 1393
Cdd:COG1196 182 EATEENLErLEDILGELERQLEPLERQaekaeryreLKEELKELEaellllklrELEAELEELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1394 VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSK 1473
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1474 YADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKT 1553
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1554 QLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL 1633
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEE-EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1634 KDLELQADSA-----IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATakENEKKAKSLEADLMQLQEDLAAAER 1708
Cdd:COG1196 501 ADYEGFLEGVkaallLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV--EDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1709 ARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQ 1788
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1789 KNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDE 1868
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1869 RKMAEQYKEqaekgnarvkqlkrqLEEAEEESQRINANRRKLQRELDEATESNEAMGReVN 1929
Cdd:COG1196 739 EELLEEEEL---------------LEEEALEELPEPPDLEELERELERLEREIEALGP-VN 783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1713 |
1.93e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 1.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 851 LLQVTRQEEEMQAKEDELQKTKERQQKAENELKELE--QKHSQLTEEKNLLQEQLQAETELyaeaEEMRVRLAAKKQELE 928
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQalLKEKREYEGYELLKEKEALERQK----EAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 929 EIlhemearLEEEEDRGQQLQAERKKMAQqMLDLEEQLEEEEAARQKLQLEKVTAEakIKKLEDEILVMDDQNNKLSKER 1008
Cdd:TIGR02169 255 KL-------TEEISELEKRLEEIEQLLEE-LNKKIKDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1009 KLLEERISDLttnLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLK---RKLEGDASDFHEQIADLQAQI 1085
Cdd:TIGR02169 325 AKLEAEIDKL---LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDkefAETRDELKDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1086 AELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDt 1165
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR- 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1166 ldstaTQQELRAKREQEVTVLKKALDEETRSHE-------------------AQVQEMRQKHAQAVE------------- 1213
Cdd:TIGR02169 481 -----VEKELSKLQRELAEAEAQARASEERVRGgraveevlkasiqgvhgtvAQLGSVGERYATAIEvaagnrlnnvvve 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1214 ---ELTEQLEQFKRAKAN----LDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSK--CSDGERARAE 1284
Cdd:TIGR02169 556 ddaVAKEAIELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTlvVEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1285 L-NDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEM 1363
Cdd:TIGR02169 636 MgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1364 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfqkEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1443
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1444 DNQRqlvsnLEKKQRKFDQLLAEEKNIsskyaderdRAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDL 1523
Cdd:TIGR02169 789 SHSR-----IPEIQAELSKLEEEVSRI---------EARLREIEQKLNRLTLEKEYLEKEIQE---------LQEQRIDL 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1524 VSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQatedaklrlevnmqalkgqferDLQARDEQNEEKRRQLQR 1603
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELER 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1604 QLHEYETELEDERKQRALAAAAKKKLEGDLKDLElQADSAIKGREEAIKQLRKLQAQMKDFQRELED-------ARASRD 1676
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*..
gi 92091586 1677 EIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1713
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
972-1619 |
1.39e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 109.26 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 972 ARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLK 1051
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1052 KEEKSRQELEklkrKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQ 1131
Cdd:COG1196 289 EEYELLAELA----RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1132 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEvtvlKKALDEETRSHEAQVQEMRQKHAQA 1211
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER----LERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1212 VEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQskcSDGERARAELNDKVHK 1291
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA---DYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1292 LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLER 1371
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1372 HISTLNIqlsdskkklqdfASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS 1451
Cdd:COG1196 598 GAAVDLV------------ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1452 NLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1531
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1532 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDaklrleVNMQALKgQFERdLQARDEQNEEKRRQLQRQLHEYET- 1610
Cdd:COG1196 746 ELLEEEALEELPEPPDLEELERELERLEREIEALGP------VNLLAIE-EYEE-LEERYDFLSEQREDLEEARETLEEa 817
|
650
....*....|.
gi 92091586 1611 --ELEDERKQR 1619
Cdd:COG1196 818 ieEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1255-1920 |
3.03e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1255 QEVEHKKKKLEAQV------QELQSKcsdGERARAELN-DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDT 1327
Cdd:COG1196 196 GELERQLEPLERQAekaeryRELKEE---LKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1328 QELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKE 1407
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1408 IENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEARE 1487
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1488 KETKALSLARALEEALEAKEELERtnkmlkaemedlvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQATED 1567
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEE------------------------EEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1568 AKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEyetelederkqralaaaakkkLEGDLKDLELQADSAIKGR 1647
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---------------------LIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1648 EEAIkqLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeELAEELASS 1727
Cdd:COG1196 548 LQNI--VVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD----ARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1728 LSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSK 1807
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1808 LHEMEgavkskfkSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKgnaRVK 1887
Cdd:COG1196 702 EEEEE--------RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELE 770
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 92091586 1888 QLKRQLEE-------AEEESQRINANRRKLQRELDEATES 1920
Cdd:COG1196 771 RLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1153-1747 |
6.04e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 6.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 EELEALKTELEDTLDSTATQQElRAKREQEvtvLKKALDEetRSHEAQVQEMRQKHAQAvEELTEQLEQFKRAKANLDKN 1232
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAE-KAERYRE---LKEELKE--LEAELLLLKLRELEAEL-EELEAELEELEAELEELEAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1233 KQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIK 1312
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1313 LAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAS 1392
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1393 TVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL----EKKQRKFDQLLAEEK 1468
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELleelAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1469 NISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELErtnkmLKAEMEDLVSSKDDVGKNVHELEKSK---RALE 1545
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-----LAAALQNIVVEDDEVAAAAIEYLKAAkagRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1546 TQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAA 1625
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1626 KKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA 1705
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 92091586 1706 AERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQ 1747
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1331-1941 |
2.51e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1331 LQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIEN 1410
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1411 LTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKET 1490
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1491 KALSLARALEEALEAKEELERTNKMLKAEMEDLVSS-----KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT 1565
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaeLKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1566 EDAKLRLEVNMQALKGQFE--RDLQARDEQNEEKRRQL---QRQLH--------------EYETELE------------- 1613
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDslERLQENLEGFSEGVKALlknQSGLSgilgvlselisvdeGYEAAIEaalggrlqavvve 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1614 -------------DERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK--------------DFQR 1666
Cdd:TIGR02168 554 nlnaakkaiaflkQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1667 ELEDARASR-DEIFATA-----------------------------KENEKKAKSLEADLMQLQEDLAAAERARKQADLE 1716
Cdd:TIGR02168 634 ALELAKKLRpGYRIVTLdgdlvrpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1717 KEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQ 1796
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1797 LERQNKELRSKLHEMEGAVKSkFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYK 1876
Cdd:TIGR02168 794 LKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE 872
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1877 EQAE-------KGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNET 1941
Cdd:TIGR02168 873 SELEallneraSLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
988-1702 |
4.11e-22 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 104.76 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 988 KKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEE-------KSRQEL 1060
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyegyellKEKEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1061 EKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALK-KIRELEGHISDLQEDLDSERA 1139
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKeKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1140 ARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVtvlkKALDEETRSHEAQVQEMRQKHAQAVEELT--- 1216
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY----AELKEELEDLRAELEEVDKEFAETRDELKdyr 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1217 EQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEV 1296
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1297 ESVTGMLNEAEGKAIKLAKDVASLSSQLQ----------DTQELLQEETRQKLNVSTKLRQLEEER---------NSLQD 1357
Cdd:TIGR02169 472 YDLKEEYDRVEKELSKLQRELAEAEAQARaseervrggrAVEEVLKASIQGVHGTVAQLGSVGERYataievaagNRLNN 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1358 -QLDEEMEAKQNlerhistlnIQLSDSKK----------KLQDFASTVEAL-EEGKKRFQKEIENLTQQYE--------- 1416
Cdd:TIGR02169 552 vVVEDDAVAKEA---------IELLKRRKagratflplnKMRDERRDLSILsEDGVIGFAVDLVEFDPKYEpafkyvfgd 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1417 -------EKAAAY-----------DKLEKT------KNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE---KN 1469
Cdd:TIGR02169 623 tlvvediEAARRLmgkyrmvtlegELFEKSgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrriEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1470 ISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQME 1549
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1550 EMK-----TQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQ----ARDEQNE--EKRRQLQRQLHEYETELEDERKQ 1618
Cdd:TIGR02169 783 DLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeyLEKEIQElqEQRIDLKEQIKSIEKEIENLNGK 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1619 RALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQ 1698
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
....
gi 92091586 1699 LQED 1702
Cdd:TIGR02169 943 DEEI 946
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
984-1563 |
6.77e-21 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 100.09 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 984 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEK-------S 1056
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKeleklnnK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1057 RQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEEL---QAALARLDDEIAQKNNALKKIRELEGHISDLQED 1133
Cdd:TIGR04523 161 YNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQE 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1134 LDSERAARNKAEKQKRDLGEELEALKTELED----------TLDSTATQ-QELRAKRE----QEVTVLKKALDEETRSHE 1198
Cdd:TIGR04523 241 INEKTTEISNTQTQLNQLKDEQNKIKKQLSEkqkeleqnnkKIKELEKQlNQLKSEISdlnnQKEQDWNKELKSELKNQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1199 AQVQEMRQ---KHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKC 1275
Cdd:TIGR04523 321 KKLEEIQNqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1276 SDGERARAELNDKVHKLQNEVEsvtgmlneaegkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSL 1355
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKE--------------LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1356 QDQLDEemeakqnLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQE 1435
Cdd:TIGR04523 467 ETQLKV-------LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1436 LDDLVVDL--DNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTN 1513
Cdd:TIGR04523 540 ISDLEDELnkDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 92091586 1514 KMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1563
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
858-1712 |
3.65e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 98.12 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 937
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 LEEEEDRGQQLQAERKKMAQQMLDLEEQLeeeeaarQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISD 1017
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKL-------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLK-----------KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIA 1086
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKeleikreaeeeEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1087 ELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTL 1166
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1167 DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGE 1246
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1247 LRVlgQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQ- 1325
Cdd:pfam02463 552 EVS--ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIl 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1326 DTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQ 1405
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1406 KEIENLTQQYEEKAAAYDKLEktKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1485
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEA--QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1486 REKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAT 1565
Cdd:pfam02463 788 VEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEE 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1566 EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERK--QRALAAAAKKKLEGDLKDLELQADSA 1643
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIeeRIKEEAEILLKYEEEPEELLLEEADE 947
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1644 IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQ 1712
Cdd:pfam02463 948 KEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1177-1931 |
4.74e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.82 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1177 AKREQEVTVLKKALDEETRSHE-AQVQEMRQKHAQAVEELTEQLEQFKRAKaNLDKNKQTLEKENADLAGELRVLGQAKQ 1255
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAfGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1256 eVEHKKKKLEAQVQELQSKCSDGERARAElndkvhKLQNEVEsvtgmlneaEGKAIKLAKDVASLSSQLQDTQELLQEET 1335
Cdd:PTZ00121 1154 -VEIARKAEDARKAEEARKAEDAKKAEAA------RKAEEVR---------KAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1336 RQklnvSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNiqlSDSKKKLQDFASTVEALEEGKKRFQKEIenltQQY 1415
Cdd:PTZ00121 1218 RK----AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEARKADEL----KKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1416 EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQllAEEKNISSKYADERDRAEAEAREKETKALSL 1495
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1496 ARALEEALEAKEELERTNKMLKAEMEdlvsskddvgKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVN 1575
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEK----------KKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1576 MQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLR 1655
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE 1514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1656 KLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSL-EADLMQLQEDLAAAERARKQADLEkeelaeelasSLSGRNAl 1734
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDK----------NMALRKA- 1583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1735 QDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNElATERSTAQKNESARQQLERQNKELRSKlhEMEGA 1814
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1815 VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLE 1894
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 92091586 1895 EAE---EESQRINANRRKLQRELDEATESNEAMGREVNAL 1931
Cdd:PTZ00121 1741 EDKkkaEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
860-1607 |
1.28e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 860 EMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKK--QELEEILHEMEAR 937
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTET---GKAEEARKAEEAKKkaEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeiLVMDDQNNKLSKERKLLEERISD 1017
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKAE 1215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 lTTNLAEEEEKAKNLTKLKnkhesmiselEVRLKKEEKSRQELEklkRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1097
Cdd:PTZ00121 1216 -EARKAEDAKKAEAVKKAE----------EAKKDAEEAKKAEEE---RNNEEIRKFEEARMAHFARRQAAIKAEEARKAD 1281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1098 ELQAALARLDDEIAQKNNALKKIRELEGHisdlQEDLDSERAARNKAEKQKRDlGEELEAlKTELEDTLDSTATQQELRA 1177
Cdd:PTZ00121 1282 ELKKAEEKKKADEAKKAEEKKKADEAKKK----AEEAKKADEAKKKAEEAKKK-ADAAKK-KAEEAKKAAEAAKAEAEAA 1355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1178 KREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAV---EELTEQLEQFKRAKANLDK-----------NKQTLEKENAD- 1242
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkaDEAKKKAEEDKKKADELKKaaaakkkadeaKKKAEEKKKADe 1435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1243 ---LAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKA-IKLAKDVA 1318
Cdd:PTZ00121 1436 akkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAeAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1319 SLSSQLQDTQELLQEETRQKlnvSTKLRQLEEERNSlqDQLDEEMEAKQNLERHistlniQLSDSKKKLQDFASTVEALE 1398
Cdd:PTZ00121 1516 KKAEEAKKADEAKKAEEAKK---ADEAKKAEEKKKA--DELKKAEELKKAEEKK------KAEEAKKAEEDKNMALRKAE 1584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1399 EGKKRFQKEIENLTQQYEE----KAAAYDKLEKTKNRlQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKY 1474
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEekkmKAEEAKKAEEAKIK-AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1475 ADERDRAEAEAREKET--KALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK 1552
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEakKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1553 TQLEELE-DELQATEDAKLRLEVNMQALKGQFERDL---QARDEQNEEKRRQLQRQLHE 1607
Cdd:PTZ00121 1744 KKAEEAKkDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKD 1802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1199-1940 |
3.60e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1199 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEK--ENADLAGELRVLGQAKQEVE-----HKKKKLEAQVQEL 1271
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1272 QSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDvaslssqlqdtqellqeetrQKLNVSTKLRQLEEE 1351
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--------------------EQLRVKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNR 1431
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1432 LQQELDDLVVDLDnqrQLVSNLEKKQRKFDQLLAEEKNISSKYADerdrAEAEAREKETKALSLARALEEALEAKEELER 1511
Cdd:TIGR02169 383 TRDELKDYREKLE---KLKREINELKRELDRLQEELQRLSEELAD----LNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1512 TNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQF-------- 1583
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVaqlgsvge 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1584 -------------------ERDLQARDEQNEEKRRQLQRQlheyeTELEDERKQRALAAAAKKKLEG------DLKDLEL 1638
Cdd:TIGR02169 536 ryataievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRA-----TFLPLNKMRDERRDLSILSEDGvigfavDLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1639 QADSAIK------GREEAIKQLRKL--QAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERAR 1710
Cdd:TIGR02169 611 KYEPAFKyvfgdtLVVEDIEAARRLmgKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1711 kqadlekeelaeelasslsgrNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKN 1790
Cdd:TIGR02169 691 ---------------------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1791 ESARQQLERQNKELRSKLHEMEgAVKSKFKSTIAALEAKIAQLE--------EQVEQEAREKQAATKSLKQKDKKLKEIL 1862
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELE-EDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1863 LQVEDERKMAEQY----KEQAEKGNARVKQLKRQLEEAEEESQRINANRR-------KLQRELDEATESNEAMGREVNAL 1931
Cdd:TIGR02169 829 EYLEKEIQELQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRdlesrlgDLKKERDELEAQLRELERKIEEL 908
|
....*....
gi 92091586 1932 KSKLRRGNE 1940
Cdd:TIGR02169 909 EAQIEKKRK 917
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
996-1573 |
4.18e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 4.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 996 VMDDQNNKLS--------KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKrkl 1067
Cdd:PRK02224 181 VLSDQRGSLDqlkaqieeKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLE--- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1068 egdasdfhEQIADLQAQIAElkmqlAKKEEElqaalaRLDDEIAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQ 1147
Cdd:PRK02224 258 --------AEIEDLRETIAE-----TERERE------ELAEEVRDLRERLE---ELEEERDDLLAEAGLDDADAEAVEAR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1148 KrdlgEELEALKTELEDTLDSTATQQElrAKREQEVTVLKKALDEETRSHEAqvQEMRQKHAQAVEELTEQLEQFKRAKA 1227
Cdd:PRK02224 316 R----EELEDRDEELRDRLEECRVAAQ--AHNEEAESLREDADDLEERAEEL--REEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1228 NLDKNKQTLEKENADLAGELrvlgqakqevehkkKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLneAE 1307
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDL--------------GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL--EA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 GKAIKLAKDVAslSSQLQDTqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQnLERHISTLNIQLSDSKKKL 1387
Cdd:PRK02224 452 GKCPECGQPVE--GSPHVET---IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVE-AEDRIERLEERREDLEELI 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1388 QDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE 1467
Cdd:PRK02224 526 AERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAE 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1468 KNISSKYADERDRAEAEAREKETkaLSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQ 1547
Cdd:PRK02224 606 DEIERLREKREALAELNDERRER--LAEKRERKRELEAEFDEARIEE-AREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
570 580
....*....|....*....|....*....
gi 92091586 1548 MEEMKTQLEELE---DELQATEDAKLRLE 1573
Cdd:PRK02224 683 IGAVENELEELEelrERREALENRVEALE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
853-1174 |
7.13e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.89 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELK-------ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 925
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEqlrkeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 926 ELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAA-------RQKLQLEKVTAEAKIKKLEDEILVMD 998
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAEltllneeAANLRERLESLERRIAATERRLEDLE 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 999 DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQI 1078
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1079 ADLQAQIAELKMQLAKKEEELQAALARLDDEIAQK-NNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1157
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDF 1004
|
330
....*....|....*..
gi 92091586 1158 LKTELEDTLDSTATQQE 1174
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEE 1021
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
859-1574 |
7.68e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.56 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 859 EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETElyAEAEEMRVRLAAKKQELEEILHEMEARL 938
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 939 eeeedrgqqlQAERKKMAQQMLDLEEQLEEEEAARQKLQLEkvtAEAKIKKLEDEILVMDDQNNKLSKERK-----LLEE 1013
Cdd:pfam15921 198 ----------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkielLLQQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1014 RISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKK-EEKSRQELEKLKRKLegdaSDFHEQIADLQAQIAELKMQL 1092
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiQEQARNQNSMYMRQL----SDLESTVSQLRSELREAKRMY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1093 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1172
Cdd:pfam15921 341 EDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1173 QELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQ 1252
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1253 AKQEVEHKKKKLEAQVQELQSKcsdgeRARAELN-DKVHKLQNEVESVTGMLNEAEGKAIKLA---KDVASLSSQLQDTQ 1328
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKL-----RSRVDLKlQELQHLKNEGDHLRNVQTECEALKLQMAekdKVIEILRQQIENMT 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1329 ELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSK--------------KKLQDFASTV 1394
Cdd:pfam15921 576 QLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlRAVKDIKQER 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1395 EALEEGKKRFQKEIENLTQQYEEKAAAY----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ-RKFDQLLAEEKN 1469
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFrnksEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDgHAMKVAMGMQKQ 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1470 ISSKyaderdRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQME 1549
Cdd:pfam15921 736 ITAK------RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNK--LSQELSTVATEKNKMAGELEVLRSQERRLKEKVA 807
|
730 740 750
....*....|....*....|....*....|..
gi 92091586 1550 EMKT-------QLEELEDELQATEDAKLRLEV 1574
Cdd:pfam15921 808 NMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
856-1575 |
8.65e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 856 RQEEEMQAKEDelQKTKERQQKAENELKELEQKHSQltEEKNLlqEQLQAETELYAEAEEmrVRLAAKKQELEEILHEME 935
Cdd:PTZ00121 1188 RKAEELRKAED--ARKAEAARKAEEERKAEEARKAE--DAKKA--EAVKKAEEAKKDAEE--AKKAEEERNNEEIRKFEE 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 936 ARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEA--ARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKE-RKLLE 1012
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKR--KLEGDASDFHEQIADLQAQIAELKM 1090
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKK 1419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1091 --QLAKKEEELQAA-LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA---RNKAEKQKRdlGEELEALKTELED 1164
Cdd:PTZ00121 1420 adEAKKKAEEKKKAdEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeaKKKAEEAKK--ADEAKKKAEEAKK 1497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1165 TLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTE--QLEQFKRA--KANLDKNKQTLEKEN 1240
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADElkKAEELKKAeeKKKAEEAKKAEEDKN 1577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1241 ADL--AGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAiklakdva 1318
Cdd:PTZ00121 1578 MALrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-------- 1649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1319 slssqlqdtQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlniqlsdSKKKLQDFASTVEALE 1398
Cdd:PTZ00121 1650 ---------EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE------------ALKKEAEEAKKAEELK 1708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1399 EGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER 1478
Cdd:PTZ00121 1709 KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1479 DRAEAEAREKETKAL--SLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEE------ 1550
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIfdNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEdgnkea 1868
|
730 740
....*....|....*....|....*.
gi 92091586 1551 -MKTQLEELEDELQATEDAKLRLEVN 1575
Cdd:PTZ00121 1869 dFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
858-1406 |
1.08e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 89.74 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKnllqEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEAR 937
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 LEEEEDRGQQLQAERKKMaqqmldleeqleeeeaarQKLQlEKVTAEAKIKKLEDEILvmdDQNNKLSKERKLLEERISD 1017
Cdd:PRK03918 268 IEELKKEIEELEEKVKEL------------------KELK-EKAEEYIKLSEFYEEYL---DELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKLKNKHESM---ISELEVRLKKEEKSRQ---ELEKLKRKLEGdasdfhEQIADLQAQIAEL--- 1088
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELekrLEELEERHELYEEAKAkkeELERLKKRLTG------LTPEKLEKELEELeka 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1089 KMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSE---------RAARNKAEKQKRDLGEELEALK 1159
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelleeyTAELKRIEKELKEIEEKERKLR 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1160 TELEDTLDSTATQQELRakREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELT--------------EQLEQFKRA 1225
Cdd:PRK03918 480 KELRELEKVLKKESELI--KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeikslkkelEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1226 KANLDKNKQTLEKENADLAGELRVLG-QAKQEVEHKKKKLEAQVQELQSkCSDGERARAELNDKVHKLQNEVESVTGMLN 1304
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEELDKAFEELA 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1305 EAEGKAIKLAKDVASLSSQLqdTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTlniqLSDSK 1384
Cdd:PRK03918 637 ETEKRLEELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAK 710
|
570 580
....*....|....*....|..
gi 92091586 1385 KKLQDFASTVEALEEGKKRFQK 1406
Cdd:PRK03918 711 KELEKLEKALERVEELREKVKK 732
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
858-1399 |
4.22e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDelQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEIlhemear 937
Cdd:PRK02224 193 KAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL------- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 leeeEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqlekvTAEAKIKKLEDEILvmDDQNNKLSKERKLLEERISD 1017
Cdd:PRK02224 264 ----RETIAETEREREELAEEVRDLRERLEELEEERDDL-----LAEAGLDDADAEAV--EARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKlknkhesMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1097
Cdd:PRK02224 333 CRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1098 ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNK----------AEKQKRDLGEELEALKTELEDTLD 1167
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1168 STATQQELRAKREQEVTVLKKALDEETRSHEAQ--VQEMRQKHAQAVEELTEQLEQFKRAKANLD-------KNKQTLEK 1238
Cdd:PRK02224 486 DLEEEVEEVEERLERAEDLVEAEDRIERLEERRedLEELIAERRETIEEKRERAEELRERAAELEaeaeekrEAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1239 ENADLAGELRVLGQAKQEVEHKKKKLEAqVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVA 1318
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFD 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1319 slSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQ---LDEEMEAKQNL-ERHistlnIQLSDSKKKLQDFASTV 1394
Cdd:PRK02224 645 --EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELrERR-----EALENRVEALEALYDEA 717
|
....*
gi 92091586 1395 EALEE 1399
Cdd:PRK02224 718 EELES 722
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
882-1488 |
4.33e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 882 LKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMaqqmld 961
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV------ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 962 LEEQLEEEEAARQKLQLEKVtaEAKIKKLEDEIlvmddqnnklskerKLLEERISDLTTNLAEEEEKAKNLTKLKNKHES 1041
Cdd:PRK03918 231 KELEELKEEIEELEKELESL--EGSKRKLEEKI--------------RELEERIEELKKEIEELEEKVKELKELKEKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1042 MIsELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIR 1121
Cdd:PRK03918 295 YI-KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1122 ELEGH--------ISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTatqQELRaKREQEVTVLKKALDEE 1193
Cdd:PRK03918 373 ELERLkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI---EELK-KAKGKCPVCGRELTEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1194 TRsheaqvQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQS 1273
Cdd:PRK03918 449 HR------KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEK 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1274 KCSDGERARAELNdKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKL-NVSTKLRQLEE-- 1350
Cdd:PRK03918 523 KAEEYEKLKEKLI-KLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVeELEERLKELEPfy 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1351 -ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRF-QKEIENLTQQYEEKAAAYDKLEKT 1428
Cdd:PRK03918 602 nEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAE 681
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1429 KNRLQQELDDLVVDLDNQRQLVSNLEKKQR---KFDQLLAEEKNISSKYADERDRAEAEAREK 1488
Cdd:PRK03918 682 LEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1043-1618 |
6.36e-17 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 87.59 E-value: 6.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1043 ISELEVRLKKEEKSRQELEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALAR----LDDEI------- 1110
Cdd:pfam12128 267 YKSDETLIASRQEERQETSAeLNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQhgafLDADIetaaadq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1111 -------AQKNNALKKIRELEGHISDLQEDLDSERAA---RNKAE----KQKRD-LGEELEALKTELEDTLDstATQQEL 1175
Cdd:pfam12128 347 eqlpswqSELENLEERLKALTGKHQDVTAKYNRRRSKikeQNNRDiagiKDKLAkIREARDRQLAVAEDDLQ--ALESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1176 RAKREQEVTVLKKALDE-ETRSHEAQVqemRQKHAQAVEELTEQLEQFKRAkanLDKNKQTLEKENA---DLAGELRVLG 1251
Cdd:pfam12128 425 REQLEAGKLEFNEEEYRlKSRLGELKL---RLNQATATPELLLQLENFDER---IERAREEQEAANAeveRLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1252 QAKQEVEHKKKKLEAQVQELQSKCsdgERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKlakdvaslSSQLQDTQ--- 1328
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSAL---DELELQLFPQAGTLLHFLRKEAPDWEQSIGKVIS--------PELLHRTDldp 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1329 ELLQEETRQKLNV-STKLR--------------QLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST 1393
Cdd:pfam12128 568 EVWDGSVGGELNLyGVKLDlkridvpewaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1394 VEALEEGKKRFQKEIENLTQQYEEK-AAAYDKLEKTKNRLQQELDDLVVDL-----DNQRQLVSNLEKKQRKFdQLLAEE 1467
Cdd:pfam12128 648 LKNARLDLRRLFDEKQSEKDKKNKAlAERKDSANERLNSLEAQLKQLDKKHqawleEQKEQKREARTEKQAYW-QVVEGA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1468 KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELerTNKMLKAEMEDLVSSKDDVGKNVHELEK-------- 1539
Cdd:pfam12128 727 LDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD--VIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqet 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1540 ---SKRALETQMEEMKTQLEELEDELQA-TEDAKLRLEVNMQALKGQfeRDLQARDEQNEEKRRQLQRQLHEYETELEDE 1615
Cdd:pfam12128 805 wlqRRPRLATQLSNIERAISELQQQLARlIADTKLRRAKLEMERKAS--EKQQVRLSENLRGLRCEMSKLATLKEDANSE 882
|
...
gi 92091586 1616 RKQ 1618
Cdd:pfam12128 883 QAQ 885
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1192-1714 |
7.65e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.02 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1192 EETRSHEAqVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENadlagelrvlgQAKQEVEhkkkKLEAQVQEL 1271
Cdd:PRK02224 200 EEKDLHER-LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE-----------ERREELE----TLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1272 QSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEE 1351
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfqkEIENLTQQYEEKAAAYDKLEKTKNR 1431
Cdd:PRK02224 344 AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1432 LQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS-------SKYADERDRAEaEAREKETKALSLARALEEALE 1504
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcgqpvegSPHVETIEEDR-ERVEELEAELEDLEEEVEEVE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1505 AKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALK---G 1581
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAReevA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1582 QFERDLQARDEQNE--EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDL-ELQADSAIKGREEAIKQLRKLQ 1658
Cdd:PRK02224 576 ELNSKLAELKERIEslERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKrERKRELEAEFDEARIEEAREDK 655
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1659 AQMKDFQRELEDA----RASRDEIFAT--AKENE-KKAKSLEADLMQLQEDLAAAERARKQAD 1714
Cdd:PRK02224 656 ERAEEYLEQVEEKldelREERDDLQAEigAVENElEELEELRERREALENRVEALEALYDEAE 718
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1812 |
1.01e-16 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 87.02 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 857 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQlqaetelYAEAEEMRVRLAAKKQELEEIlHEMEA 936
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY-------ENELDPLKNRLKEIEHNLSKI-MKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 937 RLEEEEDRGQQLQAERKKMAQQMLDLEE-QLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERI 1015
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1016 S--DLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDA-------SDFHEQIADLQAQIA 1086
Cdd:TIGR00606 350 GrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAktaaqlcADLQSKERLKQEQAD 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1087 ELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDL---QEDLDSERAARNKAEKQK--RDLGEELEALKTE 1161
Cdd:TIGR00606 430 EIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIlelDQELRKAERELSKAEKNSltETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1162 LEDTLDSTATQQELRAKREQEVTVLKKALdEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA------NLDKNKQT 1235
Cdd:TIGR00606 510 KADLDRKLRKLDQEMEQLNHHTTTRTQME-MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1236 LEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAElNDKVHKLQNEVEsvtgmlneaegkaiKLAK 1315
Cdd:TIGR00606 589 TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIE--------------KSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1316 DVASLSSqlqdtqellqeetrqKLNV-STKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLniqlsdsKKKLQDFASTV 1394
Cdd:TIGR00606 654 QRAMLAG---------------ATAVySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDL-------QSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1395 EALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLdnqRQLVSNLEKKQRKFDQLLAEEKNISSKY 1474
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI---QRLKNDIEEQETLLGTIMPEEESAKVCL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1475 ADER--DRAEAEAREKETKALSLAraleeALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK 1552
Cdd:TIGR00606 789 TDVTimERFQMELKDVERKIAQQA-----AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1553 TQLEELEDElqatedaKLRLEVNMQAlKGQFErdlqardEQNEEKRRQLQrqlhEYETELEDERKQralaaaaKKKLEGD 1632
Cdd:TIGR00606 864 SKTNELKSE-------KLQIGTNLQR-RQQFE-------EQLVELSTEVQ----SLIREIKDAKEQ-------DSPLETF 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1633 LKDLELQADSAIKGREEAIKqlrKLQAQMKDFQRELEDARASRDEIFATAKEN-EKKAKSLEADLMQLQEDLAAAERARK 1711
Cdd:TIGR00606 918 LEKDQQEKEELISSKETSNK---KAQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQE 994
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1712 QADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNE 1791
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLAL 1074
|
970 980
....*....|....*....|.
gi 92091586 1792 SARQQLERQNKELRSKLHEME 1812
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQ 1095
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
835-1489 |
1.64e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 835 KLRNWQWWRLFTKVKPLLQVTRQ---EEEMQAKEDELQKTKERQqKAEnELKELEQKHsQLTEEKNLLQEQLQAEtELYA 911
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKK-KAD-EAKKAEEKK-KADEAKKKAEEAKKAD-EAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 912 EAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQ-AERKKMAQQMlDLEEQLEEEEAARQKLQLEKVTAEAK---- 986
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEaAEEKAEAAEK-KKEEAKKKADAAKKKAEEKKKADEAKkkae 1401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 987 -IKKLEDEILVMDDQNNKLSKERKLLEE-RISDLTTNLAEEEEKAKnltKLKNKHESMISELEVRLKKEEKSRQELEKLK 1064
Cdd:PTZ00121 1402 eDKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1065 RKLEGDASDFHEQIADLQAQIAELKM--QLAKKEEELQAALARLDDEIAQKNNALKKIRELEGhisdlQEDLDSERAARN 1142
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKaaEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK-----AEEKKKADELKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1143 KAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQA-----VEELTE 1217
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAeelkkAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1218 QLEQFKRAKANLDKNKQTLEKENADlaGELRVLGQAKQEVEHKKKKLEAQVQElqskcsDGERARAELNDKVHKLQNEVE 1297
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEE--NKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAE 1705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1298 SVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQklnvSTKLRQLEEERNSLQdQLDEEMEAKQNLERHISTLN 1377
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEAV 1780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1378 IQLSDSKKKLQDFASTVEALEEGKKRFQKEIENltqqyEEKAAAYdkLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ 1457
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEG-----GKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHK 1853
|
650 660 670
....*....|....*....|....*....|..
gi 92091586 1458 RKFDQLLAEEKNISSKYADERDRAEAEAREKE 1489
Cdd:PTZ00121 1854 FNKNNENGEDGNKEADFNKEKDLKEDDEEEIE 1885
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
849-1696 |
1.95e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 849 KPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEK---------NLLQEQLQAETELYAEAEEMRVR 919
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEeyllyldylKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 920 LAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmdd 999
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL----- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1000 qnNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAsDFHEQIA 1079
Cdd:pfam02463 331 --KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK-SEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1080 DLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1159
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1160 TELEDTLDSTATQQELRAKREQEVtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKE 1239
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKV---LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1240 NADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNE--AEGKAIKLAKDV 1317
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKdtELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1318 ASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERhistLNIQLSDSKKKLQDFASTVEAL 1397
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ----LEIKKKEQREKEELKKLKLEAE 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1398 EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADE 1477
Cdd:pfam02463 721 ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1478 RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEE 1557
Cdd:pfam02463 801 EELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELE 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1558 LEDELQATEDAKLRLEVNMQALkgqfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLE 1637
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEKKEL----EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1638 LQADSAIKGrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADL 1696
Cdd:pfam02463 957 EEEERNKRL-LLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
840-1439 |
3.68e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 85.02 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 840 QWWRLFTKVKPLLQVTRQEEEMQAkedELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVR 919
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHT---ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 920 LAAKKQELEEILHEMEARLEEEEDRgQQLQAERKKMaQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDD 999
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLT-QKLQSLCKEL-DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1000 QNNKLSKERKLLEERISDLTTNLAEEEEKAKNltklknkhesmiseLEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIA 1079
Cdd:TIGR00618 446 AITCTAQCEKLEKIHLQESAQSLKEREQQLQT--------------KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1080 DLQAqiaelKMQLAKKEEELQAALARLDDEIAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEEL 1155
Cdd:TIGR00618 512 HPNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDI 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1156 EALKTELEDTLDSTATQQELR-----AKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLD 1230
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1231 KNKQTLEKENADLA------GELRVLGQAKQEVEHKKKKLeaqvQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLN 1304
Cdd:TIGR00618 667 IRVLPKELLASRQLalqkmqSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALN 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1305 EAEGKAIKLAKDV--ASLSSQLQDTQELLQEETRqklnvSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIST-----LN 1377
Cdd:TIGR00618 743 QSLKELMHQARTVlkARTEAHFNNNEEVTAALQT-----GAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdED 817
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1378 IQLSDSKKKLQDFASTVEALEEgKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1439
Cdd:TIGR00618 818 ILNLQCETLVQEEEQFLSRLEE-KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1061-1915 |
8.40e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.01 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1061 EKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQAALARLD---DEIAQKNNALKKIRELEghiSDLQEDLdse 1137
Cdd:pfam15921 74 EHIERVLE----EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQtklQEMQMERDAMADIRRRE---SQSQEDL--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1138 raarnkaEKQKRDLGEELEALKTELEDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQkhaqaveeLTE 1217
Cdd:pfam15921 144 -------RNQLQNTVHELEAAKCLKEDMLEDSNTQIE--------------QLRKMMLSHEGVLQEIRS--------ILV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1218 QLEQFKRAKANLDKNKQTLEKENADLAGElRVLGQAKQEVEHKKKKL---EAQVQELQSKCSDgeraRAELndkvhKLQN 1294
Cdd:pfam15921 195 DFEEASGKKIYEHDSMSTMHFRSLGSAIS-KILRELDTEISYLKGRIfpvEDQLEALKSESQN----KIEL-----LLQQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1295 EVESVTGMLNEAEGKAIKLAKDVASLSSQ---LQDTQELLQEETRQKlnVSTKLRQLEEERNSLQDQLDEEMEAKQNLER 1371
Cdd:pfam15921 265 HQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQEQARNQ--NSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1372 HISTLNIQLSDSKKKLqdfastVEALEEgKKRFQKEIENLTQQYEEKAAAYDKLEKTKNrLQQELDDLVVDLDNQRQLvs 1451
Cdd:pfam15921 343 KIEELEKQLVLANSEL------TEARTE-RDQFSQESGNLDDQLQKLLADLHKREKELS-LEKEQNKRLWDRDTGNSI-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1452 NLEKKQRKFDqllaeEKNIsskyadERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEdlvSSKDDVG 1531
Cdd:pfam15921 413 TIDHLRRELD-----DRNM------EVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE---STKEMLR 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1532 KNVHELEKSKRALETQ---MEEMKTQLEELEDELQAT--EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLH 1606
Cdd:pfam15921 479 KVVEELTAKKMTLESSertVSDLTASLQEKERAIEATnaEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMA 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1607 EYETELEDERKQRAlaaaakkklegDLKDLELQadsaiKGREEAIKQLRK--LQAQMKDFQRELEDARASRDEIFATAKE 1684
Cdd:pfam15921 559 EKDKVIEILRQQIE-----------NMTQLVGQ-----HGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1685 NEKKAKSLEADLMQLQEdlAAAERARKQADlekeelaeelasslsgrnaLQDEKRRLEARIAQLEEELEEEQGNMEAMSD 1764
Cdd:pfam15921 623 LEARVSDLELEKVKLVN--AGSERLRAVKD-------------------IKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1765 RVRKATQQAEQLSNELATERSTAQKN-ESARQQLERQNKelrSKLHEMEGAVKSKFKST-----IAALEAKIAQLEEQVE 1838
Cdd:pfam15921 682 NFRNKSEEMETTTNKLKMQLKSAQSElEQTRNTLKSMEG---SDGHAMKVAMGMQKQITakrgqIDALQSKIQFLEEAMT 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1839 QEAREKQAatksLKQKDKKLKEILLQVEDER-KMA---EQYKEQAEKGNARVKQLKRQLEEAEE---------ESQRINA 1905
Cdd:pfam15921 759 NANKEKHF----LKEEKNKLSQELSTVATEKnKMAgelEVLRSQERRLKEKVANMEVALDKASLqfaecqdiiQRQEQES 834
|
890
....*....|
gi 92091586 1906 NRRKLQRELD 1915
Cdd:pfam15921 835 VRLKLQHTLD 844
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1322-1940 |
8.46e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.55 E-value: 8.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1322 SQLQDT-QELLQ----EETRQKL-NVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHiSTLNiqlsdskkklqdfastve 1395
Cdd:PRK02224 149 SDRQDMiDDLLQlgklEEYRERAsDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLH-ERLN------------------ 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1396 ALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRL---QQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISS 1472
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHeerREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1473 KYADERD--RAEAEAREKETKALSLARALEEALEAKeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEE 1550
Cdd:PRK02224 290 ELEEERDdlLAEAGLDDADAEAVEARREELEDRDEE---------LRDRLEECRVAAQAHNEEAESLREDADDLEERAEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1551 MKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERkqralaaaakkkle 1630
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIE-ELRERFGDAPVDLGNAEDFLEELREERDELR-------------- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1631 GDLKDLElqadSAIKGREEAIKQLRKLQAQMK--DFQRELEDArasrdEIFATAKENEKKAKSLEADLMQLQEDLAAAER 1708
Cdd:PRK02224 426 EREAELE----ATLRTARERVEEAEALLEAGKcpECGQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1709 ARKQADLEKEELaeelasslSGRNALQDEKRRLEARIAQLEEEleeeqgnMEAMSDRVRKATQQAEQLSNELATERSTAQ 1788
Cdd:PRK02224 497 RLERAEDLVEAE--------DRIERLEERREDLEELIAERRET-------IEEKRERAEELRERAAELEAEAEEKREAAA 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1789 KNESARQQLERQNKELRSKLHEMEGAVKSKfkSTIAALEAKIAQLEEQVEqEAREKQAAtkslkqkdkklkeiLLQVEDE 1868
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-RLREKREA--------------LAELNDE 624
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1869 RKmaEQYKEQAEkgnaRVKQLKRQ-----LEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNE 1940
Cdd:PRK02224 625 RR--ERLAEKRE----RKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1057-1618 |
8.54e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 8.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1057 RQELEKLKRKLE--GDASDFHEQIADLQAQIAELKMQLA--------KKEEELQAALARLDDEIAQknnALKKIRELEGH 1126
Cdd:COG4913 241 HEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAalrlwfaqRRLELLEAELEELRAELAR---LEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1127 ISDLQEDLDSERAARNKAEkqkrdlGEELEALKTELEDTLDSTATQQELRAKREQEVtvlkKALDEETRSHEAQVQEMRQ 1206
Cdd:COG4913 318 LDALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRARLEALL----AALGLPLPASAEEFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1207 KHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLgqakqevEHKKKKLEAQVQELQskcsdgERARAELN 1286
Cdd:COG4913 388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-------ERRKSNIPARLLALR------DALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1287 DKVHKL----------------QNEVESVTG-----MLNEAEgkaikLAKDVASLSSQLQDTQEL--------LQEETRQ 1337
Cdd:COG4913 455 LDEAELpfvgelievrpeeerwRGAIERVLGgfaltLLVPPE-----HYAAALRWVNRLHLRGRLvyervrtgLPDPERP 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1338 KLNVSTKLRQLEEERNSLQDQLDEEM---------EAKQNLERHistlniqlsdskkklqDFASTVEAL-EEGKKRFQKE 1407
Cdd:COG4913 530 RLDPDSLAGKLDFKPHPFRAWLEAELgrrfdyvcvDSPEELRRH----------------PRAITRAGQvKGNGTRHEKD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1408 IEN-LTQQYEEKAAAYDKLEktknRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAR 1486
Cdd:COG4913 594 DRRrIRSRYVLGFDNRAKLA----ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1487 ----EKETKALSLARALEEAleakeelertnkmLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDEL 1562
Cdd:COG4913 670 iaelEAELERLDASSDDLAA-------------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 1563 QATEDAKLRLEVnmQALKGQFERDLQARDEQneEKRRQLQRQLHEYETELEDERKQ 1618
Cdd:COG4913 737 EAAEDLARLELR--ALLEERFAAALGDAVER--ELRENLEERIDALRARLNRAEEE 788
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1462 |
1.21e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.43 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 894 EEKNLLQ--EQLQAETELYAEAEEMRVRLAAKKQELEEIlhemearleeeEDRGQQLQAERKKMAQQmlDLEEQLEEEEA 971
Cdd:COG4913 219 EEPDTFEaaDALVEHFDDLERAHEALEDAREQIELLEPI-----------RELAERYAAARERLAEL--EYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 972 ARQKLQLekvtAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEeeKAKNLTKLKNKHESMISELEVRLK 1051
Cdd:COG4913 286 AQRRLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1052 KEEKSRQELEKLKRKLEGDASDFheqiADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAL----KKIRELEGHI 1127
Cdd:COG4913 360 RRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELreleAEIASLERRK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1128 SDLQEDLDSERAARNKAEKQKRD----LGEELEALKTELE---------------------------DTLDSTATQQELR 1176
Cdd:COG4913 436 SNIPARLLALRDALAEALGLDEAelpfVGELIEVRPEEERwrgaiervlggfaltllvppehyaaalRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1177 -------AKREQEVTVLKKALDE--ETRSHEAQ---VQEMRQKHAQAVEELTEQLEQFKRA--KANLDKNKQTL-EKENA 1241
Cdd:COG4913 516 yervrtgLPDPERPRLDPDSLAGklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAitRAGQVKGNGTRhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1242 DLAGELRVLGqakQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEgkaikLAKDVASLS 1321
Cdd:COG4913 596 RRIRSRYVLG---FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW-----DEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1322 SQLQDtqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGK 1401
Cdd:COG4913 668 REIAE----LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1402 KRFQkeIENLTQQYEEkAAAYDKLEKTKNRLQQELDDLVVDLDNQRQlvsNLEKKQRKFDQ 1462
Cdd:COG4913 744 RLEL--RALLEERFAA-ALGDAVERELRENLEERIDALRARLNRAEE---ELERAMRAFNR 798
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1043-1491 |
1.72e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.04 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1043 ISELEVRLKKEEKSRQELEKLK------RKLEGDASDFHEQIADLQAQIAELKMQLAKKE-EELQAALARLDDEI----A 1111
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRelaeryAAARERLAELEYLRAALRLWFAQRRLELLEAElEELRAELARLEAELerleA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1112 QKNNALKKIRELEGHISD--------LQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEV 1183
Cdd:COG4913 317 RLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1184 TVLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKN--------KQTLEKENADL--AGEL------ 1247
Cdd:COG4913 397 EEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllalrdalAEALGLDEAELpfVGELievrpe 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1248 ---------RVLG--------------QAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNE--------- 1295
Cdd:COG4913 473 eerwrgaieRVLGgfaltllvppehyaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKphpfrawle 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1296 -----------VESVTGMlnEAEGKAIKLA-----------KDVASLSSQL----QDTQELLQEETRQKLNVSTKLRQLE 1349
Cdd:COG4913 553 aelgrrfdyvcVDSPEEL--RRHPRAITRAgqvkgngtrheKDDRRRIRSRyvlgFDNRAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1350 EERNSLQDQLDEeMEAKQNLERHISTLN---IQLSDSKKKLQDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYD 1423
Cdd:COG4913 631 ERLEALEAELDA-LQERREALQRLAEYSwdeIDVASAEREIAELEAELERLDASSDDLaalEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1424 KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE-----------KNISSKYADERDRAEAEAREKETK 1491
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgdaveRELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1081-1922 |
1.73e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 83.10 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1081 LQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT 1160
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1161 ELEDTLDSTATQQELRAKREQEvtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKEN 1240
Cdd:pfam02463 220 ELEEEYLLYLDYLKLNEERIDL----LQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1241 ADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcsdgeraraelndkvhKLQNEVESVTGMLNEAEGKAIKLAKDVASL 1320
Cdd:pfam02463 296 EELKSELLKLERRKVDDEEKLKESEKEKKKAEK-----------------ELKKEKEEIEELEKELKELEIKREAEEEEE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1321 SSQLQdtqelLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEG 1400
Cdd:pfam02463 359 EELEK-----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1401 KKrfQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDR 1480
Cdd:pfam02463 434 EE--EESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1481 AEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1560
Cdd:pfam02463 512 LLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1561 ELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQA 1640
Cdd:pfam02463 592 KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSEL 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1641 DSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDlaAAERARKQADLEKEEL 1720
Cdd:pfam02463 672 TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK--INEELKLLKQKIDEEE 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1721 AEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKAtqQAEQLSNELATERSTAQKNESARQQLERQ 1800
Cdd:pfam02463 750 EEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKA--QEEELRALEEELKEEAELLEEEQLLIEQE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1801 NKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQaATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAE 1880
Cdd:pfam02463 828 EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL-LLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 92091586 1881 KGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNE 1922
Cdd:pfam02463 907 QKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1030-1688 |
2.96e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.61 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1030 KNLTklkNKHESMISELEVRLKK-------EEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK---KEEEL 1099
Cdd:TIGR04523 25 KNIA---NKQDTEEKQLEKKLKTiknelknKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKnkdKINKL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1100 QAALARLDDEI----AQKNNALKKIRELE--------------GHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE 1161
Cdd:TIGR04523 102 NSDLSKINSEIkndkEQKNKLEVELNKLEkqkkenkknidkflTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1162 LEDTLDSTATQQELRAKREQEVTVLKKaldeetrsheaqvqeMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENA 1241
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKK---------------KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1242 DLAGELRVLGQAKQEVEHKKKKLEAQVQELQS---KCSDGERARAELNDKVHKLQNEVESvtGMLNEAEGKAIKLAKDVA 1318
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1319 SLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALE 1398
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1399 EGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER 1478
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1479 DRAEAEAREKETKALSLARAleealeakeelertNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEEL 1558
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEE--------------KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1559 EDELQATEDAKLRLEVNMQALKgqferdLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLEL 1638
Cdd:TIGR04523 551 DFELKKENLEKEIDEKNKEIEE------LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1639 Q---ADSAIKGREEAIKQLRKLQAQMKDfqrELEDARASRDEIFATAKENEKK 1688
Cdd:TIGR04523 625 EnekLSSIIKNIKSKKNKLKQEVKQIKE---TIKEIRNKWPEIIKKIKESKTK 674
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1142-1883 |
6.43e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 81.17 E-value: 6.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1142 NKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKRE---QEVTVLKKALDEETRSHEA--QVQEMRQKHAQAVEELT 1216
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAElltLRSQLLTLCTPCMPDTYHErkQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1217 EQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELqsKCSDGERARAELNDKVHKLQNEV 1296
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1297 ESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRqklnvstkLRQLEEERNSLQDQLDEEMEakqnLERHISTL 1376
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIH--------IRDAHEVATSIREISCQQHT----LTQHIHTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1377 NIQLSDSKKKLQDFASTVEAL--EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQelddlvVDLDNQRQLVSNLE 1454
Cdd:TIGR00618 385 QQQKTTLTQKLQSLCKELDILqrEQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCA------AAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1455 KKQRKFDQLLAEEKNIsskyadERDRAEAEAREKETKALSLARALEEALEAKEELERTNKmLKAEMEDLVSSKDDVGK-- 1532
Cdd:TIGR00618 459 IHLQESAQSLKEREQQ------LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIH-PNPARQDIDNPGPLTRRmq 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1533 ----NVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKgqferdlqardEQNEEKRRQLQRQLHEY 1608
Cdd:TIGR00618 532 rgeqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK-----------EDIPNLQNITVRLQDLT 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1609 ETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMK-DFQRELEDARASRDEIFATAKENEK 1687
Cdd:TIGR00618 601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1688 KAKSLEADLMQLQEDLAAAErarkQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVR 1767
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLA----QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1768 KATQQAEQLSNELAT-ERSTAQKNESARQQLERQNKELRSKLHEM---EGAVKSKFKSTIAALEA---KIAQLEEQVEQE 1840
Cdd:TIGR00618 757 KARTEAHFNNNEEVTaALQTGAELSHLAAEIQFFNRLREEDTHLLktlEAEIGQEIPSDEDILNLqceTLVQEEEQFLSR 836
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 92091586 1841 AREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGN 1883
Cdd:TIGR00618 837 LEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1092-1678 |
8.04e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.49 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 LAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLdseraarNKAEKQKRDLGEELEALKTELEDtLDSTAT 1171
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI-------NEISSELPELREELEKLEKEVKE-LEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1172 QQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKhaqaVEELTEQLEQFKRAKAnldknkqtLEKENADLAGELRVLG 1251
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKE----IEELEEKVKELKELKE--------KAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1252 QAKQEVEHKKKKLEAQVQELQSKCSDGEraraELNDKVHKLQNEVESVTGMLNEAEGKAiKLAKDVASLSSQLQDTQELL 1331
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1332 QEETRQKLNvsTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKK-----LQDFASTVEALEEGKKRFQK 1406
Cdd:PRK03918 382 TGLTPEKLE--KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpVCGRELTEEHRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1407 EIENLTqqyEEKAAAYDKLEKTKNRLqqelddlvVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAR 1486
Cdd:PRK03918 460 ELKRIE---KELKEIEEKERKLRKEL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1487 EKETKALSLaraleealeaKEELERTNKMLKaEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMK-TQLEELEDELQAT 1565
Cdd:PRK03918 529 KLKEKLIKL----------KGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKEL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1566 E----------DAKLRLEVNMQALKGQFERDLQARDEQNEEKRR--QLQRQLHEYETELEDERKQRALAAAAKKKLEgdL 1633
Cdd:PRK03918 598 EpfyneylelkDAEKELEREEKELKKLEEELDKAFEELAETEKRleELRKELEELEKKYSEEEYEELREEYLELSRE--L 675
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 92091586 1634 KDLELQADSAIKGREEAIKQLRKLQAQ---MKDFQRELEDARASRDEI 1678
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEEleeREKAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1284-1934 |
1.48e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 79.29 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1284 ELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEM 1363
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1364 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1443
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1444 DNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1523
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1524 VSSK---DDVGKNVHELEKSKRALETQ-----MEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQ---FERDLQARDE 1592
Cdd:TIGR04523 277 EQNNkkiKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQisqLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1593 QNEEKRRQLQrqlhEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDAR 1672
Cdd:TIGR04523 357 ENSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1673 ASRDEIFATAKENEKKAKSLEADLMQLQedlaaaerarkqadlekeelaeelasslSGRNALQDEKRRLEARIAQLEEEL 1752
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLD----------------------------NTRESLETQLKVLSRSINKIKQNL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1753 EEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKS-KFKSTIAALEAKIA 1831
Cdd:TIGR04523 485 EQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKdDFELKKENLEKEID 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1832 QLEEQVEQEAREKqaatKSLKQKDKKLKEILLQVEDERKmaEQYKEQAEKGnARVKQLKRQLEEAEEESQRINANRRKLQ 1911
Cdd:TIGR04523 565 EKNKEIEELKQTQ----KSLKKKQEEKQELIDQKEKEKK--DLIKEIEEKE-KKISSLEKELEKAKKENEKLSSIIKNIK 637
|
650 660
....*....|....*....|...
gi 92091586 1912 RELDEATESNEAMGREVNALKSK 1934
Cdd:TIGR04523 638 SKKNKLKQEVKQIKETIKEIRNK 660
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
3.90e-14 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 68.23 E-value: 3.90e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 92091586 31 AAKRLVWVPSEKQGFEAASIKEEKGDEVVVELvENGKKVTVGKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
927-1671 |
5.39e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 77.85 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 927 LEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLeeeeaarQKLQLEKvTAEAKIKKLEDEilVMDDQNNKLSK 1006
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRRESQ--SQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1007 ERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEL-EVRLKKEEKSRQEL------------------EKLKRKL 1067
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrSILVDFEEASGKKIyehdsmstmhfrslgsaiSKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1068 EGDASDFHEQIADLQAQIAELKmqlAKKEEELQAALARLDDEIAQknnalkKIRELEGHISDLQEDLDSERAARNKAEKQ 1147
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALK---SESQNKIELLLQQHQDRIEQ------LISEHEVEITGLTEKASSARSQANSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1148 krdlgeeLEALKtelEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTE---QLEQFKR 1224
Cdd:pfam15921 301 -------LEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1225 AKANLDKNkqtLEKENADLAGELRVLGQAKQE--------------VEHKKKKLEAQVQELQskcsdgeRARAELNDKVH 1290
Cdd:pfam15921 371 ESGNLDDQ---LQKLLADLHKREKELSLEKEQnkrlwdrdtgnsitIDHLRRELDDRNMEVQ-------RLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1291 KLQNEVESvtgMLNEAEGKAIKLAKdVASLSSQLQDTQELL----QEETRQKLNVSTKLRQLEEERNSLQDQldeemeak 1366
Cdd:pfam15921 441 ECQGQMER---QMAAIQGKNESLEK-VSSLTAQLESTKEMLrkvvEELTAKKMTLESSERTVSDLTASLQEK-------- 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1367 qnlERHISTLNIQLSDSKK----KLQDFAStVEALEEGKKRFQKEIENLTQQYEEKaaaydklEKTKNRLQQELDDLVVD 1442
Cdd:pfam15921 509 ---ERAIEATNAEITKLRSrvdlKLQELQH-LKNEGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1443 LDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMED 1522
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQ 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1523 LV----SSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedAKLRLEVNMQALKGQFERDLQA------RDE 1592
Cdd:pfam15921 658 LLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---AQSELEQTRNTLKSMEGSDGHAmkvamgMQK 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1593 QNEEKRRQ---LQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELE 1669
Cdd:pfam15921 735 QITAKRGQidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALD 814
|
..
gi 92091586 1670 DA 1671
Cdd:pfam15921 815 KA 816
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1117-1915 |
6.67e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 77.78 E-value: 6.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1117 LKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDT------LDSTATQQELRAK-REQEVTVLKKA 1189
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNlskimkLDNEIKALKSRKKqMEKDNSELELK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1190 LDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQ 1269
Cdd:TIGR00606 292 MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1270 ELQSKCSDGERARAELND---------KVHKLQNEVESVTGMLNE-------AEGKAIKLAKDVASLSSQLQDTQELLQE 1333
Cdd:TIGR00606 372 SLATRLELDGFERGPFSErqiknfhtlVIERQEDEAKTAAQLCADlqskerlKQEQADEIRDEKKGLGRTIELKKEILEK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1334 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLER-----HISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEI 1408
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKaeknsLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1409 ENLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLlaeeknisskyadeRDRaeaea 1485
Cdd:TIGR00606 532 TTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQT--------------RDR----- 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1486 reketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGK--NVHELEKSKRALETQMEEMKTQLEELEDELQ 1563
Cdd:TIGR00606 593 ---------LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGATA 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1564 ATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRqLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSA 1643
Cdd:TIGR00606 664 VYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD-LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1644 IKGREEAIKQLRKLQAQMKDFQRELEDarasRDEIFATAKENEKKAKSLEAD---LMQLQEDLAAAERARKQadlekeel 1720
Cdd:TIGR00606 743 EKEIPELRNKLQKVNRDIQRLKNDIEE----QETLLGTIMPEEESAKVCLTDvtiMERFQMELKDVERKIAQ-------- 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1721 AEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRvRKATQQAEQLSNELATERSTAQKNESARQQLERQ 1800
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1801 NKELRSKLHEMEGAVKSKFKSTI---AALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVED-ERKMAEQYK 1876
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSpleTFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDiENKIQDGKD 969
|
810 820 830
....*....|....*....|....*....|....*....
gi 92091586 1877 EQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELD 1915
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDID 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1129-1936 |
1.95e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 76.33 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1129 DLQEDLDSERAARNKAEKQKRDLGEELEALKTE--LEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQ 1206
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEeaKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1207 KHAQAVEELTEQLEQFKRAK-----ANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERA 1281
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEevrkaEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1282 RAELNDKVHKLQNEVESVTGMLNEAEGKAiklakdvaslsSQLQDTQELLQEETRQKlnvSTKLRQLEEERNSlqdqldE 1361
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAAIKA-----------EEARKADELKKAEEKKK---ADEAKKAEEKKKA------D 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1362 EMEAKQNLERHISTLNIQLSDSKKK---LQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDD 1438
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKadaAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1439 LVVDLDNQRQLVSNLEKKQRKFDQLlaEEKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLK 1517
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADEL--KKAAAAKKKADEaKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1518 AEMEDlvSSKDDVGKNVHELEKSKRALETQMEEMKTQleelEDELQATEDAKLRLEVNMQAlkgqferdlqardeqnEEK 1597
Cdd:PTZ00121 1464 KKAEE--AKKADEAKKKAEEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKA----------------EEA 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1598 RRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQmkdfqrELEDARASRDE 1677
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE------EAKKAEEARIE 1595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1678 IFATAKENEKKAKSLEADlmQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQG 1757
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAK--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1758 NMEAmsDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKElrsklheMEGAVKSKFKSTIAALEAKIAQLEEQV 1837
Cdd:PTZ00121 1674 KKKA--EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK-------AEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1838 EQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEA 1917
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
810
....*....|....*....
gi 92091586 1918 TESNEAMGREVNALKSKLR 1936
Cdd:PTZ00121 1825 KEMEDSAIKEVADSKNMQL 1843
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
853-1598 |
3.34e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 75.47 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEaeemrVRLAAKKQELEEILH 932
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERE-----LSKAEKNSLTETLKK 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARqklqlEKVTAEAKIKKledeilvmddqnnklskerklLE 1012
Cdd:TIGR00606 502 EVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-----DKMDKDEQIRK---------------------IK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAElkmql 1092
Cdd:TIGR00606 556 SRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD----- 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1093 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA-------RNKAEKQKRDLGEELEALKTELEDT 1165
Cdd:TIGR00606 631 VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrVFQTEAELQEFISDLQSKLRLAPDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1166 LDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELteqleqfKRAKANLDKNKQTLEKENA---- 1241
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI-------QRLKNDIEEQETLLGTIMPeees 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1242 --DLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcSDGERARAELNDKVHKLQNEVESVTgmlneaegkaiklakdvas 1319
Cdd:TIGR00606 784 akVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVV------------------- 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1320 lsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNslqdQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEE 1399
Cdd:TIGR00606 843 --SKIELNRKLIQDQQEQIQHLKSKTNELKSEKL----QIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1400 GKKRFQKEIENLTQQYEEkaaaydklekTKNRLQQELDDLVVDLDNQRQLVSNLEKK--QRKFDQLLAEEKNISSKYADE 1477
Cdd:TIGR00606 917 FLEKDQQEKEELISSKET----------SNKKAQDKVNDIKEKVKNIHGYMKDIENKiqDGKDDYLKQKETELNTVNAQL 986
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1478 RDraEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEkskralETQMEEMKTQLEE 1557
Cdd:TIGR00606 987 EE--CEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMG------QMQVLQMKQEHQK 1058
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 92091586 1558 LEDELQATEDAKLRLEVNMQALKGQ---FERDLQARDEQNEEKR 1598
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1465-1962 |
5.12e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1465 AEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAE----MEDLVSSKDD----VGKNVHE 1536
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkAEEARKAEDAkrveIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1537 ---LEKSKRALETQMEEMKTQLEELE--DELQATEDAKlRLEvnmQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETE 1611
Cdd:PTZ00121 1163 arkAEEARKAEDAKKAEAARKAEEVRkaEELRKAEDAR-KAE---AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1612 LEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIK--QLRKLQAQMK--------------DFQRELEDARASr 1675
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKadELKKAEEKKKadeakkaeekkkadEAKKKAEEAKKA- 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1676 DEIFATAKENEKKAKSLEAdlmQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEAriaqleeelEEE 1755
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKK---KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA---------AKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1756 QGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNK--ELRSKLHEMEGAVKSKFKSTIA--ALEAKIA 1831
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKKADEAKKKAEEAkkAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1832 QLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQ 1911
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1912 RELDEATESNEAMGREVNALKSKLRRGNETSFVPSRRSGGRRVIENADGSE 1962
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1584 |
6.25e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 74.62 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 846 TKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELE-QKHSQLTEEKNLLQEQLQAETEL------YAEAEEMRV 918
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEiKREAEEEEEEELEKLQEKLEQLEeellakKKLESERLS 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 919 RLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMD 998
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 999 DQNNKLSKERKLLEERISDLTTNLAEEEEKA-----KNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD 1073
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERsqkesKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIST 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1074 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDseRAARNKAEKQKRDLGE 1153
Cdd:pfam02463 548 AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD--KATLEADEDDKRAKVV 625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1154 ELEALKTELEDTLDSTATQQELRAKreqevtvLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNK 1233
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRK-------GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQN--EVESVTGMLNEAEGKAI 1311
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeeKEEEKSELSLKEKELAE 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1312 KLAKDVASLSSQLQDTQELLQEETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLqDFA 1391
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEELRALE---EELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL-AEE 854
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1392 STVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS 1471
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYE 934
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1472 SKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEM 1551
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEE 1014
|
730 740 750
....*....|....*....|....*....|...
gi 92091586 1552 KTQLEELEDELQATEDAKLRLEVNMQALKGQFE 1584
Cdd:pfam02463 1015 TCQRLKEFLELFVSINKGWNKVFFYLELGGSAE 1047
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
855-1237 |
1.06e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 855 TRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhem 934
Cdd:PRK02224 359 EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 935 eARLEEEEDRGQQLQAERK-----------KMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeILVMDDQNNK 1003
Cdd:PRK02224 436 -RTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIER 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1004 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESmiselevrlKKEEKsrqeleklkrklEGDASDFHEQIADLQA 1083
Cdd:PRK02224 514 LEERREDLEELIAERRETIEEKRERAEELRERAAELEA---------EAEEK------------REAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1084 QIAELKMQLAKKEEELQaalarlddeiaqknnALKKIRELEGHISDLQEDLDS---ERAARNKAEKQKRDLGEELEALKT 1160
Cdd:PRK02224 573 EVAELNSKLAELKERIE---------------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKR 637
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1161 ELEDTLDSTATqQELRAKREQEVTVLKKAlDEETRSHEAQVQEMrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLE 1237
Cdd:PRK02224 638 ELEAEFDEARI-EEAREDKERAEEYLEQV-EEKLDELREERDDL-QAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
808-1366 |
1.37e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 73.23 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 808 LARKAFAKRQQQ---LTAMKVIQRNCaaylKLRNWQWWRLFTKVKPLLQVTRQE--EEMQAKEDELQKTKERQQKAENEL 882
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRSElrEAKRMYEDKIEELEKQLVLANSEL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 883 KELEQKHSQLTEEKNLLQEQLQA--------ETELYAEAEEMRvRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKK 954
Cdd:pfam15921 359 TEARTERDQFSQESGNLDDQLQKlladlhkrEKELSLEKEQNK-RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 955 MAQQMLDLEEQLEEEEAARQKlQLEKV---TAEAKIKKLEDEILVMDDQNNKLSKERKllEERISDLTTNLAEEEE--KA 1029
Cdd:pfam15921 438 MKSECQGQMERQMAAIQGKNE-SLEKVsslTAQLESTKEMLRKVVEELTAKKMTLESS--ERTVSDLTASLQEKERaiEA 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1030 KN--LTKLKnkhesmiSELEVRLkkeeksrQELEKLKRklEGDasdfheQIADLQAQIAELKMQLAKKE---EELQAALA 1104
Cdd:pfam15921 515 TNaeITKLR-------SRVDLKL-------QELQHLKN--EGD------HLRNVQTECEALKLQMAEKDkviEILRQQIE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1105 RLDDEIAQKNNALKKIR----ELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALktELEDTLDSTATQQELRAKRE 1180
Cdd:pfam15921 573 NMTQLVGQHGRTAGAMQvekaQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDL--ELEKVKLVNAGSERLRAVKD 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1181 ---------QEVTVLKKALDEETRSHEAQVQEMRQKhAQAVEELTEQLE-QFKRAKANLDKNKQTLEKENADLAGELRVL 1250
Cdd:pfam15921 651 ikqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNK-SEEMETTTNKLKmQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1251 GQAKQEVEHKKkkleAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQlqdTQEL 1330
Cdd:pfam15921 730 MGMQKQITAKR----GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ---ERRL 802
|
570 580 590
....*....|....*....|....*....|....*.
gi 92091586 1331 LQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAK 1366
Cdd:pfam15921 803 KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1647-1937 |
1.40e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1647 REEAIKQLRK--------------LQAQMKDFQRELEDARasrdeifaTAKENEKKAKSLEADLMQLQEDLAAAERARKQ 1712
Cdd:COG1196 174 KEEAERKLEAteenlerledilgeLERQLEPLERQAEKAE--------RYRELKEELKELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1713 ADLEKEELAEELASSLsgRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNES 1792
Cdd:COG1196 246 AELEELEAELEELEAE--LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1793 ARQQLERQNKELRSKLHEMEGAVKSKfKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMA 1872
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1873 EQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRR 1937
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1210-1948 |
1.74e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1210 QAVEELTEQLEQFKRAKANLDKnkqtlEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsDGERARAELNDKV 1289
Cdd:COG4913 225 EAADALVEHFDDLERAHEALED-----AREQIELLEPIRELAERYAAARERLAELEYLRAALRLW--FAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1290 HKLQNEVEsvtgmlneaegkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVST-KLRQLEEERNSLQDQLDEEMEAKQN 1368
Cdd:COG4913 298 EELRAELA--------------RLEAELERLEARLDALREELDELEAQIRGNGGdRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1369 LERHISTLNIQLSDSKkklQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnqRQ 1448
Cdd:COG4913 364 LEALLAALGLPLPASA---EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-------ER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1449 LVSNLEKKQRKFDQLLAEEKNISS------------KYADERDRAEAEA------------REKETKALSLARaleeaLE 1504
Cdd:COG4913 434 RKSNIPARLLALRDALAEALGLDEaelpfvgelievRPEEERWRGAIERvlggfaltllvpPEHYAAALRWVN-----RL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1505 AKEELERTNKmLKAEMEDLVSSKDDVGKNVHELE-KSKRALETQMEEMKTQLE----ELEDELQATEDAkLRLEVNMQAL 1579
Cdd:COG4913 509 HLRGRLVYER-VRTGLPDPERPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFDyvcvDSPEELRRHPRA-ITRAGQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1580 KGQFERDLQARDEQ-------NEEKRRQLQRQLHEYETELEDERKQRalaaaakkklegdlkdlelqadSAIKGREEAIK 1652
Cdd:COG4913 587 GTRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEAEERL----------------------EALEAELDALQ 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1653 QLRKLQAQMKDFQRELEDARASRDEIfaTAKENEKKAksLEA---DLMQLQEDLAAAERARKQADLEkeelaeelassls 1729
Cdd:COG4913 645 ERREALQRLAEYSWDEIDVASAEREI--AELEAELER--LDAssdDLAALEEQLEELEAELEELEEE------------- 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1730 gRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA-TQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKL 1808
Cdd:COG4913 708 -LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAALGDAVERELRENLEERIDALRARLNRAE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1809 HEMEGAV---KSKFKS-------TIAALEAKIAQLEEQVEQEAREKQAATKSLKQK--DKKLKEILLQVEDERKMAEQyk 1876
Cdd:COG4913 787 EELERAMrafNREWPAetadldaDLESLPEYLALLDRLEEDGLPEYEERFKELLNEnsIEFVADLLSKLRRAIREIKE-- 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1877 eqaekgnaRVKQLKRQLEEAE---------EESQRINANRRKLQRELDEATESNEAMGRE--------VNALKSKLRRGN 1939
Cdd:COG4913 865 --------RIDPLNDSLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEE 936
|
....*....
gi 92091586 1940 ETSFVPSRR 1948
Cdd:COG4913 937 EESDRRWRA 945
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1297 |
2.17e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 847 KVKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQE 926
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 927 LEEIlhemearleeeedrgqqlqAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVtaEAKIKKLEDEILVMDDQNNKLSK 1006
Cdd:PRK03918 354 LEEL-------------------EERHELYEEAKAKKEELERLKKRLTGLTPEKL--EKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1007 ERKLLEERISDLTTNLaEEEEKAKNLTKLKNK------HESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIAD 1080
Cdd:PRK03918 413 RIGELKKEIKELKKAI-EELKKAKGKCPVCGRelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1081 LQAQIAELKMqlAKKEEELQAALARLDDEIAQKNNAL-----KKIRELEGHISDLQEDLDSERAARNKA---EKQKRDLG 1152
Cdd:PRK03918 492 ESELIKLKEL--AEQLKELEEKLKKYNLEELEKKAEEyeklkEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 EELEALKTELEDTLDSTATQQELRAKR--------------EQEVTVLKKALDEETRSHEaQVQEMRQKHAQAVEELTEQ 1218
Cdd:PRK03918 570 EELAELLKELEELGFESVEELEERLKElepfyneylelkdaEKELEREEKELKKLEEELD-KAFEELAETEKRLEELRKE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1219 LEQFKRA-----KANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSK---CSDGERARA---ELND 1287
Cdd:PRK03918 649 LEELEKKyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAkkeLEKLEKALErveELRE 728
|
490
....*....|
gi 92091586 1288 KVHKLQNEVE 1297
Cdd:PRK03918 729 KVKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1082-1324 |
5.04e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.79 E-value: 5.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1082 QAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTE 1161
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1162 LEDTLDSTATQ--QELRAKREQEVTVLKKALDeetrshEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKE 1239
Cdd:COG4942 99 LEAQKEELAELlrALYRLGRQPPLALLLSPED------FLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1240 NADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGmlNEAEGKAIKLAKDVAS 1319
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA--EAAAAAERTPAAGFAA 250
|
....*
gi 92091586 1320 LSSQL 1324
Cdd:COG4942 251 LKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
776-1361 |
5.32e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 776 FFRTGVLahleEERDL--KITDVIMAFQAMCRgylARKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQwwRLFTKVKPLLQ 853
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARERL--AELEYLRAALR 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 854 VTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQL-----QAETELYAEAEEMRVRLAAKKQELE 928
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrgnggDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 929 EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKE- 1007
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARl 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1008 ---RKLLEERISDLTTNL---------AEEEEK--------------------------AKNLTKLKNKHEsmISELEVR 1049
Cdd:COG4913 443 lalRDALAEALGLDEAELpfvgelievRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGR--LVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1050 LKKEEKSRQELEK--LKRKLEGDASDFHEQIADL---------------------------------------------- 1081
Cdd:COG4913 521 TGLPDPERPRLDPdsLAGKLDFKPHPFRAWLEAElgrrfdyvcvdspeelrrhpraitragqvkgngtrhekddrrrirs 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1082 --------QAQIAELKMQLAKKEEELQAALARLdDEIAQKNNALKKIRELEGHISDLQ-EDLDSERAARnkaekqkrdlg 1152
Cdd:COG4913 601 ryvlgfdnRAKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQRLAEYSwDEIDVASAER----------- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 eELEALKTELEDTLDSTATQQELRAKREQevtvLKKALDEetrsHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKN 1232
Cdd:COG4913 669 -EIAELEAELERLDASSDDLAALEEQLEE----LEAELEE----LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1233 KQTLEKE-NADLAGELRVLGQAKQEvEHKKKKLEAQVQELQSKcsdGERARAELNDKVHKLQNEVESVTGMLneaeGKAI 1311
Cdd:COG4913 740 EDLARLElRALLEERFAAALGDAVE-RELRENLEERIDALRAR---LNRAEEELERAMRAFNREWPAETADL----DADL 811
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1312 KLAKDVASLSSQLQDT---------QELLQEETRQklNVSTKLRQLEEERNSLQDQLDE 1361
Cdd:COG4913 812 ESLPEYLALLDRLEEDglpeyeerfKELLNENSIE--FVADLLSKLRRAIREIKERIDP 868
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
999-1714 |
5.50e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 71.54 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 999 DQNNKLSKERKLLEERISDLTTNLaeeEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgDASDFHEQI 1078
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1079 ADLQAQIAELKMQLAKKEE-----ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGE 1153
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1154 ELEALKTELedtldstatQQELRAKREQEVTVLKKALDEETRSHEAQVQemrqKHAQAVEELTEQLEQFKRAKANLDKNK 1233
Cdd:TIGR00618 343 QRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIH----TLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVEsvtgmlneaegkaikl 1313
Cdd:TIGR00618 410 ATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ---------------- 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1314 akdvaslssQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDE-EMEAKQNLERHIST-LNIQLSDSKKKLQDFA 1391
Cdd:TIGR00618 474 ---------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTrRMQRGEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1392 STVE----ALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE 1467
Cdd:TIGR00618 545 EDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1468 KNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSkddvgknvhELEKSKRALETQ 1547
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ---------KMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1548 MEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKK 1627
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSL-GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAAL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1628 KLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEK-KAKSLEADLMQLQEDLAAA 1706
Cdd:TIGR00618 775 QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsRLEEKSATLGEITHQLLKY 854
|
....*...
gi 92091586 1707 ERARKQAD 1714
Cdd:TIGR00618 855 EECSKQLA 862
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1013-1714 |
5.79e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMIS-ELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQ 1091
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAaRERLAELEYLRAALRLWFAQRRLE----LLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 LAKKEEELQAALARLDD-EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLG--------------EELE 1156
Cdd:COG4913 311 LERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalrAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1157 ALKTELEDtldstatqqelrakreqevtvLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKN---- 1232
Cdd:COG4913 391 ALLEALEE---------------------ELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNIPARllal 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1233 ----KQTLEKENADL--AGEL---------------RVLG--------------QAKQEVEHKKKKLEAQVQELQSKCSD 1277
Cdd:COG4913 446 rdalAEALGLDEAELpfVGELievrpeeerwrgaieRVLGgfaltllvppehyaAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1278 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKdVASLsSQLQD-----TQELL--QEETRQKLNVSTKLRQ--- 1347
Cdd:COG4913 526 PERPRLDPDSLAGKLDFKPHPFRAWLEAELGRRFDYVC-VDSP-EELRRhpraiTRAGQvkGNGTRHEKDDRRRIRSryv 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1348 -----------LEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEgkkrfQKEIENLTQQYE 1416
Cdd:COG4913 604 lgfdnraklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASA-----EREIAELEAELE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1417 EKAAAYDKLEktknRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQllaeeknisskyadERDRAEAEAREKETKALSLA 1496
Cdd:COG4913 679 RLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEK--------------ELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1497 RaleeaLEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKRALETQMEEMKTQLEELEDELQATedaklrlevnM 1576
Cdd:COG4913 741 D-----LARLELRALLEERFAAALGDAV------------ERELRENLEERIDALRARLNRAEEELERA----------M 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1577 QALKGQFE---RDLQARDEQNEEKRRQLQRQ----LHEYETELEDERKQRalaaaakkkLEGDLKDLELQADSAIKGREE 1649
Cdd:COG4913 794 RAFNREWPaetADLDADLESLPEYLALLDRLeedgLPEYEERFKELLNEN---------SIEFVADLLSKLRRAIREIKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1650 AIKQL------------RKLQ--------AQMKDFQRELEDARASRDEifATAKENEKKakslEADLMQLQEDLAAAERA 1709
Cdd:COG4913 865 RIDPLndslkripfgpgRYLRlearprpdPEVREFRQELRAVTSGASL--FDEELSEAR----FAALKRLIERLRSEEEE 938
|
....*
gi 92091586 1710 RKQAD 1714
Cdd:COG4913 939 SDRRW 943
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1091-1932 |
6.58e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1091 QLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdLGEELEALKTELEDTLDSTA 1170
Cdd:COG3096 286 RALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1171 TQQELRAKREQEVTVLKkaldEETRSHEAQVQEMRQKHA---QAVEELTEQLEQFKRAKANLDKNKQTLEkeNADLAGEl 1247
Cdd:COG3096 365 EQEEVVEEAAEQLAEAE----ARLEAAEEEVDSLKSQLAdyqQALDVQQTRAIQYQQAVQALEKARALCG--LPDLTPE- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1248 rvlgQAKQEVEHKKKKLEA---QVQELQSKCSDGERARAELnDKVHKLqneVESVTGML--NEAEGKAIKLAKDVASLSS 1322
Cdd:COG3096 438 ----NAEDYLAAFRAKEQQateEVLELEQKLSVADAARRQF-EKAYEL---VCKIAGEVerSQAWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1323 QLQDTQELLQE--ETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEG 1400
Cdd:COG3096 510 LAQRLQQLRAQlaELEQRLR---QQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1401 KKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvVDLDNQRQLVSNLEKKQRKFDQLLAEEKnisskyaderDR 1480
Cdd:COG3096 587 LEQLRARIKELAARAPAWLAAQDALERLREQSGEALADS-QEVTAAMQQLLEREREATVERDELAARK----------QA 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1481 AEAEARE-------KETKALSLAraleealeakeelERTNKMLKAEMEDLVS---------------------------- 1525
Cdd:COG3096 656 LESQIERlsqpggaEDPRLLALA-------------ERLGGVLLSEIYDDVTledapyfsalygparhaivvpdlsavke 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1526 --------------------SKDDVGKNVHELEK------SKRAL----------------ETQMEEMKTQLEELEDELq 1563
Cdd:COG3096 723 qlagledcpedlyliegdpdSFDDSVFDAEELEDavvvklSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1564 atedAKLRLEVN-MQALKGQFERDL-----QARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdlkdlE 1637
Cdd:COG3096 802 ----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPDPEAELAALRQRRSELERELAQHRAQ------------------E 859
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1638 LQADSAIKGREEAIKQLRKLQAQM------------KDFQRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAA 1705
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNKLLPQAnlladetladrlEELREELDAAQEAQAFI----QQHGKALAQLEPLVAVLQSDPEQ 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1706 AERARKQADlekeelaeelasslsgrnALQDEKRRLEARIaqleeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERS 1785
Cdd:COG3096 936 FEQLQADYL------------------QAKEQQRRLKQQI--------------FALSEVVQRRPHFSYEDAVGLLGENS 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1786 TAqkNESARQQLErQNKELRSKLHEmegavkskfkstiaALEAKIAQLEE--QVEQEAREK-QAATKSLKQKDKKLKEIL 1862
Cdd:COG3096 984 DL--NEKLRARLE-QAEEARREARE--------------QLRQAQAQYSQynQVLASLKSSrDAKQQTLQELEQELEELG 1046
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1863 LQVEDErkMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1932
Cdd:COG3096 1047 VQADAE--AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAK 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1043-1460 |
9.59e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1043 ISELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQA--ALARLDDEIAQKNNALKKI 1120
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1121 RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQ 1200
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1201 VQEMRQKH-AQAVEELTEQLEQFKRAKA-------NLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQ 1272
Cdd:COG4717 229 LEQLENELeAAALEERLKEARLLLLIAAallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1273 SKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQ---------LQDTQELLQ-------EETR 1336
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqleelEQEIAALLAeagvedeEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1337 QKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIS--TLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLtqq 1414
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELAELEAELEQL--- 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 92091586 1415 yeEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKF 1460
Cdd:COG4717 466 --EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
941-1861 |
9.99e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.77 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 941 EEDRGQQL------QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEER 1014
Cdd:pfam02463 159 EEEAAGSRlkrkkkEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1015 ISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAK 1094
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA-------KEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1095 KEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDldseRAARNKAEKQKRDLGEELEALKTELEDTLdSTATQQE 1174
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIK----REAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1175 LRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQ-------AVEELTEQLEQFKRAKANLDKNKQTLE--KENADLAG 1245
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKeekkeelEILEEEEESIELKQGKLTEEKEELEKQelKLLKDELE 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1246 ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQ 1325
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1326 DTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDskkklqdfastvealeegkkrfQ 1405
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIL----------------------N 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1406 KEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1485
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1486 REKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsskddvgknvhELEKSKRALETQMEEMKTQLEELEDELQAT 1565
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL------------LADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1566 EDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERkqRALAAAAKKKLEGDLKDLELQADSAIK 1645
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL--RALEEELKEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1646 GREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADlekeelaeELA 1725
Cdd:pfam02463 831 KEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK--------KEL 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1726 SSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERStaQKNESARQQLERQNKELR 1805
Cdd:pfam02463 903 EEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN--KRLLLAKEELGKVNLMAI 980
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 1806 SKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEI 1861
Cdd:pfam02463 981 EEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKV 1036
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1297-1896 |
1.02e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1297 ESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQeetrqklnvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTL 1376
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELE-----------KLEKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1377 NIQLSDSKKKLQDFASTVEALEEGKKRFqKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKK 1456
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1457 QRKFDQLLAEEKNISSKYADERDRAEAEAREKEtkalslaraleealeakeelertnkmLKAEMEDLvsSKDDVGKNVHE 1536
Cdd:PRK03918 337 EERLEELKKKLKELEKRLEELEERHELYEEAKA--------------------------KKEELERL--KKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1537 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLqrqLHEYETELEDER 1616
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEL---LEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1617 KQRALAAAAKKKLEGDLKDLE--LQADSAIKGREEAIKQLRKLQAQMKDFQRE-LEDARASRDEIFATAKENEKKAKSLE 1693
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1694 ADLMQLQE---DLAAAERARKQADLEkeelaeelasslsgrnaLQDEKRRLEARIAQLEEELEEEQGNMEAMSDR---VR 1767
Cdd:PRK03918 546 KELEKLEElkkKLAELEKKLDELEEE-----------------LAELLKELEELGFESVEELEERLKELEPFYNEyleLK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1768 KATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAV-----------KSKFKSTIAALEAKIAQLEEQ 1836
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYseeeyeelreeYLELSRELAGLRAELEELEKR 688
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1837 VEQEAREkqaaTKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKgnarVKQLKRQLEEA 1896
Cdd:PRK03918 689 REEIKKT----LEKLKEELEEREKAKKELEKLEKALERVEELREK----VKKYKALLKER 740
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1110-1918 |
1.51e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.87 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1110 IAQKNNALKKIRELEGHISDLQEDLDSERA---ARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEVTVL 1186
Cdd:pfam12128 206 LEDDGVVPPKSRLNRQQVEHWIRDIQAIAGimkIRPEFTKLQQEF-NTLESAELRLSHLHFGYKSDETLIASRQEERQET 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1187 KKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADlagelrvlgQAKQEVEhkkkklea 1266
Cdd:pfam12128 285 SAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIE---------TAAADQE-------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1267 QVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEaegkaiKLAKDVASLSSQLQDTQEllqEETRQKLNVSTKLR 1346
Cdd:pfam12128 348 QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE------QNNRDIAGIKDKLAKIRE---ARDRQLAVAEDDLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1347 QLEEE-RNSLQDQLDEEMEAKQNLERHISTLNIQL------SDSKKKLQDFASTVEALEEGKKRFQKEIENLtqQYEEKA 1419
Cdd:pfam12128 419 ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVERL--QSELRQ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1420 A------AYDKLEKTKNRLQQ---ELDDLVVDLDNQR-QLVSNLEKKQRKFDQLLAeeKNISSKYADERDRAEAEAREKE 1489
Cdd:pfam12128 497 ArkrrdqASEALRQASRRLEErqsALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1490 TKALSL-ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA 1568
Cdd:pfam12128 575 GGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1569 KLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETEL--------EDERKQRALAAAAKKKLEGDLKDLELQA 1640
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1641 DSAIKGREEAIKqlRKLQAQMKDFQRELedarASRDEifatakeNEKKAKSLEADLMQLQEDLAAAERARKQAdleKEEL 1720
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDL----ASLGV-------DPDVIAKLKREIRTLERKIERIAVRRQEV---LRYF 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1721 AEELASSLSGRNALQDEKRRLEARIaqleeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERstaqknESARQQLERQ 1800
Cdd:pfam12128 799 DWYQETWLQRRPRLATQLSNIERAI--------------SELQQQLARLIADTKLRRAKLEMER------KASEKQQVRL 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1801 NKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ------VEDERKMAEQ 1874
Cdd:pfam12128 859 SENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNVIADhsgsglAETWESLREE 938
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 1875 YKEQAEKG-----------------NARVKQLKRQLEEA---------------EEESQRINANRRKLQRELDEAT 1918
Cdd:pfam12128 939 DHYQNDKGirlldyrklvpyleqwfDVRVPQSIMVLREQvsilgvdltefydvlADFDRRIASFSRELQREVGEEA 1014
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1337-1968 |
1.86e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1337 QKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKrfqkeIENLTQQYE 1416
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK-----AEDARKAEE 1144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1417 EKAAAYDKLEKTKNRLQqelDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEE--KNISSKYADERDRAEAEAREKETKALS 1494
Cdd:PTZ00121 1145 ARKAEDAKRVEIARKAE---DARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKAE 1221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1495 LARALEEALEAKEELERTNKMLKAE----MEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELE--DELQATEDA 1568
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEeernNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKkaDEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1569 KLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGRE 1648
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1649 EAIKQLRKLQaQMKDFQRELEDARASRDEIfATAKENEKKAKSLEadlmQLQEDLAAAERARKQADLEKEELAEELASSl 1728
Cdd:PTZ00121 1382 AAKKKAEEKK-KADEAKKKAEEDKKKADEL-KKAAAAKKKADEAK----KKAEEKKKADEAKKKAEEAKKADEAKKKAE- 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1729 SGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQL--SNELATERSTAQKNESARQQLERQNKELRS 1806
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1807 KLHEMEGAV-KSKFKSTIAALEAKIAQLEEQVEQEARE---------------------------------KQAATKSLK 1852
Cdd:PTZ00121 1535 KADEAKKAEeKKKADELKKAEELKKAEEKKKAEEAKKAeedknmalrkaeeakkaeearieevmklyeeekKMKAEEAKK 1614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1853 QKDKKLK-EILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNAL 1931
Cdd:PTZ00121 1615 AEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
650 660 670
....*....|....*....|....*....|....*..
gi 92091586 1932 KSKLRRGNETSFVPSRRSGGRRVIENADGSEEETDTR 1968
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
810-1403 |
1.99e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.78 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 810 RKAFAKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAEnelkeleqkh 889
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE---------- 1441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 890 sqlteeknllqEQLQAEtELYAEAEEMRVRLAAKKqeleeilhemearleeeedrgqqlQAERKKMAQQMLDLEEQLEEE 969
Cdd:PTZ00121 1442 -----------EAKKAD-EAKKKAEEAKKAEEAKK------------------------KAEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 970 EAARQKLQLEKVTAEAKIKKLEDEilvmddqnnKLSKERKLLEERISDLTTNLAEEEEKAKNLTKL--KNKHESMISELE 1047
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAK---------KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1048 VRlKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHI 1127
Cdd:PTZ00121 1557 LK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1128 SDLQEDLDSE--RAARNKAEKQKRDLGEELEALKTElEDTLDSTATQQELRAKREQEVTVLKKAldEETRSHEaQVQEMR 1205
Cdd:PTZ00121 1636 EQLKKKEAEEkkKAEELKKAEEENKIKAAEEAKKAE-EDKKKAEEAKKAEEDEKKAAEALKKEA--EEAKKAE-ELKKKE 1711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1206 QKHAQAVEELTEQlEQFKRAKANLDKNKQTLEKENADlagELRVLGQAKQEVEHKKKKLEAQVQELQSKCS--------- 1276
Cdd:PTZ00121 1712 AEEKKKAEELKKA-EEENKIKAEEAKKEAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavieeelde 1787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1277 DGERARAELNDKVHKLQNEVESV-------TGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1349
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANIieggkegNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKE 1867
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1350 EERNS----LQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEAL--EEGKKR 1403
Cdd:PTZ00121 1868 ADFNKekdlKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLdkDEYIKR 1927
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1121-1907 |
2.22e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1121 RELEGHISDLQEDLDSERAARNKAEK--QKRDLGEELEALKTELEDTLDSTATQQELRAKREQevtvlkkaldeetrshe 1198
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRL----------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1199 aqvqemrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKK-LEAQVQELQSKCSD 1277
Cdd:COG4913 284 -------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1278 GERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQ-ELLQEETRQKlnvsTKLRQLEEERNSLQ 1356
Cdd:COG4913 357 RERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALaEAEAALRDLR----RELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1357 DQ---LDEEM-EAKQNLERHistlniqLSDSKKKLQDFASTVEaLEEGKKRFQKEIENL-----------TQQYEEKAAA 1421
Cdd:COG4913 433 RRksnIPARLlALRDALAEA-------LGLDEAELPFVGELIE-VRPEEERWRGAIERVlggfaltllvpPEHYAAALRW 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1422 YDKLeKTKNRLQ-QELDDLVVDLDNQR----QLVSNLEKKQRKFDQLLAEEknisskYADERDRA---EAEAREKETKAL 1493
Cdd:COG4913 505 VNRL-HLRGRLVyERVRTGLPDPERPRldpdSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1494 SLARaleealeakeelertnkmlkaemedLVSSKDDVG-KNVHELEKSKRAL----ETQMEEMKTQLEELEDELQATEDA 1568
Cdd:COG4913 578 TRAG-------------------------QVKGNGTRHeKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEER 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1569 KLRLEVNMQALKGQFERDLQARDEQNEEKR-RQLQRQLHEYETELEDERKqralaaaakkkLEGDLKDLELQADSAIKGR 1647
Cdd:COG4913 633 LEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDA-----------SSDDLAALEEQLEELEAEL 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1648 EEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLmqLQEDLAAAERARKQADLekeelaeelass 1727
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGDAVEREL------------ 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1728 lsgRNALQDEKRRLEARIAQLEEELeeeqgnMEAMSDRVRKATQQAEQLSNELATERSTAQKNES-ARQQLERQNKELRS 1806
Cdd:COG4913 768 ---RENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLDRlEEDGLPEYEERFKE 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1807 KLHEMEGAVKSKFKStiaALEAKIAQLEEQVEQ------------EAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQ 1874
Cdd:COG4913 839 LLNENSIEFVADLLS---KLRRAIREIKERIDPlndslkripfgpGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDE 915
|
810 820 830
....*....|....*....|....*....|...
gi 92091586 1875 ykEQAEKGNARVKQLKRQLEEAEEESQRINANR 1907
Cdd:COG4913 916 --ELSEARFAALKRLIERLRSEEEESDRRWRAR 946
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1384 |
3.39e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 68.59 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAakkQELEEILHEMEAR 937
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLT---KELEDIKMSLQRS 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 LEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDeilVMDDQNNKLSKErkllEERISD 1017
Cdd:pfam05483 309 MSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKN----EDQLKI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEK---SRQELEKLKRKLEGDASDF-------HEQIADLQAQIAE 1087
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKlldEKKQFEKIAEELKGKEQELifllqarEKEIHDLEIQLTA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1088 LKMQLAKKEEELQAALARLDDE-------IAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK- 1159
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEklknielTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEe 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1160 --TELEDTLDStaTQQELRAKREQEVTVLKKAlDEETRSHEAQVQEMRQKHA---QAVEELTEQLEQFKRAKANLDKNKQ 1234
Cdd:pfam05483 542 keMNLRDELES--VREEFIQKGDEVKCKLDKS-EENARSIEYEVLKKEKQMKileNKCNNLKKQIENKNKNIEELHQENK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1235 TLEKENADLAGELRV----LGQAKQEVEHKKKKLEAQVQELQSKCSDG-----------ERARAELNDKVhKLQNEVE-- 1297
Cdd:pfam05483 619 ALKKKGSAENKQLNAyeikVNKLELELASAKQKFEEIIDNYQKEIEDKkiseeklleevEKAKAIADEAV-KLQKEIDkr 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1298 ---SVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHIS 1374
Cdd:pfam05483 698 cqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
570
....*....|
gi 92091586 1375 TLNIQLSDSK 1384
Cdd:pfam05483 778 ENTAILKDKK 787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1412-1936 |
4.38e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.28 E-value: 4.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1412 TQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrqlvsNLEKKQrkfdQLLAEEKNISSkyadERDRAEAE--AREKE 1489
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELK-----------ELEKKH----QQLCEEKNALQ----EQLQAETElcAEAEE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1490 TKALSLARaleealeakeelertnkmlKAEMEDLVSskdDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDA- 1568
Cdd:pfam01576 62 MRARLAAR-------------------KQELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAAr 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1569 -KLRLE-VNMQALKGQFERDLQARDEQN---EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSA 1643
Cdd:pfam01576 120 qKLQLEkVTTEAKIKKLEEDILLLEDQNsklSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1644 IKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFA--TAKENE-------------------KKAKSLEADLMQLQED 1702
Cdd:pfam01576 200 EKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAqlAKKEEElqaalarleeetaqknnalKKIRELEAQISELQED 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1703 LAAAERARKQADLEK-------EELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEA-MSDRVRKATQQAE 1774
Cdd:pfam01576 280 LESERAARNKAEKQRrdlgeelEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAqLQEMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1775 QLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAvkskfkstiaaleakiaqleeqveqeareKQAATKSLKQK 1854
Cdd:pfam01576 360 ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA-----------------------------KQDSEHKRKKL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1855 DKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSK 1934
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
..
gi 92091586 1935 LR 1936
Cdd:pfam01576 491 LR 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
948-1685 |
5.23e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 948 LQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEE---RISDLTTNLAE 1024
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcaRSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1025 EEEKAKNL-TKLKNKHESMISELEVRLKKEEKSRQELE-KLKR---KLEGDASDFHEQIADLQAQIAELKMQLAKKEEEL 1099
Cdd:pfam05483 177 EREETRQVyMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEdheKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1100 QAaLARLDDEIAQKNNALKKIRELEghisdlQEDLdseraarNKAEKQKRDLGEELEALKTELEDtldSTATQQELrakr 1179
Cdd:pfam05483 257 KD-LTFLLEESRDKANQLEEKTKLQ------DENL-------KELIEKKDHLTKELEDIKMSLQR---SMSTQKAL---- 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1180 EQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEqleqfkrakanLDKNKQTLEKenadlagelrVLGQAKQEVEH 1259
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE-----------FEATTCSLEE----------LLRTEQQRLEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1260 KKKKLEAQVQELQSKCSdgeraraelndkvhklqnEVESVTGMLNEAEgkaiklaKDVASLSSQLQDTQELLQEEtrqkl 1339
Cdd:pfam05483 375 NEDQLKIITMELQKKSS------------------ELEEMTKFKNNKE-------VELEELKKILAEDEKLLDEK----- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1340 nvstklRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALeegkkrfQKEIENLTQQYEEKA 1419
Cdd:pfam05483 425 ------KQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL-------KTELEKEKLKNIELT 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1420 AAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQ----RKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSL 1495
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEermlKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1496 ARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA---------------------LETQMEEMKTQ 1554
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKAlkkkgsaenkqlnayeikvnkLELELASAKQK 651
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1555 LEELEDELQATEDAKlrlEVNMQALKGQFERDLQARDEQ---NEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEG 1631
Cdd:pfam05483 652 FEEIIDNYQKEIEDK---KISEEKLLEEVEKAKAIADEAvklQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1632 DLKDLELQADSAIKGREeaiKQLRKLQAQMKDFQRELEDARASRDEIFATAKEN 1685
Cdd:pfam05483 729 LYKNKEQEQSSAKAALE---IELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1248 |
1.17e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA---K 1094
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAeleK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1095 KEEELQAALARLDDEIAQKNNALKKIreleGHISDLQEDLDSERAARnkAEKQKRDLGEELEALKTELEDTLDSTATQQE 1174
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRL----GRQPPLALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1175 LRAKREQEVTVLKKALDEETRSHeAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELR 1248
Cdd:COG4942 165 LRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1260-1494 |
1.18e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1260 KKKKLEAQVQELQSKcsdgeraRAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEetrqkl 1339
Cdd:COG4942 21 AAAEAEAELEQLQQE-------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1340 nVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHiSTLNIQLS-----DSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1415 YEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALS 1494
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1043-1228 |
1.31e-10 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 63.41 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1043 ISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAlKKIRE 1122
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1123 LEghisDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQEVTVLKKALDEETRSHEAQVQ 1202
Cdd:COG1579 91 YE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|....*..
gi 92091586 1203 EMRQKHAQAVEELTEQL-EQFKRAKAN 1228
Cdd:COG1579 160 ELEAEREELAAKIPPELlALYERIRKR 186
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1421 |
1.45e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1199 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDG 1278
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1279 ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQklnVSTKLRQLEEERNSLQDQ 1358
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE---LAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1359 LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1421
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
853-1668 |
1.65e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETelyAEAEEMRVRLAAKKQELEEILH 932
Cdd:TIGR00606 313 TVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARD---SLIQSLATRLELDGFERGPFSE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQAerkKMAQQMLDleeqleeeeaarqKLQLEKVTAEAKIKKLEDEilvMDDQNNKLSKERKLLE 1012
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEA---KTAAQLCA-------------DLQSKERLKQEQADEIRDE---KKGLGRTIELKKEILE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMI-SELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ 1091
Cdd:TIGR00606 451 KKQEELKFVIKELQQLEGSSDRILELDQELRkAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 LAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISD------LQEDLDSERAARNKAEKQKRDLGEELEALKTeledt 1165
Cdd:TIGR00606 531 TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQ----- 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1166 lDSTATQQELRAKREQEVTVLKKALDE-ETRSHEAQVQEMRQKhaqaVEELTEQLEQFKRAKANLDKNKQTLEKENADLA 1244
Cdd:TIGR00606 606 -NKNHINNELESKEEQLSSYEDKLFDVcGSQDEESDLERLKEE----IEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1245 GELRVLGQAKQEVEHKKKKLEA-------QVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDV 1317
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1318 ASLSSQLQDTQELLqeetrQKLNVSTKLRQLEEERNSLQDQLDEEMEakqNLERHISTLNIQLSDSkkklqDFASTVEAL 1397
Cdd:TIGR00606 761 QRLKNDIEEQETLL-----GTIMPEEESAKVCLTDVTIMERFQMELK---DVERKIAQQAAKLQGS-----DLDRTVQQV 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1398 EEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDldnQRQLVSNLEKKQRKFDQLLAEEKNISSKYADE 1477
Cdd:TIGR00606 828 NQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE---KLQIGTNLQRRQQFEEQLVELSTEVQSLIREI 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1478 RDRAEAEAREKETKALSLARALEEALEAKEelerTNKMLKAEMEDLVSSKDDVGKNVHELEKS-KRALETQMEEMKTQLE 1556
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKET----SNKKAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELN 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1557 ELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEgdLKD 1635
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIDtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE--HQK 1058
|
810 820 830
....*....|....*....|....*....|...
gi 92091586 1636 LELQADSAIKGREEAIKQLRKLQAQMKDFQREL 1668
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1076-1870 |
2.53e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.13 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1076 EQIADLQAQIAELKMQLAKKEEelqaALARLDDEIAQKNNALKkirELEGHISDLQEDLDSERAARNKAEKQKRdLGEEL 1155
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQY----RLVEMARELAELNEAES---DLEQDYQAASDHLNLVQTALRQQEKIER-YQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1156 EALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEeTRSHEAQVQemrqkhaQAVEELTEQLEQFKRAKANLDKNKQT 1235
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDE-LKSQLADYQ-------QALDVQQTRAIQYQQAVQALERAKQL 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1236 LEKENADLAGelrvLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK---VHKLQNEVESvtgmlNEAEGKAIK 1312
Cdd:PRK04863 430 CGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1313 LAKDVASLSSQLQDTQELLQE--ETRQKLNvstKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDskkkLQDF 1390
Cdd:PRK04863 501 LLRRLREQRHLAEQLQQLRMRlsELEQRLR---QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLES----LSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1391 ASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDldnqRQLVSNLEKkqrkfdQLLAEEKNI 1470
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFED----SQDVTEYMQ------QLLEREREL 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1471 SSkyadERDRAEAEAREKETKALSLA-RALEEALEAKEELERTNKMLKAEM----------------------------- 1520
Cdd:PRK04863 644 TV----ERDELAARKQALDEEIERLSqPGGSEDPRLNALAERFGGVLLSEIyddvsledapyfsalygparhaivvpdls 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1521 -------------EDL------VSSKDDVGKNVHELEKS----------------------KRALETQMEEMKTQLEELE 1559
Cdd:PRK04863 720 daaeqlagledcpEDLyliegdPDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1560 DELqatedAKLRLEVN-MQALKGQFERDLQ-----ARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDL 1633
Cdd:PRK04863 800 ERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1634 KDL-ELQADSAIKGREEAIKQLRKLQAQMKdfqrELEDARASRDEIFATAKENEKKAKSLEAD---LMQLQEDLAAAERA 1709
Cdd:PRK04863 875 SALnRLLPRLNLLADETLADRVEEIREQLD----EAEEAKRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDYQQAQQT 950
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1710 RKQADLEKEelaeelasslsgrnALQD-EKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERST-A 1787
Cdd:PRK04863 951 QRDAKQQAF--------------ALTEvVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQlA 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1788 QKNE------SARQQLERQNKELRSKLHEM-----EGAV------KSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKS 1850
Cdd:PRK04863 1017 QYNQvlaslkSSYDAKRQMLQELKQELQDLgvpadSGAEerararRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
890 900
....*....|....*....|
gi 92091586 1851 LKQKDKKLKEILLQVEDERK 1870
Cdd:PRK04863 1097 LRKLERDYHEMREQVVNAKA 1116
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1289 |
2.67e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.81 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMrvrlaaKKQELEEILH 932
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLN---QLKSEISDL------NNQKEQDWNK 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1012
Cdd:TIGR04523 311 ELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL 1092
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1093 AKKEEELQA----------ALARLDDEIAQKNNALKKI----RELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEAL 1158
Cdd:TIGR04523 464 ESLETQLKVlsrsinkikqNLEQKQKELKSKEKELKKLneekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1159 KTEL---EDTLDSTATQQELRAKrEQEVTVLKKALDEETRSHEaQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT 1235
Cdd:TIGR04523 544 EDELnkdDFELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1236 LEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKV 1289
Cdd:TIGR04523 622 AKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKI 675
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
853-1218 |
3.48e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 65.52 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQK----------TKERQQKAENELK----ELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRV 918
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKvssltaqlesTKEMLRKVVEELTakkmTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 919 RLAAKKQELEEILHEMEARLEEEED-RGQQLQ-AERKK----MAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKI--KKL 990
Cdd:pfam15921 525 RVDLKLQELQHLKNEGDHLRNVQTEcEALKLQmAEKDKvieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIndRRL 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 991 E-DEILVMDDQNNKLSKErklLEERISDLTTN----LAEEEEKAKNLTKLKNKHESMISELevrlkkeEKSRQELEKLKR 1065
Cdd:pfam15921 605 ElQEFKILKDKKDAKIRE---LEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLNEV-------KTSRNELNSLSE 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1066 KLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNAL-------KKIRELEGHISDLQEDLDSER 1138
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMkvamgmqKQITAKRGQIDALQSKIQFLE 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1139 AARNKAEKQKRDLGEElealKTELEDTLDSTATQQ-----ELRAKREQE------VTVLKKALDEETRSHeAQVQEMRQK 1207
Cdd:pfam15921 755 EAMTNANKEKHFLKEE----KNKLSQELSTVATEKnkmagELEVLRSQErrlkekVANMEVALDKASLQF-AECQDIIQR 829
|
410
....*....|.
gi 92091586 1208 HAQAVEELTEQ 1218
Cdd:pfam15921 830 QEQESVRLKLQ 840
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1678-1938 |
3.55e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1678 IFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelasslsgRNALQDEKRRLEARIAQLEEELEEEQG 1757
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1758 NMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNK-ELRSKLHEMEGAVKSK--FKSTIAALEAKIAQLE 1834
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRRLqyLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1835 EQVEQEAREKQAATKSLKQKDKKLKEillQVEDERKMAEQYKEQAEKgnarVKQLKRQLEEAEEESQRINANRRKLQREL 1914
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKL----LARLEKELAELAAELAELQQEAEELEALI 229
|
250 260
....*....|....*....|....
gi 92091586 1915 DEATESNEAMGREVNALKSKLRRG 1938
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALKG 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
870-1466 |
4.02e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 870 KTKERQQKAENELKELEQKHSQLTeekNLLQEQLQAETELYAEAEEMRVRLAAKkqeleeilhemearLEEEEDRGQQLQ 949
Cdd:pfam05483 166 RSAEKTKKYEYEREETRQVYMDLN---NNIEKMILAFEELRVQAENARLEMHFK--------------LKEDHEKIQHLE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 950 AERKKMAQQmldleeqleeeeaARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKerklLEERISDLTTNLAEEEEKA 1029
Cdd:pfam05483 229 EEYKKEIND-------------KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ----LEEKTKLQDENLKELIEKK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1030 KNLTK-LKNKHESMISELEVRLKKEEK---SRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALAR 1105
Cdd:pfam05483 292 DHLTKeLEDIKMSLQRSMSTQKALEEDlqiATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQR 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1106 LDDEIAQknnaLKKIR-ELEGHISDLQEDLDSERAARNKAEKQKRDLGEElealKTELEDTLDSTATQQELRAKrEQEVT 1184
Cdd:pfam05483 372 LEKNEDQ----LKIITmELQKKSSELEEMTKFKNNKEVELEELKKILAED----EKLLDEKKQFEKIAEELKGK-EQELI 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1185 VLKKALDEETRSHEAQVQEMR---QKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELR----VLGQAKQEV 1257
Cdd:pfam05483 443 FLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDI 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1258 EHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ 1337
Cdd:pfam05483 523 INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1338 KLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQkeiENLTQQYEE 1417
Cdd:pfam05483 603 IENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE---EKLLEEVEK 679
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 92091586 1418 KAAAYDKLEKtknrLQQELDDLVvdLDNQRQLVSNLEKKQRKFDQLLAE 1466
Cdd:pfam05483 680 AKAIADEAVK----LQKEIDKRC--QHKIAEMVALMEKHKHQYDKIIEE 722
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1514-1922 |
4.80e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1514 KMLKAEMEDLVSSKDDVGK-NVHELEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFER-DLQARD 1591
Cdd:COG4717 49 ERLEKEADELFKPQGRKPElNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1592 EQNEEKRRQLQRQLHEYET---ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQlrklqaQMKDFQREL 1668
Cdd:COG4717 128 LPLYQELEALEAELAELPErleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1669 EDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQ- 1747
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1748 -----------LEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVK 1816
Cdd:COG4717 282 vlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1817 skfKSTIAALEAKIAQLEEQV----EQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGN--ARVKQLK 1890
Cdd:COG4717 362 ---ELQLEELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELE 438
|
410 420 430
....*....|....*....|....*....|..
gi 92091586 1891 RQLEEAEEESQRINANRRKLQRELDEATESNE 1922
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
854-1377 |
5.19e-10 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 64.86 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 854 VTRQEEEMQAKEDEL-QKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEemRVRLAAKKQELEEI-- 930
Cdd:pfam12128 317 VAKDRSELEALEDQHgAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN--RRRSKIKEQNNRDIag 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 931 LHEMEARLEEEEDRG--------QQLQAE-RKKMAQQMLD--LEEQLEEEEAARQKLQLEKVTAEakikkledEILVMDD 999
Cdd:pfam12128 395 IKDKLAKIREARDRQlavaeddlQALESElREQLEAGKLEfnEEEYRLKSRLGELKLRLNQATAT--------PELLLQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1000 QNNKlskerKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRK-----------LE 1068
Cdd:pfam12128 467 ENFD-----ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhfLR 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1069 GDASDFHEQIADLQAQIAELKMQL------AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARN 1142
Cdd:pfam12128 542 KEAPDWEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1143 KAEKQKRDLGEELEALKTELEDTL----DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQ 1218
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARtalkNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAW 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1219 LEQFKRAKANLDKNKQTLEKEnadLAGELRV-LGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1297
Cdd:pfam12128 702 LEEQKEQKREARTEKQAYWQV---VEGALDAqLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIR 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1298 SVTGMLNEAEGKAIKLA---------------KDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEE 1362
Cdd:pfam12128 779 TLERKIERIAVRRQEVLryfdwyqetwlqrrpRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRL 858
|
570
....*....|....*
gi 92091586 1363 MEAKQNLERHISTLN 1377
Cdd:pfam12128 859 SENLRGLRCEMSKLA 873
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1234-1710 |
9.66e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 9.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKENADLageLRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgERARAELNDKVHKLQNEVESVTGMLNEAEGK--AI 1311
Cdd:COG4717 49 ERLEKEADEL---FKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREEleKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1312 KLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQlsdSKKKLQDFA 1391
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1392 STVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQE-----------LDDLVVDLDNQRQLVSNLEKKQRKF 1460
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1461 DQLLAEeknISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKS 1540
Cdd:COG4717 279 LFLVLG---LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1541 KRALETQMeemktQLEELEDELQATedaklrlevnMQALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDERKQRA 1620
Cdd:COG4717 356 AEELEEEL-----QLEELEQEIAAL----------LAEAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1621 LAAAAKKKL--EGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDF--QRELEDARASRDEIFATAKENEKKAKSLEADL 1696
Cdd:COG4717 420 ELLEALDEEelEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
490
....*....|....
gi 92091586 1697 MQLQEDLAAAERAR 1710
Cdd:COG4717 500 ELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1638-1909 |
1.03e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1638 LQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQadlek 1717
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1718 eelaeelasslsgrnaLQDEKRRLEARIAQLEeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQL 1797
Cdd:COG4942 88 ----------------LEKEIAELRAELEAQK----------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1798 ERQNKELRSKLHEMEgAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKE 1877
Cdd:COG4942 142 KYLAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260 270
....*....|....*....|....*....|..
gi 92091586 1878 QAEKGNARVKQLKRQLEEAEEESQRINANRRK 1909
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
943-1172 |
1.30e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 943 DRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNL 1022
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1023 AEEEEKAKNLTKLKNKHeSMISELEVRLKKEEKSRQE--LEKLKRKLEGDASDFhEQIADLQAQIAELKMQLAKKEEELQ 1100
Cdd:COG4942 100 EAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVrrLQYLKYLAPARREQA-EELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1101 AALARLDDEIAQKNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQ 1172
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
857-1087 |
1.85e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 857 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEmrvRLAAKKQELEEiLHEMEA 936
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAE-LEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 937 RLEEEEDRGQQLQAERKKMAQQMLDLEEQL------EEEEAARQKLQLEKVTAEakikkLEDEILVMDDQNNKLSKERKL 1010
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPA-----RREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1011 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAE 1087
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
852-1380 |
3.64e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.11 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 852 LQVTRQEEEMQAKEDELQKTKeRQQKAenelkELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLaakkQELEEil 931
Cdd:pfam01576 639 LSLARALEEALEAKEELERTN-KQLRA-----EMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQL----EELED-- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 932 hemearleeeedrgqQLQAerkkmaqqmldleeqleeeeAARQKLQLEkVTAEAKIKKLEDEILVMDDQNNklsKERKLL 1011
Cdd:pfam01576 707 ---------------ELQA--------------------TEDAKLRLE-VNMQALKAQFERDLQARDEQGE---EKRRQL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1012 EERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKlegdasdfheqiadLQAQIAELkmq 1091
Cdd:pfam01576 748 VKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK--------------LQAQMKDL--- 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 lakkEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSeraarnkAEKQKRDLGEELEALKTELEDTLDSTAT 1171
Cdd:pfam01576 811 ----QRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAA-------SERARRQAQQERDELADEIASGASGKSA 879
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1172 QQELRAKREQEVTVLKKALDEETRSHEAQVQEMRqKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVL- 1250
Cdd:pfam01576 880 LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLR-KSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMe 958
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1251 GQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQEL 1330
Cdd:pfam01576 959 GTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQ 1038
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1331 LQ--EETRQKLNVStklrqleeeRNSLQDQLDEEMEAKQNLERHISTLNIQL 1380
Cdd:pfam01576 1039 LEeaEEEASRANAA---------RRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
979-1291 |
1.16e-08 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 60.07 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 979 EKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEE---EEKAKNLTKLKNKHESMISEL--EVRLKKE 1053
Cdd:pfam13166 90 ESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkKIKRKKNSALSEALNGFKYEAnfKSRLLRE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1054 EKSRQE-------LEKLKRKLEG-----------------DASDFHEQIADLQ------AQIAELKMQLAKKE------- 1096
Cdd:pfam13166 170 IEKDNFnagvllsDEDRKAALATvfsdnkpeiapltfnviDFDALEKAEILIQkvigksSAIEELIKNPDLADwveqgle 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1097 -----------------EELQAALAR-LDDEIAQKNNALKK-IRELEGHISDLQEDLDSeRAARNKAEKQKRDLGEELEA 1157
Cdd:pfam13166 250 lhkahldtcpfcgqplpAERKAALEAhFDDEFTEFQNRLQKlIEKVESAISSLLAQLPA-VSDLASLLSAFELDVEDIES 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1158 LKTELEDTLDSTatQQELRAKREQEVTV--LKKALDEETRSHEAQVQ---------EMRQKHAQAVEELTEQLEQFKRAK 1226
Cdd:pfam13166 329 EAEVLNSQLDGL--RRALEAKRKDPFKSieLDSVDAKIESINDLVASineliakhnEITDNFEEEKNKAKKKLRLHLVEE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1227 AnlDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHK 1291
Cdd:pfam13166 407 F--KSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKA 469
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1927 |
1.22e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1639 QADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASR----DEIFATAKENEKKAKSLEADLMQLQEdlaaaERARKQAD 1714
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQ-----EERKRELE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1715 LEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEamsDRVRKATQQAEQLSnELATERSTAQKNESAR 1794
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1795 QQLERQNKELRSKLHEMEGAVK-SKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAE 1873
Cdd:pfam17380 440 LEEERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1874 qyKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESN---EAMGRE 1927
Cdd:pfam17380 520 --KEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERsrlEAMERE 574
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1217-1901 |
1.43e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.12 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1217 EQLEQFKRAKANLDKNKQTLEKENADLAGELRvlgQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEV 1296
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELK---QKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1297 ESvtgmlNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ-----------KLNVSTKLR-QLEEERNSLQDQLDEEME 1364
Cdd:pfam05483 148 KE-----NNATRHLCNLLKETCARSAEKTKKYEYEREETRQvymdlnnniekMILAFEELRvQAENARLEMHFKLKEDHE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1365 AKQNLERhistlniqlsDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKtKNRLQQEldDLVVDLD 1444
Cdd:pfam05483 223 KIQHLEE----------EYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEE-KTKLQDE--NLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1445 NQRQLVSNLEkkqrkfDQLLAEEKNISSKYADERDRAEAearekeTKAL-SLARALEEALEAKEELERTNKMLKAEMEDL 1523
Cdd:pfam05483 290 KKDHLTKELE------DIKMSLQRSMSTQKALEEDLQIA------TKTIcQLTEEKEAQMEELNKAKAAHSFVVTEFEAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1524 VSSKDDVGKNVHE-LEKSKRALETQMEEMKTQLEELEDELQATEDAklrlEVNMQALKGQFERDLQARDEQNEEKRrqLQ 1602
Cdd:pfam05483 358 TCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELEEMTKFKNNK----EVELEELKKILAEDEKLLDEKKQFEK--IA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1603 RQLHEYETELEDERKQRalaaaakkklEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATA 1682
Cdd:pfam05483 432 EELKGKEQELIFLLQAR----------EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1683 KENEKKAKSLEADLMQLQEDLaaaERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAM 1762
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDI---INCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1763 SDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKlhemeGAVKSKfksTIAALEAKIAQLEEQVEQEAR 1842
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAENK---QLNAYEIKVNKLELELASAKQ 650
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1843 EKQAATKSLKQkdkklkeillQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQ 1901
Cdd:pfam05483 651 KFEEIIDNYQK----------EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1656-1940 |
1.63e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1656 KLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE-------------ADLMQLQEDLAA-----AERARKQADLEK 1717
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLErqaekaerykelkAELRELELALLVlrleeLREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1718 EELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQL 1797
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1798 ERQNKELRSKLHEMEgAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKE 1877
Cdd:TIGR02168 329 ESKLDELAEELAELE-EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1878 QAEKGNARVKQLKRQLEEAEEESQRINANRRK-----LQRELDEATESNEAMGREVNALKSKLRRGNE 1940
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQaeleeLEEELEELQEELERLEEALEELREELEEAEQ 475
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1077-1314 |
1.64e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1077 QIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDserAARNKAEKQKRDLGEELE 1156
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1157 ALKTE------LEDTLDSTATQQELrakreQEVTVLKKALDeetrsheaqvqemrqKHAQAVEELTEQLEQFKRAKANLD 1230
Cdd:COG3883 94 ALYRSggsvsyLDVLLGSESFSDFL-----DRLSALSKIAD---------------ADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1231 KNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKA 1310
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
....
gi 92091586 1311 IKLA 1314
Cdd:COG3883 234 AAAA 237
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1636-1910 |
1.73e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.65 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1636 LELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKenekkAKSLEADLMQLQEDLAAAERARKQAdl 1715
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE-----AKLLLQQLSELESQLAEARAELAEA-- 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1716 ekeelaeelasslsgrnalQDEKRRLEARIAQLEEELEEEQGNmeamsDRVRKATQQAEQLSNELATERSTAQKNESARQ 1795
Cdd:COG3206 239 -------------------EARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1796 QLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEarekQAATKSLKQKDKKLKEILLQVEDERKMAEQY 1875
Cdd:COG3206 295 ALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESL 370
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 92091586 1876 ---------KEQAEKGNARVkqlkrqLEEAEEESQRINANRRKL 1910
Cdd:COG3206 371 lqrleearlAEALTVGNVRV------IDPAVVPLKPVSPKKLLI 408
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1004-1713 |
2.04e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.97 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1004 LSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHES------MISELEVRLKKEEKSRQELEKLKRKLEGDAS---DF 1074
Cdd:PRK04863 295 LYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdhlnLVQTALRQQEKIERYQADLEELEERLEEQNEvveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1075 HEQIADLQAQ-------IAELKMQLAkkeeELQAALARLDDEIAQKNNALKKIRELEG--HISDLQEDLDSERAARNKAE 1145
Cdd:PRK04863 375 DEQQEENEARaeaaeeeVDELKSQLA----DYQQALDVQQTRAIQYQQAVQALERAKQlcGLPDLTADNAEDWLEEFQAK 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1146 KQkrDLGEELEALKTELEDTlDSTATQQELRAK----------REQEVTVLKKALD--EETRSHEAQVQEMRQKHAQAVE 1213
Cdd:PRK04863 451 EQ--EATEELLSLEQKLSVA-QAAHSQFEQAYQlvrkiagevsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQ 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1214 ELTEQ------LEQF-KRAKANLDKN------KQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgER 1280
Cdd:PRK04863 528 RLRQQqraerlLAEFcKRLGKNLDDEdeleqlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR----AP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1281 ARAELNDKVHKLQnevesvtgmlnEAEGKAIKlakDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD--- 1357
Cdd:PRK04863 604 AWLAAQDALARLR-----------EQSGEEFE---DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQpgg 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1358 -------QLDE--------------------EMEAKQNLERHISTLNiQLSDSKKKL-----------------QDFAST 1393
Cdd:PRK04863 670 sedprlnALAErfggvllseiyddvsledapYFSALYGPARHAIVVP-DLSDAAEQLagledcpedlyliegdpDSFDDS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1394 VEALEEGKK--------------RF-----------QKEIENLTQQYEEKAAAYDKLE---------------------- 1426
Cdd:PRK04863 749 VFSVEELEKavvvkiadrqwrysRFpevplfgraarEKRIEQLRAEREELAERYATLSfdvqklqrlhqafsrfigshla 828
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1427 -----------KTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER--DRAEaEAREKETKAL 1493
Cdd:PRK04863 829 vafeadpeaelRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVE-EIREQLDEAE 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1494 SLARALeealeakeeleRTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDA 1568
Cdd:PRK04863 908 EAKRFV-----------QQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDA 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1569 KLRLEVNMQ---ALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaik 1645
Cdd:PRK04863 977 AEMLAKNSDlneKLRQRLEQAEQERTRAREQ-LRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS--- 1052
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1646 GREEaikqlrKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1713
Cdd:PRK04863 1053 GAEE------RARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1057-1839 |
2.11e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.58 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1057 RQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKK---EEELQAALARLDDEIAQKNNALK---KIRELEGHISDL 1130
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELsarESDLEQDYQAASDHLNLVQTALRqqeKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1131 QEDLDSERAARNKAEKQKRDLGEELEA-------LKTELED---TLDSTAT-----QQELRAKRE-QEVTVLKKALDEET 1194
Cdd:COG3096 360 TERLEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVQQTraiqyQQAVQALEKaRALCGLPDLTPENA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1195 RSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKenadLAGEL---RVLGQAKQEVEH--KKKKLEAQVQ 1269
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK----IAGEVersQAWQTARELLRRyrSQQALAQRLQ 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1270 ELQSKCSDGERARAElndkvhklQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1349
Cdd:COG3096 516 QLRAQLAELEQRLRQ--------QQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1350 EERNSLQDQLDEE----MEAKQNLERHISTLNIQLSDSKKKLQDFASTVEA----------LEEGKKRFQKEIENLTQqy 1415
Cdd:COG3096 588 EQLRARIKELAARapawLAAQDALERLREQSGEALADSQEVTAAMQQLLERereatverdeLAARKQALESQIERLSQ-- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1416 eeKAAAYD-KLEKTKNRLQQEL-----DDLVVD--------LDNQRQ--LVSNLEKKQRKFDQLlaeEKNISSKYADERD 1479
Cdd:COG3096 666 --PGGAEDpRLLALAERLGGVLlseiyDDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGL---EDCPEDLYLIEGD 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1480 RAEAEAREKETKALSLARALEEALEAKE-----------ELERTNKM--LKAEMEDLVSSKDDVGKNVHELEKSKRAL-- 1544
Cdd:COG3096 741 PDSFDDSVFDAEELEDAVVVKLSDRQWRysrfpevplfgRAAREKRLeeLRAERDELAEQYAKASFDVQKLQRLHQAFsq 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1545 --------------ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE--RDLQAR-----DEQNEEKRRQLQR 1603
Cdd:COG3096 821 fvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1604 QLHEYEtELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqrELEDARASRdEIFATAK 1683
Cdd:COG3096 901 ELDAAQ-EAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIF----ALSEVVQRR-PHFSYED 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1684 ENEKKAKS------LEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLeeeleeeqg 1757
Cdd:COG3096 975 AVGLLGENsdlnekLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL--------- 1045
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1758 NMEAMSDRVRKATQQAEQLSNELATERstaqkneSARQQLERQNKELRSklhEMEGAVKskfksTIAALEAKIAQLEEQV 1837
Cdd:COG3096 1046 GVQADAEAEERARIRRDELHEELSQNR-------SRRSQLEKQLTRCEA---EMDSLQK-----RLRKAERDYKQEREQV 1110
|
..
gi 92091586 1838 EQ 1839
Cdd:COG3096 1111 VQ 1112
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
860-1297 |
2.54e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.47 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 860 EMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETE-----LYAEA---EEMRVRLAAKKQELEEIL 931
Cdd:pfam12128 486 EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGtllhfLRKEApdwEQSIGKVISPELLHRTDL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 932 HEMEARLEEEEDR---GQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQlekvTAEAKIKKLEDEilvmddqnnkLSKER 1008
Cdd:pfam12128 566 DPEVWDGSVGGELnlyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQ----SAREKQAAAEEQ----------LVQAN 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1009 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESM----ISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIadlQAQ 1084
Cdd:pfam12128 632 GELEKASREETFARTALKNARLDLRRLFDEKQSEkdkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQ---KEQ 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1085 IAELKMQLAKK----EEELQAALARLDDEIAQKNNALKKirelegHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT 1160
Cdd:pfam12128 709 KREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAKA------ELKALETWYKRDLASLGVDPDVIAKLKREIRTLER 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1161 ELEDTldstatqqelrAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQL----EQFKRAKANLDKNKQTL 1236
Cdd:pfam12128 783 KIERI-----------AVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLarliADTKLRRAKLEMERKAS 851
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1237 EKENADLAGELRVLGQAKQEVehKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1297
Cdd:pfam12128 852 EKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK 910
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
851-1637 |
2.91e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.21 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 851 LLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaAKKQELEEI 930
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL----QQTQQSHAY 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 931 LHEMEARLEEEEDRGQQLQAERkkmaqqmldleeqleeeeaarqklqlekvtaeAKIKKLEDEILVMDDQNNKLSKERKL 1010
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLR--------------------------------ARIEELRAQEAVLEETQERINRARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1011 LEerisdlttnLAEEeekAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRklegdasdfheQIADLQAQIAELKM 1090
Cdd:TIGR00618 293 AP---------LAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK-----------QQSSIEEQRRLLQT 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1091 QLAKKEEelqaaLARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEelEALKTELEDTLDSTA 1170
Cdd:TIGR00618 350 LHSQEIH-----IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQR--EQATIDTRTSAFRDL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1171 TQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQaveelteQLEQFKRAKANLDKNKQTLEKENAdlagelrvl 1250
Cdd:TIGR00618 423 QGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-------ESAQSLKEREQQLQTKEQIHLQET--------- 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1251 gQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELND------KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQL 1324
Cdd:TIGR00618 487 -RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1325 QDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNL----ERHISTLNIQLSDSKKKLQDfASTVEALEEG 1400
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLaceqHALLRKLQPEQDLQDVRLHL-QQCSQELALK 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1401 KKRFQKEIENLTQQYEEKAAAY----------------DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLL 1464
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALSirvlpkellasrqlalQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIE 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1465 AEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSskddvgknvhELEKSKRAL 1544
Cdd:TIGR00618 725 NASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA----------EIQFFNRLR 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1545 ETQMEEMKTQLEELEDELQATEDAKLrlevnmqALKGQFERDLQARDEQNEEKRRQLQRQLHEYEtELEDERKQRALAAA 1624
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILN-------LQCETLVQEEEQFLSRLEEKSATLGEITHQLL-KYEECSKQLAQLTQ 866
|
810
....*....|...
gi 92091586 1625 AKKKLEGDLKDLE 1637
Cdd:TIGR00618 867 EQAKIIQLSDKLN 879
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
770-1444 |
3.29e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 770 IGQSKIFFRTGVLAHLEEERDL---------KITDVIMAFQAMCRGYLARKafakrqqqlTAMKVIQRNCAAYLKLRNwq 840
Cdd:PRK01156 122 LGISKDVFLNSIFVGQGEMDSLisgdpaqrkKILDEILEINSLERNYDKLK---------DVIDMLRAEISNIDYLEE-- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 841 wwRLFTKVKPLLQVTRQEEEMQAKEDELQKTKER-------QQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEA 913
Cdd:PRK01156 191 --KLKSSNLELENIKKQIADDEKSHSITLKEIERlsieynnAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 914 EEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqlekvtaeAKIKKLEDE 993
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYND 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 994 ILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD 1073
Cdd:PRK01156 341 YIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQD 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1074 FHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGE 1153
Cdd:PRK01156 421 ISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEK---IREIEIEVKDIDE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1154 ELEALKtELEDTLDSTATQQELRAKReqevtvLKKALDEETRSHEAQVQEMRQKHAQAvEELTEQLEQFKRakANLDKNK 1233
Cdd:PRK01156 498 KIVDLK-KRKEYLESEEINKSINEYN------KIESARADLEDIKIKINELKDKHDKY-EEIKNRYKSLKL--EDLDSKR 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKENADLAG-ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGErarAELNDKVHKLQNEVESVTGMLNEAEGKAI- 1311
Cdd:PRK01156 568 TSWLNALAVISLiDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---SYIDKSIREIENEANNLNNKYNEIQENKIl 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1312 -----KLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKK 1386
Cdd:PRK01156 645 ieklrGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINET 724
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1387 LQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQ---ELDDLVVDLD 1444
Cdd:PRK01156 725 LESMKKIKKAIGDLKRLREAFDKSGVPAMIRKSASQAMTSLTRKYLFEfnlDFDDIDVDQD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1271-1465 |
3.45e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.87 E-value: 3.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1271 LQSKCSDGERARAELNDKVHKLQNEVESVtgmlnEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1350
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1351 ERNSLQDQLDEEMEAK---------QNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQ-------- 1413
Cdd:COG3206 241 RLAALRAQLGSGPDALpellqspviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQrilaslea 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1414 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLA 1465
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQ 372
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1511-1919 |
3.84e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1511 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqALKGQFE------ 1584
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELKEEIEelekel 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1585 RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQaDSAIKGREEAIKQLRKLQAQMKDF 1664
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY-EEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1665 QRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAERARkqadlekeelaeelasslsgrnALQDEKRRLEAR 1744
Cdd:PRK03918 327 EERIKELEEKEERL----EELKKKLKELEKRLEELEERHELYEEAK----------------------AKKEELERLKKR 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1745 IAQLEEeleeeqGNMEAMSDRVRKATQQAEQLSNELATERStaqknesarqQLERQNKELRSKLHEMEGA---------- 1814
Cdd:PRK03918 381 LTGLTP------EKLEKELEELEKAKEEIEEEISKITARIG----------ELKKEIKELKKAIEELKKAkgkcpvcgre 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1815 --------VKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDK--KLKEILLQVEDERKM--------AEQYK 1876
Cdd:PRK03918 445 lteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKlkkynleeLEKKA 524
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 92091586 1877 EQAEKGNARVKQLKRQLEEAEEESQRINA---NRRKLQRELDEATE 1919
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEE 570
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1536-1747 |
5.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1536 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLHEYETELEDE 1615
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1616 RKQ-RALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEA 1694
Cdd:COG4942 103 KEElAELLRALYRLGRQPPLALLLSPEDF----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1695 DLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQ 1747
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1726-1919 |
6.31e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1726 SSLSGRNALQDEKRRLEARI--AQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKE 1803
Cdd:COG3206 172 EARKALEFLEEQLPELRKELeeAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1804 LRSKLHEMEGAvkskfkSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDE-RKMAEQYKEQAEKG 1882
Cdd:COG3206 252 GPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaQRILASLEAELEAL 325
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 92091586 1883 NARVKQLKRQLEEAEEESQRINANRRK---LQRELDEATE 1919
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
853-1618 |
7.10e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEI-- 930
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAkq 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 931 -LHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKIKKLEDEILVMDDQNNKLSKERK 1009
Cdd:PRK04863 429 lCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS--QFEQ--AYQLVRKIAGEVSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1010 LLEERI------------SDLTTNLAEEEEKAKNLTKLKNKHESMI---SELEVRLKKEEKSRQELEKLKRKLEGDASDF 1074
Cdd:PRK04863 505 LREQRHlaeqlqqlrmrlSELEQRLRQQQRAERLLAEFCKRLGKNLddeDELEQLQEELEARLESLSESVSEARERRMAL 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1075 HEQIADLQAQIAELKmQLAKKEEELQAALARLDDeiaQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEE 1154
Cdd:PRK04863 585 RQQLEQLQARIQRLA-ARAPAWLAAQDALARLRE---QSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1155 LEALkteledTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMR---QKHAQAVEELTeqleqfkRAKANLDK 1231
Cdd:PRK04863 661 IERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAIVVPDLS-------DAAEQLAG 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1232 NKQTLEkenaDL---AGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSD-------GERARAELndkVHKLQNEVESVTG 1301
Cdd:PRK04863 728 LEDCPE----DLyliEGDPDSFDDSVFSVEELEKAVVVKIADRQWRYSRfpevplfGRAAREKR---IEQLRAEREELAE 800
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1302 MLNEAEGKAIKLAKDVASLSSQL---------QDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERH 1372
Cdd:PRK04863 801 RYATLSFDVQKLQRLHQAFSRFIgshlavafeADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1373 ISTLNIQLSDS-KKKLQDFASTVEALEEGK---KRFQKEIENLT----------QQYEEKAAAYDKLEKTKNRLQQELDD 1438
Cdd:PRK04863 881 LPRLNLLADETlADRVEEIREQLDEAEEAKrfvQQHGNALAQLEpivsvlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFA 960
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1439 LvVDLdNQRQLVSNLEKKQrkfdQLLAEEKNISSKYADERDRAEAEAREketkalslaraleealeakeelertnkmLKA 1518
Cdd:PRK04863 961 L-TEV-VQRRAHFSYEDAA----EMLAKNSDLNEKLRQRLEQAEQERTR----------------------------ARE 1006
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1519 EMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELedELQATEDAKLRLEVNmqalkgqfERDLQARDEQNEEKR 1598
Cdd:PRK04863 1007 QLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL--GVPADSGAEERARAR--------RDELHARLSANRSRR 1076
|
810 820
....*....|....*....|
gi 92091586 1599 RQLQRQLHEYETELEDERKQ 1618
Cdd:PRK04863 1077 NQLEKQLTFCEAEMDNLTKK 1096
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1002-1713 |
7.35e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1002 NKLSKERKLLEEriSDLT-TNLAEEEEKAKnlTKLKNKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFH 1075
Cdd:COG3096 420 QALEKARALCGL--PDLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAW 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1076 EQIADLQAQIAELKMQlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISDLQEDLDSERaarnkaekqkrDLGEEL 1155
Cdd:COG3096 495 QTARELLRRYRSQQAL-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAAE-----------ELEELL 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1156 EALKTELEDTLDSTATQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQKH------AQAVEELTEQL-EQFKRAKAN 1228
Cdd:COG3096 560 AELEAQLEELEEQAAEAVEQRSELRQQ-------LEQ----LRARIKELAARApawlaaQDALERLREQSgEALADSQEV 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1229 LDKNKQTLEKEnadlagelRVLGQAKQEVEHKKKKLEAQVQELQSKCS--DGERAR----------AELNDKVhKLQN-- 1294
Cdd:COG3096 629 TAAMQQLLERE--------REATVERDELAARKQALESQIERLSQPGGaeDPRLLAlaerlggvllSEIYDDV-TLEDap 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1295 EVESVTGMLNEA------EGKAIKLAK-------------DVASLSSQLQDTQEL-----LQEETRQkLNVST------- 1343
Cdd:COG3096 700 YFSALYGPARHAivvpdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplf 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1344 -------KLRQLEEERNSLQDQLDEEMEAKQNLERhistLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:COG3096 779 graarekRLEELRAERDELAEQYAKASFDVQKLQR----LHQAFSQfvGGHLAVAFAPDPEAELAALRQRRSELERELAQ 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1415 YEEKAAaydklektknRLQQELDDLVVDLDNQRQLVSNLEkkqrkfdqLLAEEknisskyaDERDRAEaEAREKETKALS 1494
Cdd:COG3096 855 HRAQEQ----------QLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQE 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1495 LARALEEALEAKeelertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAK 1569
Cdd:COG3096 908 AQAFIQQHGKAL-----------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAV 976
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1570 LRLEVN---MQALKGQFERDLQARDEQNEeKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKG 1646
Cdd:COG3096 977 GLLGENsdlNEKLRARLEQAEEARREARE-QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEE 1055
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1647 ReeaikqlrklqaqmkdfqreledARASRDEIFATAKEN-------EKKAKSLEADLMQLQEDLAAAER----ARKQA 1713
Cdd:COG3096 1056 R-----------------------ARIRRDELHEELSQNrsrrsqlEKQLTRCEAEMDSLQKRLRKAERdykqEREQV 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1535-1921 |
8.07e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1535 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQNEEKRRQLQRQLHEYEtELE 1613
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEERLEELRELEEELE-ELE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1614 DERKQRALAAAAKKKLEGDLKDLELQadSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE 1693
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQ--DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1694 ADLMQLQED----------------------------LAAAERARKQADLEKEELAEELASSLSGRNALQDEK-RRLEAR 1744
Cdd:COG4717 248 ARLLLLIAAallallglggsllsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1745 IAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNE--------------------SARQQLERQNKEL 1804
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvedeeelraaleqaEEYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1805 RSKLHEMEGAVKSKFKS-TIAALEAKIAQLEEQVEQEAREKQAatksLKQKDKKLKEILLQVEDERKMAEQYKEQAEkgn 1883
Cdd:COG4717 408 EEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEE----LREELAELEAELEQLEEDGELAELLQELEE--- 480
|
410 420 430
....*....|....*....|....*....|....*...
gi 92091586 1884 arvkqLKRQLEEAEEESQRINANRRKLQRELDEATESN 1921
Cdd:COG4717 481 -----LKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
853-1271 |
8.14e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELyaeaeemrvrlaakkQELEEILH 932
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY---------------QELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1012
Cdd:COG4717 140 ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHE--------SMISELEVRLKKEEKSRQELEKLKRKLEG----DASDFHEQIAD 1080
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEarlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1081 LQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQ--KRDLGEELEAL 1158
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1159 KTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQemrqkhAQAVEELTEQLEQFKRAKANLDKNKQTLEK 1238
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE------ALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|....*
gi 92091586 1239 ENADLAGELRVL--GQAKQEVEHKKKKLEAQVQEL 1271
Cdd:COG4717 454 ELAELEAELEQLeeDGELAELLQELEELKAELREL 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
909-1356 |
8.14e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 909 LYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEeeaarqkLQLEKVTAEAKIK 988
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-------LEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 989 KLEDEIlvmddQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEvrlKKEEKSRQELEKLKRKLE 1068
Cdd:COG4717 120 KLEKLL-----QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1069 GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD--EIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEK 1146
Cdd:COG4717 192 EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQleNELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1147 QKRDLG-------------EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVE 1213
Cdd:COG4717 272 ILTIAGvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1214 ELTEQLEQFKRAK--ANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKvhK 1291
Cdd:COG4717 352 LLREAEELEEELQleELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE--E 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1292 LQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQD--TQELLQEETRQKLNVSTKLRQLEEERNSLQ 1356
Cdd:COG4717 430 LEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1287-1496 |
8.44e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1287 DKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAK 1366
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1367 QNLERHISTLNIQLSDskKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEkaaaydkLEKTKNRLQQELDDLVVDLDNQ 1446
Cdd:COG3883 96 YRSGGSVSYLDVLLGS--ESFSDFLDRLSALSKIADADADLLEELKADKAE-------LEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 92091586 1447 RQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLA 1496
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1044-1352 |
9.41e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.08 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1044 SELEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKnnalkkiRE 1122
Cdd:pfam00038 28 KLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1123 LEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKT-------ELEDTLDSTATQQELRAKREQEVTVLkkaldeetr 1195
Cdd:pfam00038 101 AENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnheeevrELQAQVSDTQVNVEMDAARKLDLTSA--------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1196 sheaqVQEMRQKHAQAVEELTEQLEQFKRAKanLDKNKQTLEKENADlagelrvLGQAKQEV---EHKKKKLEAQVQELQ 1272
Cdd:pfam00038 172 -----LAEIRAQYEEIAAKNREEAEEWYQSK--LEELQQAAARNGDA-------LRSAKEEItelRRTIQSLEIELQSLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1273 SKCSDGERARAELNDkvhKLQNEVESVTGMLNEAEGkaiKLAKDVASLSSQLQDTQELLQEETRQKLNVST--KLRQLEE 1350
Cdd:pfam00038 238 KQKASLERQLAETEE---RYELQLADYQELISELEA---ELQETRQEMARQLREYQELLNVKLALDIEIATyrKLLEGEE 311
|
..
gi 92091586 1351 ER 1352
Cdd:pfam00038 312 CR 313
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1182-1455 |
1.10e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.95 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1182 EVTVLKKALDEETRShEAQVQEMRQKHAQAVEELTE--QLEQFKRAKANLDKnKQTLEKENADLAGELrvlgqaKQEVEh 1259
Cdd:PHA02562 167 EMDKLNKDKIRELNQ-QIQTLDMKIDHIQQQIKTYNknIEEQRKKNGENIAR-KQNKYDELVEEAKTI------KAEIE- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1260 kkkKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTgmlneaegKAIKLAKD---VASLSSQLQDTQELLQEETR 1336
Cdd:PHA02562 238 ---ELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQ--------KVIKMYEKggvCPTCTQQISEGPDRITKIKD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1337 QKLNVSTKLRQLEEERNSLQDQLDEEMEA---KQNLERHISTLNIQLSDSKKKLqdfastvealeegkKRFQKEIENLTQ 1413
Cdd:PHA02562 307 KLKELQHSLEKLDTAIDELEEIMDEFNEQskkLLELKNKISTNKQSLITLVDKA--------------KKVKAAIEELQA 372
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 92091586 1414 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnQRQLVSNLEK 1455
Cdd:PHA02562 373 EFVDNAEELAKLQDELDKIVKTKSELVKEKY-HRGIVTDLLK 413
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1160-1488 |
1.20e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.79 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1160 TELEDTLDSTatqqelrakrEQEVTVLKKALDEETRSHE---AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTL 1236
Cdd:pfam06160 89 DEIEELLDDI----------EEDIKQILEELDELLESEEknrEEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1237 EK---------ENADLAGELRVLGQAKQEVEHKKKKLEaQVQELQSKCSDgeraraELNDKVHKLQNEVESVtgmlnEAE 1307
Cdd:pfam06160 159 EEefsqfeeltESGDYLEAREVLEKLEEETDALEELME-DIPPLYEELKT------ELPDQLEELKEGYREM-----EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 G---KAIKLAKDVASLSSQLQDTQELLqEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLsdsk 1384
Cdd:pfam06160 227 GyalEHLNVDKEIQQLEEQLEENLALL-ENLELD-EAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYL---- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1385 kklqdfastvEALEEGKKRFQKEIENLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQ 1457
Cdd:pfam06160 301 ----------EHAEEQNKELKEELERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVayseLQEELEEIL 370
|
330 340 350
....*....|....*....|....*....|.
gi 92091586 1458 RKFDQLLAEEKNISSKYADERDrAEAEAREK 1488
Cdd:pfam06160 371 EQLEEIEEEQEEFKESLQSLRK-DELEAREK 400
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
974-1122 |
1.42e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 974 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEleVRLKKE 1053
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGN--VRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1054 EKSRQ-ELEKLKRK---LEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRE 1122
Cdd:COG1579 91 YEALQkEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
894-1713 |
1.44e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.88 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 894 EEKNLLQEQLQAETELYAEAEEmrvrLAAKKQELEEILHEMEARLEEEEDRGQQLQAE-------RKKMAQQ-------- 958
Cdd:COG3096 279 ERRELSERALELRRELFGARRQ----LAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnlvQTALRQQekieryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 959 -MLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEI-----------LVMDDQN----------NKLSKERKLLEEriS 1016
Cdd:COG3096 355 dLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQtraiqyqqavQALEKARALCGL--P 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1017 DLT-TNLAEEEEKAKnlTKLKNKHESMIsELEVRLKKEEKSRQELEK---LKRKLEG--DASDFHEQIADLQAQIAELKM 1090
Cdd:COG3096 433 DLTpENAEDYLAAFR--AKEQQATEEVL-ELEQKLSVADAARRQFEKayeLVCKIAGevERSQAWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1091 QlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISDLQEDLDSEraarnkaekqkRDLGEELEALKTELEDTLDSTA 1170
Cdd:COG3096 510 L-AQRLQQLRAQLAELEQRLRQQQNA---ERLLEEFCQRIGQQLDAA-----------EELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1171 TQQELRAKREQEvtvlkkaLDEetrsHEAQVQEMRQKH------AQAVEELTEQL-EQFKRAKANLDKNKQTLEKEnadl 1243
Cdd:COG3096 575 EAVEQRSELRQQ-------LEQ----LRARIKELAARApawlaaQDALERLREQSgEALADSQEVTAAMQQLLERE---- 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1244 agelRVLGQAKQEVEHKKKKLEAQVQELQ--SKCSDGERAR----------AELNDKVhKLQN--EVESVTGMLNEA--- 1306
Cdd:COG3096 640 ----REATVERDELAARKQALESQIERLSqpGGAEDPRLLAlaerlggvllSEIYDDV-TLEDapYFSALYGPARHAivv 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1307 ---EGKAIKLAK-------------DVASLSSQLQDTQEL-----LQEETRQkLNVST--------------KLRQLEEE 1351
Cdd:COG3096 715 pdlSAVKEQLAGledcpedlyliegDPDSFDDSVFDAEELedavvVKLSDRQ-WRYSRfpevplfgraarekRLEELRAE 793
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERhistLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAaydklektk 1429
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQR----LHQAFSQfvGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQ--------- 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1430 nRLQQELDDLVVDLDNQRQLVSNLEkkqrkfdqLLAEEknisskyaDERDRAEaEAREKETKALSLARALEEALEAKeel 1509
Cdd:COG3096 861 -QLRQQLDQLKEQLQLLNKLLPQAN--------LLADE--------TLADRLE-ELREELDAAQEAQAFIQQHGKAL--- 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1510 ertnkmlkAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQ-----ATEDAKLRLEVN---MQALKG 1581
Cdd:COG3096 920 --------AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfSYEDAVGLLGENsdlNEKLRA 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1582 QFERDLQARDEQNeEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSaikGREEaikqlrKLQAQM 1661
Cdd:COG3096 992 RLEQAEEARREAR-EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADA---EAEE------RARIRR 1061
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1662 KDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQA 1713
Cdd:COG3096 1062 DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
984-1922 |
1.71e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 56.98 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 984 EAKIKKLEDEILVMDDQNNKLSKERklLEERISDLTTNLAEEE-----EKAKNLTKLKNKHESMISELEVRLKKEEKSRQ 1058
Cdd:TIGR01612 702 KSKIDKEYDKIQNMETATVELHLSN--IENKKNELLDIIVEIKkhihgEINKDLNKILEDFKNKEKELSNKINDYAKEKD 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1059 ELEKLKRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIREleGHISDLQEDLDSER 1138
Cdd:TIGR01612 780 ELNKYKSKISEIKNHYNDQINIDNIKDEDAK-QNYDKSKEYIKTISIKEDEIFKIINEMKFMKD--DFLNKVDKFINFEN 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1139 AARNKAEKQKRDLGEELEALKTELEDtldstatqqELRAKREQEVTVLKKALDEETRSHEAQVQEMR-----QKHAQAVE 1213
Cdd:TIGR01612 857 NCKEKIDSEHEQFAELTNKIKAEISD---------DKLNDYEKKFNDSKSLINEINKSIEEEYQNINtlkkvDEYIKICE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1214 ELTEQLEQFK----RAKANLDKNKQTLEKENADlagELRVLGQAKQEVEHKKKKLEAQVQELQskCSDGERARAEL---- 1285
Cdd:TIGR01612 928 NTKESIEKFHnkqnILKEILNKNIDTIKESNLI---EKSYKDKFDNTLIDKINELDKAFKDAS--LNDYEAKNNELikyf 1002
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1286 ND--------KVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKL--NVSTKLRQLEEERNSL 1355
Cdd:TIGR01612 1003 NDlkanlgknKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIgkNIELLNKEILEEAEIN 1082
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1356 QDQLDEEMEAKQ--NLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQY-EEKAAAYDKLEKTKNR- 1431
Cdd:TIGR01612 1083 ITNFNEIKEKLKhyNFDDFGKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYiDEIKAQINDLEDVADKa 1162
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1432 --------LQQELDDLVVDLDNQRQLVSNLEK------KQRKFDQLLAEEKNISSKYA------------DERDRAE--A 1483
Cdd:TIGR01612 1163 isnddpeeIEKKIENIVTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGINLSYGknlgklflekidEEKKKSEhmI 1242
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1484 EAREKETKALSLARALEEALEAKEELERTnkmLKAEMEDLVSSKDDVgKNVHELEKSKRALETQMEEMKTQLEELEDELQ 1563
Cdd:TIGR01612 1243 KAMEAYIEDLDEIKEKSPEIENEMGIEMD---IKAEMETFNISHDDD-KDHHIISKKHDENISDIREKSLKIIEDFSEES 1318
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1564 ATEDAKLRLEVNM-QALKGQFERDLQARDEQN------EEKRRQLQRQLHEYETELEDERKQ------RALAAAAKKKLE 1630
Cdd:TIGR01612 1319 DINDIKKELQKNLlDAQKHNSDINLYLNEIANiynilkLNKIKKIIDEVKEYTKEIEENNKNikdeldKSEKLIKKIKDD 1398
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1631 GDLKDLELQADSAIKGRE--EAIKQLRKLQAQMKDfqreledARASRDEIFATAKENEKK----------AKSLEADLMQ 1698
Cdd:TIGR01612 1399 INLEECKSKIESTLDDKDidECIKKIKELKNHILS-------EESNIDTYFKNADENNENvlllfkniemADNKSQHILK 1471
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1699 LQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSN 1778
Cdd:TIGR01612 1472 IKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIK 1551
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1779 EL--ATERSTAQKNESARQQLERQNKELRSklhEMEGAVKSKFKSTIAALEAKIAQLEEQV---------------EQEA 1841
Cdd:TIGR01612 1552 EIkdAHKKFILEAEKSEQKIKEIKKEKFRI---EDDAAKNDKSNKAAIDIQLSLENFENKFlkisdikkkindclkETES 1628
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1842 REKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQaekgnarvkqlKRQLEEAEEESQRINANRRKLQRELDEATESN 1921
Cdd:TIGR01612 1629 IEKKISSFSIDSQDTELKENGDNLNSLQEFLESLKDQ-----------KKNIEDKKKELDELDSEIEKIEIDVDQHKKNY 1697
|
.
gi 92091586 1922 E 1922
Cdd:TIGR01612 1698 E 1698
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
986-1167 |
2.00e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.16 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 986 KIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKr 1065
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1066 klegdasdfheQIADLQAQIAELKMQLAKKEEELQAALARLDdeiaqknNALKKIRELEGHISDLQEDLDSERAARNKAE 1145
Cdd:COG1579 90 -----------EYEALQKEIESLKRRISDLEDEILELMERIE-------ELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|..
gi 92091586 1146 KQKRDLGEELEALKTELEDTLD 1167
Cdd:COG1579 152 AELEAELEELEAEREELAAKIP 173
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1516-1714 |
2.37e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1516 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNE 1595
Cdd:COG4942 39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1596 EKR----------RQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQ 1665
Cdd:COG4942 119 QPPlalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 92091586 1666 RELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQAD 1714
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1364-1618 |
3.13e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1364 EAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDL 1443
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1444 DNQRQLVSNLEKKQRKFDQLLAEEKNISSKyaderDRAEAEAREKETKALSLARaleealeakeelertnkmlKAEMEDL 1523
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPE-----DFLDAVRRLQYLKYLAPAR-------------------REQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1524 VSSKDdvgknvhELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDlQARDEQNEEKRRQLQR 1603
Cdd:COG4942 156 RADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL-AAELAELQQEAEELEA 227
|
250
....*....|....*
gi 92091586 1604 QLHEYETELEDERKQ 1618
Cdd:COG4942 228 LIARLEAEAAAAAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1308-1920 |
3.28e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 55.61 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 GKAIKLAKDVASLSSQLQDTQEL--------LQEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAkqnlerhistLNIQ 1379
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLhfgyksdeTLIASRQE-ERQETSAELNQLLRTLDDQWKEKRDE----------LNGE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1380 LSDSKKKLQDFASTVEALEEGKKRFQK--------EIENLTQ---QYEEKAAAYDKLEKTKNRLQQELDDLV--VDLDNQ 1446
Cdd:pfam12128 310 LSAADAAVAKDRSELEALEDQHGAFLDadietaaaDQEQLPSwqsELENLEERLKALTGKHQDVTAKYNRRRskIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1447 RQLVSN---LEKKQRKFDQLLAEEKN----ISSKYADERDRAEAEAREKEtKALSLARALEEALEAKEELERTNKMLKAE 1519
Cdd:pfam12128 390 RDIAGIkdkLAKIREARDRQLAVAEDdlqaLESELREQLEAGKLEFNEEE-YRLKSRLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1520 MEDLVSSKDD----VGKNVHELEKSKRALETQMEEmktQLEELEDELQATEDAKLRLEVNMQALKGQ------FERDLQA 1589
Cdd:pfam12128 469 FDERIERAREeqeaANAEVERLQSELRQARKRRDQ---ASEALRQASRRLEERQSALDELELQLFPQagtllhFLRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1590 RDEQNEEK---RRQLQR--------------QLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIK 1652
Cdd:pfam12128 546 DWEQSIGKvisPELLHRtdldpevwdgsvggELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1653 QLRKLQAQMKDFQRELEDARAsrdeifaTAKENEKKAKSLEADLMQLQEDLAAAERARKQAdlekeelaeelasslsgrn 1732
Cdd:pfam12128 626 QLVQANGELEKASREETFART-------ALKNARLDLRRLFDEKQSEKDKKNKALAERKDS------------------- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1733 aLQDEKRRLEAriaQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTA-----QKNESARQQLERQNKELRSK 1807
Cdd:pfam12128 680 -ANERLNSLEA---QLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQlallkAAIAARRSGAKAELKALETW 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1808 LHEmEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATkslkQKDKKLKEILLQVEDERKMAeqyKEQAEKGNARVK 1887
Cdd:pfam12128 756 YKR-DLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL----RYFDWYQETWLQRRPRLATQ---LSNIERAISELQ 827
|
650 660 670
....*....|....*....|....*....|....
gi 92091586 1888 -QLKRQLEEAEEESQRINANRRKLQRELDEATES 1920
Cdd:pfam12128 828 qQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1596-1847 |
4.77e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1596 EKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADsaikgreEAIKQLRKLQAQMKDFQRELedarasr 1675
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA-------ALARRIRALEQELAALEAEL------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1676 deifataKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEelassLSGRNALQDEKRR--LEARIAQLEEELE 1753
Cdd:COG4942 86 -------AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALL-----LSPEDFLDAVRRLqyLKYLAPARREQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1754 EEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKfKSTIAALEAKIAQL 1833
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL-QQEAEELEALIARL 232
|
250
....*....|....
gi 92091586 1834 EEQVEQEAREKQAA 1847
Cdd:COG4942 233 EAEAAAAAERTPAA 246
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1052-1462 |
5.12e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.92 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1052 KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKK------IRELEG 1125
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETREtlstlsLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1126 HISDLQEDLDSERAARNKAEKQkrdlgeeLEALKTELEDTLDSTATQQelraKREQEVTVLKKALDEETRSHEAQVQEMR 1205
Cdd:PRK11281 129 RLAQTLDQLQNAQNDLAEYNSQ-------LVSLQTQPERAQAALYANS----QRLQQIRNLLKGGKVGGKALRPSQRVLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1206 QKHAQAVEelteqleqfkrakANLDKNKQTLEKENadlagELRVLGQAKQ-EVEHKKKKLEAQVQELQSKCSDGERARAE 1284
Cdd:PRK11281 198 QAEQALLN-------------AQNDLQRKSLEGNT-----QLQDLLQKQRdYLTARIQRLEHQLQLLQEAINSKRLTLSE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1285 lnDKVHKLQNEVESvtgmlNEAEGKAIkLAKDVAS---LSSQLQDTQELLQEETRQKLNVSTKL-------RQLEEERNS 1354
Cdd:PRK11281 260 --KTVQEAQSQDEA-----ARIQANPL-VAQELEInlqLSQRLLKATEKLNTLTQQNLRVKNWLdrltqseRNIKEQISV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1355 LQ------------------DQLDEEMeAKQ--NLERHISTLNIQlsdsKKKLQDFASTVEALEEG-KKRFQKEIEN-LT 1412
Cdd:PRK11281 332 LKgslllsrilyqqqqalpsADLIEGL-ADRiaDLRLEQFEINQQ----RDALFQPDAYIDKLEAGhKSEVTDEVRDaLL 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 92091586 1413 QQYEEKAAAYDKLEKTKNRLQQELDDLVVdldNQRQLVSNLEKKQRKFDQ 1462
Cdd:PRK11281 407 QLLDERRELLDQLNKQLNNQLNLAINLQL---NQQQLLSVSDSLQSTLTQ 453
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1006-1417 |
5.28e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.05 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1006 KERKLLEERISDLTTNL----AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADL 1081
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLrlapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1082 QAQIAELKMQLAKKE--EELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQkrdlgEELEALK 1159
Cdd:TIGR00606 768 EEQETLLGTIMPEEEsaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-----HELDTVV 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1160 TELEDTldstatqQELRAKREQEVTVLKKALDeETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQtlekE 1239
Cdd:TIGR00606 843 SKIELN-------RKLIQDQQEQIQHLKSKTN-ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKE----Q 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1240 NADLAGELRVLGQAKQEVEHKK----KKLEAQVQELQSKCSDGERARAELNDKVH--------KLQNEVESVTGMLNEAE 1307
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKetsnKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddylkQKETELNTVNAQLEECE 990
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 GKAIKLAKDVASLSSQL--QDTQELLQEETRQKLNVSTKLRQLEEERNSL-----QDQLDEEMEAKQNLERHISTLNIQL 1380
Cdd:TIGR00606 991 KHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHlkemgQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
410 420 430
....*....|....*....|....*....|....*..
gi 92091586 1381 SDSKKKLQDFASTVEALEegKKRFQKEIENLTQQYEE 1417
Cdd:TIGR00606 1071 VLALGRQKGYEKEIKHFK--KELREPQFRDAEEKYRE 1105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
843-1242 |
5.78e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 843 RLFTKVKPLLQVTRQEEEMQAKEDELQKTKERQQKAE------NELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEM 916
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEEL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 917 RVRLAAKKQELEEILHEMEARLEEE-----------EDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEA 985
Cdd:COG4717 169 EAELAELQEELEELLEQLSLATEEElqdlaeeleelQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 986 KIK-KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKaknLTKLKNKHESMISELEVRLKKEEKSRQELEKLK 1064
Cdd:COG4717 249 RLLlLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL---LAREKASLGKEAEELQALPALEELEEEELEELL 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1065 RKLEGDASDFHEQIADLQAQIAELKMQLAKKEEE----------------LQAALARLDDEIAQKNNALKKIRELEGHIS 1128
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELeeelqleeleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1129 DLQEDLDSERAARNK--AEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKaldeetrshEAQVQEMRQ 1206
Cdd:COG4717 406 ELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE---------DGELAELLQ 476
|
410 420 430
....*....|....*....|....*....|....*....
gi 92091586 1207 KHAQAVEELTEQLEQFKR---AKANLDKNKQTLEKENAD 1242
Cdd:COG4717 477 ELEELKAELRELAEEWAAlklALELLEEAREEYREERLP 515
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
853-1269 |
6.17e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 6.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKaENELKELEQKHsQLTEEKNLLQEQLQAETELYAEAEEM---------RVRLAAK 923
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEK-EEKAREVERRR-KLEEAEKARQAEMDRQAAIYAEQERMamerereleRIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 924 KQELEEIlhemearleeeedRGQQLQAERKKMAQQmldleeqleeeeaarQKLQLEKVTAEAKIKkledeilvmddQNNK 1003
Cdd:pfam17380 359 KRELERI-------------RQEEIAMEISRMREL---------------ERLQMERQQKNERVR-----------QELE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1004 LSKERKLLEErisdlttnlaEEEEKAKnltklknkhESMISELEVRLKKEEKSRQELEKLkrklegdasdfheqiadlqa 1083
Cdd:pfam17380 400 AARKVKILEE----------ERQRKIQ---------QQKVEMEQIRAEQEEARQREVRRL-------------------- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1084 qiaelkmqlakkEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLgeeleaLKTELE 1163
Cdd:pfam17380 441 ------------EEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI------LEKELE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1164 DTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDknkqTLEKEnadl 1243
Cdd:pfam17380 503 ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLE----AMERE---- 574
|
410 420
....*....|....*....|....*.
gi 92091586 1244 agelRVLGQAKQEVEHKKKKLEAQVQ 1269
Cdd:pfam17380 575 ----REMMRQIVESEKARAEYEATTP 596
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1200-1713 |
6.58e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1200 QVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGE 1279
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1280 RARAELNDKVHKLQ------NEVESVTGMLNEAEGKA-----------IKLAKDVASLSSQLQDTQELLQ--EETRQKLN 1340
Cdd:PRK01156 253 RYESEIKTAESDLSmeleknNYYKELEERHMKIINDPvyknrnyindyFKYKNDIENKKQILSNIDAEINkyHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1341 VSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEAL----EEGKKRFQKEIENLTQQYE 1416
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiSEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1417 EKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQR--KFDQLLAEEK--NISSKYADERDRAEAEAREKETKA 1492
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpVCGTTLGEEKsnHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1493 LSLaraleeALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETqMEEMKTQLEELEDELQAT--EDAKL 1570
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINE-LKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1571 RLEVNMQALKGQFERDLQARDEQNEEKRRQL---QRQLHEYETELEDERKqralaaaakkKLEGDLKDLELQADSAikgr 1647
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKS----------YIDKSIREIENEANNL---- 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1648 EEAIKQLRKLQAQMKDFQRELEDAR---ASRDEIFATAKENEKKAKSLEADLMQL--QEDLAAAERARKQA 1713
Cdd:PRK01156 632 NNKYNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSrkALDDAKANRARLES 702
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1040-1237 |
7.07e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1040 ESMISELEVRLkkeEKSRQELEKLKRK-----LEGDASDFHEQIADLQAQIAELKMQLAkkeeELQAALARLDDEIAQKN 1114
Cdd:COG3206 181 EEQLPELRKEL---EEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELA----EAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1115 NALKKIRELEGhISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELedtldstatqQELRAKREQEVTVLKKALDEET 1194
Cdd:COG3206 254 DALPELLQSPV-IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQI----------AALRAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 92091586 1195 RSHEAQVQEMRQKHAQA---VEELTEQLEQFKRAKANLDKNKQTLE 1237
Cdd:COG3206 323 EALQAREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYE 368
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
891-1223 |
8.80e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 891 QLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMldleeqLEEEE 970
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK------NKALA 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 971 AARQKLQLEKVTAEAKIKKLEDEILVMDDQnnklsKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRL 1050
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEE-----QKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAEL 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1051 KKEEKSRqeleklKRKLEGDASDfHEQIADLQAQIAELKMQLAKKEEELQAALA-----------RLDDEIAQKNNALKK 1119
Cdd:pfam12128 750 KALETWY------KRDLASLGVD-PDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERA 822
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1120 IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQElRAKREQevtvlkkaLDEETRSHEA 1199
Cdd:pfam12128 823 ISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKE-DANSEQ--------AQGSIGERLA 893
|
330 340
....*....|....*....|....
gi 92091586 1200 QVQEMRQKHAQAVEELTEQLEQFK 1223
Cdd:pfam12128 894 QLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1497 |
9.50e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 9.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 857 QEEEMQAKEDELQKTKERQQKAENELKELEQKHSQlteeknllqeQLQAETELYAEAEEMRVRLAAKKQELEEIlhemEA 936
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGK----------NLDDEDELEQLQEELEARLESLSESVSEA----RE 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 937 RLEEEEDRGQQLQAERKKMAQQmldleeqLEEEEAARQKL-QLEKVTAEAkikkLEDEILVMDDQNNKLSKERKLLEERI 1015
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAAR-------APAWLAAQDALaRLREQSGEE----FEDSQDVTEYMQQLLERERELTVERD 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1016 sDLTTNLAEEEEKAKNL--------TKLKNKHE----SMISELEVRLKKEE---------KSRQ-----ELEKLKRKLEG 1069
Cdd:PRK04863 649 -ELAARKQALDEEIERLsqpggsedPRLNALAErfggVLLSEIYDDVSLEDapyfsalygPARHaivvpDLSDAAEQLAG 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1070 dASDFHEQIADLQAQIAELKMQLAKKEEELQAALarldDEIAQKNNALKKIREL--------EGHISDLQEDLD--SERA 1139
Cdd:PRK04863 728 -LEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVV----VKIADRQWRYSRFPEVplfgraarEKRIEQLRAEREelAERY 802
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1140 ARNKAEKQKrdLGEELEALKTELEDTL------DSTATQQELRAKREQEVTVLKkALDEETRSHEAQVQEMRQK------ 1207
Cdd:PRK04863 803 ATLSFDVQK--LQRLHQAFSRFIGSHLavafeaDPEAELRQLNRRRVELERALA-DHESQEQQQRSQLEQAKEGlsalnr 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1208 ------------HAQAVEELTEQLEQFKRAKANLDKNKQTLEKenadLAGELRVLGQAKQEVEHKKKKLEaQVQELQSKC 1275
Cdd:PRK04863 880 llprlnlladetLADRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSDPEQFEQLKQDYQ-QAQQTQRDA 954
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1276 SDGERARAELNDKVHKLQNEvESVtGMLNEAegkaiklakdvASLSSQLQdtqellqeetrqklnvsTKLRQLEEERnsl 1355
Cdd:PRK04863 955 KQQAFALTEVVQRRAHFSYE-DAA-EMLAKN-----------SDLNEKLR-----------------QRLEQAEQER--- 1001
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1356 qDQLDEEMEAKQNlerhistlniQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAydklektknRLQQE 1435
Cdd:PRK04863 1002 -TRAREQLRQAQA----------QLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEE---------RARAR 1061
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 1436 LDDLVVDLDNQRQLVSNLEKKQRKF----DQLLAEEKNISSKYADERDRAEAeAREKETKALSLAR 1497
Cdd:PRK04863 1062 RDELHARLSANRSRRNQLEKQLTFCeaemDNLTKKLRKLERDYHEMREQVVN-AKAGWCAVLRLVK 1126
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1352-1810 |
1.04e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERHISTLNI-QLSDSKKKLQDFASTVEALEEgkkrFQKEIENLTQQYEEKAAAYDKLEKTKN 1430
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLkELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1431 RLQQELDdLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKyADERDRAEAEAREKETKALSLARaleealeakeele 1510
Cdd:COG4717 120 KLEKLLQ-LLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAELAELQEELEELLE------------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1511 RTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAK---------------LRLEVN 1575
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEErlkearlllliaaalLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1576 MQALKGQFER----------------DLQARDEQNEEKRRQLQRQLHEYE----TELEDERKQRALAAAAKKKLEGDLKD 1635
Cdd:COG4717 265 GGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEeleeEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1636 LELQADSAIKGREEAIKQLRkLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQAdl 1715
Cdd:COG4717 345 RIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL-- 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1716 ekeelaeelasslsgrnALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERstaqknesARQ 1795
Cdd:COG4717 422 -----------------LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE--------LLQ 476
|
490
....*....|....*
gi 92091586 1796 QLERQNKELRSKLHE 1810
Cdd:COG4717 477 ELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1198-1434 |
1.07e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1198 EAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKEN--ADLAGELRVLGQAKQEvehkkkkLEAQVQELQSKc 1275
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSE-------LESQLAEARAE- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1276 sdgeraRAELNDKVHKLQNEVESVTGMLNEAEGKAIklakdVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSL 1355
Cdd:COG3206 235 ------LAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1356 QDQLDEEmeakqnLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRF---QKEIENLTQQYEEKAAAYDKLEktkNRL 1432
Cdd:COG3206 304 RAQLQQE------AQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLL---QRL 374
|
..
gi 92091586 1433 QQ 1434
Cdd:COG3206 375 EE 376
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
989-1295 |
1.08e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 53.15 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 989 KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLE 1068
Cdd:pfam19220 66 KLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1069 GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEG-------HISDLQEDLDSERAAR 1141
Cdd:pfam19220 146 EEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETqldatraRLRALEGQLAAEQAER 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1142 NKAEKQkrdLGEELEALKTEL-----------------EDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEM 1204
Cdd:pfam19220 226 ERAEAQ---LEEAVEAHRAERaslrmklealtaraaatEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1205 RQKHAQaveeLTEQLEQFKRAKANLDKNKQTLEKEnadLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAE 1284
Cdd:pfam19220 303 EADLER----RTQQFQEMQRARAELEERAEMLTKA---LAAKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRR 375
|
330
....*....|.
gi 92091586 1285 LNDkvhKLQNE 1295
Cdd:pfam19220 376 LKE---ELQRE 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-1038 |
1.40e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAE----TELYAEAEEMRVRLAAKKQELEE---- 929
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAEllra 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 930 -------------------------------ILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQL 978
Cdd:COG4942 113 lyrlgrqpplalllspedfldavrrlqylkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 979 EKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNK 1038
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1011-1930 |
1.54e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 53.68 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1011 LEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQElEKLKRKLEGD-------ASDFHEQIADLQA 1083
Cdd:PTZ00440 510 IKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKNDiknkikyIEENVDHIKDIIS 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1084 QIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIREL--EGHISDLQEDLDS-------------ERAARNKAEKQK 1148
Cdd:PTZ00440 589 LNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYIlnKFYKGDLQELLDElshflddhkylyhEAKSKEDLQTLL 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1149 RDLGEELEALKTELEDTLDSTAtqQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKAN 1228
Cdd:PTZ00440 669 NTSKNEYEKLEFMKSDNIDNII--KNLKKELQNLLSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEK 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1229 LDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKcsdgeraRAELNDKVHKLQNEVESVTGMLNEAEG 1308
Cdd:PTZ00440 747 LEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNK-------ENKISNDINILKENKKNNQDLLNSYNI 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1309 KAIKLAKDVASLSSQLQDTQELLQEEtrqklNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIqLSDSKKKLQ 1388
Cdd:PTZ00440 820 LIQKLEAHTEKNDEELKQLLQKFPTE-----DENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIKT-LNIAINRSN 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1389 DFASTVEALEEGKKRFQKEIENLTQQYE--------EKAAAYDKLEKTKNRLQQELDDLVVDldnqrQLVSNLEKKQRKF 1460
Cdd:PTZ00440 894 SNKQLVEHLLNNKIDLKNKLEQHMKIINtdniiqknEKLNLLNNLNKEKEKIEKQLSDTKIN-----NLKMQIEKTLEYY 968
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1461 DQLlaeEKNISSKyaDERDRAEAEAREKETKALSlARALEEALEAKEELERTNKMLKAEMEDLV--SSKDDVGKNvHELE 1538
Cdd:PTZ00440 969 DKS---KENINGN--DGTHLEKLDKEKDEWEHFK-SEIDKLNVNYNILNKKIDDLIKKQHDDIIelIDKLIKEKG-KEIE 1041
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1539 KSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQ 1618
Cdd:PTZ00440 1042 EKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVE-ALLKKIDENKNKLIEIKNKSHEHVVNADKEKNK 1120
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1619 ralAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMkdfQRELEDARASRDEIFATAKENEKKAKSLEADLMQ 1698
Cdd:PTZ00440 1121 ---QTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVN---EIEIEYERILIDHIVEQINNEAKKSKTIMEEIES 1194
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1699 LQEDLaaaerarKQADLEKEELAEELASSLSgRNALQDEKRRLEARIAQLEEELEEEQGNMEAmSDRVRKATQQAEQLSN 1778
Cdd:PTZ00440 1195 YKKDI-------DQVKKNMSKERNDHLTTFE-YNAYYDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQVFS 1265
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1779 ELATERSTAQKNESARQQLERQNKELRS---------------KLHEMEGAVKSKFKST---IAALEAKIAQLEE----- 1835
Cdd:PTZ00440 1266 YLQQVIKENNKMENALHEIKNMYEFLISidsekilkeilnstkKAEEFSNDAKKELEKTdnlIKQVEAKIEQAKEhknki 1345
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1836 -------QVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQleEAEEESQRINANRR 1908
Cdd:PTZ00440 1346 ygsledkQIDDEIKKIEQIKEEISNKRKEINKYLSNIKSNKEKCDLHVRNASRGKDKIDFLNKH--EAIEPSNSKEVNII 1423
|
970 980
....*....|....*....|...
gi 92091586 1909 KLQRELDEATE-SNEAMGREVNA 1930
Cdd:PTZ00440 1424 KITDNINKCKQySNEAMETENKA 1446
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1180-1488 |
1.86e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.92 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1180 EQEVTVLKKALDEETRSHE---AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLE---------KENADLAGEL 1247
Cdd:PRK04778 118 EEDIEQILEELQELLESEEknrEEVEQLKDLYRELRKSLLANRFSFGPALDELEKQLENLEeefsqfvelTESGDYVEAR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1248 RVLGQAKQEVEHKKKKLEaQVQELQSKCSDgeraraELNDKVHKLQNEVESVTgmlneAEG---KAIKLAKDVASLSSQL 1324
Cdd:PRK04778 198 EILDQLEEELAALEQIME-EIPELLKELQT------ELPDQLQELKAGYRELV-----EEGyhlDHLDIEKEIQDLKEQI 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1325 QDTQELLqEETRQKlNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLsdskkklqdfastvEALEEGKKRF 1404
Cdd:PRK04778 266 DENLALL-EELDLD-EAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFL--------------EHAKEQNKEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1405 QKEIENLTQQY---EEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQ----LVSNLEKKQRKFDQLLAEEKNISSKYADE 1477
Cdd:PRK04778 330 KEEIDRVKQSYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIayseLQEELEEILKQLEEIEKEQEKLSEMLQGL 409
|
330
....*....|.
gi 92091586 1478 RDrAEAEAREK 1488
Cdd:PRK04778 410 RK-DELEAREK 419
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
1118-1488 |
1.94e-06 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443574 [Multi-domain] Cd Length: 567 Bit Score: 52.92 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1118 KKIRELEGHISDLQEDLDSERAarNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSH 1197
Cdd:COG4477 78 KQLPEIEELLFDAEEAADKFRF--KKAKKALDEIEQLLDEIEEEIEEILEELEELLESEEKNREEIEELKEKYRELRKTL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1198 EAQvqemRQKHAQAVEELTEQLEQFKrakANLDKNKQTLEKENADLAGElrVLGQAKQEVEHKKKKLEaQVQELQSKCSD 1277
Cdd:COG4477 156 LAH----RHSFGPAAEELEKQLEELE---PEFEEFEELTESGDYLEARE--ILEQLEEELNALEELME-EIPPLLKELQT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1278 geraraELNDKVHKLQNEVESVtgmlnEAEG---KAIKLAKDVASLSSQLQDTQELLqEETRQKlNVSTKLRQLEEERNS 1354
Cdd:COG4477 226 ------ELPDQLEELKSGYREM-----KEQGyvlEHLNIEKEIEQLEEQLKEALELL-EELDLD-EAEEELEEIEEEIDE 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1355 LQDQLDEEMEAKQNLERHISTLniqlsdskkklqdfASTVEALEEGKKRFQKEIENLTQQY---EEKAAAYDKLEKTKNR 1431
Cdd:COG4477 293 LYDLLEKEVEAKKYVDKNQEEL--------------EEYLEHLKEQNRELKEEIDRVQQSYrlnENELEKVRNLEKQIEE 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1432 LQQELDDLVVDLDNQR----QLVSNLEKKQRKFDQLLAEEKNISSKYADERDRaEAEAREK 1488
Cdd:COG4477 359 LEKRYDEIDERIEEEKvaysELQEELEEIEEQLEEIEEEQEEFSEKLKSLRKD-ELEAREK 418
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1108-1473 |
1.97e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.99 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1108 DEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKrdlgEELEALKTELEDtldstATQQELRAKReqEVTVLK 1187
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQK----EETEQLKQQLAQ-----APAKLRQAQA--ELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1188 KALDEETRSH---------EAQVQEMRQKHAQAVEELTE-------QLEQFKRAKANLDKNKQTLEKENADLAG------ 1245
Cdd:PRK11281 108 DDNDEETRETlstlslrqlESRLAQTLDQLQNAQNDLAEynsqlvsLQTQPERAQAALYANSQRLQQIRNLLKGgkvggk 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1246 ----ELRVLGQAKQ-----EVEHKKKKLEA--QVQELqskcsdGERARAELNDKVHKLQNEVESVTGMLNEaegKAIKLA 1314
Cdd:PRK11281 188 alrpSQRVLLQAEQallnaQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAINS---KRLTLS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1315 KDVASLSSQLQDTQE-----LLQEETRQKLNVSTKLRQLEEERNSL-QD------QLDEEMEAKQNLERHISTLNIQLSD 1382
Cdd:PRK11281 259 EKTVQEAQSQDEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLtQQnlrvknWLDRLTQSERNIKEQISVLKGSLLL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1383 SK------------KKLQDFAST-----VEALEEGKKR---FQKE--IENLTQQYEEKA-----AAYDKLEKTKNRLqqe 1435
Cdd:PRK11281 339 SRilyqqqqalpsaDLIEGLADRiadlrLEQFEINQQRdalFQPDayIDKLEAGHKSEVtdevrDALLQLLDERREL--- 415
|
410 420 430
....*....|....*....|....*....|....*...
gi 92091586 1436 LDDLVVDLDNQRQLVSNLEKKQRkfdQLLAEEKNISSK 1473
Cdd:PRK11281 416 LDQLNKQLNNQLNLAINLQLNQQ---QLLSVSDSLQST 450
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
972-1184 |
1.98e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 972 ARQKLQlekvTAEAKIK--KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISEL--E 1047
Cdd:COG3206 187 LRKELE----EAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1048 VRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAkkeEELQAALARLDDEIAQknnALKKIRELEGHI 1127
Cdd:COG3206 263 PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---QEAQRILASLEAELEA---LQAREASLQAQL 336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1128 SDLQEDLDSEraarNKAEKQKRDLGEELEALKTELEDTLdstATQQELRAKREQEVT 1184
Cdd:COG3206 337 AQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVG 386
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1545-1787 |
2.01e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.14 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1545 ETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAA 1624
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1625 AKKKLEGDLKDLE--LQADSAikgrEEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQED 1702
Cdd:COG3883 94 ALYRSGGSVSYLDvlLGSESF----SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1703 LAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELAT 1782
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
....*
gi 92091586 1783 ERSTA 1787
Cdd:COG3883 250 GAAGA 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1304-1903 |
2.14e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.82 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1304 NEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDS 1383
Cdd:pfam05557 16 NEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1384 KKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKaaaydklEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQrkfdql 1463
Cdd:pfam05557 96 ESQLADAREVISCLKNELSELRRQIQRAELELQST-------NSELEELQERLDLLKAKASEAEQLRQNLEKQQ------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1464 laeeknisskyadeRDRAEAEAREKEtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1543
Cdd:pfam05557 163 --------------SSLAEAEQRIKE---LEFEIQSQEQDSEIVKNSKSELARIPELEKELERLREHNKHLNENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1544 LETQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKGQFE---------RDLQARDEQNEEKRRQLQRQLHEYETE 1611
Cdd:pfam05557 226 LKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1612 LEDERKQRALAAAAKKKLEGDLKDLElqadsaiKGREEAIKQLRKLQAQMKDFQRELEDARA---SRDEIFATAKENEKK 1688
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLN-------KKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1689 AKSLE--ADLMQLQEDLAAAERARKQADLEKEELAEELASSLsgrnalqdekrrleariaqleeeleeeqgnmEAMSDRV 1766
Cdd:pfam05557 379 LERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-------------------------------ERELQAL 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1767 RKATQQAEQLS--NELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTiaaleaKIAQLEEQVEQEAREK 1844
Cdd:pfam05557 428 RQQESLADPSYskEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKT------KVLHLSMNPAAEAYQQ 501
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1845 QAA-TKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNAR-VKQLKRQLEEAEEESQRI 1903
Cdd:pfam05557 502 RKNqLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKeVLDLRKELESAELKNQRL 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1328-1543 |
2.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1328 QELLQEETRQKLN-VSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQK 1406
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1407 EIENLTQQYEEKAAAYDKLEKTKNRL----QQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAE 1482
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1483 AEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRA 1543
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1023-1619 |
2.53e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1023 AEEEEKAKNLTKLKNKHESMISELEVRLK----KEEKSRQELEKLKRK-----LEGDASDFHEQIADLQAQIAELKMQLA 1093
Cdd:pfam10174 123 SEHERQAKELFLLRKTLEEMELRIETQKQtlgaRDESIKKLLEMLQSKglpkkSGEEDWERTRRIAEAEMQLGHLEVLLD 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1094 KKEEELQAalarLDDEIAQKNNALKKIREleghISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtLDSTATQQ 1173
Cdd:pfam10174 203 QKEKENIH----LREELHRRNQLQPDPAK----TKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL--LHTEDREE 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1174 ELRAKreqevtvlkkaldEETRSHEaqvQEMRQKHAQAVEELTEQLEQFKRAKANLDknkqTLEKENADlagelrvlgqA 1253
Cdd:pfam10174 273 EIKQM-------------EVYKSHS---KFMKNKIDQLKQELSKKESELLALQTKLE----TLTNQNSD----------C 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1254 KQEVEHKKKKLEAQVQelqskcsdgeRArAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQE 1333
Cdd:pfam10174 323 KQHIEVLKESLTAKEQ----------RA-AILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1334 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKR----FQKEIE 1409
Cdd:pfam10174 392 KERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRERedreRLEELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1410 NLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-----------RQLVSNLEKKQRKFDQLLAEEKNISSKYADER 1478
Cdd:pfam10174 472 SLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklKSLEIAVEQKKEECSKLENQLKKAHNAEEAVR 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1479 DRAEAEAREKETKAlSLARALEEALEAKEELERTNKMLKaEMEDLVSSKDdvgKNVHELE------------KSKRALET 1546
Cdd:pfam10174 552 TNPEINDRIRLLEQ-EVARYKEESGKAQAEVERLLGILR-EVENEKNDKD---KKIAELEsltlrqmkeqnkKVANIKHG 626
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1547 QMEEMKTQLEELEDELQATEDAKLR-LEVNMQALKGQFERDLQARDEqNEEKRRQLQRQLHEYETELEDERKQR 1619
Cdd:pfam10174 627 QQEMKKKGAQLLEEARRREDNLADNsQQLQLEELMGALEKTRQELDA-TKARLSSTQQSLAEKDGHLTNLRAER 699
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1046-1413 |
2.55e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1046 LEVRLKKEEKSRQEL----EKLKRKLEGDASD-------FHEQIADLQAQIAELKMQLAKKEEEL------QAALARLDD 1108
Cdd:pfam07888 32 LQNRLEECLQERAELlqaqEAANRQREKEKERykrdreqWERQRRELESRVAELKEELRQSREKHeeleekYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1109 EIAQKNNAL--------KKIRELEGHISDLQE-------DLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqq 1173
Cdd:pfam07888 112 ELSEEKDALlaqraaheARIRELEEDIKTLTQrvleretELERMKERAKKAGAQRKEEEAERKQLQAKLQQT-------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1174 elrakreqevtvlkkalDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTlEKENADLAGELRVLgqa 1253
Cdd:pfam07888 184 -----------------EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRK-EAENEALLEELRSL--- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1254 KQEVEHKKKKLEAQVQELQSKCSDGERARAELndkvHKLQNEVESVTGMLNEAegkAIKLAKDVASLSSQLQDTQELLQE 1333
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQRDRTQAEL----HQARLQAAQLTLQLADA---SLALREGRARWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1334 ETRQKLNVSTKLRQLEEernSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQ 1413
Cdd:pfam07888 316 DKDRIEKLSAELQRLEE---RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
853-1219 |
2.57e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAetelyAEAEEmrvRLAAKKQELEEILh 932
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV-----ASAER---EIAELEAELERLD- 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 emearleEEEDRGQQLQAERKKmaqqmldleeqleeEEAARQKLQLEKVTAEAKIKKLEDEIlvmDDQNNKLSKERKLLE 1012
Cdd:COG4913 682 -------ASSDDLAALEEQLEE--------------LEAELEELEEELDELKGEIGRLEKEL---EQAEEELDELQDRLE 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELE-KLKRKLEGDASDFHEQIADLQAQIAELkmq 1091
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEeELERAMRAFNREWPAETADLDADLESL--- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 lakkeEELQAALARLDDE--IAQKNNALKKIRELEGH-ISDLQEDLDSERAArnkAEKQKRDLGEELEALKTELEDTLds 1168
Cdd:COG4913 815 -----PEYLALLDRLEEDglPEYEERFKELLNENSIEfVADLLSKLRRAIRE---IKERIDPLNDSLKRIPFGPGRYL-- 884
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1169 tatQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQL 1219
Cdd:COG4913 885 ---RLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1733-1942 |
2.80e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1733 ALQDEKRRLEAriaqleeeleeeqgnmEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEME 1812
Cdd:COG1196 217 ELKEELKELEA----------------ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1813 GAvkskfkstIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQ 1892
Cdd:COG1196 281 LE--------LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 92091586 1893 LEEAEeeSQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNETS 1942
Cdd:COG1196 353 LEEAE--AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
874-1370 |
3.19e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.50 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 874 RQQKAENELKELEQKHSQLTEEKNLLQEQLQA----ETELYAEAEEMRVRLAAKKQELEEIlhemeARLEEEEDRGQQLQ 949
Cdd:PRK10246 420 EQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNvtqeQTQRNAALNEMRQRYKEKTQQLADV-----KTICEQEARIKDLE 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 950 AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmddqnNKLSKERKLLEERISDLTTNLAEEEEKA 1029
Cdd:PRK10246 495 AQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALEKEV-------KKLGEEGAALRGQLDALTKQLQRDESEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1030 KNLTK----LKNKHESMISELEVR----------LKKEEKSRQELEKLKRKLEGDAsdfheQIADLQAQIAELKMQLAKK 1095
Cdd:PRK10246 568 QSLRQeeqaLTQQWQAVCASLNITlqpqddiqpwLDAQEEHERQLRLLSQRHELQG-----QIAAHNQQIIQYQQQIEQR 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1096 EEELQAALARLDDEIAQKNNalkkireleghisdlQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1175
Cdd:PRK10246 643 QQQLLTALAGYALTLPQEDE---------------EASWLATRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDL 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1176 RAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANldknkqtleKENADLAGELRVL--GQA 1253
Cdd:PRK10246 708 PHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQA---------SVFDDQQAFLAALldEET 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1254 KQEVEHKKKKLEAQVQELQSKCSDGERARAElndkvHKLQNEvesvtgmlneaegKAIKLAKDVASLSSQLQDTQELLQE 1333
Cdd:PRK10246 779 LTQLEQLKQNLENQRQQAQTLVTQTAQALAQ-----HQQHRP-------------DGLDLTVTVEQIQQELAQLAQQLRE 840
|
490 500 510
....*....|....*....|....*....|....*..
gi 92091586 1334 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLE 1370
Cdd:PRK10246 841 NTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1103-1274 |
4.61e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1103 LARLDDEIAQKNnalKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTldstatqQELRAKREQE 1182
Cdd:COG1579 12 LQELDSELDRLE---HRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-------EARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1183 VTVLKKALDEETRSHEAQVQEMRQKHAQavEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKK 1262
Cdd:COG1579 82 LGNVRNNKEYEALQKEIESLKRRISDLE--DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|..
gi 92091586 1263 KLEAQVQELQSK 1274
Cdd:COG1579 160 ELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
946-1124 |
4.80e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 946 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEIlvmDDQNNKLSKERKLLEERISDL------- 1018
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGERARALyrsggsv 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1019 --------TTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKM 1090
Cdd:COG3883 103 syldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190
....*....|....*....|....*....|....
gi 92091586 1091 QLAKKEEELQAALARLDDEIAQKNNALKKIRELE 1124
Cdd:COG3883 183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1380-1912 |
4.85e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1380 LSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRK 1459
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1460 FDQLLAEEKNISSKYADERDRA------EAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1533
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNnyykelEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1534 VHELEKSKraleTQMEEMKTQLEELE---DELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQlheyET 1610
Cdd:PRK01156 331 LSVLQKDY----NDYIKKKSRYDDLNnqiLELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQ----EI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1611 ELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKdfqRELEDARASRDEIFATAKENEKKAK 1690
Cdd:PRK01156 403 DPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSV---CPVCGTTLGEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1691 SLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKA- 1769
Cdd:PRK01156 480 RLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLk 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1770 ----TQQAEQLSNELATERST-AQKNESARQQLERQNKELRSKLHEMEGA---VKSKFKSTIAALEAKIAQLEEQVeQEA 1841
Cdd:PRK01156 560 ledlDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGfpdDKSYIDKSIREIENEANNLNNKY-NEI 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1842 REKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEA------------------EEESQRI 1903
Cdd:PRK01156 639 QENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAkanrarlestieilrtriNELSDRI 718
|
....*....
gi 92091586 1904 NANRRKLQR 1912
Cdd:PRK01156 719 NDINETLES 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1040-1256 |
5.06e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1040 ESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKK 1119
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1120 IRELEGHISDLQEDLDSE----------------RAARNKAEKQKRDLgEELEALKTELEDTLDSTATQQELRAKREQEV 1183
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSEsfsdfldrlsalskiaDADADLLEELKADK-AELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1184 TVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQE 1256
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1006-1466 |
5.65e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 5.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1006 KERKLLEERISDLTTNLAEEEEKAKNLT-------KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQI 1078
Cdd:pfam05557 27 RARIELEKKASALKRQLDRESDRNQELQkrirlleKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1079 ADLQAQIAELKMQLAKKEEELQAALARLDD-------------EIAQKNNALK-----------KIRELEGHI------S 1128
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEElqerldllkakasEAEQLRQNLEkqqsslaeaeqRIKELEFEIqsqeqdS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1129 DLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETR-SHEAQVQEMRQK 1207
Cdd:pfam05557 187 EIVKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEkEKLEQELQSWVK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1208 HAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELND 1287
Cdd:pfam05557 267 LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQR 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1288 KVHKLQNEVESVTGMLnEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQ---LDEEME 1364
Cdd:pfam05557 347 RVLLLTKERDGYRAIL-ESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQaqtLERELQ 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1365 AK--QNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ---------------------YEEKAAA 1421
Cdd:pfam05557 426 ALrqQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQgdydpkktkvlhlsmnpaaeaYQQRKNQ 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 92091586 1422 YDKLEKTKNRLQQELDDLVVDLDNQRQL-VSNLEKKQRKFDQLLAE 1466
Cdd:pfam05557 506 LEKLQAEIERLKRLLKKLEDDLEQVLRLpETTSTMNFKEVLDLRKE 551
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
854-1305 |
5.73e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 854 VTRQEEEMQAKEDELQKTKE----RQQKAENELKELEQKHSQLTEEKNLLQEQlqaETELYAEAEEMRVRLAAKKQELEE 929
Cdd:PRK02224 312 VEARREELEDRDEELRDRLEecrvAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 930 IlhemearleeeedrgqqlqaerkkmaqqmldlEEQLEEEEAA--------------RQKLQLEKVTAEAKIKKLEDEIL 995
Cdd:PRK02224 389 L--------------------------------EEEIEELRERfgdapvdlgnaedfLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 996 VMDdqnNKLSKERKLLE------------------------ERISDLTTNLAEEEEKaknLTKLKNKHESM--ISELEVR 1049
Cdd:PRK02224 437 TAR---ERVEEAEALLEagkcpecgqpvegsphvetieedrERVEELEAELEDLEEE---VEEVEERLERAedLVEAEDR 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1050 LKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDeiaqknnALKKIRELEGHISD 1129
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE-------AREEVAELNSKLAE 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1130 LQEDLDSERAARNKAEKQKrDLGEELEALKTELEDtldsTATQQELRAKREQEVTVLKKALDEETrsHEAQVQEMRQKHA 1209
Cdd:PRK02224 584 LKERIESLERIRTLLAAIA-DAEDEIERLREKREA----LAELNDERRERLAEKRERKRELEAEF--DEARIEEAREDKE 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1210 QAV---EELTEQLEQFKRAKANLDKNKQTLEKENAdlagELRVLGQAKQEVEHKKKKLEA---QVQELQSKCSDgerARA 1283
Cdd:PRK02224 657 RAEeylEQVEEKLDELREERDDLQAEIGAVENELE----ELEELRERREALENRVEALEAlydEAEELESMYGD---LRA 729
|
490 500
....*....|....*....|..
gi 92091586 1284 ELNdkvhklQNEVESVTGMLNE 1305
Cdd:PRK02224 730 ELR------QRNVETLERMLNE 745
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
856-1494 |
6.19e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 51.29 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 856 RQEEEMQAKEDELQKTKERQQKAENELKELeQKHSQLTEEKNLLQE-QLQAETELYAEAEEMRVRLAAKKQELEEILHEM 934
Cdd:pfam07111 43 GQGPGRRGRSLELEGSQALSQQAELISRQL-QELRRLEEEVRLLREtSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 935 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKlQLEKVTAEAKikKLEDEILVMDDQNNKLSKERKLLEER 1014
Cdd:pfam07111 122 AALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQAHEE-ALSSLTSKAE--GLEKSLNSLETKRAGEAKQLAEAQKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1015 ISDLTTNLAEEEEKAKNLTKLKNKHESMISEL---EVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ 1091
Cdd:pfam07111 199 AELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1092 LAKKEEELQAALARLDdeiAQKNNALKKIRELeghISDLQEDLDSERAARNKAEKQKRDLGEELEalkteledtlDSTAT 1171
Cdd:pfam07111 279 LALQEEELTRKIQPSD---SLEPEFPKKCRSL---LNRWREKVFALMVQLKAQDLEHRDSVKQLR----------GQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1172 QQELRAKREQEVTVLKKALDEETRshEAQVQEMRQKHAQAveelteqleQFKRAKANLDKNKQTLEKENADLAGELRVLG 1251
Cdd:pfam07111 343 LQEQVTSQSQEQAILQRALQDKAA--EVEVERMSAKGLQM---------ELSRAQEARRRQQQQTASAEEQLKFVVNAMS 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1252 QAKQEVEHKKKKLEAQVQELQSkcsdgeraraeLNDKVHKLQNEVESVTGMlneaegkaikLAKDVAsLSSQLQDTQELL 1331
Cdd:pfam07111 412 STQIWLETTMTRVEQAVARIPS-----------LSNRLSYAVRKVHTIKGL----------MARKVA-LAQLRQESCPPP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1332 QEETRQKLNVSTKLRQLEEERNSLQDQLD--------------EEMEA-KQNLERHISTLNIQLSDSKKKLQDFASTVEA 1396
Cdd:pfam07111 470 PPAPPVDADLSLELEQLREERNRLDAELQlsahliqqevgrarEQGEAeRQQLSEVAQQLEQELQRAQESLASVGQQLEV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1397 LEEGKKRFQKEIENLTQQYEEKAAAY-----DKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIS 1471
Cdd:pfam07111 550 ARQGQQESTEEAASLRQELTQQQEIYgqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERN 629
|
650 660
....*....|....*....|...
gi 92091586 1472 SkyadERDRAEAEAREKETKALS 1494
Cdd:pfam07111 630 Q----ELRRLQDEARKEEGQRLA 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1457-1919 |
6.24e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1457 QRKFDQLLAEEKNISskyADERDRAEAEAREKETKALSLARALEEALEAKEELERTNkmLKAEMEDLVSSKDDVGKNVHE 1536
Cdd:TIGR00606 172 KQKFDEIFSATRYIK---ALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1537 LEKSKRALEtQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYE------- 1609
Cdd:TIGR00606 247 LDPLKNRLK-EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKErelvdcq 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1610 TELEDERKQRALAAAAKKKLEGDLKDLELQAD---SAIKGREEAIKQLrKLQAQMKDFQRELEDARASRDEIFATAKENE 1686
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARDSLIQSL-ATRLELDGFERGPFSERQIKNFHTLVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1687 KKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEelasslsgrnALQDEKRRLEARIAQLEEELEEEQgNMEAMSDRV 1766
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGR----------TIELKKEILEKKQEELKFVIKELQ-QLEGSSDRI 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1767 RKATQQAEQLSNELaterSTAQKNESARQQLERQnKELRSKlhemegavKSKFKSTIAALEAKIAQLE------EQVEQE 1840
Cdd:TIGR00606 474 LELDQELRKAEREL----SKAEKNSLTETLKKEV-KSLQNE--------KADLDRKLRKLDQEMEQLNhhtttrTQMEML 540
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1841 AREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATE 1919
Cdd:TIGR00606 541 TKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1191-1421 |
6.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1191 DEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAgelrvlgQAKQEVEHKKKKLEAQVQE 1270
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-------KLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1271 LqskcsdGERARAelndkvhklQNEVESVTGMLNeaegkAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEE 1350
Cdd:COG3883 88 L------GERARA---------LYRSGGSVSYLD-----VLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1351 ERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1421
Cdd:COG3883 148 KKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1457-1874 |
8.40e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 50.66 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1457 QRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHE 1536
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1537 LEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQnEEKRRQLQRQLHEYETELEDER 1616
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEE-EAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1617 KQRALaaaakkklegdLKDLELQADSAIKGREEAIKQLRKL--QAQMKDFQRE--LEDARASRDEIFATakenEKKAKSL 1692
Cdd:pfam07888 192 KEFQE-----------LRNSLAQRDTQVLQLQDTITTLTQKltTAHRKEAENEalLEELRSLQERLNAS----ERKVEGL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1693 EADL--MQLQEDLAAAE--RARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRK 1768
Cdd:pfam07888 257 GEELssMAAQRDRTQAElhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1769 ATQQAEQLSNELATERSTaqkNESARQQLERQNKELRSKLHEMEGAvKSKFKSTIAALEAKIAQLEEQVEQEAREKQAAT 1848
Cdd:pfam07888 337 ERMEREKLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAKWSEA 412
|
410 420
....*....|....*....|....*.
gi 92091586 1849 KSLkqKDKKLKEILLQVEDERKMAEQ 1874
Cdd:pfam07888 413 ALT--STERPDSPLSDSEDENPEALQ 436
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1032-1414 |
9.32e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1032 LTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1111
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1112 QKNNALKKIRELEGHISDLQEDLDSeraarnkaekqkrdLGEELEALKTELEDtldstaTQQELRAKReQEVTVLKKALD 1191
Cdd:pfam05557 84 YLEALNKKLNEKESQLADAREVISC--------------LKNELSELRRQIQR------AELELQSTN-SELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1192 EEtrsheaqvqemrQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEH--KKKKLEAQVQ 1269
Cdd:pfam05557 143 LL------------KAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1270 ELQSKCSDGERARAELNDKVHKLQNEVESVTGMlneaEGKAIKLAKDVASLSSQLQDTQELLQE---ETRQKLNVSTKLR 1346
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEVEDLKRKLEREEKY----REEAATLELEKEKLEQELQSWVKLAQDtglNLRSPEDLSRRIE 286
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1347 QLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:pfam05557 287 QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
859-1062 |
1.06e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 859 EEMQAKEDELQKT-KERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAE-EMRVRLAAKKQELEEILHE--M 934
Cdd:PRK00409 519 NELIASLEELERElEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIKElrQ 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 935 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLqleKVTAEAKIKKLED--EILVMDDQNN--------KL 1004
Cdd:PRK00409 596 LQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL---KVGDEVKYLSLGQkgEVLSIPDDKEaivqagimKM 672
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1005 SKERKLLEerisdLTTNLAEEEEKAKNLTKLKNKHESMisELEVRLKKEEKSRQELEK 1062
Cdd:PRK00409 673 KVPLSDLE-----KIQKPKKKKKKKPKTVKPKPRTVSL--ELDLRGMRYEEALERLDK 723
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1258-1485 |
1.08e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1258 EHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQ 1337
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1338 KLNVSTKLRQLEE--ERNSLQDQLDEemeakqnlerhISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQY 1415
Cdd:COG3883 95 LYRSGGSVSYLDVllGSESFSDFLDR-----------LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1416 EEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEA 1485
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQL------SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1306-1489 |
1.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1306 AEGKAIKLAKDVASLSSQLQDTQELLQeetrqklNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKK 1385
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD-------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1386 KLQDFA----------STVEALEEGK--KRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNL 1453
Cdd:COG3883 87 ELGERAralyrsggsvSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 92091586 1454 EKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKE 1489
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1385-1798 |
1.33e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 50.12 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1385 KKLQDFASTVEALEEGKKRFQKE--IENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnQRQLVSNLEKKQRKFDq 1462
Cdd:pfam17380 221 KEVQGMPHTLAPYEKMERRKESFnlAEDVTTMTPEYTVRYNGQTMTENEFLNQLLHIV-----QHQKAVSERQQQEKFE- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1463 llaeeknissKYADERDRAEAEAREKEtkaLSLARALEEALEAKEELERTNKMLKAEMEDLVsskddvgknvheLEKSKR 1542
Cdd:pfam17380 295 ----------KMEQERLRQEKEEKARE---VERRRKLEEAEKARQAEMDRQAAIYAEQERMA------------MERERE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1543 ALETQMEEMKTQLEELEDELQATEDAKLRlevnmqalkgQFERdLQARDEQNEEKRRQlqrqlheyetELEDERKQRALA 1622
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMR----------ELER-LQMERQQKNERVRQ----------ELEAARKVKILE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1623 AAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFaTAKENEKKAKSLEADLMQLQED 1702
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERL-RQQEEERKRKKLELEKEKRDRK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1703 LAAAER---------ARKQADLEKEELAEELASSLSGR-NALQDEKRRleaRIAQLEEELEEEQGNMEAMSDRVRKATQQ 1772
Cdd:pfam17380 488 RAEEQRrkilekeleERKQAMIEEERKRKLLEKEMEERqKAIYEEERR---REAEEERRKQQEMEERRRIQEQMRKATEE 564
|
410 420
....*....|....*....|....*....
gi 92091586 1773 AEQLsNELATERSTAQK---NESARQQLE 1798
Cdd:pfam17380 565 RSRL-EAMEREREMMRQiveSEKARAEYE 592
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1280 |
1.37e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.61 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 856 RQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQL-QAETELYAEAEEMRVRLAAKKQELEeilheM 934
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLD-----K 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 935 EARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEdeilvmdDQNNKLSKERKLLEER 1014
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE-------TWYKRDLASLGVDPDV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1015 ISDLTTNLAEEEEKAKNLTklKNKHESmiseLEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAK 1094
Cdd:pfam12128 770 IAKLKREIRTLERKIERIA--VRRQEV----LRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAK 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1095 KEEELQAalarLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAA-------------RNKAEKQKRDLGEELEALKTE 1161
Cdd:pfam12128 844 LEMERKA----SEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQgsigerlaqledlKLKRDYLSESVKKYVEHFKNV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1162 LEDTLDSTATQQELRAkREQEVTVLKKALDEETRSHEAQV----------------QEMRQKHAQAVEELTEQLEQFKRA 1225
Cdd:pfam12128 920 IADHSGSGLAETWESL-REEDHYQNDKGIRLLDYRKLVPYleqwfdvrvpqsimvlREQVSILGVDLTEFYDVLADFDRR 998
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1226 KANLDKNKQTLEKENADLAG--ELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGER 1280
Cdd:pfam12128 999 IASFSRELQREVGEEAFFEGvsESAVRIRSKVSELEYWPELRVFVKAFRLWKSDGFG 1055
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1112-1338 |
1.44e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1112 QKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEdtldstATQQELrAKREQEVTVLKKALD 1191
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID------KLQAEI-AEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1192 EETRSheAQVQEMRQKHAQAV---EELTEQLEQFKRAKANLDKNKQTLEKenadlagelrvLGQAKQEVEHKKKKLEAQV 1268
Cdd:COG3883 90 ERARA--LYRSGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLEE-----------LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1269 QELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1338
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
851-1450 |
1.60e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 50.18 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 851 LLQVTRQEE---EMQAKEDELQKTKERQQKAENELKELE--QKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQ 925
Cdd:PRK10246 246 LNWLTRLDElqqEASRRQQALQQALAAEEKAQPQLAALSlaQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 926 ELEEILHEMEARLeeeedrgQQLQAERKKMAQQMldleeqleeeeaarqklqlekvTAEAKIKKLEDEILVMDDQNNKLS 1005
Cdd:PRK10246 326 LRARIRHHAAKQS-------AELQAQQQSLNTWL----------------------AEHDRFRQWNNELAGWRAQFSQQT 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1006 KERklleERISDLTTNLAEEEEKAKNLTKLKnkheSMISELEVRLKKEEKSRQeleklkRKLEGDASDFHEQIADLQAQI 1085
Cdd:PRK10246 377 SDR----EQLRQWQQQLTHAEQKLNALPAIT----LTLTADEVAAALAQHAEQ------RPLRQRLVALHGQIVPQQKRL 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1086 AELKMQLAKKEEELQAALARLDD------EIAQKNNALKKIRELEGHISDLQE--------------------------- 1132
Cdd:PRK10246 443 AQLQVAIQNVTQEQTQRNAALNEmrqrykEKTQQLADVKTICEQEARIKDLEAqraqlqagqpcplcgstshpaveayqa 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1133 -DLDSERAARNKAEKQKRDLGEELEALKTELEdtldsTATQQELRAKRE-QEVTVLKKALDEETRSHEAQVQEMRQKHaq 1210
Cdd:PRK10246 523 lEPGVNQSRLDALEKEVKKLGEEGAALRGQLD-----ALTKQLQRDESEaQSLRQEEQALTQQWQAVCASLNITLQPQ-- 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1211 avEELTEQLEQFKRAKANLDKNKQTLEKEnADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDK-- 1288
Cdd:PRK10246 596 --DDIQPWLDAQEEHERQLRLLSQRHELQ-GQIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRqq 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1289 -----------VHKLQNEVESVTGMLN--EAEGKAIKLAKDVA------------SLSSQLQDTQELLQEET------RQ 1337
Cdd:PRK10246 673 eaqswqqrqneLTALQNRIQQLTPLLEtlPQSDDLPHSEETVAldnwrqvheqclSLHSQLQTLQQQDVLEAqrlqkaQA 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1338 KLNVSTKLRQLEEERNSLQDQLDEEMEA-----KQNLERHISTLNIQLSDSKKKLQ----------DFASTVEALeegkk 1402
Cdd:PRK10246 753 QFDTALQASVFDDQQAFLAALLDEETLTqleqlKQNLENQRQQAQTLVTQTAQALAqhqqhrpdglDLTVTVEQI----- 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1403 rfQKEIENLTQQYEEKAAAYDKLEK-----TKNRLQQEldDLVVDLDNQRQLV 1450
Cdd:PRK10246 828 --QQELAQLAQQLRENTTRQGEIRQqlkqdADNRQQQQ--ALMQQIAQATQQV 876
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1076-1215 |
1.61e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 49.19 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1076 EQIADLQAQIAELKMQLA---KKEEELQAALARLDDEIAQKnnalkkirelEGHISDLQEDLDSERAARNKAEKQKRDLG 1152
Cdd:PRK09039 53 SALDRLNSQIAELADLLSlerQGNQDLQDSVANLRASLSAA----------EAERSRLQALLAELAGAGAAAEGRAGELA 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1153 EELEALKTELEDTLDSTAT-QQELRAKREQeVTVLKKALD-EETRSHEAQVQ------EMRQKHAQAVEEL 1215
Cdd:PRK09039 123 QELDSEKQVSARALAQVELlNQQIAALRRQ-LAALEAALDaSEKRDRESQAKiadlgrRLNVALAQRVQEL 192
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
858-1116 |
2.04e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAEAEEMRVRLAAKKQELEeilhemear 937
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---ALQAEIDKLQAEIAEAEAEIE--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 leeeedrgqQLQAERKKMAQQMldleeqleeeeaARQKLQLEKVTAEAKIKKLEDEIlvmdDQNNKLSKERKLLEERISD 1017
Cdd:COG3883 83 ---------ERREELGERARAL------------YRSGGSVSYLDVLLGSESFSDFL----DRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEE 1097
Cdd:COG3883 138 LKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
250
....*....|....*....
gi 92091586 1098 ELQAALARLDDEIAQKNNA 1116
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAA 236
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1379-1602 |
2.20e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1379 QLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQR 1458
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1459 K-------FDQLLAeekniSSKYADERDRAEAeareketkalsLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVG 1531
Cdd:COG3883 97 RsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1532 KNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1602
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1032-1166 |
2.31e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 49.47 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1032 LTKLKNKHESMISELEVRLKK-EEKSRQELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKE---EELQAALARLD 1107
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEhEERELTEEEEEIRRLE-------EQVERLEAEVEELEAELEEKDeriERLERELSEAR 454
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1108 DEIAQKNNALKKIRELEGHISDLQEDLDSEraaRNKAEKQKRDLGEELEALKTELEDTL 1166
Cdd:COG2433 455 SEERREIRKDREISRLDREIERLERELEEE---RERIEELKRKLERLKELWKLEHSGEL 510
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1394-1936 |
2.60e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1394 VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVS-------NLEKKQRKFDQLLAE 1466
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlkeqakkALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1467 EKNISSKY----ADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKR 1542
Cdd:pfam02463 224 EYLLYLDYlklnEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1543 ALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALA 1622
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1623 AAAKKKLEGDLKDLELQ------ADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADL 1696
Cdd:pfam02463 384 ERLSSAAKLKEEELELKseeekeAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1697 MQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQL 1776
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1777 SNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAK-------IAQLEEQVEQEAREKQAATK 1849
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVleidpilNLAQLDKATLEADEDDKRAK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1850 SLKQKDKKLKEILLQVEDERKMAEQYK-EQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREV 1928
Cdd:pfam02463 624 VVEGILKDTELTKLKESAKAKESGLRKgVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
....*...
gi 92091586 1929 NALKSKLR 1936
Cdd:pfam02463 704 KEQREKEE 711
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1602-1936 |
3.26e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1602 QRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFAT 1681
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1682 AKENEKKAkslEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEA 1761
Cdd:pfam07888 120 LLAQRAAH---EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1762 MSDRVRKATQQAEQLSNELAT---ERSTAQKNESARQQLERQNKELRSKLHEMEGAV---KSKFKSTIAALEAKIAQLEE 1835
Cdd:pfam07888 197 LRNSLAQRDTQVLQLQDTITTltqKLTTAHRKEAENEALLEELRSLQERLNASERKVeglGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1836 QVEQEARekqaATKSLKQKDKKLKEILLQVEDERKMAEQykeQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELD 1915
Cdd:pfam07888 277 ARLQAAQ----LTLQLADASLALREGRARWAQERETLQQ---SAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELG 349
|
330 340
....*....|....*....|....*
gi 92091586 1916 EATESNEAM----GREVNALKSKLR 1936
Cdd:pfam07888 350 REKDCNRVQlsesRRELQELKASLR 374
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
851-1175 |
3.37e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 851 LLQVTRQE--EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELE 928
Cdd:pfam07888 35 RLEECLQEraELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 929 EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKER 1008
Cdd:pfam07888 115 EEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1009 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE------------ 1076
Cdd:pfam07888 195 QELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSmaaqrdrtqael 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1077 -----QIADLQAQIAELKMQL-------AKKEEELQAA-------LARLDDEIAQKNNALKKIR-ELEGHISDLQEDLDS 1136
Cdd:pfam07888 275 hqarlQAAQLTLQLADASLALregrarwAQERETLQQSaeadkdrIEKLSAELQRLEERLQEERmEREKLEVELGREKDC 354
|
330 340 350
....*....|....*....|....*....|....*....
gi 92091586 1137 ERAARNKAEKQKRDLGEELEALKTELEDTLdstATQQEL 1175
Cdd:pfam07888 355 NRVQLSESRRELQELKASLRVAQKEKEQLQ---AEKQEL 390
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1078-1229 |
3.51e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.19 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1078 IADLQAQIAELKMQLAKkeeeLQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEA 1157
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1158 LKTELEDTL---DSTATQQELRAKREQEVTVLKKALD----EETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANL 1229
Cdd:pfam00529 129 RRVLAPIGGisrESLVTAGALVAQAQANLLATVAQLDqiyvQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
865-1068 |
3.94e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 865 EDELQKTKERQQKAENELKELEQKHS--QLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEE 942
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 943 D-------RGQQLQAERkKMAQQMLDLEEQLEEEEAARQKLQlekvTAEAKIKKLEDEILVmddqnnKLSKERKLLEERI 1015
Cdd:COG3206 261 QspviqqlRAQLAELEA-ELAELSARYTPNHPDVIALRAQIA----ALRAQLQQEAQRILA------SLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1016 SDLTTNLAEEEEKAKNLTKLKNKHESMISELEVrlkkeekSRQELEKLKRKLE 1068
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEV-------ARELYESLLQRLE 375
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
992-1364 |
4.65e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 48.70 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 992 DEILVMDDQnnKLSKERKLLEERISDLTTNLAEEEEKAKNLtKLKNKHESMISELEVRLKK----------------EEK 1055
Cdd:PLN03229 383 DELGKMDTE--ELLKHRMLKFRKIGGFQEGVPVDPERKVNM-KKREAVKTPVRELEGEVEKlkeqilkakessskpsELA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1056 SRQELEKLKRKLEGDASDFHEQIAdLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLD 1135
Cdd:PLN03229 460 LNEMIEKLKKEIDLEYTEAVIAMG-LQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1136 SERAA-RNKAEKQKRDLGEELealKTELEDTLDSTATQQELRAKREqevtvlkkALDEETRSHEAQvqemrqKHAQAVEE 1214
Cdd:PLN03229 539 MLNEFsRAKALSEKKSKAEKL---KAEINKKFKEVMDRPEIKEKME--------ALKAEVASSGAS------SGDELDDD 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1215 LTEQLEqfkrakanldKNKQTLEKEnadLAGELRVLGQAKQEVEHKKKKLEAQ--VQELQSKCsdgERARAELNDKVHKL 1292
Cdd:PLN03229 602 LKEKVE----------KMKKEIELE---LAGVLKSMGLEVIGVTKKNKDTAEQtpPPNLQEKI---ESLNEEINKKIERV 665
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1293 QNevesVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEME 1364
Cdd:PLN03229 666 IR----SSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARE 733
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
880-1479 |
4.83e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 880 NELKELEQKHSQLTEEKNLLQEQLQAETELYAEAeemrvrlaakKQELEEILHEMEARleeeedrgqqlqAERKKMAQQM 959
Cdd:TIGR01612 1486 NELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY----------KKDVTELLNKYSAL------------AIKNKFAKTK 1543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 960 LDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQ---NNKLSK------------ERKLLeeRISDLTTN--- 1021
Cdd:TIGR01612 1544 KDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakNDKSNKaaidiqlslenfENKFL--KISDIKKKind 1621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1022 -LAEEEEKAKNLTKLK-NKHESMISELEVRLKKEEKSRQELEKLKRKLEgdasDFHEQIADLQAQIAELKMQLAKKEEEL 1099
Cdd:TIGR01612 1622 cLKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIE----DKKKELDELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1100 QAALARLDDEIAQKN-NALKKIRELeghisdLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELrak 1178
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANkEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNI--- 1768
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1179 reqeVTVLKKALDEETRSHEaqvqEMRQKHAQAVEELTEQLEQFKRAKANLDKnkqtLEKENADlagelRVLGQAKQEVE 1258
Cdd:TIGR01612 1769 ----IAGCLETVSKEPITYD----EIKNTRINAQNEFLKIIEIEKKSKSYLDD----IEAKEFD-----RIINHFKKKLD 1831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1259 HKKKKLEAQVQELQ------SKCSDGERARAELNDKVHKLQNEVESVTGMLN--------EAEGKAIKLAKDVASLSSQL 1324
Cdd:TIGR01612 1832 HVNDKFTKEYSKINegfddiSKSIENVKNSTDENLLFDILNKTKDAYAGIIGkkyysykdEAEKIFINISKLANSINIQI 1911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1325 QDTQEL-------------LQEETRQKLNVSTKLRQLEEE----RNSLQDQLDEEMEAKQNLERHISTLNI-----QLSD 1382
Cdd:TIGR01612 1912 QNNSGIdlfdniniailssLDSEKEDTLKFIPSPEKEPEIytkiRDSYDTLLDIFKKSQDLHKKEQDTLNIifenqQLYE 1991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1383 SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEE---------------KAAAYDKLEKTKNRLQQELDDLVVDLDNQ- 1446
Cdd:TIGR01612 1992 KIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDFDVKa 2071
|
650 660 670
....*....|....*....|....*....|....
gi 92091586 1447 -RQLVSNLEKKQRKFDQLLAEEKNISSKYADERD 1479
Cdd:TIGR01612 2072 mEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
859-1087 |
5.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 859 EEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARL 938
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKEL 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 939 EEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDqnnklsKERKLLEERISDL 1018
Cdd:PRK03918 598 EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE------EEYEELREEYLEL 671
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92091586 1019 TTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEgDASDFHEQIADLQAQIAE 1087
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
858-1685 |
5.85e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.41 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKE--RQQKA----ENELKELEQK---HSQLTEEKNLLQEQLQAETELY-AEAEEMRVRLAAKKQEL 927
Cdd:COG3096 326 EQDYQAASDHLNLVQTalRQQEKieryQEDLEELTERleeQEEVVEEAAEQLAEAEARLEAAeEEVDSLKSQLADYQQAL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 928 --------------------EEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQklQLEKvtAEAKI 987
Cdd:COG3096 406 dvqqtraiqyqqavqalekaRALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARR--QFEK--AYELV 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 988 KKLEDEIlvmdDQNNKLSKERKLLEE---------RISDLTTNLAEEEEKAKNltklKNKHESMISELEVRLKKEEKSRQ 1058
Cdd:COG3096 482 CKIAGEV----ERSQAWQTARELLRRyrsqqalaqRLQQLRAQLAELEQRLRQ----QQNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1059 ELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL----AKKEE---------ELQAALARLDDEIAQknnALKKIRELEG 1125
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLeqlrARIKElaarapawlAAQDALERLREQSGE---ALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1126 HisdLQEDLDSERAA---RNKAEKQKRDLGEELEALkteledTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQ 1202
Cdd:COG3096 631 A---MQQLLEREREAtveRDELAARKQALESQIERL------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYF 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1203 EMR---QKHAQAVEELT---EQLEQFKRAKANL-----------DKNKQTLEKENADLAG----ELRV--------LGQA 1253
Cdd:COG3096 702 SALygpARHAIVVPDLSavkEQLAGLEDCPEDLyliegdpdsfdDSVFDAEELEDAVVVKlsdrQWRYsrfpevplFGRA 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1254 KQevEHKKKKLEAQVQELqskcsdgERARAELNDKVHKLQNEVESVTGMLneAEGKAIKLAKDVAslssqlqdtqELLQE 1333
Cdd:COG3096 782 AR--EKRLEELRAERDEL-------AEQYAKASFDVQKLQRLHQAFSQFV--GGHLAVAFAPDPE----------AELAA 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1334 ETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDS-KKKLQDFASTVEALEEGK---KRFQKEIE 1409
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETlADRLEELREELDAAQEAQafiQQHGKALA 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1410 NLT----------QQYEEKAAAYDKLEKTKNRLQQELDDLVvdldnqrQLVSNLEKkqrkfdqlLAeeknisskYADerd 1479
Cdd:COG3096 921 QLEplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALS-------EVVQRRPH--------FS--------YED--- 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1480 raeAEAREKETKALslaraleealeakeelertNKMLKAemedlvsskddvgknvhELEKSKRALETQMEEMKTQLEELE 1559
Cdd:COG3096 975 ---AVGLLGENSDL-------------------NEKLRA-----------------RLEQAEEARREAREQLRQAQAQYS 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1560 DELQATEDAKLRLEVNMQALKgQFERDLQA----RDEQNEEKRRQLQRQLHEyetELEDERKQRALAAAAKKKLEGDLKD 1635
Cdd:COG3096 1016 QYNQVLASLKSSRDAKQQTLQ-ELEQELEElgvqADAEAEERARIRRDELHE---ELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 92091586 1636 LElqadsaikgreeaiKQLRKLQAQMKDFQRELEDARASRDEIFATAKEN 1685
Cdd:COG3096 1092 LQ--------------KRLRKAERDYKQEREQVVQAKAGWCAVLRLARDN 1127
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1032-1456 |
6.23e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1032 LTKLKNKHESMISELEVRLKKEEKSRQELEKLKrklegdasdfhEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1111
Cdd:pfam06160 95 LDDIEEDIKQILEELDELLESEEKNREEVEELK-----------DKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1112 QKNN---------ALKKIRELEGHISDLQEDLDseraarnkaekqkrDLGEELEALKTELEDTLDS-TATQQELrakREQ 1181
Cdd:pfam06160 164 QFEEltesgdyleAREVLEKLEEETDALEELME--------------DIPPLYEELKTELPDQLEElKEGYREM---EEE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1182 EVTVLKKALDEETRSHEAQVQEmrqkhaqaVEELTEQLEqFKRAKANLDKNKQTLEKENADLAGELrvlgQAKQEVEHKK 1261
Cdd:pfam06160 227 GYALEHLNVDKEIQQLEEQLEE--------NLALLENLE-LDEAEEALEEIEERIDQLYDLLEKEV----DAKKYVEKNL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1262 KKLEAQVQELQskcsdgeraraelnDKVHKLQNEVESVT---GMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEET--- 1335
Cdd:pfam06160 294 PEIEDYLEHAE--------------EQNKELKEELERVQqsyTLNENELERVRGLEKQLEELEKRYDEIVERLEEKEvay 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1336 ---RQKLNVSTK-LRQLEEERNSLQDQL----DEEMEAKQNLERhistLNIQLSDSKKKLQdfastvealeegkkrfQKE 1407
Cdd:pfam06160 360 selQEELEEILEqLEEIEEEQEEFKESLqslrKDELEAREKLDE----FKLELREIKRLVE----------------KSN 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1408 IENLTQQYEE-KAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKK 1456
Cdd:pfam06160 420 LPGLPESYLDyFFDVSDEIEDLADELNEvplNMDEVNRLLDEAQDDVDTLYEK 472
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1148-1323 |
6.87e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1148 KRDLGEELEALKTELEDTLDstATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA 1227
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1228 NLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKleaQVQELQSKCS-DGERARAELNDKV-HKLQNEVES-VTGMLN 1304
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEE---QLQELERISGlTAEEAKEILLEKVeEEARHEAAVlIKEIEE 180
|
170
....*....|....*....
gi 92091586 1305 EAEGKAIKLAKDVASLSSQ 1323
Cdd:PRK12704 181 EAKEEADKKAKEILAQAIQ 199
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
857-1417 |
7.29e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 857 QEEEMQAKEDELQKTKERQQKAENELKELEQKHS-QLTEEKNL--LQEQLQAETE-LYAEAEEMRVRLAAKKQELEEI-- 930
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGqQLDAAEELeeLLAELEAQLEeLEEQAAEAVEQRSELRQQLEQLra 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 931 ----LHEMEARLEEEEDRGQQLQ-------AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKL------ED- 992
Cdd:COG3096 593 rikeLAARAPAWLAAQDALERLReqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLsqpggaEDp 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 993 ---------------EI----------------------LVMDDqnnkLSKERKLLEERiSDLTTNL------------- 1022
Cdd:COG3096 673 rllalaerlggvllsEIyddvtledapyfsalygparhaIVVPD----LSAVKEQLAGL-EDCPEDLyliegdpdsfdds 747
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1023 ---AEEEEKA---------------------------KNLTKLKNKHEsmisELEVRLKKEEKSRQELEklkrKLEGDAS 1072
Cdd:COG3096 748 vfdAEELEDAvvvklsdrqwrysrfpevplfgraareKRLEELRAERD----ELAEQYAKASFDVQKLQ----RLHQAFS 819
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1073 DF---HEQIA---DLQAQIAELKMQLAkkeeELQAALARLDDEIAQKNNALKKIRE---------------LEGHISDLQ 1131
Cdd:COG3096 820 QFvggHLAVAfapDPEAELAALRQRRS----ELERELAQHRAQEQQLRQQLDQLKEqlqllnkllpqanllADETLADRL 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1132 EDLDSERAARNKAEKQKRDLGEELEALKTELeDTLDSTATQQElrakreqevtvlkkALDEETRSHEAQVQEMRQKhAQA 1211
Cdd:COG3096 896 EELREELDAAQEAQAFIQQHGKALAQLEPLV-AVLQSDPEQFE--------------QLQADYLQAKEQQRRLKQQ-IFA 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1212 VEELTEQLEQFKRAKAnldknkQTLEKENADLagelrvlgqakqevehkkkkleaqVQELQSKCSDGERARAELNDKVHK 1291
Cdd:COG3096 960 LSEVVQRRPHFSYEDA------VGLLGENSDL------------------------NEKLRARLEQAEEARREAREQLRQ 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1292 LQNEVESVTGMLneaegkaiklakdvASLSSQLQDTQELLQEetrqklnvstklrqLEEERNSLQDQLDEEMEAKQNLER 1371
Cdd:COG3096 1010 AQAQYSQYNQVL--------------ASLKSSRDAKQQTLQE--------------LEQELEELGVQADAEAEERARIRR 1061
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 92091586 1372 hiSTLNIQLSDSKKKLqdfastvEALEEGKKRFQKEIENLTQQYEE 1417
Cdd:COG3096 1062 --DELHEELSQNRSRR-------SQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
984-1560 |
7.29e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 984 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLtTNLAEEEEKAKNLTKLKNKHESMISELEV--------RLKKEEK 1055
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNI-SDKNEYIKKAIDLKKIIENNNAYIDELAKispyqvpeHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1056 SRQELE-KLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEI----------------AQKNNALK 1118
Cdd:TIGR01612 657 IYSTIKsELSKIYEDDIDALYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIqnmetatvelhlsnieNKKNELLD 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1119 KIRELEGHI-SDLQEDLDSERAARNKAEKQkrdLGEELEALKTELEDTLDSTATQQELRAKREQEVTVlKKALDEETRSH 1197
Cdd:TIGR01612 737 IIVEIKKHIhGEINKDLNKILEDFKNKEKE---LSNKINDYAKEKDELNKYKSKISEIKNHYNDQINI-DNIKDEDAKQN 812
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1198 EAQVQEMRQKHAQAVEELTEQLEQFKR------AKANLDKNKQTLEKENADLAGE--LRVLGQAKQEVEhkkkklEAQVQ 1269
Cdd:TIGR01612 813 YDKSKEYIKTISIKEDEIFKIINEMKFmkddflNKVDKFINFENNCKEKIDSEHEqfAELTNKIKAEIS------DDKLN 886
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1270 ELQSKCSDGERARAELNDKVHKLQNEVESvtgmLNEAEGkAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE 1349
Cdd:TIGR01612 887 DYEKKFNDSKSLINEINKSIEEEYQNINT----LKKVDE-YIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIE 961
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1350 EernSLQDQLDEEMEAKQN-LERHISTLNIQLSDSKKKlqdfaSTVEALEEGKKRFQKEIEN-LTQQYEEKaaaydklEK 1427
Cdd:TIGR01612 962 K---SYKDKFDNTLIDKINeLDKAFKDASLNDYEAKNN-----ELIKYFNDLKANLGKNKENmLYHQFDEK-------EK 1026
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1428 TKNRLQQELDDLVVDLDNQRQLV-SNLEKKQRKFDQLLAeeKNISSKYADERDRAEAEAREKETKALSLARALEEALEAK 1506
Cdd:TIGR01612 1027 ATNDIEQKIEDANKNIPNIEIAIhTSIYNIIDEIEKEIG--KNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGKE 1104
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1507 EELERTNKMLKAEmEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1560
Cdd:TIGR01612 1105 ENIKYADEINKIK-DDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED 1157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
974-1203 |
7.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 974 QKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKlknkhesmisELEVRLKKE 1053
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE----------ELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1054 EKSRQELEKLKRKLE-GDASDFHEQIADLQaQIAELKMQLAKKEEELQAALARLDDEI-AQKNNALKKIRELEGHISDLQ 1131
Cdd:COG3883 96 YRSGGSVSYLDVLLGsESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELeAKLAELEALKAELEAAKAELE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1132 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQE 1203
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1153-1425 |
8.21e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 47.00 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKN 1232
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1233 KQTLEKENADLA-----GELRVLGQ--AKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNE 1305
Cdd:pfam04108 83 LDKLRNTPVEPAlppgeEKQKTLLDfiDEDSVEILRDALKELIDELQAAQESLDSDLKRFDDDLRDLQKELESLSSPSES 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1306 AE------GKAIKLAKDVASLSSQL------------------QDTQELLQEETRQKLNVSTKLR----QLEEERNSLQD 1357
Cdd:pfam04108 163 ISliptllKELESLEEEMASLLESLtnhydqcvtavklteggrAEMLEVLENDARELDDVVPELQdrldEMENNYERLQK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1358 QLDEEMEAKQNLE---RHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKL 1425
Cdd:pfam04108 243 LLEQKNSLIDELLsalQLIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSELEDLREFYEGFPSAYGSL 313
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1535-1937 |
8.41e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1535 HELEKSKRAL---ETQMEEMKTQLEE-------LEDELQATEDaKLRLEVNMQALKGQFER------DLQARDEQNEEKR 1598
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD-HLNLVQTALRQQEKIERyqedleELTERLEEQEEVV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1599 RQLQRQLHEYETELEderkqralaaaakkKLEGDLKDLELQ-ADsaikgREEAI--KQLRKLQAQMKdfQRELEDARA-- 1673
Cdd:COG3096 371 EEAAEQLAEAEARLE--------------AAEEEVDSLKSQlAD-----YQQALdvQQTRAIQYQQA--VQALEKARAlc 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1674 -----SRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLekeelaeelasslsgrnALQdekrrLEARIAQL 1748
Cdd:COG3096 430 glpdlTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEK-----------------AYE-----LVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1749 EEELEEEQGNMEAMSD--RVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEgavksKFKSTIAAL 1826
Cdd:COG3096 488 VERSQAWQTARELLRRyrSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-----ELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1827 EAKIAQLEEQVEqEAREKQAATKSlkqkdkKLKEILLQVEDERKMAEQYKeqaeKGNARVKQLKRQLEEAEEESQRINAN 1906
Cdd:COG3096 563 EAQLEELEEQAA-EAVEQRSELRQ------QLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAA 631
|
410 420 430
....*....|....*....|....*....|.
gi 92091586 1907 RRKLQRELDEATESNEAMGREVNALKSKLRR 1937
Cdd:COG3096 632 MQQLLEREREATVERDELAARKQALESQIER 662
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
913-1271 |
8.66e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 913 AEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLED 992
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 993 EILVMDDQNNKLSKERKLLEERISDLttnlaeeEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAS 1072
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIREL-------EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1073 DFHEQIADLQAQIAELKMQLAKKEEELQaalaRLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLG 1152
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVL----QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 EELEALKTELEDTL------------------DSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEE 1214
Cdd:pfam07888 258 EELSSMAAQRDRTQaelhqarlqaaqltlqlaDASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1215 LTEQleqfKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQEL 1271
Cdd:pfam07888 338 RMER----EKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1053-1453 |
8.68e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.74 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1053 EEKSRQELEKLKrklegDASDFHeqiadlQAQIAElkmqlakkeeELQAALARLDDeiaqKNNALKKIRELEGHISDLqe 1132
Cdd:PRK10929 25 EKQITQELEQAK-----AAKTPA------QAEIVE----------ALQSALNWLEE----RKGSLERAKQYQQVIDNF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1133 dldseraarnkaEKQKRDLGEELEALKTELEdTLDSTATQQELrakrEQEVTVLKKALDEETRSHEaQVQEMRQKHAQAV 1212
Cdd:PRK10929 78 ------------PKLSAELRQQLNNERDEPR-SVPPNMSTDAL----EQEILQVSSQLLEKSRQAQ-QEQDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1213 EELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAkqEVEHKKKKLE----AQV-----QELQskcsdgeRARA 1283
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQA--ESAALKALVDelelAQLsannrQELA-------RLRS 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1284 ELNDKVH-KLQNEVESVTGMLN-----EAEgKAIK----LAKDVASL----SSQLQDTQELLQE--ETRQKLN-VSTKLR 1346
Cdd:PRK10929 211 ELAKKRSqQLDAYLQALRNQLNsqrqrEAE-RALEstelLAEQSGDLpksiVAQFKINRELSQAlnQQAQRMDlIASQQR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1347 QLEEERNSLQDQLDEEMEAKQNLERHIS---TLNIQLSD--SKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAA 1421
Cdd:PRK10929 290 QAASQTLQVRQALNTLREQSQWLGVSNAlgeALRAQVARlpEMPKPQQLDTEMAQLRVQRLRYEDLLNKQPQLRQIRQAD 369
|
410 420 430
....*....|....*....|....*....|..
gi 92091586 1422 YDKLEKTKNRLqqeLDDLvvdLDNQRQLVSNL 1453
Cdd:PRK10929 370 GQPLTAEQNRI---LDAQ---LRTQRELLNSL 395
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
865-1112 |
9.21e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 865 EDELQKTKE---RQQKAENELKELEQKHSQLTEEKNLLQEQLQaetELYAeaeemrvrLAAKKQELEEilhemearleee 941
Cdd:COG0497 154 EELLEEYREayrAWRALKKELEELRADEAERARELDLLRFQLE---ELEA--------AALQPGEEEE------------ 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 942 edrgqqLQAERKKMAQqmldLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEE---RISDL 1018
Cdd:COG0497 211 ------LEEERRRLSN----AEKLREALQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESaliELEEA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1019 TTN--------------LAEEEEKAKNLTKLKNKHESMISELevrLKKEEKSRQELEKLkrklegdaSDFHEQIADLQAQ 1084
Cdd:COG0497 281 ASElrryldslefdperLEEVEERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL--------ENSDERLEELEAE 349
|
250 260 270
....*....|....*....|....*....|..
gi 92091586 1085 IAELKMQLAKKEEEL----QAALARLDDEIAQ 1112
Cdd:COG0497 350 LAEAEAELLEAAEKLsaarKKAAKKLEKAVTA 381
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
664-688 |
9.28e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 45.03 E-value: 9.28e-05
10 20
....*....|....*....|....*
gi 92091586 664 YKEQLGKLMTTLRNTTPNFVRCIIP 688
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
865-1569 |
9.54e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 865 EDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEemrvRLAAKKQELEEIlhEMEARLEEEEDR 944
Cdd:COG3096 440 EDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVE----RSQAWQTARELL--RRYRSQQALAQR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 945 GQQLQAE----RKKMAQQmldleeqleeEEAARQKLQLEKVTAeakiKKLEDEILVMDDQNNklskerklLEERISDLTT 1020
Cdd:COG3096 514 LQQLRAQlaelEQRLRQQ----------QNAERLLEEFCQRIG----QQLDAAEELEELLAE--------LEAQLEELEE 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1021 NLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLkRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQ 1100
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-REQSGEALADSQEVTAAMQQLLEREREATVERDELA 650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1101 AALARLDDEIAQKNNA-------LKKIRELEGH--ISDLQEDLDSERA----ARNKAEKQK---RDLGEELEALKTeLED 1164
Cdd:COG3096 651 ARKQALESQIERLSQPggaedprLLALAERLGGvlLSEIYDDVTLEDApyfsALYGPARHAivvPDLSAVKEQLAG-LED 729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1165 TL--------------DSTATQQEL-------------------------RAKREQEVTVLKKALDEETRSHeAQVQEMR 1205
Cdd:COG3096 730 CPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQY-AKASFDV 808
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1206 QKHaqavEELTEQLEQFKRAKANLdknkqtleKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAEL 1285
Cdd:COG3096 809 QKL----QRLHQAFSQFVGGHLAV--------AFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLL 876
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1286 NDKVHK--------LQNEVESVTGMLNEAEGKAIKLAKDVASLsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQD 1357
Cdd:COG3096 877 NKLLPQanlladetLADRLEELREELDAAQEAQAFIQQHGKAL-AQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1358 QLDEEMEAKQNLErHIStlniqLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYdklektkNRLQQELD 1437
Cdd:COG3096 956 QIFALSEVVQRRP-HFS-----YEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQY-------SQYNQVLA 1022
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1438 DLVVDLDNQRQLVSNLEkkqRKFDQL-LAEEKNISSKYADERDRAEAEAREKETKALSL----ARALEEALEAKEELERT 1512
Cdd:COG3096 1023 SLKSSRDAKQQTLQELE---QELEELgVQADAEAEERARIRRDELHEELSQNRSRRSQLekqlTRCEAEMDSLQKRLRKA 1099
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1513 NKMLKAEMEDLVSSK------------DDVGKNVHELE--------------KSKRALETQMEEmktqLEELEDELQATE 1566
Cdd:COG3096 1100 ERDYKQEREQVVQAKagwcavlrlardNDVERRLHRRElaylsadelrsmsdKALGALRLAVAD----NEHLRDALRLSE 1175
|
...
gi 92091586 1567 DAK 1569
Cdd:COG3096 1176 DPR 1178
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1770-1941 |
9.65e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.70 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1770 TQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHemegavKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATK 1849
Cdd:PTZ00491 645 TRDSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLE------RQKMHDKAKAEEQRTKLLELQAESAAVESSGQSR 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1850 SlkQKDKKLKEILLQVEDERKMAEqYKEQAEK--GNARVKQLKRQLEEAEEESQRINANRRKLQRELDEaTESN------ 1921
Cdd:PTZ00491 719 A--EALAEAEARLIEAEAEVEQAE-LRAKALRieAEAELEKLRKRQELELEYEQAQNELEIAKAKELAD-IEATkferiv 794
|
170 180
....*....|....*....|
gi 92091586 1922 EAMGREvnALKSKLRRGNET 1941
Cdd:PTZ00491 795 EALGRE--TLIAIARAGPEL 812
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
848-1414 |
9.96e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 9.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 848 VKPLLQVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLA------ 921
Cdd:pfam10174 160 IKKLLEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTviemkd 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 922 AKKQELEEILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQN 1001
Cdd:pfam10174 240 TKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQN 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1002 NKLSKERKLLEErisdlttNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE----- 1076
Cdd:pfam10174 320 SDCKQHIEVLKE-------SLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvk 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1077 --QIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRdlgEE 1154
Cdd:pfam10174 393 erKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL---EE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1155 LEALKTELEDTLDSTATQQELRAKREQEVTVLKkaldeETRSHEAQVQEMRQKHAQAVE-ELTEQLEQFKRAKANLDKNK 1233
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTEKESSLIDLK-----EHASSLASSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAH 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1234 QTLEKEnadlagelrvlgQAKQEVEHKKKKLEaqvQELQSKCSDGERARAELN---DKVHKLQNEVESVTGMLNEAEGKA 1310
Cdd:pfam10174 545 NAEEAV------------RTNPEINDRIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIAELESLT 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1311 IKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKlRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDF 1390
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEK 688
|
570 580
....*....|....*....|....
gi 92091586 1391 ASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:pfam10174 689 DGHLTNLRAERRKQLEEILEMKQE 712
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1241-1619 |
1.04e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1241 ADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGkaiklakDVASL 1320
Cdd:pfam19220 16 ADRLEDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1321 SSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQ----DFASTVEA 1396
Cdd:pfam19220 89 VARLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQraegELATARER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1397 ---LEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLvvdldnQRQLVSNLEKKQRKFDQLLAEEKNISSK 1473
Cdd:pfam19220 169 lalLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRAL------EGQLAAEQAERERAEAQLEEAVEAHRAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1474 YADERDRAEA-EAREKET-KALSLARALEEAleakeeleRTNKMLKAE--MEDLVSSKDDVGKNVHELEKSKRALETQME 1549
Cdd:pfam19220 243 RASLRMKLEAlTARAAATeQLLAEARNQLRD--------RDEAIRAAErrLKEASIERDTLERRLAGLEADLERRTQQFQ 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1550 EMKTQLEELEDE-------LQATEDAKLRLEVNMQALKGQFErDLQARDEQneeKRRQLQRQLHEYETELEDERKQR 1619
Cdd:pfam19220 315 EMQRARAELEERaemltkaLAAKDAALERAEERIASLSDRIA-ELTKRFEV---ERAALEQANRRLKEELQRERAER 387
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1013-1280 |
1.09e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKmql 1092
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1093 aKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSER----------AARNKAEKQKRDLGEELEALKTEL 1162
Cdd:COG1340 78 -EERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1163 EDTLDSTATQQELRAKREQ--EVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT---LE 1237
Cdd:COG1340 157 EKNEKLKELRAELKELRKEaeEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEiieLQ 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 92091586 1238 KENADLAGELRVL--GQAKQEVEHKKKKLEAQVQELQSKCSDGER 1280
Cdd:COG1340 237 KELRELRKELKKLrkKQRALKREKEKEELEEKAEEIFEKLKKGEK 281
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1027-1148 |
1.10e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.13 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1027 EKAK-NLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLakkEEELQAALAR 1105
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 92091586 1106 LDDEIAQknnALKKIRELE--GHISDLQEDLDSERAARNKAEKQK 1148
Cdd:PRK00409 582 AKKEADE---IIKELRQLQkgGYASVKAHELIEARKRLNKANEKK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1527-1713 |
1.15e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1527 KDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQAtedakLRLEVNMQALKGQfERDLQARDEQNEEKRRQLQRQLH 1606
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1607 EYETELEDERKQRALAAAAKKKLEGD--LKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARAS-RDEIFATAK 1683
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILA 316
|
170 180 190
....*....|....*....|....*....|
gi 92091586 1684 ENEKKAKSLEADLMQLQEDLAAAERARKQA 1713
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAEL 346
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1732-1882 |
1.17e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1732 NALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNEsARQQLERQNKELRSKLHEM 1811
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE-EQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1812 EGAVK--SKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKG 1882
Cdd:COG1579 99 ESLKRriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1642-1931 |
1.55e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1642 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfataKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELA 1721
Cdd:PRK11281 39 ADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKI----DRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1722 EELASSLSgrnalqdeKRRLEARIAQLEEELEEEQGNMeamsdrvrkATQQAEQLSNELATERstAQKNESARQQlerQN 1801
Cdd:PRK11281 115 RETLSTLS--------LRQLESRLAQTLDQLQNAQNDL---------AEYNSQLVSLQTQPER--AQAALYANSQ---RL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1802 KELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATkslkqkdkklkeiLLQvederkmaEQYKEQAEK 1881
Cdd:PRK11281 173 QQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNT-------------QLQ--------DLLQKQRDY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1882 GNARVKQLKRQLEEAEEEsqrINANRRKL-QRELDEATESNEAMGREVNAL 1931
Cdd:PRK11281 232 LTARIQRLEHQLQLLQEA---INSKRLTLsEKTVQEAQSQDEAARIQANPL 279
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
809-1081 |
1.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 809 ARKAFAKRQQQLTAMkviQRNCAAYLKLRNWQWwrlftkvkPLLQVTRQEEEMQAKEDELqktkERQQKAENELKELEQK 888
Cdd:COG4913 629 AEERLEALEAELDAL---QERREALQRLAEYSW--------DEIDVASAEREIAELEAEL----ERLDASSDDLAALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 889 HSQLTEEKNLLQEQLQAETELYAEAEEmrvRLAAKKQELEEilhemeaRLEEEEDRGQQLQAERKKMAQQMLDLEEQLEE 968
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEK---ELEQAEEELDE-------LQDRLEAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 969 EEAARQKLQLEKVTAEAKIKKLEDEIlvmddqNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHesmISELEV 1048
Cdd:COG4913 764 ERELRENLEERIDALRARLNRAEEEL------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG---LPEYEE 834
|
250 260 270
....*....|....*....|....*....|....*
gi 92091586 1049 RLK--KEEKSRQELEKLKRKLEGDASDFHEQIADL 1081
Cdd:COG4913 835 RFKelLNENSIEFVADLLSKLRRAIREIKERIDPL 869
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1764-1940 |
1.71e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1764 DRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKskfkstIAALEAKIAQLEEQVEQEARE 1843
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ------LLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1844 KQAatksLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKR-QLEEAEEESQRINANRRKLQRELDEATESNE 1922
Cdd:COG4717 148 LEE----LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170
....*....|....*...
gi 92091586 1923 AMGREVNALKSKLRRGNE 1940
Cdd:COG4717 224 ELEEELEQLENELEAAAL 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
858-1149 |
1.75e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 858 EEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRvrlaakKQELEEIlhemear 937
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKR------DELNEKV------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 938 leeeedrgQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLeERISD 1017
Cdd:COG1340 74 --------KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELV-EKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1018 LTTNLaeeeEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKlegdASDFHEQIADLQAQIAELKMQLAKKEE 1097
Cdd:COG1340 145 LEKEL----EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEE----AQELHEEMIELYKEADELRKEADELHK 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1098 ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKR 1149
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1315-1489 |
1.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1315 KDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLE----EERNSLQDQLD-----------------EEMEAKQNLERHI 1373
Cdd:PRK11637 82 EAISQASRKLRETQNTLNQLNKQIDELNASIAKLEqqqaAQERLLAAQLDaafrqgehtglqlilsgEESQRGERILAYF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1374 STLNIQLSDSKKKLQDFASTV---EALEEGKKRFQKEIenLTQQYEEKAaaydKLEKTKNRLQQELDdlvvdldnqrQLV 1450
Cdd:PRK11637 162 GYLNQARQETIAELKQTREELaaqKAELEEKQSQQKTL--LYEQQAQQQ----KLEQARNERKKTLT----------GLE 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 92091586 1451 SNLEKKQRKFDQLLAEEKNISSKYAD-ERD---RAEAEAREKE 1489
Cdd:PRK11637 226 SSLQKDQQQLSELRANESRLRDSIARaEREakaRAEREAREAA 268
|
|
| ASY3-like |
pfam20435 |
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ... |
1015-1120 |
2.09e-04 |
|
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.
Pssm-ID: 466584 [Multi-domain] Cd Length: 793 Bit Score: 46.42 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1015 ISDLTTNLAEEEEKAKNLTKLKNKHEsmiselEVRLK-KEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLA 1093
Cdd:pfam20435 667 LENIKSHIITEAGKTSNLAKTKRKHA------ETRLQeQEEKMRMIHEKFKDDVSHHLEDFKSTIEELEANQSELKGSIK 740
|
90 100
....*....|....*....|....*...
gi 92091586 1094 KKEEELQAALARLDDEIAQK-NNALKKI 1120
Cdd:pfam20435 741 KQRTSHQKLIAHFEGGIETKlDDATKRI 768
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1649-1935 |
2.37e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1649 EAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEAdlmqlQEDLAAAERAR-----KQADLEKEELAEE 1723
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER-----RRKLEEAEKARqaemdRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1724 LASSLSGRNALQDEKRRLEARIAQLEEELEEEQgnMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKE 1803
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISR--MRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1804 LRSKLHEMEGAVKSKFKstiaALEAKIAQLEEQVEQEAREKQAATKSLKQKD---KKLKEILLQVEDERKMAEQY----- 1875
Cdd:pfam17380 422 MEQIRAEQEEARQREVR----RLEEERAREMERVRLEEQERQQQVERLRQQEeerKRKKLELEKEKRDRKRAEEQrrkil 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1876 -KEQAEKGNARV------KQLKRQLEE-----AEEESQRINANRRKLQRELDEATESNEAMgREVNALKSKL 1935
Cdd:pfam17380 498 eKELEERKQAMIeeerkrKLLEKEMEErqkaiYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
862-1225 |
2.45e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 45.90 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 862 QAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQlqAETELYAEAEEMrvrlaaKKQELEEILHEMEARLEEE 941
Cdd:pfam09731 81 EPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPK--SEQEKEKALEEV------LKEAISKAESATAVAKEAK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 942 EDRGQQLQAERKKMAQQMLDLEEQLEEeeAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTN 1021
Cdd:pfam09731 153 DDAIQAVKAHTDSLKEASDTAEISREK--ATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDN 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1022 LAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSR--------QELEKL-KRKLEGDASDFHEQIADLQAQIAELKMQL 1092
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIfpdiipvlKEDNLLsNDDLNSLIAHAHREIDQLSKKLAELKKRE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1093 AKK-EEELQAALARLDDEIAQKNNALKKIRELEghISDLQEDLDSERAARNKAEKQKrdLGEELEALKTELEDTLDSTAT 1171
Cdd:pfam09731 311 EKHiERALEKQKEELDKLAEELSARLEEVRAAD--EAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1172 QQELRAKREQEvtvlkkaldeetRSHEAQVQEMRQKHAQAVEELTEQLEQFKRA 1225
Cdd:pfam09731 387 EQEIELQREFL------------QDIKEKVEEERAGRLLKLNELLANLKGLEKA 428
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1285-1537 |
2.71e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1285 LNDKVHKLQNEVESVTGMLNEAEGKaIKLAKDvaslssqLQDTQELLQEETRQKL-NVSTKLRQLEEERNSLQDQLDEEM 1363
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQ-IKTYNK-------NIEEQRKKNGENIARKqNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1364 EA----KQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKkrfqkEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDL 1439
Cdd:PHA02562 244 LNlvmdIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGG-----VCPTCTQQISEGPDRITKIKDKLKELQHSLEKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1440 VVDLDNQRQLVSNLEKKQRKFDQLLAEEKNIssKYADERDRAEAEAREKETKALSLARALEEALEakeelertnKMLKAE 1519
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELKNKISTN--KQSLITLVDKAKKVKAAIEELQAEFVDNAEEL---------AKLQDE 387
|
250
....*....|....*...
gi 92091586 1520 MEDLVSSKDDVGKNVHEL 1537
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHR 405
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1078-1299 |
2.79e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 46.37 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1078 IADLQAQIAELKMQlAKKEEELQAALArlDDEIAQKNNAL---KKIRELEgHISDLQEDLDS--ERAARNKAEKQKRDLG 1152
Cdd:NF012221 1537 TSESSQQADAVSKH-AKQDDAAQNALA--DKERAEADRQRleqEKQQQLA-AISGSQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1153 EELEALKTELE------DTLDSTATQQELRAKREQE------VTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLE 1220
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDQWRNpfagglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1221 QFKRAKANLDKNKQTLEKENADLA--GELR---VLGQaKQEVEHKKKKLEAQVQELQSKcsdGERARAELNDKVHKLQNE 1295
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDIDDAKadAEKRkddALAK-QNEAQQAESDANAAANDAQSR---GEQDASAAENKANQAQAD 1768
|
....
gi 92091586 1296 VESV 1299
Cdd:NF012221 1769 AKGA 1772
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1536-1937 |
3.12e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1536 ELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRrqlqrqlheYETELEDE 1615
Cdd:PRK04863 294 ELYTSRRQLAAEQY----RLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIER---------YQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1616 RKQRALAAAAKKKLEGDLKDLELQADSAikgrEEAIKQLRKlqaQMKDFQRELeDARASRDEIFATAKENEKKAKSLeAD 1695
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAA----EEEVDELKS---QLADYQQAL-DVQQTRAIQYQQAVQALERAKQL-CG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1696 LMQLQ----EDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSD--RVRKA 1769
Cdd:PRK04863 432 LPDLTadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRlrEQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1770 TQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLhemegavkskfkSTIAALEakiaQLEEQVEQEAREKQAATK 1849
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNL------------DDEDELE----QLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1850 SLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVN 1929
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQ 655
|
....*...
gi 92091586 1930 ALKSKLRR 1937
Cdd:PRK04863 656 ALDEEIER 663
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1088-1258 |
3.12e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 45.34 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1088 LKMQLAKKEEelqaALARLDDEIAQKNNALKkireLE-GHISDLQEDLDSERAARNKAEkqkrdlgeeleALKTELEDTL 1166
Cdd:PRK09039 44 LSREISGKDS----ALDRLNSQIAELADLLS----LErQGNQDLQDSVANLRASLSAAE-----------AERSRLQALL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1167 DSTATQQELRAKREQEvtvLKKALDEE-TRSHEAQVQemrqkhaqaVEELTEQLEQFKRAKANLDKNKQTLEKEN----- 1240
Cdd:PRK09039 105 AELAGAGAAAEGRAGE---LAQELDSEkQVSARALAQ---------VELLNQQIAALRRQLAALEAALDASEKRDresqa 172
|
170 180
....*....|....*....|.
gi 92091586 1241 --ADLAGELRV-LGQAKQEVE 1258
Cdd:PRK09039 173 kiADLGRRLNVaLAQRVQELN 193
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
853-1143 |
4.09e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILH 932
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLE 1012
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1013 ERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQL 1092
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1093 AKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNK 1143
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1242-1448 |
4.43e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.07 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1242 DLAGELRVLGQAKQEVEHKKKKLEAQVQELQS-KCSDGEraRAELNDKVHKLQN------EVESVTGMLNEAE------- 1307
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAaALQPGE--EEELEEERRRLSNaeklreALQEALEALSGGEggaldll 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 GKAIKLAKDVASLSSQLQDTQELLQEetrqklnVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNiQLsdsKKKl 1387
Cdd:COG0497 247 GQALRALERLAEYDPSLAELAERLES-------ALIELEEAASELRRYLDSLEFDPERLEEVEERLALLR-RL---ARK- 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1388 qdFASTVEALEEGKKRFQKEIENLTQQYEEKAAaydkLEKTKNRLQQELDDLVVDLDNQRQ 1448
Cdd:COG0497 315 --YGVTVEELLAYAEELRAELAELENSDERLEE----LEAELAEAEAELLEAAEKLSAARK 369
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1343-1491 |
4.78e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.76 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1343 TKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQ---------KEIENLTQ 1413
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnvrnnKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1414 QYEEKAAAYDKLEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETK 1491
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1238-1602 |
4.95e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.11 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1238 KENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCsDGERARAELNDKVHKL-------------QNEVESVTGMLN 1304
Cdd:pfam17380 259 RYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREVerrrkleeaekarQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1305 EAEGKAIKLAKDVA--SLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlnIQLSD 1382
Cdd:pfam17380 338 EQERMAMERERELEriRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVK-------ILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1383 SKKKLQDFASTVEAL-EEGKKRFQKEIENLTqqyEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRkfD 1461
Cdd:pfam17380 411 RQRKIQQQKVEMEQIrAEQEEARQREVRRLE---EERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKR--D 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1462 QLLAEEKNisskyadeRDRAEAEAREKETKALslaraleealeakeELERTNKMLKAEMEDLvsskddvGKNVHELEKSK 1541
Cdd:pfam17380 486 RKRAEEQR--------RKILEKELEERKQAMI--------------EEERKRKLLEKEMEER-------QKAIYEEERRR 536
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1542 RAletqmEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQ 1602
Cdd:pfam17380 537 EA-----EEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1151-1434 |
4.97e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1151 LGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALD---EETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKA 1227
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1228 NLDKNKQTLEKENAD-------LAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVT 1300
Cdd:pfam07888 112 ELSEEKDALLAQRAAhearireLEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1301 GMLNEAEGkaiKLAKDVASLsSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQL 1380
Cdd:pfam07888 192 KEFQELRN---SLAQRDTQV-LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1381 SDSKKKLQ-----------DFASTVEALEEGKKRFQKEIENLTQQYEekaAAYDKLEKTKNRLQQ 1434
Cdd:pfam07888 268 DRTQAELHqarlqaaqltlQLADASLALREGRARWAQERETLQQSAE---ADKDRIEKLSAELQR 329
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
947-1117 |
6.05e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 947 QLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQ--NNKLSKERKLLEERISDLTTNLAE 1024
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1025 EEEKAKNLTKLKNKHESMISELEVRLKKEEKsrqELEKLKRKLEgdasdfhEQIADLQAQIAELKMQLAKKEEELQAALA 1104
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELD-------EELAELEAELEELEAEREELAAKIPPELL 177
|
170
....*....|...
gi 92091586 1105 RLDDEIAQKNNAL 1117
Cdd:COG1579 178 ALYERIRKRKNGL 190
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1211-1601 |
6.07e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1211 AVEELTEQLEQFKRAKANLDKNKQTLE---KENADLAGELRVLGQAKQE-VEHKKKKLEAQVQelQSKcsdGERARAELN 1286
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVemaRELAELNEAESDLEQDYQAaSDHLNLVQTALRQ--QEK---IERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1287 DKVHKL--QNE-VESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQE-ETR-----QKLNVSTKLRQL--------- 1348
Cdd:PRK04863 359 ELEERLeeQNEvVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVqQTRaiqyqQAVQALERAKQLcglpdltad 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1349 --EEERNSLQDQLDEEMEAKQNLERhistlniQLSDSKKKLQDFASTVEALE------EGKKRFQKEIENLTQQYEEKAA 1420
Cdd:PRK04863 439 naEDWLEEFQAKEQEATEELLSLEQ-------KLSVAQAAHSQFEQAYQLVRkiagevSRSEAWDVARELLRRLREQRHL 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1421 AyDKLEKtknrLQQELDDLVVDLDNQRQLVsnlekkqrkfdQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALE 1500
Cdd:PRK04863 512 A-EQLQQ----LRMRLSELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVS 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1501 EALEAKEELERTNKMLKAEMEDLvSSKDDVGKNVHEL-----EKSKRALETQ---MEEMKTQLEElEDELQATEDaklRL 1572
Cdd:PRK04863 576 EARERRMALRQQLEQLQARIQRL-AARAPAWLAAQDAlarlrEQSGEEFEDSqdvTEYMQQLLER-ERELTVERD---EL 650
|
410 420
....*....|....*....|....*....
gi 92091586 1573 EVNMQALKGQFERdLQARDEQNEEKRRQL 1601
Cdd:PRK04863 651 AARKQALDEEIER-LSQPGGSEDPRLNAL 678
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
879-1363 |
6.30e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 879 ENELKELeQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEeilhemearleeeedrgqqlQAERKkmaqq 958
Cdd:PRK11281 42 QAQLDAL-NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA--------------------QAPAK----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 959 mldleeqleeeeaarqklqLEKVTAE-AKIKKLEDEilVMDDQNNKLSKER--KLLEERISDLTT---NLAEEEEKAKNL 1032
Cdd:PRK11281 96 -------------------LRQAQAElEALKDDNDE--ETRETLSTLSLRQleSRLAQTLDQLQNaqnDLAEYNSQLVSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1033 TKLKNKHESMISELEVRLkkeeksrQELEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIA 1111
Cdd:PRK11281 155 QTQPERAQAALYANSQRL-------QQIRNlLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1112 QKNNALKKIRELEGHISDLQEDLDSERaarnkaekqkrdlgeelealKTELEDTLDSTATQQElrAKREQEVTVLKKALD 1191
Cdd:PRK11281 228 QRDYLTARIQRLEHQLQLLQEAINSKR--------------------LTLSEKTVQEAQSQDE--AARIQANPLVAQELE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1192 EETrsheaqvqEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQT---LEKENADLAGEL---RVLGQAKQEVEHKK--KK 1263
Cdd:PRK11281 286 INL--------QLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSernIKEQISVLKGSLllsRILYQQQQALPSADliEG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1264 LEAQVQELQSKCSDGERARAEL---NDKVHKL-QNEVESVTGMLNEAegkaiklakdvasLSSQLQDTQELLQEETRQ-- 1337
Cdd:PRK11281 358 LADRIADLRLEQFEINQQRDALfqpDAYIDKLeAGHKSEVTDEVRDA-------------LLQLLDERRELLDQLNKQln 424
|
490 500 510
....*....|....*....|....*....|.
gi 92091586 1338 -KLNVSTKL----RQLEEERNSLQDQLDEEM 1363
Cdd:PRK11281 425 nQLNLAINLqlnqQQLLSVSDSLQSTLTQQI 455
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1218-1937 |
6.49e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1218 QLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELnDKVHKLQNEVE 1297
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENEL-DPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1298 svtgmlnEAEGKAIKLAKDVASLSSQlqdtqellqEETRQKLNvstklRQLEEERNSLQDQLDEEM-EAKQNLERHISTL 1376
Cdd:TIGR00606 259 -------HNLSKIMKLDNEIKALKSR---------KKQMEKDN-----SELELKMEKVFQGTDEQLnDLYHNHQRTVREK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1377 NIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYE---EKAAAYDkLEKTKNRLQQELDDLVVDLDNQRQLVSNL 1453
Cdd:TIGR00606 318 ERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADrhqEHIRARD-SLIQSLATRLELDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1454 EKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKN 1533
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1534 VHELEKSKRALEtqmeemktqleeLEDELQATEDAKLRlEVNMQALKGQFERDLQARDEQNEEKRRQlqrqlheyetele 1613
Cdd:TIGR00606 477 DQELRKAERELS------------KAEKNSLTETLKKE-VKSLQNEKADLDRKLRKLDQEMEQLNHH------------- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1614 derkqralaaaakkklegdlKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLE 1693
Cdd:TIGR00606 531 --------------------TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTR 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1694 ADLMQLQEDLAAAErarkqadlekeelaeelasslSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRvrkatqqa 1773
Cdd:TIGR00606 591 DRLAKLNKELASLE---------------------QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL-------- 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1774 eqlsnelaterstaqknESARQQLERQNKELrsklhemegavkskfkstiAALEAKIAQLEEQVEQEAREKQAATKSLKQ 1853
Cdd:TIGR00606 642 -----------------ERLKEEIEKSSKQR-------------------AMLAGATAVYSQFITQLTDENQSCCPVCQR 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1854 KDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKS 1933
Cdd:TIGR00606 686 VFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
....
gi 92091586 1934 KLRR 1937
Cdd:TIGR00606 766 DIEE 769
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1002-1136 |
6.70e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 43.90 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1002 NKLSKERKLLEERISDLTTNLAE-EEEKAKNLTKLKNKHESMISELEvrLKKEEKSRQELEKLKRKLEGD----ASDFHE 1076
Cdd:cd22656 124 DDLLKEAKKYQDKAAKVVDKLTDfENQTEKDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLneeyAAKLKA 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1077 QIADLQAQIAELKMQLAKKE---EELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDS 1136
Cdd:cd22656 202 KIDELKALIADDEAKLAAALrliADLTAADTDLDNLLALIGPAIPALEKLQGAWQAIATDLDS 264
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
967-1473 |
6.96e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 967 EEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLS---KERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMI 1043
Cdd:PRK01156 207 ADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKII 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1044 SElevrlkKEEKSRQELEKLkRKLEGDASDFHEQIADLQAQIAELKmQLAKKEEELQAALARLDDEIAQKNNALKKIREL 1123
Cdd:PRK01156 287 ND------PVYKNRNYINDY-FKYKNDIENKKQILSNIDAEINKYH-AIIKKLSVLQKDYNDYIKKKSRYDDLNNQILEL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1124 EGHISDLQEDLDS----ERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQ---EVTVLKKALDeETRS 1196
Cdd:PRK01156 359 EGYEMDYNSYLKSieslKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDissKVSSLNQRIR-ALRE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1197 HEAQVQE-MRQKHAQAV----------EELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKK-KKL 1264
Cdd:PRK01156 438 NLDELSRnMEMLNGQSVcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEiNKS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1265 EAQVQELQSKCSDGERARAELN------DKVHKLQNEVESVTgmLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1338
Cdd:PRK01156 518 INEYNKIESARADLEDIKIKINelkdkhDKYEEIKNRYKSLK--LEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1339 LN-VSTKLRQLE---EERNSLQDQLDEEMEAKQNLerhistlniqLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQ 1414
Cdd:PRK01156 596 LNdLESRLQEIEigfPDDKSYIDKSIREIENEANN----------LNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1415 YEEKAAAYDKLEKTKNRLQQ---ELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAE-EKNISSK 1473
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKsrkALDDAKANRARLESTIEILRTRINELSDRINDiNETLESM 728
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1228-1419 |
7.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1228 NLDKNKQTLEKENADlagelRVLGQAKQEVEHKKKKLEAQVQElqskcsdgeraraelndKVHKLQNEVEsvtgmlneae 1307
Cdd:PRK12704 27 KIAEAKIKEAEEEAK-----RILEEAKKEAEAIKKEALLEAKE-----------------EIHKLRNEFE---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1308 gkaiklaKDVASLSSQLQDTQELLQeetRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKL 1387
Cdd:PRK12704 75 -------KELRERRNELQKLEKRLL---QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQEL 144
|
170 180 190
....*....|....*....|....*....|....*...
gi 92091586 1388 QDFA--STVEA----LEEGKKRFQKEIENLTQQYEEKA 1419
Cdd:PRK12704 145 ERISglTAEEAkeilLEKVEEEARHEAAVLIKEIEEEA 182
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
985-1192 |
7.86e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 985 AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTT----NLAEEEEKAKNLTKLKNKHESMISELEVRLKkeeksrqEL 1060
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELL-------NL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1061 EKLKRKLEGDASDFHEQIADLQAQIAELK--MQLAKKEEELQAALARLDDE------IAQKNNAL-KKIRELEGHISDLQ 1131
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQkvIKMYEKGGVCPTCTQQISEGpdritkIKDKLKELqHSLEKLDTAIDELE 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1132 EDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKR---EQEVTVLKKALDE 1192
Cdd:PHA02562 327 EIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFvdnAEELAKLQDELDK 390
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1691-1839 |
7.99e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.95 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1691 SLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQG--NMEAMSDRVRK 1768
Cdd:pfam00529 62 SAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARrrVLAPIGGISRE 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1769 ATQQAEQLSNEL-ATERSTAQKNESARQQLERQNKELRSKLhemegavkskfKSTIAALEAKIAQLEEQVEQ 1839
Cdd:pfam00529 142 SLVTAGALVAQAqANLLATVAQLDQIYVQITQSAAENQAEV-----------RSELSGAQLQIAEAEAELKL 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
876-1062 |
8.01e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 876 QKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILhemearleeeedrgQQLQAERKKM 955
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI--------------EEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 956 AQQMLDLEEQLEEeeaarQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEeekaknltkl 1035
Cdd:COG1579 79 EEQLGNVRNNKEY-----EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK---------- 143
|
170 180
....*....|....*....|....*..
gi 92091586 1036 KNKHESMISELEVRLKKEEKSRQELEK 1062
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAA 170
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
883-1133 |
8.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 883 KELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEilhemearleeeedrgqQLQAERKKMAQQMLDL 962
Cdd:PHA02562 177 RELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYD-----------------ELVEEAKTIKAEIEEL 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 963 EEQLEEEEaarqkLQLEKVTAEakIKKLEDEILVMDDQNNKLSKERKLLEE---------RISDLTTNLAEEEEKAKNLT 1033
Cdd:PHA02562 240 TDELLNLV-----MDIEDPSAA--LNKLNTAAAKIKSKIEQFQKVIKMYEKggvcptctqQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1034 KLKNKHESMISELEVRLKKEEKSRQELEKLKRKLE---GDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEI 1110
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKIStnkQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|...
gi 92091586 1111 AQKNNALKKIRELeGHISDLQED 1133
Cdd:PHA02562 393 KTKSELVKEKYHR-GIVTDLLKD 414
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
989-1340 |
8.08e-04 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 44.08 E-value: 8.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 989 KLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEkakNLTKLKNKHESMIS--ELEVRLKKEEKSrqeLEKLKRK 1066
Cdd:pfam03148 61 ELEKELEELDEEIELLLEEKRRLEKALEALEEPLHIAQE---CLTLREKRQGIDLVhdEVEKELLKEVEL---IEGIQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1067 LEGDASDFHEQIADLQAQIAELKMQLAKKEE-----ELQAALARLDDEIAQKNNALKkireLEGHISDLQEDLDSERAAR 1141
Cdd:pfam03148 135 LQRTLEQAWEQLRLLRAARHKLEKDLSDKKEaleidEKCLSLNNTSPNISYKPGPTR----IPPNSSTPEEWEKFTQDNI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1142 NKAEKQKRDLgeelEALKTELEDTLdstatqqelrakreqevtvlkkaldeetrsheAQVQEMRQKHAQAVEE-LTEQLE 1220
Cdd:pfam03148 211 ERAEKERAAS----AQLRELIDSIL--------------------------------EQTANDLRAQADAVNFaLRKRIE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1221 QFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKK----KLEAQVQ----ELqskCSDgeRARAELNDKVHKL 1292
Cdd:pfam03148 255 ETEDAKNKLEWQLKKTLQEIAELEKNIEALEKAIRDKEAPLKlaqtRLENRTYrpnvEL---CRD--EAQYGLVDEVKEL 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 92091586 1293 QNEVESVTGMLNEAEgkaiklakdvASLsSQLQDTQELLQEETRQKLN 1340
Cdd:pfam03148 330 EETIEALKQKLAEAE----------ASL-QALERTRLRLEEDIAVKAN 366
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
874-1072 |
8.19e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.17 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 874 RQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAE--------AEEMRVRlaakKQELEEilhEMEARLEEEEDRG 945
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREEleleqqrrFEEIRLR----KQRLEE---ERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 946 QQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEilvmddqnnKLSKERKLLEErisdlttnLAEE 1025
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEM---------QLAEEQKRLME--------MAEE 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 92091586 1026 EEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDAS 1072
Cdd:pfam15709 475 ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1066-1220 |
8.44e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.25 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1066 KLEGDASDFHEQIADLQAQIAELKMQLAKK-EEELQAALARLDDEIAQKNNALKKIRE-----LEGHISDLQEDLDSE-R 1138
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRlEKETEALRERLQKDLEEVRAKLEPYLEelqakLGQNVEELRQRLEPYtE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1139 AARNKAEKQKRDLGEELEALKTELEDTLDSTATQ---------QELRAKREQEVTVLKKALDEETRSHEAQ----VQEMR 1205
Cdd:pfam01442 81 ELRKRLNADAEELQEKLAPYGEELRERLEQNVDAlrarlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQELR 160
|
170
....*....|....*
gi 92091586 1206 QKHAQAVEELTEQLE 1220
Cdd:pfam01442 161 EKLEPQAEDLREKLD 175
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1649-1849 |
8.54e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1649 EAIKQLRKLQAQMKDFQRELEDARASRDEIFATA-KENEkkakslEADLMQLQEDLAAAERARKQADLEKEELAEELASS 1727
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAAAlQPGE------EEELEEERRRLSNAEKLREALQEALEALSGGEGGA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1728 LSgrnALQDEKRRLEaRIAQleeeleeEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLE-RQN----- 1801
Cdd:COG0497 243 LD---LLGQALRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEFDPERLEEVEeRLAllrrl 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 1802 ---------------KELRSKLHEMEGAvkskfKSTIAALEAKIAQLEEQVEQEARE-----KQAATK 1849
Cdd:COG0497 312 arkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaarKKAAKK 374
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1055-1272 |
9.30e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1055 KSRQELEKLKRKLEGDASDFHEQIADLQAQIAEL-KMQLAKKE-EELQAALARLD--DEIAQK-NNALKKIRELEGHISD 1129
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEERRRLSnaEKLREAlQEALEALSGGEGGALD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1130 LQEDLDSERAARNKAEKQKRDLGEELEALKTELED---TLDSTATQQELRAKREQEVtvlkkaldeETRSheAQVQEMRQ 1206
Cdd:COG0497 245 LLGQALRALERLAEYDPSLAELAERLESALIELEEaasELRRYLDSLEFDPERLEEV---------EERL--ALLRRLAR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1207 KHAQAVEELTEQLEQFKRAKANL---DKNKQTLEKENADLAGELRVLGQAKQEVEHKK-KKLEAQV-QELQ 1272
Cdd:COG0497 314 KYGVTVEELLAYAEELRAELAELensDERLEELEAELAEAEAELLEAAEKLSAARKKAaKKLEKAVtAELA 384
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1818-1936 |
9.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1818 KFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKG-NAR--------VKQ 1888
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKeyealqkeIES 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 92091586 1889 LKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1936
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1450-1895 |
9.43e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1450 VSNLEKKQRKFDQLLAEEKNISS---KYADERDRAEAEAREKETKAlslARALEEALEAKEELERTNKMLKAemedlVSS 1526
Cdd:COG3096 274 MRHANERRELSERALELRRELFGarrQLAEEQYRLVEMARELEELS---ARESDLEQDYQAASDHLNLVQTA-----LRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1527 KDDVGKNVHELEKSKRALETQMEemktQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARDEQneeKRRQLQRQlh 1606
Cdd:COG3096 346 QEKIERYQEDLEELTERLEEQEE----VVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQ---QTRAIQYQ-- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1607 EYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARA-----SRDEIFAT 1681
Cdd:COG3096 417 QAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKiagevERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1682 AKENEKKAKSLEA---DLMQLQEDLAAAERA---RKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQleeeleee 1755
Cdd:COG3096 497 ARELLRRYRSQQAlaqRLQQLRAQLAELEQRlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE-------- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1756 qgnmeaMSDRVRKATQQAEQLSNELaterstaqknesarQQLERQNKELRSKLHEMegavkskfkstiAALEAKIAQLEE 1835
Cdd:COG3096 569 ------LEEQAAEAVEQRSELRQQL--------------EQLRARIKELAARAPAW------------LAAQDALERLRE 616
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1836 QVEQEAREKQAATKSLKQkdkklkeillQVEDERKmAEQYKEQAEkgnARVKQLKRQLEE 1895
Cdd:COG3096 617 QSGEALADSQEVTAAMQQ----------LLERERE-ATVERDELA---ARKQALESQIER 662
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1536-1935 |
1.01e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.19 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1536 ELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFErdlQARDEQNEEKRRQLQRQLHEYETELEDE 1615
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1616 RKQRALaaaakkklegdlkdleLQADSAikGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakeneKKAKSLEAD 1695
Cdd:TIGR00618 327 LMKRAA----------------HVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATSIREIS--------CQQHTLTQH 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1696 LMQLQEDLAAAE---RARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQ 1772
Cdd:TIGR00618 381 IHTLQQQKTTLTqklQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1773 AEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQeaREKQAATKSLK 1852
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLT--RRMQRGEQTYA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1853 QKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1932
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL 618
|
...
gi 92091586 1933 SKL 1935
Cdd:TIGR00618 619 RKL 621
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1788-1936 |
1.03e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1788 QKNESARQQLERQNKELRSKLHEMEGAVK------SKFKSTIAALEAKIAQLEEQVEQ-EAREKQAATKSLKQKD-KKLK 1859
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAalearlEAAKTELEDLEKEIKRLELEIEEvEARIKKYEEQLGNVRNnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1860 EILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLR 1936
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1150-1282 |
1.03e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1150 DLGEELEALKTELEDTLdstatqQELRAKReQEVTVLKKALDEETRS----HEAQVQEMRQKHAQAVEELTEQLEQFKRA 1225
Cdd:PRK00409 520 ELIASLEELERELEQKA------EEAEALL-KEAEKLKEELEEKKEKlqeeEDKLLEEAEKEAQQAIKEAKKEADEIIKE 592
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1226 KANLDKNKQTLEKENaDLAGELRVLGQAKQEVEHKKKKLEAQVQELQSkcsdGERAR 1282
Cdd:PRK00409 593 LRQLQKGGYASVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELKV----GDEVK 644
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
971-1112 |
1.05e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.30 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 971 AARQKLQLEKVTAEakIKKLEDEILVMDDQNNKLSKERKLL-EERISDLTTNLAEEEEKaknltklknkhesmISELEVR 1049
Cdd:COG0542 399 AARVRMEIDSKPEE--LDELERRLEQLEIEKEALKKEQDEAsFERLAELRDELAELEEE--------------LEALKAR 462
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 92091586 1050 LKKEEKSRQELEKLKRKLEGDasdfHEQIADLQAQIAELKMQLAKKEEELQAALArlDDEIAQ 1112
Cdd:COG0542 463 WEAEKELIEEIQELKEELEQR----YGKIPELEKELAELEEELAELAPLLREEVT--EEDIAE 519
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1070-1215 |
1.06e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.50 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1070 DASDFHEQIADLQAQIAELKMQLAKKE---------EELQAALARLDDEIAQKNNALKKIREL--EGHISdlQEDLDSER 1138
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARLEaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALykKGAVS--QQELDEAR 154
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1139 AARNKAEKQkrdlgeeLEALKTELEDTLDSTATQQELRAKreqevtvlkkaldeetrshEAQVQEMRQKHAQAVEEL 1215
Cdd:COG1566 155 AALDAAQAQ-------LEAAQAQLAQAQAGLREEEELAAA-------------------QAQVAQAEAALAQAELNL 205
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
853-1298 |
1.25e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQKTKERqqkaeneLKELEQKHSQLTEeknlLQEQLQAETELYAEAEEmrvrlaaKKQELEEILH 932
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEAEQ----LRQNLEKQQSSLAEAEQ-------RIKELEFEIQ 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 933 EMEARLEEEEDRGQQLQ--AERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLE---DEILVMDDQNNKLSKE 1007
Cdd:pfam05557 181 SQEQDSEIVKNSKSELAriPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1008 RKLLEERISDLTTNLAEEEEKAKNLTKLKNK---HESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQ 1084
Cdd:pfam05557 261 LQSWVKLAQDTGLNLRSPEDLSRRIEQLQQReivLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1085 IAELKMQLA---KKEEELQAALARLDDEIAQKNNALKK---IRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEAL 1158
Cdd:pfam05557 341 VRRLQRRVLlltKERDGYRAILESYDKELTMSNYSPQLlerIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1159 KTELedTLDSTATQQELRAKREQEVTVLKKALDEetrsHEAQVQEMRQKhaqaVEELTEQLEQFK-RAKANLDKNKQTLE 1237
Cdd:pfam05557 421 EREL--QALRQQESLADPSYSKEEVDSLRRKLET----LELERQRLREQ----KNELEMELERRClQGDYDPKKTKVLHL 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1238 KENADLAGELR---VLGQAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVES 1298
Cdd:pfam05557 491 SMNPAAEAYQQrknQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELES 554
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1420-1647 |
1.32e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1420 AAYDKLEKTKNR-LQQELDDLVVDLDN-------QRQLVSNLEK--------KQRKFDQLLAEEKNISSKYADERDRAEA 1483
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHiqqqiktYNKNIEEQRKkngeniarKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1484 EAREKETKALSLARALEEALEAKEELERTNKMLK---------AEMEDLVSSKDDVGK---NVHELEKSKRALETQMEEm 1551
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQISEGPDRITKikdKLKELQHSLEKLDTAIDE- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1552 ktqLEELEDELQATEDAKLRLEVNMQALKGQFER-DLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLE 1630
Cdd:PHA02562 325 ---LEEIMDEFNEQSKKLLELKNKISTNKQSLITlVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
250
....*....|....*....
gi 92091586 1631 GDLKDL--ELQADSAIKGR 1647
Cdd:PHA02562 402 KYHRGIvtDLLKDSGIKAS 420
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1585-1919 |
1.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1585 RDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDF 1664
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1665 QRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEAR 1744
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1745 IAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKSTIA 1824
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1825 ALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRIN 1904
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDN 353
|
330
....*....|....*
gi 92091586 1905 ANRRKLQRELDEATE 1919
Cdd:COG4372 354 DVLELLSKGAEAGVA 368
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
985-1168 |
1.47e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.82 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 985 AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKlknkhesmiselevRLKKEEKSRQELEKLK 1064
Cdd:pfam13851 26 ELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRK--------------QLENYEKDKQSLKNLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1065 RKLEgdasDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDD---EIAQKnnALKKIRELEGHISDLQEDLDSERAAR 1141
Cdd:pfam13851 92 ARLK----VLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAaiqDVQQK--TGLKNLLLEKKLQALGETLEKKEAQL 165
|
170 180
....*....|....*....|....*..
gi 92091586 1142 NKAEKQKRDLGEELEALKTELEDTLDS 1168
Cdd:pfam13851 166 NEVLAAANLDPDALQAVTEKLEDVLES 192
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1222-1692 |
1.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1222 FKRAKANLDKNKQTLEkenadlagELRVLGQAKQEVEHkkkKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTG 1301
Cdd:PRK04863 232 FQDMEAALRENRMTLE--------AIRVTQSDRDLFKH---LITESTNYVAADYMRHANERRVHLEEALELRRELYTSRR 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1302 MLNEAEGKAIKLAKDVASLSSQLQDTQELLQeETRQKLN-VSTKLRQLEEErnslqDQLDEEMEAkqnlerhistLNIQL 1380
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEAESDLEQDYQ-AASDHLNlVQTALRQQEKI-----ERYQADLEE----------LEERL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1381 SDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQElddlVVDLDNQRQLVSNLEKKQRKF 1460
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQA----VQALERAKQLCGLPDLTADNA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1461 DQLLAEEKNISSKYADERDRAE------AEAREKETKALSLARAleealeakeelertnkmLKAEMEDlvSSKDDVGKNV 1534
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEqklsvaQAAHSQFEQAYQLVRK-----------------IAGEVSR--SEAWDVAREL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1535 HELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLevnmQALKGQFERDLQARDEQnEEKRRQLQRQLHEYETELED 1614
Cdd:PRK04863 502 LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLL----AEFCKRLGKNLDDEDEL-EQLQEELEARLESLSESVSE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1615 ERKQRALAAAAKKKLEGDLKDLELQA-------DSAIKGRE---EAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKE 1684
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARApawlaaqDALARLREqsgEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
....*...
gi 92091586 1685 NEKKAKSL 1692
Cdd:PRK04863 657 LDEEIERL 664
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1823-1928 |
1.57e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1823 IAALEAKIAQLEEQVEQEAREKQAATKSLKQKDK-KLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQ 1901
Cdd:COG0542 406 IDSKPEELDELERRLEQLEIEKEALKKEQDEASFeRLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYG 485
|
90 100
....*....|....*....|....*..
gi 92091586 1902 RINANRRKLQrELDEATESNEAMGREV 1928
Cdd:COG0542 486 KIPELEKELA-ELEEELAELAPLLREE 511
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1823-1929 |
1.77e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1823 IAALEAKIAQLEEQVEQEAREKQAATKslkqkdKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQR 1902
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASF------ERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
|
90 100
....*....|....*....|....*..
gi 92091586 1903 INAnrrkLQRELDEATESNEAMGREVN 1929
Cdd:COG0542 487 IPE----LEKELAELEEELAELAPLLR 509
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1126-1908 |
1.91e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1126 HISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTAT-------------QQELRAKREQeVTVLKKALDE 1192
Cdd:NF041483 16 HLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASrpaydgadigyqaEQLLRNAQIQ-ADQLRADAER 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1193 ETRSHEAQVQEMRQKHAQAVEEL-----TEQLEQFKRAKANLDKNKQTLE---KENADLAGEL---------RVLGQAKQ 1255
Cdd:NF041483 95 ELRDARAQTQRILQEHAEHQARLqaelhTEAVQRRQQLDQELAERRQTVEshvNENVAWAEQLrartesqarRLLDESRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1256 EVEHKKKKLEAQVQEL-----QSKCSDGERARAELNDKVHKLQNEVESvtgMLNEAEGKaiklAKDVASLSSQLQDTQEL 1330
Cdd:NF041483 175 EAEQALAAARAEAERLaeearQRLGSEAESARAEAEAILRRARKDAER---LLNAASTQ----AQEATDHAEQLRSSTAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1331 LQEETRQKlnvSTKLRQLEEERnsLQDQLDEEMEAKQNLERhistlniQLSDSKKKLQDFASTVEALEEGKKRFQK-EIE 1409
Cdd:NF041483 248 ESDQARRQ---AAELSRAAEQR--MQEAEEALREARAEAEK-------VVAEAKEAAAKQLASAESANEQRTRTAKeEIA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1410 NLTQQYEEKAaaydklEKTKNRLQQELDDLVVDLDnqrQLVSNLEKKQRkfdQLLAEEKnisskyADERDRAEAEAREKE 1489
Cdd:NF041483 316 RLVGEATKEA------EALKAEAEQALADARAEAE---KLVAEAAEKAR---TVAAEDT------AAQLAKAARTAEEVL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1490 TKALSLARALEEALEAKEELERTNKmlKAEMEDLVSSKDDVGknvhelEKSKRALETQMEEMKTQLEELEDELQatedaK 1569
Cdd:NF041483 378 TKASEDAKATTRAAAEEAERIRREA--EAEADRLRGEAADQA------EQLKGAAKDDTKEYRAKTVELQEEAR-----R 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1570 LRLEVNmqalkgQFERDLQARDEQ-NEEKRRQLQRQLHEYETELEDerkqralaaaAKKKLEGDLKDLELQADS-AIKGR 1647
Cdd:NF041483 445 LRGEAE------QLRAEAVAEGERiRGEARREAVQQIEEAARTAEE----------LLTKAKADADELRSTATAeSERVR 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1648 EEAIKQLRKLQAQMKDfqrELEDARASRDEIFATAKENEKKAKS-LEADLMQLQEDLAAAERARK-QADLEKEELAEELA 1725
Cdd:NF041483 509 TEAIERATTLRRQAEE---TLERTRAEAERLRAEAEEQAEEVRAaAERAARELREETERAIAARQaEAAEELTRLHTEAE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1726 SSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAmsDRVRKATQQAEQLSNELATErsTAQKNESARQQLERQNKELR 1805
Cdd:NF041483 586 ERLTAAEEALADARAEAERIRREAAEETERLRTEAA--ERIRTLQAQAEQEAERLRTE--AAADASAARAEGENVAVRLR 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1806 SKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLqvEDERKMAEQYKEQA-EKGNA 1884
Cdd:NF041483 662 SEAAAEAERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETL--GSARAEADQERERArEQSEE 739
|
810 820
....*....|....*....|....*.
gi 92091586 1885 RVKQLKRQLEEAEEESQRI--NANRR 1908
Cdd:NF041483 740 LLASARKRVEEAQAEAQRLveEADRR 765
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1768-1935 |
1.92e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.36 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1768 KATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEgavKSKFKSTIAALEAKIAQLEEQVEQEAREKQAA 1847
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKE---REELGATMLALSQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1848 TKSLKQKDKKLKEillQVEDERKMAEQYKEQaekgnarVKQLKRQLEEAEEESQRInanRRKLQRELDEATESNEAMGRE 1927
Cdd:pfam15964 430 VSQLEEAQKQLAS---QEMDVTKVCGEMRYQ-------LNQTKMKKDEAEKEHREY---RTKTGRQLEIKDQEIEKLGLE 496
|
....*...
gi 92091586 1928 VNALKSKL 1935
Cdd:pfam15964 497 LSESKQRL 504
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1263-1444 |
1.98e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 42.03 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1263 KLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVS 1342
Cdd:pfam17078 21 QLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESNKQLKKRLENSS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1343 TKLRQLEEERNSLQDQ----LDEEMEAKQNLERHISTLNIQLSDSKKKLQDFastVEALEEGKKRFQKEIENLTQQYEEK 1418
Cdd:pfam17078 101 ASETTLEAELERLQIQydalVDSQNEYKDHYQQEINTLQESLEDLKLENEKQ---LENYQQRISSNDKDIDTKLDSYNNK 177
|
170 180
....*....|....*....|....*..
gi 92091586 1419 AAAYDKLEKTKN-RLQQELDDLVVDLD 1444
Cdd:pfam17078 178 FKNLDNIYVNKNnKLLTKLDSLAQLLD 204
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1639-1929 |
2.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1639 QADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKE 1718
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1719 ELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELAterstAQKNESARQQLE 1798
Cdd:COG4372 112 ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ-----ALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1799 RQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQ 1878
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1879 AEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVN 1929
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1552-1848 |
2.07e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1552 KTQLEELEDELQATEDAKLRLEVNMQALkgqfERDLQARdeqnEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEG 1631
Cdd:PRK05035 435 KAEIRAIEQEKKKAEEAKARFEARQARL----EREKAAR----EARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1632 DLKDLELQADSAIKGREEAikqlRKLQAQmkdfqreledARASRDEifATAKENEKKAKsleadlmqlqedlAAAERARK 1711
Cdd:PRK05035 507 VIKAGARPDNSAVIAAREA----RKAQAR----------ARQAEKQ--AAAAADPKKAA-------------VAAAIARA 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1712 QADlekeeLAEELASSLSGRNALQDEKRRLEARIAQLEEeleeeqgnmeamsdrvRKATQQAEQLSNELATERSTAQKNE 1791
Cdd:PRK05035 558 KAK-----KAAQQAANAEAEEEVDPKKAAVAAAIARAKA----------------KKAAQQAASAEPEEQVAEVDPKKAA 616
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1792 ----SARQQLERQNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQL---EEQVEQEAREKQAAT 1848
Cdd:PRK05035 617 vaaaIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQqqaNAEPEEAEDPKKAAV 680
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1096-1864 |
2.17e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1096 EEELQAALARLDDEIAQKnnaLKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQEL 1175
Cdd:pfam07111 54 ELEGSQALSQQAELISRQ---LQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1176 RAKREQEVtvlKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKqtlekenadlAGELRVLGQAKQ 1255
Cdd:pfam07111 131 RKNLEEGS---QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKR----------AGEAKQLAEAQK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1256 EVEHKKKKLEAQVQELQSKCSDGERARAELNDKVhklQNEVESVTGMLNEAEgkAIKLAKDVASLSSQLQDTQELLQEET 1335
Cdd:pfam07111 198 EAELLRKQLSKTQEELEAQVTLVESLRKYVGEQV---PPEVHSQTWELERQE--LLDTMQHLQEDRADLQATVELLQVRV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1336 rQKLNVSTKLRQLEEERN-SLQDQLDEEMEAK-----QNLERHISTLNIQL-------SDSKKKLQDfasTVEALEEGKK 1402
Cdd:pfam07111 273 -QSLTHMLALQEEELTRKiQPSDSLEPEFPKKcrsllNRWREKVFALMVQLkaqdlehRDSVKQLRG---QVAELQEQVT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1403 RFQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKkQRKFdqllaeeknISSKYADERDRAE 1482
Cdd:pfam07111 349 SQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEE-QLKF---------VVNAMSSTQIWLE 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1483 AeareketkalSLARALEEALEAKEELERTNKMLKA--EMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELED 1560
Cdd:pfam07111 419 T----------TMTRVEQAVARIPSLSNRLSYAVRKvhTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1561 ElqatedaKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQralaaaakkklegdLKDLELQA 1640
Cdd:pfam07111 489 E-------RNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQES--------------LASVGQQL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1641 DSAIKGREEAIKQLRKLQAQMKDFQreledarasrdEIFATAkenekkaksleadlmqLQEDLAAAE-RARKQadlekee 1719
Cdd:pfam07111 548 EVARQGQQESTEEAASLRQELTQQQ-----------EIYGQA----------------LQEKVAEVEtRLREQ------- 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1720 laeelasslsgrnaLQDEKRRL-EARIAQLEEELEEEQGNmeamsdrvRKATQQAEQlSNELATERSTAQKNESAR---- 1794
Cdd:pfam07111 594 --------------LSDTKRRLnEARREQAKAVVSLRQIQ--------HRATQEKER-NQELRRLQDEARKEEGQRlarr 650
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1795 -QQLERQNKELRSKLHEMEGAVKSKFKSTIAAL----EAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQ 1864
Cdd:pfam07111 651 vQELERDKNLMLATLQQEGLLSRYKQQRLLAVLpsglDKKSVVSSPRPECSASAPIPAAVPTRESIKGSLTVLLD 725
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1562-1905 |
2.22e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 42.70 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1562 LQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQAD 1641
Cdd:COG0840 6 LLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1642 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELA 1721
Cdd:COG0840 86 LALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1722 EELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSN-ELATERSTAQKNESArqQLERQ 1800
Cdd:COG0840 166 LLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEgDLTVRIDVDSKDEIG--QLADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1801 NKELRSKLHEMEGAVKS---KFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKE 1877
Cdd:COG0840 244 FNRMIENLRELVGQVREsaeQVASASEELAASAEELAAGAEEQAASLEETAAAMEELSATVQEVAENAQQAAELAEEASE 323
|
330 340
....*....|....*....|....*...
gi 92091586 1878 QAEKGNARVKQLKRQLEEAEEESQRINA 1905
Cdd:COG0840 324 LAEEGGEVVEEAVEGIEEIRESVEETAE 351
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1390-1714 |
2.32e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.75 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1390 FASTVEALEEGKKR---FQKEIENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLdnqRQLVSNLEKKQRKFDQLLAE 1466
Cdd:pfam19220 36 IEAILRELPQAKSRlleLEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARL---AKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1467 EKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsskddvgknvHELEKSKRALET 1546
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERL-----------ALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1547 QMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFERDLQARdeqneekrrqlQRQLHEYETELEDERKQRALAAAAk 1626
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAER-----------ERAEAQLEEAVEAHRAERASLRMK- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1627 kklegdLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIfatakenEKKAKSLEADLMQLQEDLAAA 1706
Cdd:pfam19220 250 ------LEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTL-------ERRLAGLEADLERRTQQFQEM 316
|
....*...
gi 92091586 1707 ERARKQAD 1714
Cdd:pfam19220 317 QRARAELE 324
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1813-1933 |
2.64e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 42.92 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1813 GAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQ 1892
Cdd:COG5283 6 GAVDKPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQAGIDTRQLSAA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 92091586 1893 LEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKS 1933
Cdd:COG5283 86 QRRLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR 126
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
972-1221 |
2.72e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.75 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 972 ARQKLQLEKVTAE-AKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTT-NLAEEEEKAknltkLKNKHEsmiselevR 1049
Cdd:COG0497 151 AGLEELLEEYREAyRAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEEEE-----LEEERR--------R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1050 LKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELkmqlAKKEEELQAALARLDDEIAQKNNAlkkIRELEGHISD 1129
Cdd:COG0497 218 LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLESALIELEEA---ASELRRYLDS 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1130 LqeDLDSERAA-----RNKAEKQKRDLG---EELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETrsheAQV 1201
Cdd:COG0497 291 L--EFDPERLEeveerLALLRRLARKYGvtvEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----EKL 364
|
250 260
....*....|....*....|.
gi 92091586 1202 QEMRQKHAQAVEE-LTEQLEQ 1221
Cdd:COG0497 365 SAARKKAAKKLEKaVTAELAD 385
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1516-1663 |
2.78e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1516 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRL---EVNMQALKGQFE---RDLQA 1589
Cdd:pfam05667 340 LQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVE 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1590 RDEQNEEKRRQL---QRQLHEYETELEDERKQRALAAAAkkklegdLKDLELQADSAIKGREEAIKQlrkLQAQMKD 1663
Cdd:pfam05667 420 LAGQWEKHRVPLieeYRALKEAKSNKEDESQRKLEEIKE-------LREKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
983-1266 |
2.96e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 983 AEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKaknLTKLKNKHEsmisELEVRLKKEEKSRQELEK 1062
Cdd:PTZ00440 1054 MKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNK---LIEIKNKSH----EHVVNADKEKNKQTEHYN 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1063 LKRKlegDASDFHEQIADLQAQIAELKMQLAKKEE----ELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSer 1138
Cdd:PTZ00440 1127 KKKK---SLEKIYKQMEKTLKELENMNLEDITLNEvneiEIEYERILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQ-- 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1139 aARNKAEKQKRDLGEELE---------ALKTELEDTLDSTATQQEL--RAKREQEVTVLKKALDEETRSHEAQVQEMRQK 1207
Cdd:PTZ00440 1202 -VKKNMSKERNDHLTTFEynayydkatASYENIEELTTEAKGLKGEanRSTNVDELKEIKLQVFSYLQQVIKENNKMENA 1280
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92091586 1208 HAQaVEELTEQLEQFK--RAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEA 1266
Cdd:PTZ00440 1281 LHE-IKNMYEFLISIDseKILKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKE 1340
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1199-1362 |
3.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1199 AQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRvlgQAKQEVEHKKKKLEA-----QVQELQS 1273
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE---EVEARIKKYEEQLGNvrnnkEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1274 KCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEEtrqklnvstkLRQLEEERN 1353
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE----------LEELEAERE 166
|
....*....
gi 92091586 1354 SLQDQLDEE 1362
Cdd:COG1579 167 ELAAKIPPE 175
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1222-1694 |
3.22e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1222 FKRAKANLDKNKQTLEkenadlagELRVlgqaKQEVEHKKKKLEAQVQELQSkcSDGERARAELNDKVhklqnevesvtg 1301
Cdd:COG3096 231 FQDMEAALRENRMTLE--------AIRV----TQSDRDLFKHLITEATNYVA--ADYMRHANERRELS------------ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1302 mlneaeGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVSTKLRQLEEERNSLQDQLDEEMEAKQNLErhistlniqls 1381
Cdd:COG3096 285 ------ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE----------- 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1382 dskkKLQDFASTVEALEEgKKRFQKEI-ENLTQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQ-------RQLVSNL 1453
Cdd:COG3096 348 ----KIERYQEDLEELTE-RLEEQEEVvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyQQAVQAL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1454 EKKQRkfdqlLAEEKNISSKYADERdRAEAEAREKE--TKALSLARALEEALEAKEELERTNKMLKAeMEDLVSSKD--D 1529
Cdd:COG3096 423 EKARA-----LCGLPDLTPENAEDY-LAAFRAKEQQatEEVLELEQKLSVADAARRQFEKAYELVCK-IAGEVERSQawQ 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1530 VGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvnmqALKGQFERDLQARDEQnEEKRRQLQRQLHEYE 1609
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEEL-EELLAELEAQLEELE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1610 TELEDERKQRALAAAAKKKLEGDLKDLELQA-------DSAIKGREEAIKQLRKLQAQMKDFQRELEDARA---SRDEIF 1679
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAAMQQLLEREREatvERDELA 650
|
490
....*....|....*
gi 92091586 1680 ATAKENEKKAKSLEA 1694
Cdd:COG3096 651 ARKQALESQIERLSQ 665
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
984-1073 |
3.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 984 EAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKL 1063
Cdd:COG2433 419 EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
90
....*....|
gi 92091586 1064 KRKLEGDASD 1073
Cdd:COG2433 499 KELWKLEHSG 508
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1284-1491 |
3.47e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1284 ELNDKVHKLQNE-VESVTGMLNEAEGKAIKLAKDVASLSS--------QLQDTQELLQEETRQKLNVSTKLRQLEEERNS 1354
Cdd:PRK05771 32 HIEDLKEELSNErLRKLRSLLTKLSEALDKLRSYLPKLNPlreekkkvSVKSLEELIKDVEEELEKIEKEIKELEEEISE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1355 LQDQLDEemeakqnLERHISTL----NIQLSDSkkKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEK--- 1427
Cdd:PRK05771 112 LENEIKE-------LEQEIERLepwgNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYVyvv 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1428 --TKNRLQQELDDLVVDLDNQR----------QLVSNLEKK----QRKFDQLLAEEKNISSKYAD-----------ERDR 1480
Cdd:PRK05771 183 vvVLKELSDEVEEELKKLGFERleleeegtpsELIREIKEEleeiEKERESLLEELKELAKKYLEellalyeyleiELER 262
|
250
....*....|.
gi 92091586 1481 AEAEAREKETK 1491
Cdd:PRK05771 263 AEALSKFLKTD 273
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1071-1284 |
3.50e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.99 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1071 ASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQK-- 1148
Cdd:PRK11637 42 ASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQaa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1149 --RDLGEELEAL-----KTELEDTLDSTATQQE---------LRAKREQEVTVLKKaldeeTRSH-EAQVQEMRQKHAQA 1211
Cdd:PRK11637 122 qeRLLAAQLDAAfrqgeHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQ-----TREElAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 92091586 1212 VEELTEQLEQfkrakanldknKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDGER---ARAE 1284
Cdd:PRK11637 197 KTLLYEQQAQ-----------QQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEReakARAE 261
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1325-1792 |
3.58e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.34 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1325 QDTQELLQEETRQKLNVSTKLR------------QLEEERnsLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAS 1392
Cdd:PTZ00108 900 EDYKEFLESETLKEKDVIVDYRdystantvhftvKLNDGV--LEQWEEEGIEKVFKLKSTISTTNMVLFDENGKIKKYSD 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1393 TVEALEEgkkrFqkeienltqqYEEKAAAYdklEKTKNRLQQELDDLVVDLDNQRQLV-----SNLEKKQRKFDQLLAE- 1466
Cdd:PTZ00108 978 ALDILKE----F----------YLVRLDLY---KKRKEYLLGKLERELARLSNKVRFIkhvinGELVITNAKKKDLVKEl 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1467 EKNISSKYADERDRAEAE--AREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLvsSKDDVGKNVHELEKSKRAL 1544
Cdd:PTZ00108 1041 KKLGYVRFKDIIKKKSEKitAEEEEGAEEDDEADDEDDEEELGAAVSYDYLLSMPIWSL--TKEKVEKLNAELEKKEKEL 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1545 E----TQMEEM-KTQLEELEDELQATE--DAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERK 1617
Cdd:PTZ00108 1119 EklknTTPKDMwLEDLDKFEEALEEQEevEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNS 1198
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1618 QRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKlqAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLM 1697
Cdd:PTZ00108 1199 KRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKK--SSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPK 1276
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1698 QLQEDLAAAERARKQADlekeelAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLS 1777
Cdd:PTZ00108 1277 RVSAVQYSPPPPSKRPD------GESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSS 1350
|
490
....*....|....*
gi 92091586 1778 NELATERSTAQKNES 1792
Cdd:PTZ00108 1351 RLLRRPRKKKSDSSS 1365
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
872-1145 |
3.60e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 872 KERQQKAENELKELEQKHSQ---LTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEEDRGQQL 948
Cdd:pfam19220 114 RDKTAQAEALERQLAAETEQnraLEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 949 QAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIkkledeilvmDDQNNKLSKERKLLEERISDLTTNLAEEEEK 1028
Cdd:pfam19220 194 TRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQL----------EEAVEAHRAERASLRMKLEALTARAAATEQL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1029 AKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQ---LAKKEEELQAALAR 1105
Cdd:pfam19220 264 LAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERaemLTKALAAKDAALER 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 92091586 1106 LDDEIA---QKNNALKKIRE-----LEGHISDLQEDLDSERAARNKAE 1145
Cdd:pfam19220 344 AEERIAslsDRIAELTKRFEveraaLEQANRRLKEELQRERAERALAQ 391
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1136-1369 |
3.84e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 42.15 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1136 SERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKR-EQEVTVLKKALdeetrsheaqvqemrQKHAQAVEE 1214
Cdd:pfam09726 356 TSSSSSKNSKKQKGPGGKSGARHKDPAENCIPNNQLSKPDALVRlEQDIKKLKAEL---------------QASRQTEQE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1215 LTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQE---------------------------VEHKKKKLE-- 1265
Cdd:pfam09726 421 LRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKdkqtvqqlekrlkaeqearasaekqlaEEKKRKKEEea 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1266 ------AQVQELQSKCSDG-ERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKL------AKDVASLSSQLQDTQEL-- 1330
Cdd:pfam09726 501 taaravALAAASRGECTESlKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELrkykesEKDTEVLMSALSAMQDKnq 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 92091586 1331 -----LQEETRQKLNVSTKL----RQLEEERNSLQDQLDEEMEAKQNL 1369
Cdd:pfam09726 581 hlensLSAETRIKLDLFSALgdakRQLEIAQGQIYQKDQEIKDLKQKI 628
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1009-1159 |
4.03e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1009 KLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASD----FHEQIADLQAQ 1084
Cdd:smart00787 140 KLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTeldrAKEKLKKLLQE 219
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1085 IAELKMQLAKKEEELQAalarLDDEIAQKNNalkKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1159
Cdd:smart00787 220 IMIKVKKLEELEEELQE----LESKIEDLTN---KKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1023-1361 |
4.09e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1023 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1102
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1103 LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQE 1182
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1183 VTVLKKAL----DEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVE 1258
Cdd:COG4372 166 LAALEQELqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1259 HKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQK 1338
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|...
gi 92091586 1339 LNVSTKLRQLEEERNSLQDQLDE 1361
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLV 348
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1011-1143 |
4.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.49 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1011 LEERISDLTTNLAEEEEKAKNLtklknkhESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHE-------------- 1076
Cdd:PRK09039 58 LNSQIAELADLLSLERQGNQDL-------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGragelaqeldsekq 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92091586 1077 -------QIADLQAQIAELKMQLAKKEEELQAALARlddeiaqknnalkkIRELEGHISDLQEDLDSERAARNK 1143
Cdd:PRK09039 131 vsaralaQVELLNQQIAALRRQLAALEAALDASEKR--------------DRESQAKIADLGRRLNVALAQRVQ 190
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
853-989 |
4.32e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 853 QVTRQEEEMQAKEDELQktkERQQKAENE-LKELEQKHSQLTEEKNLLQEQLQAETE---------LYAEAEEMRVRLAA 922
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQ---ERLKQLEKErLAAQEQKKQAEEAAKQAALKQKQAEEAaakaaaaakAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 92091586 923 KKQELE-EILHEMEARLEEEEDRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQlEKVTAEAKIKK 989
Cdd:PRK09510 161 KKAAAEaKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAK-KKAAAEAKAAA 227
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
987-1297 |
4.33e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.20 E-value: 4.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 987 IKKLEDEILVMD-------DQNNKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEvRLKKEEKSRQE 1059
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLE-KLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1060 LEK-LKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEElQAALARLDDEIAQKNNALkkiRELEGHISDLQEDLdser 1138
Cdd:PLN02939 216 TEGlCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAET-EERVFKLEKERSLLDASL---RELESKFIVAQEDV---- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1139 aarNKAEKQKRD-LGEELEalktELEDTLDSTATQQelrakrEQEVTVLKkaldeetrsheaQVQEMRQKhaqaVEELTE 1217
Cdd:PLN02939 288 ---SKLSPLQYDcWWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDKLEA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1218 QLEQfkrakANLDKnkqtLEKENADLagelrvlgqAKQEVEHKKKKLEAQVQELQSKCSDGERARAELNDKVHKLQNEVE 1297
Cdd:PLN02939 339 SLKE-----ANVSK----FSSYKVEL---------LQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1352-1592 |
4.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1352 RNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFAST--VEALEEGKKRFQKEIENLTQQYEEKAAAYDKLEKTK 1429
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1430 NRLQQELDDLVVDLDNQRQLVSNLEKKQRkFDQLLAEEKNISSKYADE-RDRAEAEAREKETKALslaraleealeakee 1508
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQ-LAELEAELAELSARYTPNhPDVIALRAQIAALRAQ--------------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1509 lertnkmLKAEMEDLVSSkddvgknvheLEKSKRALETQMEEMKTQLEELEDELQ---ATEDAKLRLEVNMQALKGQFER 1585
Cdd:COG3206 307 -------LQQEAQRILAS----------LEAELEALQAREASLQAQLAQLEARLAelpELEAELRRLEREVEVARELYES 369
|
....*..
gi 92091586 1586 DLQARDE 1592
Cdd:COG3206 370 LLQRLEE 376
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
978-1240 |
4.75e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 978 LEKVTAEAKIKKLEDEIlvmddqnnKLSKERKLLEERISDLTTNLAEEEEKAKNLTKLKNKHESMISELEVRLKkeeksr 1057
Cdd:PRK05771 59 LDKLRSYLPKLNPLREE--------KKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1058 qELEKLKrKLEGDASDF-------------HEQIADLQAQIAELK----------------MQLAKKEEELQAALARLD- 1107
Cdd:PRK05771 125 -RLEPWG-NFDLDLSLLlgfkyvsvfvgtvPEDKLEELKLESDVEnveyistdkgyvyvvvVVLKELSDEVEEELKKLGf 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1108 --DEIAQKNNALKKIRELEGHISDLqedldseraarnkaEKQKRDLGEELEALKTELEDTLdsTATQQELRAKREQEVTV 1185
Cdd:PRK05771 203 erLELEEEGTPSELIREIKEELEEI--------------EKERESLLEELKELAKKYLEEL--LALYEYLEIELERAEAL 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 92091586 1186 LKKALDEETRSHEAQVQEMRqkhaqaVEELTEQLEQFKRAKANLDKNKQTLEKEN 1240
Cdd:PRK05771 267 SKFLKTDKTFAIEGWVPEDR------VKKLKELIDKATGGSAYVEFVEPDEEEEE 315
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1530-1695 |
5.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1530 VGKNVHELEKSKRALETQmEEMKTQLEELEDELQATEDAKLrLEVN--MQALKGQFERDLQARDEQNEEKRRQLQRQLHE 1607
Cdd:PRK12704 20 IGYFVRKKIAEAKIKEAE-EEAKRILEEAKKEAEAIKKEAL-LEAKeeIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1608 YETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRE--LEDARA-SRDEIFATAKE 1684
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKE 177
|
170
....*....|.
gi 92091586 1685 NEKKAKsLEAD 1695
Cdd:PRK12704 178 IEEEAK-EEAD 187
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1536-1907 |
5.30e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1536 ELEKSKRALETQMEEMKTQLEELEDELQATEDAklrlevnmQALKGQFERDLQARDEQNEEkRRQLQRQLHEYETELEDE 1615
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1616 RKQRALAAAAKKKLEGDLKDLELQADSaikgreEAIKQLRKlqaQMKDFQRELEDARASRDEIFATAKENEKKAKSLEAD 1695
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAAPLAAHI------KAVTQIEQ---QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1696 LMQLQEDLAAAERARKQADLEKeelaeelasslsGRNALQDEKRRLEARIAQLeeeleeeQGNMEAMSDRVRKATQQAEQ 1775
Cdd:TIGR00618 344 RRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQHIHTL-------QQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1776 LSNELATERSTAQKNESARQQLERQNKELRSKLhemegavksKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKD 1855
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGQLAHAKKQQELQQ---------RYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQL 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1856 KKLKEILlqvederkmaEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANR 1907
Cdd:TIGR00618 476 QTKEQIH----------LQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1030-1298 |
5.43e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 41.07 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1030 KNLTKLKNKHESMISELEVRLKKEEKSRQEL-EKLKRKLEGDASdfHEQIADLQAQIAELKmqlakkeeELQAALARLDD 1108
Cdd:pfam13949 27 DDLPKLKQRNREILDEAEKLLDEEESEDEQLrAKYGTRWTRPPS--SELTATLRAEIRKYR--------EILEQASESDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1109 EIAQK-NNALKKIRELEGHISDLQEDLDSERAARNKAEKQK-----RDLGEELEALKTELEDTLdstatqQELRAKREQ- 1181
Cdd:pfam13949 97 QVRSKfREHEEDLELLSGPDEDLEAFLPSSRRAKNSPSVEEqvaklRELLNKLNELKREREQLL------KDLKEKARNd 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1182 ---EVTVLKKALDEETRSHEAQVQEMRQKHaqavEELTEQLEQFKRAKANLDKNkqtLEKENADLAGELRVLGQAKQEVE 1258
Cdd:pfam13949 171 disPKLLLEKARLIAPNQEEQLFEEELEKY----DPLQNRLEQNLHKQEELLKE---ITEANNEFLQDKRVDSEKQRQRE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 92091586 1259 HKKKKLEAQVQ---ELQSKCSDGERARAELNDKVHKLQNEVES 1298
Cdd:pfam13949 244 EALQKLENAYDkykELVSNLQEGLKFYNDLTEILEKLLKKVKD 286
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1787-1912 |
5.51e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1787 AQKNESARQQLERQNKELRSKLHEMEGAVKSKFKstiaaleakiaQLEEQVEQEAREKQaatKSLKQKDKKLKEILLQVE 1866
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIH-----------KLRNEFEKELRERR---NELQKLEKRLLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 92091586 1867 DERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRR-KLQR 1912
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLqELER 146
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1366-1686 |
5.74e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 41.68 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1366 KQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENltqqyEEKAAAYDKLEKTKNrlqqelddlvvdldn 1445
Cdd:pfam18971 558 RRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAE-----AKSTGNYDEVKKAQK--------------- 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1446 qrqlvsNLEKKQRKFDQLLAE-EKNISSKYADE-RDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDL 1523
Cdd:pfam18971 618 ------DLEKSLRKREHLEKEvEKKLESKSGNKnKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDK 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1524 VS--SKD--DVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEvNMQALKGQFerdlqaRDEQNEEKRR 1599
Cdd:pfam18971 692 LEkiSKDlkDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVE-NLNAALNEF------KNGKNKDFSK 764
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1600 QLQRQlheyeTELEDERKQRALAAAAKkklegDLKDLELQADSAIKGREEaIKQLRKLQAQMKDFQRELEDARASRDEIF 1679
Cdd:pfam18971 765 VTQAK-----SDLENSVKDVIINQKVT-----DKVDNLNQAVSVAKAMGD-FSRVEQVLADLKNFSKEQLAQQAQKNEDF 833
|
....*..
gi 92091586 1680 ATAKENE 1686
Cdd:pfam18971 834 NTGKNSE 840
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1264-1596 |
5.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1264 LEAQVQELQSKCSDGERARAELNDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLSSQLQDTQELLQEETRQKLNVST 1343
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1344 KLRQLEEERNSLQDQLDEEMEAKQNLERHISTLNIQLSDSKKKLQDFASTVEALEEGKKRFQKEIENLTQQYEEKAAAYD 1423
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1424 KLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADER----DRAEAEAREKETKALSLARAL 1499
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEleedKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1500 EEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQAL 1579
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330
....*....|....*..
gi 92091586 1580 KGQFERDLQARDEQNEE 1596
Cdd:COG4372 349 GLLDNDVLELLSKGAEA 365
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
856-959 |
5.90e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.90 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 856 RQEEEMQAkeDELQKTKERQQKAENELKELEQKH----SQLTEEKNLLQEQLQAETELYAEAEemrVRLAAKKQELEEIL 931
Cdd:pfam09787 53 RQERDLLR--EEIQKLRGQIQQLRTELQELEAQQqeeaESSREQLQELEEQLATERSARREAE---AELERLQEELRYLE 127
|
90 100
....*....|....*....|....*...
gi 92091586 932 HEMEARLEEEEDRGQQLQAERKKMAQQM 959
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKLRNQL 155
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1827-1937 |
5.95e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1827 EAKIAQLEEQVEQEAREKQAATKSLKqkdkklKEILLQVEDE--RKMAEQYKEQAEKgNARVKQLKRQLEEAEEESQRIN 1904
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIK------KEALLEAKEEihKLRNEFEKELRER-RNELQKLEKRLLQKEENLDRKL 102
|
90 100 110
....*....|....*....|....*....|...
gi 92091586 1905 ANRRKLQRELDEATESNEAMGREVNALKSKLRR 1937
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1534-1941 |
6.45e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.55 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1534 VHELEKSKRAletqMEEMKTQLEELE-DELQATED---AKLRLEvNMQalKGQFERDLQARDEQNEEKRRQLQRQLHEYE 1609
Cdd:pfam05701 69 LEELESTKRL----IEELKLNLERAQtEEAQAKQDselAKLRVE-EME--QGIADEASVAAKAQLEVAKARHAAAVAELK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1610 T---ELEDERKQRAlaaaakkklegdlkDLELQADSAIKGREEAI-------KQLRKLQAQMKDFQRELEDARASRDEI- 1678
Cdd:pfam05701 142 SvkeELESLRKEYA--------------SLVSERDIAIKRAEEAVsaskeieKTVEELTIELIATKESLESAHAAHLEAe 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1679 -----FATAKEN-----EKKAKSLEADLMQLQEDLAAAERARKQADLEkeelaeelaSSLsgrnaLQDEKRRLEARIAQL 1748
Cdd:pfam05701 208 ehrigAALAREQdklnwEKELKQAEEELQRLNQQLLSAKDLKSKLETA---------SAL-----LLDLKAELAAYMESK 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1749 EEELEEEQGNMEAMSDRVRKATQQAEqlsNELATERSTAQKNESARQQLERQNKELRSKLhEMEGAVKSKFKSTIAALEA 1828
Cdd:pfam05701 274 LKEEADGEGNEKKTSTSIQAALASAK---KELEEVKANIEKAKDEVNCLRVAAASLRSEL-EKEKAELASLRQREGMASI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1829 KIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRR 1908
Cdd:pfam05701 350 AVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLE 429
|
410 420 430
....*....|....*....|....*....|....
gi 92091586 1909 KLQRELDEATESNEAMGREVNAL-KSKLRRGNET 1941
Cdd:pfam05701 430 AVLKEIEAAKASEKLALAAIKALqESESSAESTN 463
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1175-1427 |
6.71e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 40.71 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1175 LRAKRE--QEVTVLKKALDEETRSHEAQVQEMRQKHAQAVEELTEQLEQFKRAKANLDKNKQTLekenadlagelrvLGQ 1252
Cdd:pfam15397 1 IRNRRTslEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKLLQQYEKFGTIISILEYSNKKQ-------------LQQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1253 AKQEVEHKKKKLEAQVQELqskcsdgERARAELNDKVHKLQNEVESV-TGMLNEAEGKAIKlakdVASLSSQLQDTQELL 1331
Cdd:pfam15397 68 AKAELQEWEEKEESKLNKL-------EQQLEQLNAKIQKTQEELNFLsTYKDKEYPVKAVQ----IANLVRQLQQLKDSQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1332 QEEtRQKLNvstklRQLEEERNSLQDQLDEEmeaKQNLERHIStLNIQLSdSKKKLQDFASTVEALEEGKKRFQKEIENL 1411
Cdd:pfam15397 137 QDE-LDELE-----EMRRMVLESLSRKIQKK---KEKILSSLA-EKTLSP-YQESLLQKTRDNQVMLKEIEQFREFIDEL 205
|
250
....*....|....*.
gi 92091586 1412 TQQYEEKAAAYDKLEK 1427
Cdd:pfam15397 206 EEEIPKLKAEVQQLQA 221
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
863-1159 |
6.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 863 AKEDELQKTKERQQKAENELKELEQKHSQLTEEKNLLQEQLQAETELYAEAEEMRVRLAAKKQELEEILHEMEARLEEEE 942
Cdd:COG4372 28 ALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 943 DRGQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDEILVMDDQNNKLSKERKLLEERISDLTTNL 1022
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1023 AEEEEKAKNLTKLKNKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAA 1102
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 92091586 1103 LARLDDEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALK 1159
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1642-1941 |
6.83e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1642 SAIKGREEAIKQLRKLQAQMKDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAA--AERARKQADLEKEE 1719
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEkiAEYTKSIDIKKATE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1720 LAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQgnmEAMSDRVRKATQQAEQLSNELATERSTAQKNeSARQQLEr 1799
Cdd:COG5185 313 SLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQ---ESLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIE- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1800 qnkELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVEDERKMAEQyKEQA 1879
Cdd:COG5185 388 ---STKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADE-ESQS 463
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1880 EKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNET 1941
Cdd:COG5185 464 RLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAES 525
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1422-1866 |
7.22e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.05 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1422 YDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQRKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEE 1501
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1502 ALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKG 1581
Cdd:COG5278 161 LALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALAL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1582 QFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQM 1661
Cdd:COG5278 241 ALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAA 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1662 KDFQRELEDARASRDEIFATAKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNALQDEKRRL 1741
Cdd:COG5278 321 AAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1742 EARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLHEMEGAVKSKFKS 1821
Cdd:COG5278 401 AAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAA 480
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 92091586 1822 TIAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEILLQVE 1866
Cdd:COG5278 481 AAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAAL 525
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1776-1932 |
8.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1776 LSNELAT-----ERSTAQKNESARQ-QLERQNKelrsklHEMEGAVkSKFKSTIAALEAKIAQLEEQVEQEAREKQAATK 1849
Cdd:PRK09039 44 LSREISGkdsalDRLNSQIAELADLlSLERQGN------QDLQDSV-ANLRASLSAAEAERSRLQALLAELAGAGAAAEG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1850 SLKQKDKKLKEillqvedERKMAEQYKEQAEKGNARVKQLKRQL---EEAEEESQ-RINANRRKLQrelDEATESNEAMG 1925
Cdd:PRK09039 117 RAGELAQELDS-------EKQVSARALAQVELLNQQIAALRRQLaalEAALDASEkRDRESQAKIA---DLGRRLNVALA 186
|
....*..
gi 92091586 1926 REVNALK 1932
Cdd:PRK09039 187 QRVQELN 193
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1516-1656 |
8.36e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1516 LKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEELEDELQATEDAKLRLEVNMQALKGQFE-RDLQARDEQN 1594
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIESL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1595 EEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRK 1656
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1704-1954 |
8.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1704 AAAERARKQADLEKEELAEELASSLSGRNALQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATQQAEQLSNELATE 1783
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1784 RSTAQKNESARQQLER-----------QNKELRSKLHEMEGAVKSKFKSTIAALEAKIAQLEEQVEQEAREKQAATKSLK 1852
Cdd:COG3883 92 ARALYRSGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1853 QKDKKLKEILLQVEDERKMAEQYKEQAEKGNARVKQLKRQLEEAEEESQRINANRRKLQRELDEATESNEAMGREVNALK 1932
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|..
gi 92091586 1933 SKLRRGNETSFVPSRRSGGRRV 1954
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAG 273
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1051-1340 |
8.66e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1051 KKEEKSRQELEKLKRkLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAAlarlddeIAQKNNALKKIRELEGHISDL 1130
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAA-------VREKTSLSASVASLEKQLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1131 QE--DLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQElraKREQEVTVLKKALdEETRSHEAQVQEMRQKH 1208
Cdd:pfam15905 135 TRvnELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQE---GMEGKLQVTQKNL-EHSKGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1209 AQAVEELTEQLEQFKRAKANLDKNKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEAQVQELQSKCSDgeraraeLNDK 1288
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD-------LNEK 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 92091586 1289 VHKLQNEVESvtgMLNEAEGKAIKLAKDVASLSSQLQdtqelLQEETRQKLN 1340
Cdd:pfam15905 284 CKLLESEKEE---LLREYEEKEQTLNAELEELKEKLT-----LEEQEHQKLQ 327
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1759-1849 |
9.67e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 40.03 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92091586 1759 MEAMSDRVRKATQQAEQLSNELATERSTAqKNESARQQLERQNKELRSKLHEMEGAVKSkfkSTIAALEAKIAQLEEQVE 1838
Cdd:COG4223 2 IAALEAAVAELPAQLTALEQRLAALEAAP-AAAAATAALEARLAALRAALAAAREAVAA---AAAAALEARLAALEAKAA 77
|
90
....*....|.
gi 92091586 1839 QEAREKQAATK 1849
Cdd:COG4223 78 APEAEAAAAAR 88
|
|
| |
