|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-768 |
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: 1379.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGESLHGAVKTRKGMFRTVGQ 652
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 653 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 732
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 319655760 733 IPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14932 641 IPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
93-768 |
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: 1320.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK---KKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYR-FLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFKLTDEAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQT 411
Cdd:cd01377 238 DILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 412 QEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 491
Cdd:cd01377 318 KEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 492 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgpPGILALLDEECWFPKATDKSFVEKVVQE-LGNNPKFQKPKKLKDD 570
Cdd:cd01377 397 LEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPN--MGILSILDEECVFPKATDKTFVEKLYSNhLGKSKNFKKPKPKKSE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 571 ADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRivgldkvagmGESLHGAVKTRKGMFRTV 650
Cdd:cd01377 475 AHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE----------SGGGGGKKKKKGGSFRTV 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 651 GQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 730
Cdd:cd01377 545 SQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAP 624
|
650 660 670
....*....|....*....|....*....|....*...
gi 319655760 731 NAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01377 625 NAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
845-1925 |
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: 1300.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 845 TRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHEL 924
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 925 ESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEER 1004
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1005 ISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAK 1084
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1085 KEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQE 1164
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1165 LRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSK 1244
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1245 NDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEE 1324
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1325 TRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQ 1404
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1405 LEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLT 1484
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1485 LARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEV 1564
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1565 NMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQL 1644
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1645 KKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLS 1724
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1725 SDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGA 1804
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1805 VKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLE 1884
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 319655760 1885 ETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKL 1925
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-768 |
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: 1289.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14920 157 YIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14920 317 EQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd14920 397 EQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGESLHGA-VKTRKGMFRTVG 651
Cdd:cd14920 477 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSaYKTKKGMFRTVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 652 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 731
Cdd:cd14920 557 QLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 636
|
650 660 670
....*....|....*....|....*....|....*..
gi 319655760 732 AIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14920 637 AIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
93-768 |
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: 1247.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGEsLHGAVKTRKGMFRTVGQ 652
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE-MPGAFKTRKGMFRTVGQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 653 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 732
Cdd:cd15896 560 LYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 319655760 733 IPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd15896 640 IPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-768 |
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: 1208.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14919 154 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14919 234 IMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14919 314 EQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFIL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd14919 394 EQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGES-LHGAVKTRKGMFRTVG 651
Cdd:cd14919 474 FCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETaLPGAFKTRKGMFRTVG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 652 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 731
Cdd:cd14919 554 QLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 633
|
650 660 670
....*....|....*....|....*....|....*..
gi 319655760 732 AIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14919 634 SIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
93-768 |
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: 1165.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14921 157 YIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14921 317 EQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFIL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd14921 397 EQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGE-SLHGAVKTRKGMFRTVG 651
Cdd:cd14921 477 FSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTEsSLPSASKTKKGMFRTVG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 652 QLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 731
Cdd:cd14921 557 QLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAAN 636
|
650 660 670
....*....|....*....|....*....|....*..
gi 319655760 732 AIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14921 637 AIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-768 |
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: 1142.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASS-----FKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 247
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 248 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAET 327
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 328 IDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQ 407
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 408 KAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 487
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 488 TMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKpKKL 567
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDrIVGLDKVAgMGESLHGAvKTRKGMF 647
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA-RTRKGMF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14911 554 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 319655760 728 LTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14911 634 LTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
81-768 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1095.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 81 VEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM 160
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 161 QDREDQSILCTGESGAGKTENTKKVIQYLAYVASSfktkkdqsSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRF 240
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGS--------GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 241 GKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQ 319
Cdd:pfam00063 153 GKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTIDGID 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 320 DRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRI 399
Cdd:pfam00063 233 DSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 400 KVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNE 479
Cdd:pfam00063 313 KTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 480 KLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNP 559
Cdd:pfam00063 393 KLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 560 KFQKPkKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGEslhGA 639
Cdd:pfam00063 470 HFQKP-RLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKS---TP 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 640 VKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 719
Cdd:pfam00063 546 KRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQ 625
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 319655760 720 EFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:pfam00063 626 EFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
93-768 |
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: 1087.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGV----PGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQdRELFAETIDAFR 332
Cdd:cd14930 157 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14930 236 VLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14930 316 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD 572
Cdd:cd14930 396 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 573 FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGMGESLHGAvKTRKGMFRTVGQ 652
Cdd:cd14930 476 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG-RPRRGMFRTVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 653 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 732
Cdd:cd14930 555 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 319655760 733 IPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14930 635 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
74-780 |
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: 1007.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 74 NPPKFSKVEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITD 153
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 154 TAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVASSFKtkkdqssialSHGELEKQLLQANPILEAFGNAKTVK 233
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT----------EVGSVEDQILESNPILEAFGNAKTLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 234 NDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN- 312
Cdd:smart00242 151 NNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGc 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 313 VTIPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDT-AAQKVSHLLGMNVTDFT 391
Cdd:smart00242 231 LTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 392 RAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQ 471
Cdd:smart00242 311 KALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 472 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKV 551
Cdd:smart00242 390 LCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEKK--PPGILSLLDEECRFPKGTDQTFLEKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 552 VQELGNNPKFQKPKKlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivgldkvag 631
Cdd:smart00242 467 NQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 632 mgeslHGAVKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQG 711
Cdd:smart00242 534 -----GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAG 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 712 FPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFRAGVLAHLEEERD 780
Cdd:smart00242 609 FPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
30-1155 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 885.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 30 VWVPSEKLGFEAGSIKEETGDECLVELA---DSGKKIKVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLRERYY 104
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 105 SGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKK 184
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 185 VIQYLAYVassfktkkdQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIETYLL 264
Cdd:COG5022 172 IMQYLASV---------TSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 265 EKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVT-IPGQQDRELFAETIDAFRIMGIPEDEQTG 343
Cdd:COG5022 243 EKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 344 LLKVVSAVLQLGNMSFKKERNsDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALA 423
Cdd:COG5022 323 IFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 424 KATYERLFRWLVMRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE 503
Cdd:COG5022 402 KALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 504 WSFIDFgLDLQPCIELIEKPNgPPGILALLDEECWFPKATDKSFVEKVVQEL--GNNPKFQKPkKLKDDAdFCIIHYAGK 581
Cdd:COG5022 481 WSFIDY-FDNQPCIDLIEKKN-PLGILSLLDEECVMPHATDESFTSKLAQRLnkNSNPKFKKS-RFRDNK-FVVKHYAGD 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 582 VDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVgldkvagmgeslhgavktRKGMFRTVGQLYKEQLMNL 661
Cdd:COG5022 557 VEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE------------------SKGRFPTLGSRFKESLNSL 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 662 MTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA----IPKGF 737
Cdd:COG5022 619 MSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWK 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 738 MDGKQACVLMVKALELDSNLYRIGQSKVFFRAGVLAHLEEERDMKITDVIINFQAWCRGYVARRAFAKRQQQLTAMRVIQ 817
Cdd:COG5022 699 EDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 818 RNCAAYLKLRNWQWWRLFTKVKPLLQvTRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLaLQEQLQAET 897
Cdd:COG5022 779 HGFRLRRLVDYELKWRLFIKLQPLLS-LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVL-IQKFGRSLK 856
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 898 ELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKvtmDAKL 977
Cdd:COG5022 857 AKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTEL---IARL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 978 KKIEEDLMVIEDQNAKLSKEKKqmEERISEFTTNLAEEEEKSKSLQKLKTKHEtmitdledrlRKEEKMRQELEKNRRKL 1057
Cdd:COG5022 934 KKLLNNIDLEEGPSIEYVKLPE--LNKLHEVESKLKETSEEYEDLLKKSTILV----------REGNKANSELKNFKKEL 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1058 egdsTELHDQIAELQAQIAELRaQLAKKEEELQAALARIEEEAALK---NAAQKSIREMEAQISELQEDLelekaarnKA 1134
Cdd:COG5022 1002 ----AELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSESTELsilKPLQKLKGLLLLENNQLQARY--------KA 1068
|
1130 1140
....*....|....*....|.
gi 319655760 1135 EKQRRDLGEELEALKTELEDT 1155
Cdd:COG5022 1069 LKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
93-768 |
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: 871.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-----SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFL-----SNGNVTIPGQQDRELFAE 326
Cdd:cd00124 156 GRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 327 TIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNS--DQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRD 404
Cdd:cd00124 236 LLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 405 FVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 483
Cdd:cd00124 316 TITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 484 LFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQK 563
Cdd:cd00124 396 FFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 564 PKKLKDDAdFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQsvdkfvselwkdvdrivgldkvagmgeslhgavktr 643
Cdd:cd00124 473 KKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRS------------------------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 644 kgmfrtvGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 723
Cdd:cd00124 516 -------GSQFRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 319655760 724 RYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd00124 589 RYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
93-768 |
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: 783.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKT--KKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 250
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGpgKKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 251 NGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLED--YNkYRFLSNGNVTIPGQQDRELFAETI 328
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMnpYD-YHFCSQGVTTVDNMDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 329 DAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQK 408
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 409 AQTQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 488
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 489 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKP--- 564
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYdNHLGKSPNFQKPrpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 565 KKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdriVGLDKVagmGESLHGAVKTRK 644
Cdd:cd14927 476 KKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENY---VGSDST---EDPKSGVKEKRK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 645 --GMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 722
Cdd:cd14927 550 kaASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFK 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 319655760 723 QRYEILTPNAIPK-GFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14927 630 QRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
93-768 |
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: 774.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSsialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAK----SKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRsELCL--EDYNKYRFLSNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14909 157 KLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVK-EMCLlsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14909 316 NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPKKLK- 568
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTnTHLGKSAPFQKPKPPKp 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 --DDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivgLDKVAGMGESLHGAVKTRKGM 646
Cdd:cd14909 472 gqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFAD------HAGQSGGGEQAKGGRGKKGGG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14909 546 FATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYK 625
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 727 ILTPNAIpKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14909 626 ILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
94-768 |
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: 773.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKM--KGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYNKYR--FLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNPYDypFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KL 567
Cdd:cd14913 397 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKvvKG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrIVGLDkvagmGESLHGAVKTRKG-M 646
Cdd:cd14913 474 RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT---FATAD-----ADSGKKKVAKKKGsS 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14913 546 FQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYR 625
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 319655760 727 ILTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14913 626 VLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
93-768 |
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: 744.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD------GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14934 155 KLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKpELIESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQITDVAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQT 411
Cdd:cd14934 235 DVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 412 QEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 491
Cdd:cd14934 315 MEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 492 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGppgILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPKKLKD- 569
Cdd:cd14934 394 LEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMG---IFSILEEQCVFPKATDATFKAALYdNHLGKSSNFLKPKGGKGk 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 570 --DADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSvDKFVSELWKDVDrivgldkvagmgESLHGAVKTRKGM- 646
Cdd:cd14934 471 gpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKS-SLGLLALLFKEE------------EAPAGSKKQKRGSs 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14934 538 FMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQ 617
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 727 ILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14934 618 VLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
94-768 |
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: 707.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTP---GKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLED--YNkYRFLSNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNnpYD-YAFISQGETTVASIDDAEELMATDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd14917 238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 489
Cdd:cd14917 317 QNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 490 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPKKLK 568
Cdd:cd14917 396 FVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFdNHLGKSNNFQKPRNIK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 D--DADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdriVGLDKVAGMGESlhgavKTRKG- 645
Cdd:cd14917 473 GkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGADAPIEKGKG-----KAKKGs 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 646 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 725
Cdd:cd14917 545 SFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 726 EILTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14917 625 RILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
93-768 |
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: 704.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKL-------GALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAgDKLRsELCLEDYN--KYRFLSNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14929 154 MLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGK-KELR-DLLLVSANpsDFHFCSCGAVAVESLDDAEELLATEQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14929 232 MDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14929 312 NIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KL 567
Cdd:cd14929 391 VLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFdNHFGKSVHFQKPKpdKK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivglDKVAGMGESLhGAVKTRKGM- 646
Cdd:cd14929 468 KFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTDSAIQF-GEKKRKKGAs 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14929 540 FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYC 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 319655760 727 ILTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14929 620 ILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
94-768 |
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: 702.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSfktKKDQSSIalshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS---SSGETQV-------EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELFAETIDAF 331
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGsPVIDGVDDAAEFEETRKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQT 411
Cdd:cd01380 232 TLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 412 QEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd01380 312 LQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEkpnGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPK--FQKPKkLK 568
Cdd:cd01380 392 KLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR-FS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 DDAdFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSvdkfvselwkdvdrivgldkvagmgeslhgavKTRKgmfR 648
Cdd:cd01380 467 NTA-FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS--------------------------------KNRK---K 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 649 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 728
Cdd:cd01380 511 TVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVL 590
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 319655760 729 TPNAIPKGfMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01380 591 LPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
94-768 |
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: 697.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQT 411
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 412 QEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 491
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 492 LEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KLK 568
Cdd:cd14910 400 LEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpaKGK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 DDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdriVGLDKVAGMGESlhgAVKTRKGMFR 648
Cdd:cd14910 477 VEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA---AAAEAEEGGGKK---GGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 649 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 728
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 319655760 729 TPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14910 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
95-768 |
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: 695.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 95 VLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGES 174
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 175 GAGKTENTKKVIQYLAYVASSFKTKKDQSsiALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYI 254
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 255 VGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG-DKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFRI 333
Cdd:cd14918 161 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKpDLIEMLLITTNPYDYAFVSQGEITVPSIDDQEELMATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 334 MGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQ 412
Cdd:cd14918 241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 413 EQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 492
Cdd:cd14918 320 QQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 493 EQEEYQREGIEWSFIDFGLDLQPCIELIEKpngPPGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KLKD 569
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEK---PLGIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKvvKGKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 570 DADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdrivgldKVAGMGESLHGAVKTRKGMFRT 649
Cdd:cd14918 476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY-------ASAEADSGAKKGAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 650 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 729
Cdd:cd14918 549 VSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 319655760 730 PNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14918 629 ASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
94-768 |
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: 692.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYNKYR--FLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPEL-IEMLLITTNPYDypFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KL 567
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPKvvKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGldkvAGMGESLHGAVKTRKGMF 647
Cdd:cd14912 476 KAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG----ASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 728 LTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-768 |
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: 691.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQPGKM-QGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYNKYR--FLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDfpFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KL 567
Cdd:cd14923 398 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKPKpaKG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdriVGLDKVAGMGESLHGavKTRKGMF 647
Cdd:cd14923 475 KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG--KKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 728 LTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
94-768 |
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: 687.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVAS-SFKTKKDQSSIalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNA--NKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLED--YNkYRFLSNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNnpYD-YAFVSQGEVSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDTA-AQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 489
Cdd:cd14916 318 QSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 490 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--K 566
Cdd:cd14916 397 FVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRnvK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 567 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdrivgldKVAGMGESLHGAVKTRKG- 645
Cdd:cd14916 474 GKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY-------ASADTGDSGKGKGGKKKGs 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 646 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 725
Cdd:cd14916 547 SFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRY 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 726 EILTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14916 627 RILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
94-768 |
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: 687.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLrSELCLEDYNKYRF--LSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmPDDT-AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVV-QELGNNPKFQKPK--KL 567
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSNNFQKPKpaKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKdvdrivGLDKVAGMGESLHGAVKTRKGMF 647
Cdd:cd14915 476 KAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS------GGQTAEAEGGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14915 550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 728 LTPNAIPKG-FMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14915 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
94-768 |
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: 667.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASsfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTN-------------NHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG--DKLRSELCLEDYNKYRFLS-NGNVTIPGQQDRELFAETIDA 330
Cdd:cd14883 149 IKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKhsKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQK-VSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd14883 229 MNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEILKiVAKLLGVDPDKLKKALTIRQINVRGNVTEIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 489
Cdd:cd14883 309 LKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 490 FILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKD 569
Cdd:cd14883 388 FKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 570 DADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDrIVGLDKVAGMGESLHGAVKTRKGMfRT 649
Cdd:cd14883 465 KTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGK-PT 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 650 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 729
Cdd:cd14883 543 VGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD 622
|
650 660 670
....*....|....*....|....*....|....*....
gi 319655760 730 PNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14883 623 PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
94-768 |
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: 653.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAyvassfktkkdqssiALSHGE--LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd01383 80 SGAGKTETAKIAMQYLA---------------ALGGGSsgIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELFAETIDA 330
Cdd:cd01383 145 GKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd01383 225 LDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd01383 305 TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKpkklKDD 570
Cdd:cd01383 385 KLEQEEYELDGIDWTKVDF-EDNQECLDLIEKK--PLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 571 ADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLL----NQSVDKFVSELWKDVDRIVGLDKVAGMGeslhgavktrkGM 646
Cdd:cd01383 458 GAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLsscsCQLPQLFASKMLDASRKALPLTKASGSD-----------SQ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd01383 527 KQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYG 606
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 727 ILTPNAIpKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01383 607 FLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
94-768 |
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: 645.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASsfktkKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSG-----GSESEV----ERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd01378 153 PVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIPEDEQTGLLKVVSAVLQLGNMSFkKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVG---RDFVQKA 409
Cdd:cd01378 233 VIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 489
Cdd:cd01378 312 LNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 490 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFP-KATDKSFVEKVVQELGNNPKFQKPKKLK 568
Cdd:cd01378 392 LKAEQEEYVREGIEWTPIKY-FNNKIICDLIEEK--PPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 D--DADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivgldkvagmgeslhGAVKTRKGM 646
Cdd:cd01378 469 ElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE------------------GVDLDSKKR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd01378 531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 727 ILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
93-768 |
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: 627.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASsfKTKKDQSSIalshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG--RAVTEGRSV-------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELFAETIDA 330
Cdd:cd01384 152 GRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKcFELDGVDDAEEYRATRRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTA---AQKVSHLLGMNVTDFTRAILSpRIKVGRD-FV 406
Cdd:cd01384 232 MDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCK-RVIVTPDgII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 407 QKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL--DKTKRqgaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 484
Cdd:cd01384 311 TKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIgqDPNSK---RLIGVLDIYGFESFKTNSFEQFCINLANEKLQQH 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 485 FNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKpnGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKP 564
Cdd:cd01384 388 FNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 565 KklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRivgldkvagmgeslHGAVKTRK 644
Cdd:cd01384 465 K--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR--------------EGTSSSSK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 645 gmFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 724
Cdd:cd01384 529 --FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDR 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 725 YEILTPNAiPKGFMDGKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd01384 607 FGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
93-768 |
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: 613.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAyvassfktkkdqsSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd01381 81 ESGAGKTESTKLILQYLA-------------AISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELFAETIDAF 331
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIRSAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKK--ERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd01381 228 KVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 487
Cdd:cd01381 308 LSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 488 TMFILEQEEYQREGIEWSFIDFgLDLQPCIELIekPNGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKl 567
Cdd:cd01381 388 HIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLI--ALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWkdvdrivglDKVAGMGESlhgavkTRKGMf 647
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF---------NEDISMGSE------TRKKS- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd01381 528 PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRV 607
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 319655760 728 LTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01381 608 LVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
93-768 |
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: 582.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS------------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELcledynkyrflsngnVTIPGQQDRELFAETIDAF 331
Cdd:cd01382 149 SSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL---------------LKDPLLDDVGDFIRMDKAM 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNS-------DQASMPDDTAAqkvSHLLGMNVTDF-----TRAILSPRI 399
Cdd:cd01382 214 KKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 400 KVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKrqGASFIGILDIAGFEIFELNSFEQLCINYTNE 479
Cdd:cd01382 291 GAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCNE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 480 KLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNGppGILALLDEECWFPKATDKSFVEKVVQELGNNP 559
Cdd:cd01382 369 KLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHF 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 560 KFQKPKK--------LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRivgldkvag 631
Cdd:cd01382 446 RLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTN--------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 632 mgESLHGAVKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQG 711
Cdd:cd01382 517 --NNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGG 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 712 FPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01382 595 FPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
93-768 |
0e+00 |
|
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: 565.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQ----DREDQS 167
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 168 ILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSH------GELEKQLLQANPILEAFGNAKTVKNDNSSRFG 241
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEaieqtlGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 242 KFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDR 321
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 322 ELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASmpDDTAAQKVSH---LLGMNVTDFTRAILSPR 398
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLKLaaeLLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 399 IKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTN 478
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 479 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIE-KPNGPPGILALLDeECWFPKAT--DKSFVEKVVQEL 555
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASF 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 556 G-------------NNPKFQKPkKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSvdkfvselwkdvdr 622
Cdd:cd14890 476 GrksgsggtrrgssQHPHFVHP-KFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQS-------------- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 623 ivgldkvagmGESLHGAvktrkgmfrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVL 702
Cdd:cd14890 541 ----------RRSIREV---------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 703 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
93-768 |
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: 563.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSfktkkdqssialsHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGS-------------TNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAgdKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELFAETIDAF 331
Cdd:cd14872 148 RICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLAM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDT---AAQKVSHLLGMNVTDFTRAILSPRIKV-GRDFVQ 407
Cdd:cd14872 226 EQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVAnrdVLKEVATLLGVDAATLEEALTSRLMEIkGCDPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 408 KAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 487
Cdd:cd14872 306 IPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 488 TMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKL 567
Cdd:cd14872 386 YTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKK--QPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFvselwkdvdrivgldkVAGMGESLHGAVKTRKGmf 647
Cdd:cd14872 463 TSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL----------------IAVLFPPSEGDQKTSKV-- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 rTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14872 525 -TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRF 603
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 728 LtPNAIPKGFM-DGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14872 604 L-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
93-768 |
1.38e-176 |
|
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: 551.69 E-value: 1.38e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSFktkkDQSSIalshgeleKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGL----NDSTI--------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKlrSELCLEDYNKYRFL-SNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14903 149 GTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVE--ERLFLDSANECAYTgANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASM--PDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQK 408
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 409 AQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 488
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 489 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIEkpnGPPGILALLDEECWFPKATDKSFVEKVV---QELGNNPKFQKPK 565
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLSsihKDEQDVIEFPRTS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 566 KlkddADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKdvDRIVGLDKVAGMGESLHGAVKTRKG 645
Cdd:cd14903 462 R----TQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK--EKVESPAAASTSLARGARRRRGGAL 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 646 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 725
Cdd:cd14903 536 TTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKF 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 726 EILTPNAiPKGFMDGKQACVLMVKALELDS-NLYRIGQSKVFFR 768
Cdd:cd14903 616 WLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
93-768 |
5.31e-176 |
|
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: 550.13 E-value: 5.31e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVAssfktkkdQSSIALshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNG 252
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN--------QRRNNL----VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNG-NVTIPGQQDRELFAETIDAF 331
Cdd:cd01387 148 VIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKK---ERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQK 408
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 409 AQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 488
Cdd:cd01387 308 PLTIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLS-IAILDIFGFEDLSENSFEQLCINYANENLQYYFNKH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 489 MFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKklK 568
Cdd:cd01387 387 VFKLEQEEYIREQIDWTEIAF-ADNQPVINLISKK--PVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--M 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 569 DDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDV--DRIVGLDKVAgmgeslHGAVKTRKGM 646
Cdd:cd01387 462 PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHraQTDKAPPRLG------KGRFVTMKPR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd01387 536 TPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 727 ILTPNAIPKGfmDGKQACVLMVKALE--LDSNLYRIGQSKVFFR 768
Cdd:cd01387 616 CLVALKLPRP--APGDMCVSLLSRLCtvTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
93-766 |
1.17e-171 |
|
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: 538.22 E-value: 1.17e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMY------KGKKRHEMPPHIYAITDTAYRSMMQDRE-- 164
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 165 --DQSILCTGESGAGKTENTKKVIQYLAYVASsfKTKKDQSsiALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 242
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSS--ATTHGQN--ATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 243 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTI--PGQQD 320
Cdd:cd14901 157 FIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrrDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 321 RELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF-KKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRI 399
Cdd:cd14901 237 SVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 400 KVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGAS-FIGILDIAGFEIFELNSFEQLCINYTN 478
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 479 EKLQQLFNHTMFILEQEEYQREGIEWSFIDFgldlqP----CIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQE 554
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFEAR--PTGLFSLLDEQCLLPRGNDEKLANKYYDL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 555 LGNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSElwkdvdrivgldkvagmge 634
Cdd:cd14901 470 LAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 635 slhgavktrkgmfrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPN 714
Cdd:cd14901 531 --------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPV 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 715 RIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDSNL-----YRIGQSKVF 766
Cdd:cd14901 597 RFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
93-768 |
2.16e-171 |
|
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: 538.89 E-value: 2.16e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLayvaSSFKTKKDQSSIalshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd01385 81 ESGSGKTESTNFLLHHL----TALSQKGYGSGV-------EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLS-NGNVTIPGQQDRELFAETIDAF 331
Cdd:cd01385 150 MVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQAM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKER-NSDQASMPDDTAAQK-VSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd01385 230 EMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDiISELLRVKEETLLEALTTKKTVTVGETLILP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKAL----DKTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 485
Cdd:cd01385 310 YKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 486 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPK 565
Cdd:cd01385 389 NQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISKK--PTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 566 KlKDDAdFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELwkdvdriVGLDKVA--------------- 630
Cdd:cd01385 466 V-MEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwavlrafframa 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 631 -----GMG-----------------ESLHGAVKTRKGMfrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLA 688
Cdd:cd01385 537 afreaGRRraqrtaghsltlhdrttKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 689 HHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd01385 615 DELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
94-768 |
2.48e-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: 522.99 E-value: 2.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA------------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTG-AGDKLRSELCLEDYNKYRFLSNGNVTIPG----QQDRELFAETI 328
Cdd:cd01379 150 VTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGlAEDKKLAKYKLPENKPPRYLQNDGLTVQDivnnSGNREKFEEIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 329 DAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF----KKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRD 404
Cdd:cd01379 230 QCFKVIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 405 FVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL--DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 482
Cdd:cd01379 310 TIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 483 QLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIE-LIEKPNgppGILALLDEECWFPKATDKSFVEKVVQELGNNPkF 561
Cdd:cd01379 390 YYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-Y 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 562 QKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSElwkdvdrivgldkvagmgeslhgavk 641
Cdd:cd01379 465 WRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ-------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 642 trkgmfrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 721
Cdd:cd01379 517 -------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADF 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 319655760 722 RQRYEILTPNAIPKGFMDgKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd01379 590 LKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
93-768 |
1.03e-165 |
|
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: 521.56 E-value: 1.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKK-RHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTEN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQD-------RELF 324
Cdd:cd14897 149 GQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseeleyyRQMF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 325 AETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRD 404
Cdd:cd14897 229 HDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 405 FVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL----DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 480
Cdd:cd14897 309 RIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNER 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 481 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPK 560
Cdd:cd14897 389 LQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFKK--PLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPR 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 561 FQKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKdvdrivgldkvagmgeslhgav 640
Cdd:cd14897 466 YVASP--GNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 641 ktrkgmfrtvgQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 720
Cdd:cd14897 522 -----------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYED 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 319655760 721 FRQRYEILTPNAiPKGFMDGKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd14897 591 FVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
93-768 |
3.13e-165 |
|
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: 520.89 E-value: 3.13e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVAssfktkkdQSSIALSHGE----LEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 247
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIS--------QQSLELSLKEktscVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 248 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLS-NGNVTIPGQQDRELFAE 326
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 327 TIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKkerNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFV 406
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 407 QKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALdkTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 486
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 487 HTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKpngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKk 566
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEK---KLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPR- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 567 lKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRivgldkvAGMGESLHGAVKTRKgm 646
Cdd:cd14873 463 -VAVNNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSS-------RNNQDTLKCGSKHRR-- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 fRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14873 533 -PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYK 611
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 727 ILTPNAIPKGFMDGKqaCVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14873 612 VLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
93-768 |
1.58e-163 |
|
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: 516.23 E-value: 1.58e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEM---PPHIYAITDTAYRSMMQDR----ED 165
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 166 QSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 245
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 246 INFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPGQQDRELF 324
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDATEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 325 AETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF----KKERNSDQASMPDDTAaqKVSHLLGMNVTDFTRAILSPRIK 400
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenaDDEDVFAQSADGVNVA--KAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 401 VGR-DFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAldkTKRQG------------ASFIGILDIAGFEIFELN 467
Cdd:cd14892 319 TARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINAC---HKQQTsgvtggaasptfSPFIGILDIFGFEIMPTN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 468 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFP-KATDKS 546
Cdd:cd14892 396 SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 547 FVEKVVQE-LGNNPKFQKPKKLKDdaDFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSvdkfvselwkdvdrivg 625
Cdd:cd14892 473 LLTIYHQThLDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSS----------------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 626 ldkvagmgeslhgavktRKgmFRTvgqlykeQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGI 705
Cdd:cd14892 534 -----------------SK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 706 RICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACVLMVKALE-----LDSNLYRIGQSKVFFR 768
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARKKCEEivaraLERENFQLGRTKVFLR 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
93-730 |
1.59e-159 |
|
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: 505.77 E-value: 1.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKgKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSFKTKKDQssialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD-- 249
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSL---------VEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSkl 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 250 -------VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSN------------ 310
Cdd:cd14888 151 kskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGAdakpisidmssf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 311 ------------GNVTIPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQ- 377
Cdd:cd14888 231 ephlkfryltksSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDd 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 378 --KVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGI 455
Cdd:cd14888 311 leKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 456 LDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEkpNGPPGILALLDE 535
Cdd:cd14888 391 LDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 536 ECWFPKATDKSFVEKVVQELGNNPKFQKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSE 615
Cdd:cd14888 468 ECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 616 LWKD-VDRIVGLdkvagmgeslhgavKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLD 694
Cdd:cd14888 546 LFSAyLRRGTDG--------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNE 611
|
650 660 670
....*....|....*....|....*....|....*.
gi 319655760 695 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 730
Cdd:cd14888 612 QLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
95-768 |
2.45e-150 |
|
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: 480.17 E-value: 2.45e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 95 VLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMM----QDREDQSILC 170
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 171 TGESGAGKTENTKKVIQYLayvassfktkkdqssIALSHG--ELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 248
Cdd:cd14889 83 SGESGAGKTESTKLLLRQI---------------MELCRGnsQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 249 DvNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSN--GNVTIPgQQDRELFAE 326
Cdd:cd14889 148 R-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNgaGCKREV-QYWKKKYDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 327 TIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKkernsdqasmPDDTAAQKVSH-----------LLGMNVTDFTRAIL 395
Cdd:cd14889 226 VCNAMDMVGFTEQEEVDMFTILAGILSLGNITFE----------MDDDEALKVENdsngwlkaaagQFGVSEEDLLKTLT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 396 SPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQG--ASFIGILDIAGFEIFELNSFEQLC 473
Cdd:cd14889 296 CTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 474 INYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIekPNGPPGILALLDEECWFPKATDKSFVEKVVQ 553
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKLNI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 554 ELGNNPKFQKPKklKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVG--LDKVAG 631
Cdd:cd14889 453 HFKGNSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGtlMPRAKL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 632 MGESLHGAVKTRKgmfRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQG 711
Cdd:cd14889 531 PQAGSDNFNSTRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREG 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 712 FPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd14889 608 FSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
93-731 |
6.06e-148 |
|
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: 474.13 E-value: 6.06e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRH--------EMPPHIYAITDTAYRSMMQDR 163
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 164 EDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKD-----QSSIALSHGE--LEKQLLQANPILEAFGNAKTVKNDN 236
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEvltltSSIRATSKSTksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 237 SSRFGKFIRINFD-VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYNKYRFLS---NG 311
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnQLSGDRYDYlkkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 312 NVTIPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQA--SMPDDTAAQKVSHLLGMNVTD 389
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 390 FTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL-------DKTKRQGASFIGILDIAGFE 462
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 463 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFP 540
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 541 KATDKSFVEKVVQELGNNPKFQKPKKLKDDAdFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDV 620
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 621 DRIVGLDKvagmgeslHGAVKTRKGMfRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNG 700
Cdd:cd14907 557 DGSQQQNQ--------SKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLG 627
|
650 660 670
....*....|....*....|....*....|.
gi 319655760 701 VLEGIRICRQGFPNRIVFQEFRQRYEILTPN 731
Cdd:cd14907 628 VLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
94-728 |
5.74e-143 |
|
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: 458.62 E-value: 5.74e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMY-----------KGKKRHEMPPHIYAITDTAYRSMMQ 161
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 162 ----DREDQSILCTGESGAGKTENTKKVIQYLAYV-----ASSFKTKKDQSSIAlshgeleKQLLQANPILEAFGNAKTV 232
Cdd:cd14900 82 glngVMSDQSILVSGESGSGKTESTKFLMEYLAQAgdnnlAASVSMGKSTSGIA-------AKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 233 KNDNSSRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGdklrselcledynkyrflsngn 312
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGAS---------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 313 vtiPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSD-QASMPDDTAAQKV------SHLLGM 385
Cdd:cd14900 213 ---EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSV 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 386 NVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL---DKTKRQGAS-FIGILDIAGF 461
Cdd:cd14900 290 DATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 462 EIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFPK 541
Cdd:cd14900 370 EVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISQR--PTGILSLIDEECVMPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 542 ATDKSFVEKVVQELGNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNdnvatllNQSVDkfvselwkdvd 621
Cdd:cd14900 447 GSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKDVLH-------QEAVD----------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 622 rivgldkvagmgeslhgavktrkgMFRTVGQlYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGV 701
Cdd:cd14900 509 ------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660
....*....|....*....|....*..
gi 319655760 702 LEGIRICRQGFPNRIVFQEFRQRYEIL 728
Cdd:cd14900 564 MEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
93-768 |
9.48e-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: 458.74 E-value: 9.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKYLPiytEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE---D 165
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 166 QSILCTGESGAGKTENTKKVIQYL---AYVASSFKTKKDQSSIALSHG---ELEKQLLQANPILEAFGNAKTVKNDNSSR 239
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLttrAVGGKKASGQDIEQSSKKRKLsvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 240 FGKFIRINFDVNGY-IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGN-VTIPG 317
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 318 QQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNS----DQASMPDDTAAQKVSHLLGMNVTDFTRA 393
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTSegeaEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 394 ILSPRIkVGRD--FVQKaQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKtKRQGASFIGILDIAGFEIFEL-NSFE 470
Cdd:cd14891 316 ITQREI-VTRGetFTIK-RNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 471 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIE-----WSfidfglDLQPCIELI-EKPNgppGILALLDEECWFPKATD 544
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDvgvitWP------DNRECLDLIaSKPN---GILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 545 KSFVEKVVQELGNNPKFQKPKKlKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSvdkfvselwkdvdri 623
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 624 vgldkvagmgeslhgavktrkgmfrtvgQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLE 703
Cdd:cd14891 528 ----------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQ 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 704 GIRICRQGFPNRIVFQEFRqryEILTPNAIPKGF-MDGKQACVL---MVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14891 580 TCEVLKVGLPTRVTYAELV---DVYKPVLPPSVTrLFAENDRTLtqaILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
93-751 |
2.74e-141 |
|
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: 457.43 E-value: 2.74e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYK--------GKKRHEMPPHIYAITDTAYRSMMQ-D 162
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 163 REDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALshgELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 242
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV---EIGKRILQTNPILESFGNAQTIRNDNSSRFGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 243 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVT-----IPG 317
Cdd:cd14902 158 FIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSfarkrAVA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 318 QQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAA---QKVSHLLGMNVTDFTRAI 394
Cdd:cd14902 238 DKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 395 LSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALD--------KTKRQGASFIGILDIAGFEIFEL 466
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 467 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIE-KPNgppGILALLDEECWFPKATDK 545
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSN---GLFSLLDQECLMPKGSNQ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 546 SFVEKVVQELGNnpkfqkpkklkdDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSElwkdvdrIVG 625
Cdd:cd14902 474 ALSTKFYRYHGG------------LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVA-------IGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 626 LDKVAGMGESLHGAVKTRKGMFRT--VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLE 703
Cdd:cd14902 535 DENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLE 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 704 GIRICRQGFPNRIVFQEFRQRYEIL-----TPNAIPK-GFMDGKQA--CVLMVKAL 751
Cdd:cd14902 615 AVRIARHGYSVRLAHASFIELFSGFkcflsTRDRAAKmNNHDLAQAlvTVLMDRVL 670
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
93-768 |
1.39e-138 |
|
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: 447.47 E-value: 1.39e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSfktkKDQSSIAlshgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGG----RKDKTIA--------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFL--SNGNVTIPGQQDRELFAETID 329
Cdd:cd14904 149 GKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 330 AFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQkVSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd14904 229 SLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTVP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 489
Cdd:cd14904 308 LAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 490 FILEQEEYQREGIEWSFIDFGlDLQPCIELIEkpnGPPGILALLDEECWFPKATDKSFVEKV---VQELGNNPKFQKPKK 566
Cdd:cd14904 388 FKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 567 LKddADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDrivgldkvaGMGESLHGAVKTRKGM 646
Cdd:cd14904 464 KR--TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKSGKGTKA 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 647 FRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14904 533 PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYA 612
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 319655760 727 ILTPNAIPKGfmDGKQACVLMVKALELDSNL-YRIGQSKVFFR 768
Cdd:cd14904 613 IMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
93-768 |
1.36e-135 |
|
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: 440.11 E-value: 1.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYK--GKKRHE-------MPPHIYAITDTAYRSMMQD- 162
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 163 REDQSILCTGESGAGKTENTKKVIQYLAYVASSfKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 242
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNG-EEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 243 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDY--------NKYRFLSNGNVT 314
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGitgglqlpNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 315 IPGQ-QDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQ---ASMPDDTAAQKVSHLLGMNVTDF 390
Cdd:cd14908 240 DLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAaeiAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 391 TRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGA-SFIGILDIAGFEIFELNSF 469
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 470 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPngPPGILALLDEECWFP-KATDKSFV 548
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQAK--KKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 549 EKVV--------QELGNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLM-KNMDPLNdnvatllnqsvdkfvselwkd 619
Cdd:cd14908 477 SRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP--------------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 620 vdrivgldkvagmgeslhgavKTRKGMFRTvGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCN 699
Cdd:cd14908 536 ---------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYG 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 700 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK----GFMDGKQACVLMVKALELDSNLYR---------------- 759
Cdd:cd14908 594 GVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlsWSMERLDPQKLCVKKMCKDLVKGVlspamvsmknipedtm 672
|
730
....*....|
gi 319655760 760 -IGQSKVFFR 768
Cdd:cd14908 673 qLGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
93-768 |
1.14e-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: 436.13 E-value: 1.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLayvaSSFKTKKDQSSIAlshgelekQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvNG 252
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL----SSLYQDQTEDRLR--------QPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNV-TIPGQQDRELFAETIDAF 331
Cdd:cd14896 148 VIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFEGLLKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKK-ERNSDQ-ASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKA 409
Cdd:cd14896 228 QGLGLCAEELTAIWAVLAAILQLGNICFSSsERESQEvAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 410 QTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 488
Cdd:cd14896 308 LPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 489 MFILEQEEYQREGIEWSFIDfGLDLQPCIELI-EKPNgppGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKkl 567
Cdd:cd14896 388 LLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPH---SLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQ-- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGmgeslhgavktrkgmf 647
Cdd:cd14896 462 LPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP---------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 rTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14896 526 -TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 319655760 728 LTpNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14896 605 LG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
91-811 |
2.55e-134 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 441.39 E-value: 2.55e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 91 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHE-MPPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 170 CTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshgelekqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 249
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFASSKSGNMDLKIQNAI-----------MAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 250 VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETID 329
Cdd:PTZ00014 257 EEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVME 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 330 AFRIMGIPEDEQTGLLKVVSAVLQLGNMSFK-KERN--SDQASMPDDTAA--QKVSHLLGMNVTDFTRAILSPRIKVGRD 404
Cdd:PTZ00014 337 SFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGglTDAAAISDESLEvfNEACELLFLDYESLKKELTVKVTYAGNQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 405 FVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 484
Cdd:PTZ00014 417 KIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 485 FNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELI-EKPNgppGILALLDEECWFPKATDKSFVEKVVQELGNNPKFqK 563
Cdd:PTZ00014 496 FVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGK---SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKY-K 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 564 PKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGldkvagmgeslhgavKTR 643
Cdd:PTZ00014 571 PAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG---------------KLA 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 644 KGMFrtVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 723
Cdd:PTZ00014 636 KGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLS 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 724 RYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR---AGVLAHLEEERDMKITDVIINFQAWCRGYVAR 800
Cdd:PTZ00014 714 QFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKK 793
|
730
....*....|.
gi 319655760 801 RAFAKRQQQLT 811
Cdd:PTZ00014 794 RKVRKNIKSLV 804
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
94-768 |
1.27e-127 |
|
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: 418.59 E-value: 1.27e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPiyteeivEMYKGKKRHE-------MPPHIYAITDTAYRSMMQ----- 161
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 162 --DREDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSialSHGELEKQLLQANPILEAFGNAKTVKNDNSSR 239
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKR---RRAISGSELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 240 FGKFIRINF-----DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYN--KYRFLSNGN 312
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 313 --VTIPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSD---------------QASMPDDTA 375
Cdd:cd14895 232 cyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 376 AQK---VSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTK------ 446
Cdd:cd14895 312 QQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpn 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 447 ----RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDlQPCIELIEK 522
Cdd:cd14895 392 kaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 523 PngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVA 602
Cdd:cd14895 471 R--PSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELF 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 603 TLLNQSVDKFVSELWKDVDRIVGLDKVAGMGESLHgavktRKGMFRTV--GQLYKEQLMNLMTTLRNTNPNFVRCIIPNH 680
Cdd:cd14895 549 SVLGKTSDAHLRELFEFFKASESAELSLGQPKLRR-----RSSVLSSVgiGSQFKQQLASLLDVVQQTQTHYIRCIKPND 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 681 EKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELdsnlyri 760
Cdd:cd14895 624 ESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATASALIETLKVDHAEL------- 696
|
....*...
gi 319655760 761 GQSKVFFR 768
Cdd:cd14895 697 GKTRVFLR 704
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
93-766 |
1.34e-124 |
|
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: 407.84 E-value: 1.34e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRH-EMPPHIYAITDTAYRSMMQDREDQSILCT 171
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshgelekqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd14876 81 GESGAGKTEATKQIMRYFASAKSGNMDLRIQTAI-----------MAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAF 331
Cdd:cd14876 150 GGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLESL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKErnsDQASMPDdtAA----------QKVSHLLGMNVTDFTRAILSPRIKV 401
Cdd:cd14876 230 KSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 402 GRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTNEKL 481
Cdd:cd14876 305 GGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEML 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 482 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNGppGILALLDEECWFPKATDKSFVEKVVQELGNNPKF 561
Cdd:cd14876 384 QKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 562 qKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVdrIVGLDKVAgmgeslhgavk 641
Cdd:cd14876 461 -KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV--VVEKGKIA----------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 642 trKGMFrtVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 721
Cdd:cd14876 527 --KGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 319655760 722 RQRYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVF 766
Cdd:cd14876 603 LYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
93-768 |
9.26e-123 |
|
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: 404.00 E-value: 9.26e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSfktkkdqSSIALShgeLEKqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGS-------VGGVLS---VEK--LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKyrflsNGNVTIPG-------QQDRELF 324
Cdd:cd01386 149 GQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE-----SNSFGIVPlqkpedkQKAAAAF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 325 AETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAIL--------- 395
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 396 ----SPRIKVGRDFVQKAQTQEQAEfAVEALAKATYERLFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELN---- 467
Cdd:cd01386 304 qsttSSGQESPARSSSGGPKLTGVE-ALEGFAAGLYSELFAAVVSLINRSL-SSSHHSTSSITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 468 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNG------------PPGILALL 533
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqalvrsdlrdedRRGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 534 DEECWFPKATDKSFVEKVVQELG--NNPKFQKPKKLKDDA-DFCIIHYAGK--VDYKANEWLMK-NMDPLNDNVATLLNQ 607
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 608 SVDKFvselwkdvdrivgldkvagmgeslhGAVKtRKGMFRTVgqlyKEQLMNLMTTLRNTNPNFVRCIIPNHE------ 681
Cdd:cd01386 542 SQKET-------------------------AAVK-RKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHNagkder 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 682 KKAGKLAHHLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACVLMVKA 750
Cdd:cd01386 592 STSSPAAGDELLDvpllrsQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEE 671
|
730
....*....|....*...
gi 319655760 751 LELDSNLYRIGQSKVFFR 768
Cdd:cd01386 672 LDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
93-764 |
1.50e-118 |
|
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: 393.19 E-value: 1.50e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDREDQSILC 170
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 171 TGESGAGKTENTKKVIQYLayVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYL--INTSSSNQQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 250 VNGYIVGANIETYLLEKSR-AIRQAKDERAFHIFYYLLTGAGDKLRSELCLE-DYNKYRFL--------------SNGNV 313
Cdd:cd14906 159 SDGKIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLdarddvissfksqsSNKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 314 TIPGQQDR-ELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDT---AAQKVSHLLGMNVTD 389
Cdd:cd14906 239 NHNNKTESiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKvtaSLESVSKLLGYIESV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 390 FTRAILSPRIKVGRDFVQKAQTQE--QAEFAVEALAKATYERLFRWLVMRINKALDK----------TKRQGASFIGILD 457
Cdd:cd14906 319 FKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 458 IAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNGppGILALLDEEC 537
Cdd:cd14906 399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDEC 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 538 WFPKATDKSFVEKVVQELGNNPKFQKPKKLKddADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELW 617
Cdd:cd14906 476 IMPKGSEQSLLEKYNKQYHNTNQYYQRTLAK--GTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 618 KdvdrivgldkvagMGESLHGAVKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLR 697
Cdd:cd14906 554 Q-------------QQITSTTNTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLR 620
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 698 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSK 764
Cdd:cd14906 621 NVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
93-766 |
1.27e-117 |
|
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: 388.44 E-value: 1.27e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKR-HEMPPHIYAITDTAYRSMMQDRE--DQSI 168
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 169 LCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlshgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 248
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAE----RIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 249 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIpgqqDRELFAETI 328
Cdd:cd14880 157 NRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 329 DAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVS---HLLGMNVTDFTRAILSPRIKVGRDF 405
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRtsaLLLKLPEDHLLETLQIRTIRAGKQQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 406 V--QKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 483
Cdd:cd14880 313 QvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 484 LFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEkpNGPPGILALLDEECWFPKATDKS-FVEKVVQELGNNPKFQ 562
Cdd:cd14880 393 HFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 563 KpKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLDKVAGmgeslhgavkT 642
Cdd:cd14880 470 H-NKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG----------Q 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 643 RKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 722
Cdd:cd14880 539 SRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFV 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 319655760 723 QRYEILTPN--AIPKGFMDGKQAcvlmvkalELDSNLYRIGQSKVF 766
Cdd:cd14880 619 ERYKLLRRLrpHTSSGPHSPYPA--------KGLSEPVHCGRTKVF 656
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
93-768 |
5.76e-113 |
|
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: 375.30 E-value: 5.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKYLPIYTEEIVEMY-KGKKRHEMPPHIYAITDTAYRSM-MQDREDQSIL 169
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 170 CTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIAlshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 249
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSNTSQRSIA---DKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 250 -VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELC-LEDYNKYRFLSNGNVTI----PGQ--QDR 321
Cdd:cd14875 158 pTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELGgLKTAQDYKCLNGGNTFVrrgvDGKtlDDA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 322 ELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNsDQASMPDDTAAQKVSHLLGMNVTDFTRAILsprIKV 401
Cdd:cd14875 238 HEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 402 GRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALD-KTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEK 480
Cdd:cd14875 314 KTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANES 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 481 LQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPNgpPGILALLDEECWFPKATDKSFVEKVVQELGN-NP 559
Cdd:cd14875 394 LQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDQKR--TGIFSMLDEECNFKGGTTERFTTNLWDQWANkSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 560 KFQKPKKLKDDaDFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivgldkvaGMGESlhga 639
Cdd:cd14875 471 YFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLST-----------EKGLA---- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 640 vkTRKgmfRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 719
Cdd:cd14875 535 --RRK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIE 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 720 EFRQRYEILTPNAIPKGFMDGK--QACVLMvkaLELDSNLYR-------IGQSKVFFR 768
Cdd:cd14875 610 QFCRYFYLIMPRSTASLFKQEKysEAAKDF---LAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
93-768 |
1.30e-112 |
|
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: 373.84 E-value: 1.30e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRH-----EMPPHIYAITDTAYRSMMQDREDQ 166
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 167 SILCTGESGAGKTENTKKVIQYLAYVASSFKTKkdqssialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 246
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSSTD------------VQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 247 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNV-TIPGQQDRELFA 325
Cdd:cd14886 149 LVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGIDDQKEFA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 326 ETIDAFRIMgIPEDEQTGLLKVVSAVLQLGNMSFKKERNS---DQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVG 402
Cdd:cd14886 229 PVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVIN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 403 RDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALdKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 482
Cdd:cd14886 308 NETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEII-QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 483 QLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKPNgpPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFq 562
Cdd:cd14886 387 QYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPN--LSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFI- 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 563 kPKKlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRIVGLdkvagmgeslhgavkt 642
Cdd:cd14886 463 -PGK-GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN---------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 643 RKGMFrtVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 722
Cdd:cd14886 525 MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 319655760 723 QRYEILT--PNAIPKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14886 603 HRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
93-725 |
1.77e-105 |
|
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: 355.56 E-value: 1.77e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMY----------KGKKRHEMPPHIYAITDTAYRSMMQ 161
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 162 DREDQSILCTGESGAGKTENTKKVIQYLAYVAS-----SFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDN 236
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgnnnLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 237 SSRFGKFIRINF-DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSE----LCLED-YNKYRFLSN 310
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEqkqvLALSGgPQSFRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 311 GNVTI--PGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF-----KKERNS--DQASMPDDTAA----- 376
Cdd:cd14899 241 SLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafdhf 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 377 QKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL-------------- 442
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgadesd 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 443 DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEk 522
Cdd:cd14899 401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE- 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 523 pNGPPGILALLDEECWFPKATDKSFVEKVVQEL---GNNPKFQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLND 599
Cdd:cd14899 479 -HRPIGIFSLTDQECVFPQGTDRALVAKYYLEFekkNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 600 NVATLLNQSVDKFVSELW--KDVDRIVGLDKVAGMGESLHGAVKTRKGMFrTVGQLYKEQLMNLMTTLRNTNPNFVRCII 677
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAV-SVGTQFKIQLNELLSTVRATTPRYVRCIK 636
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 319655760 678 PNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 725
Cdd:cd14899 637 PNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
93-768 |
4.06e-101 |
|
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: 342.78 E-value: 4.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRE 164
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 165 DQSILCTGESGAGKTENTKKVIQYLAYVaSSFKTKKDQSSialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 244
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAV-SDRRHGADSQG-------LEARLLQSGPVLEAFGNAHTVLNANSSRFGKML 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 245 RINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAgdklrselcledynkyrFLSNGNVTIPGQQDRELF 324
Cdd:cd14887 153 LLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAA-----------------VAAATQKSSAGEGDPEST 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 325 A--ETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF--------KKERNSDQASMPDDTAAQKVSHLL-------GMNV 387
Cdd:cd14887 216 DlrRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFttdqepetSKKRKLTSVSVGCEETAADRSHSSevkclssGLKV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 388 TDFTRAILS--------PRIKVGRDFV------------QKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKR 447
Cdd:cd14887 296 TEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAK 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 448 -------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGI----EWSFI 507
Cdd:cd14887 376 psesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqDCSAF 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 508 DFGLDLQPCI--------------------ELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQELGN-------NPK 560
Cdd:cd14887 456 PFSFPLASTLtsspsstspfsptpsfrsssAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNkniinsaKYK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 561 FQKPKKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNqSVDKFVSElwkdvdriVGLDKVAGMgeslhGAV 640
Cdd:cd14887 536 NITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFL-ACSTYTRL--------VGSKKNSGV-----RAI 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 641 KTRKgmfRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 720
Cdd:cd14887 602 SSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 319655760 721 FRQRYEILTPNAIpKGFMDGKQACVLMVKALELDSNLYRIGQSKVFFR 768
Cdd:cd14887 679 LWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-768 |
3.04e-94 |
|
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: 320.04 E-value: 3.04e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEivemYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINE----YKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYlaYVASsfkTKKDQssialshgELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSG---VKEDN--------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDAFR 332
Cdd:cd14937 144 NIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISFD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIpEDEQTGLLKVVSAVLQLGNMSFK---KERNSDQASMPDDT--AAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQ 407
Cdd:cd14937 224 KMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 408 KAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 487
Cdd:cd14937 303 IPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 488 TMFILEQEEYQREGIEWSFIDFGLDlQPCIELIEkpnGPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKl 567
Cdd:cd14937 382 IVYEKETELYKAEDILIESVKYTTN-ESIIDLLR---GKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKK- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 568 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDrivgldkvagMGESLhgavkTRKGMf 647
Cdd:cd14937 457 DINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE----------VSESL-----GRKNL- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 648 rtVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQEFRQRYEI 727
Cdd:cd14937 521 --ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEY 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 319655760 728 LTPNAIPKGFMDGKQACVLMVKAlELDSNLYRIGQSKVFFR 768
Cdd:cd14937 598 LDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
93-768 |
5.31e-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: 317.14 E-value: 5.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMY---KGKKRHEMPPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 170 CTGESGAGKTENTKKVIQYLAYVASSFKTKkdqssialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF- 248
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT------------FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFc 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 249 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNG----NVTIPGQQDRELF 324
Cdd:cd14878 149 ERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmredVSTAERSLNREKL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 325 AETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRD 404
Cdd:cd14878 229 AVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 405 FVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL---DKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 481
Cdd:cd14878 309 MIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 482 QQLFNHTMFILEQEEYQREGI----------EWSFIDFgldlqpcieLIEKPNgppGILALLDEECWFPKATDKSFVEKV 551
Cdd:cd14878 389 HHYINEVLFLQEQTECVQEGVtmetayspgnQTGVLDF---------FFQKPS---GFLSLLDEESQMIWSVEPNLPKKL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 552 --VQELGNNPKFQKPKK-------LKDD-ADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKdvd 621
Cdd:cd14878 457 qsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ--- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 622 rivglDKVAgmgeslhgavktrkgmfrTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGV 701
Cdd:cd14878 534 -----SKLV------------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGV 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 702 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAI-PKGFMDGKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd14878 591 LEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
90-767 |
3.23e-92 |
|
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: 314.49 E-value: 3.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 90 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKYLPI--------YTEEIVEMYKGKKRHEMPpHIYAITDTAYRS 158
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSnsdaslgeYGSEYYDTTSGSKEPLPP-HAYDLAARAYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 159 MMQDREDQSILCTGESGAGKTENTKKVI-QYLAYVASSFKTKKdqssialshgeLEKQLLQANPILEAFGNAKTVKNDNS 237
Cdd:cd14879 78 MRRRSEDQAVVFLGETGSGKSESRRLLLrQLLRLSSHSKKGTK-----------LSSQISAAEFVLDSFGNAKTLTNPNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 238 SRFGKFIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFL--SNGNVT- 314
Cdd:cd14879 147 SRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGCHPLp 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 315 -IPGQQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFkkernSDQASMPDDTAA-------QKVSHLLGMN 386
Cdd:cd14879 227 lGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEF-----TYDHEGGEESAVvkntdvlDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 387 VTDFtRAILSPRIK-VGRD----FVQKAQTQEQAefavEALAKATYERLFRWLVMRINKALDKTKRQGASFIGILDIAGF 461
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQR----DELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 462 EIF---ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEEC- 537
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTr 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 538 WFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD---FCIIHYAGKVDYKANEWLMKNMDPLndnvatllnqSVDkFVS 614
Cdd:cd14879 454 RMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 615 elwkdvdrivgldkvagmgeslhgavktrkgMFRTVGQLyKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLD 694
Cdd:cd14879 523 -------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKA 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319655760 695 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACVLMVKALELDSNLYRIGQSKVFF 767
Cdd:cd14879 571 QIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
94-732 |
3.09e-91 |
|
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: 309.52 E-value: 3.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKylPIYTEEIVEMYKGKKRHeMPPHIYAITDTAYRSMMQdREDQSILCTGE 173
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYvassfKTKKDQSsialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvnGY 253
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----RTASTTS--------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSelcleDYNKYRF-LSNGNVTIPGQQDRELfaeTIDAFR 332
Cdd:cd14898 143 ITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKN-----DFIDTSStAGNKESIVQLSEKYKM---TCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 333 IMGIP--EDEQTGLLkvvsAVLQLGNMSFKkerNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQ 410
Cdd:cd14898 215 SLGIAnfKSIEDCLL----GILYLGSIQFV---NDGILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 411 TQEQAEFAVEALAKATYERLFRWLVMRINKALDKTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 490
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 491 ILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKdd 570
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNGFINTKARDKIK-- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 571 adfcIIHYAGKVDYKANEWLMKNMDplndnvatllnqsvdkfvselwKDVDRIVGLDKVAGMGESlhgavktrkgmfRTV 650
Cdd:cd14898 439 ----VSHYAGDVEYDLRDFLDKNRE----------------------KGQLLIFKNLLINDEGSK------------EDL 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 651 GQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 730
Cdd:cd14898 481 VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
..
gi 319655760 731 NA 732
Cdd:cd14898 561 TL 562
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
93-720 |
1.40e-81 |
|
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: 284.49 E-value: 1.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKGKKRHE-------MPPHIYAITDTAYRSMMQDRE 164
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 165 DQSILCTGESGAGKTENTKKVIQYLAYVASSfktkkdqssiaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFI 244
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD-----------SQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRIN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 245 RINFD---------VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSE-----------LCLEDYNK 304
Cdd:cd14884 150 LLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARrnlvrncgvygLLNPDESH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 305 YRFLSNGNVTIPG----------QQDRELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKernsdqasmpddt 374
Cdd:cd14884 230 QKRSVKGTLRLGSdsldpseeekAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 375 aaqkVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGA---- 450
Cdd:cd14884 297 ----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdne 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 451 -------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGlDLQPCIELIEKp 523
Cdd:cd14884 373 diysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 524 ngppgILALLDE-----ECWFPKATDKSFV-----EKVVQELGN------NPKFQ----KPKKLKDDAdFCIIHYAGKVD 583
Cdd:cd14884 451 -----IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKvsygfvLNHDAdgtaKKQNIKKNI-FFIRHYAGLVT 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 584 YKANEWLMKNMDPLNDNVATLLNQSVDKFVSElwkdvdrivgldkvagmgeslhGAVKTRKGMFRTVGQLYKEQLMNLMT 663
Cdd:cd14884 525 YRINNWIDKNSDKIETSIETLISCSSNRFLRE----------------------ANNGGNKGNFLSVSKKYIKELDNLFT 582
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 664 TLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 720
Cdd:cd14884 583 QLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
94-744 |
3.90e-77 |
|
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: 270.06 E-value: 3.90e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKY----LPIYTEEIVEMYkgkkrhempPHIYAITDTAYRSMMQDREDQSIL 169
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 170 CTGESGAGKTENTKKVIQYLAYVASsfktkkdqssialshGELE----KQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 245
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAG---------------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 246 INFdVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYN--KYRFLSNGNVTIPGQQDREL 323
Cdd:cd14881 138 VQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 324 FAETIDAFRIMGIPedeQTGLLKVVSAVLQLGNMSFKkERNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGR 403
Cdd:cd14881 217 FQAWKACLGILGIP---FLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 404 DFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKaldkTKRQGAS--------FIGILDIAGFEIFELNSFEQLCIN 475
Cdd:cd14881 293 QLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCIN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 476 YTNEKLQQLFNHTMFILEQEEYQREGIEWSF-IDFgLDLQPCIELIEkpNGPPGILALLDEECwFPKATDKSFVEKVVQE 554
Cdd:cd14881 369 LCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 555 LGNNPKFQKPKKlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFvselwkdvdrivgldkvagmge 634
Cdd:cd14881 445 HRQNPRLFEAKP-QDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNF---------------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 635 slhgavktrkgMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPN 714
Cdd:cd14881 502 -----------GFATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPH 570
|
650 660 670
....*....|....*....|....*....|
gi 319655760 715 RIVFQEFRQRYEILTPNAIPKGFMDGKQAC 744
Cdd:cd14881 571 RMRFKAFNARYRLLAPFRLLRRVEEKALED 600
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
94-721 |
1.57e-73 |
|
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: 260.41 E-value: 1.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLP-IYTEEIVEMYKgkKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLayvassFKTKKDQSSIalshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 252
Cdd:cd14905 80 ESGSGKSENTKIIIQYL------LTTDLSRSKY------LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 253 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSN-GNVTIPGQQDRELFAETIDAF 331
Cdd:cd14905 148 EIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMSF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 332 RIMGIPEDEQTGLLKVVSAVLQLGNMSFKKErnSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKVGRDFVQKAqt 411
Cdd:cd14905 228 VFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 412 qeqaefavEALAKATYERLFRWLVMRINKALDKTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 491
Cdd:cd14905 304 --------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 492 LEQEEYQREGIEW-SFIDFGlDLQPCIELIEKpngppgILALLDEECWFPKATDKSFVEKVVQELGNNPKF-QKPKKlkd 569
Cdd:cd14905 374 QEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPNK--- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 570 dadFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELwkdvDRIVGLD-KVAGMGESLHGAVKTRKGMFR 648
Cdd:cd14905 444 ---FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFSR----DGVFNINaTVAELNQMFDAKNTAKKSPLS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 649 TVGQLYKEQLMN-----------------------------LMTTLRNTNP---------NFVRCIIPNHEKKAGKLAHH 690
Cdd:cd14905 517 IVKVLLSCGSNNpnnvnnpnnnsgggggggnsgggsgsggsTYTTYSSTNKainnsncdfHFIRCIKPNSKKTHLTFDVK 596
|
650 660 670
....*....|....*....|....*....|....*
gi 319655760 691 LVLDQLRCNGVLEGIRICRQGFP----NRIVFQEF 721
Cdd:cd14905 597 SVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRF 631
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
93-733 |
1.23e-71 |
|
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: 253.64 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 93 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYkgkkrhemppHIYAITDTAYRSMMQDRED-QSILCT 171
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 172 GESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshgelekqllqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 251
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAI--------------ESVFKSFGCAKTLKNDEATRFGCSIDLLYKRN 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 252 gYIVGANIE-TYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDRELFAETIDA 330
Cdd:cd14874 137 -VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLEDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 331 FRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKERNS----DQASMPDDTAAQKVSHLLGMNVTDFTrAILSPRIKVGRDFv 406
Cdd:cd14874 216 LHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPnveqDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDGTTI- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 407 qkaqTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 486
Cdd:cd14874 294 ----DLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 487 HTMFILEQEEYQREGIEwsfIDF----GLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQ 562
Cdd:cd14874 368 KHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLFKK--PYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 563 KPKKlKDDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivgldkvagmgeslHGAvkT 642
Cdd:cd14874 443 KARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFES-----------------YSS--N 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 643 RKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 722
Cdd:cd14874 503 TSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFA 582
|
650
....*....|.
gi 319655760 723 QRYEILTPNAI 733
Cdd:cd14874 583 RQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
94-768 |
2.63e-68 |
|
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: 244.26 E-value: 2.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 173
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 174 SGAGKTENTKKVIQYLAYVASSfktkkdqssialSHGELEKqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDG------------NRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 254 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTG--AGDKLRsELCLEDYNKYRFLsNGNVTIPG----------QQDR 321
Cdd:cd14882 149 MSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYL-RIPPEVPPsklkyrrddpEGNV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 322 ELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNMSFKKerNSDQASMPDDTAAQKVSHLLGMNVTDFTRAILSPRIKV 401
Cdd:cd14882 227 ERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 402 GRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKrqgASF-----IGILDIAGFEIFELNSFEQLCINY 476
Cdd:cd14882 305 GGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 477 TNEKLQQLFNHTMFI---LEQEEYQREGIEWSFIDFGLDLQpciELIEKPNgppGILALLDEECwfPKATDKSFVEKVVQ 553
Cdd:cd14882 382 LNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVD---QLMTKPD---GLFYIIDDAS--RSCQDQNYIMDRIK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 554 ElgNNPKFQKPKKlkdDADFCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDvdrivglDKVAGMg 633
Cdd:cd14882 454 E--KHSQFVKKHS---AHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 634 eslhgavKTRKGMFRTVGQlykEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFP 713
Cdd:cd14882 521 -------RTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFS 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 714 NRIVFQEFRQRYEILTPNAIPKGFMDgKQACVLMVKALELDSnlYRIGQSKVFFR 768
Cdd:cd14882 591 YRIPFQEFLRRYQFLAFDFDETVEMT-KDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
96-726 |
4.62e-67 |
|
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: 242.95 E-value: 4.62e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 96 LHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYT----------EEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDRED 165
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTpdhmqaynksREQTPLYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 166 QSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 245
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 246 INFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAG------DKLRSELCLEDYNKYRFLSN--GNVTIPG 317
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdptlrDSLEMNKCVNEFVMLKQADPlaTNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 318 QQDRELFAetidAFRIMGIPEDEQTGLLKVVSAVLQLGNMSF------KKERN-------SDQAS--MPDDTAAQKVSHL 382
Cdd:cd14893 244 RDYRDLMS----SFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGgansttvSDAQScaLKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 383 LGMN--VTD---FTRAILSpriKVGRDFVQ--KAQTQEQAEFAVEALAKATYERLFRWLVMRINKAL----DKTKRQG-- 449
Cdd:cd14893 320 LEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNiv 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 450 --ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWSFIDFGLDLQPCIE 518
Cdd:cd14893 397 inSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 519 LIEKPngPPGILALLDEECWFPKATDKSFVEKVVQELGNNPKFQKPKKLKDDAD------------FCIIHYAGKVDYKA 586
Cdd:cd14893 477 LFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNG 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 587 NEWLMKNMDPLNDNVATLLNQSVDKfvselwkdVDRIVGLDKVAGMGESLHGAVKTRKG----MFRTVGQLYKE------ 656
Cdd:cd14893 555 KGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAAASSEKAAKQTEERGstssKFRKSASSAREsknitd 626
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 657 --------QLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 726
Cdd:cd14893 627 saatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-253 |
3.24e-59 |
|
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: 201.42 E-value: 3.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 115 FCVVINPYKYLPIYTEEIV-EMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGESGAGKTENTKKVIQYLAYVA 193
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319655760 194 SSFKTKKDQSS---IALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 253
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 ... |
94-766 |
7.72e-58 |
|
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: 214.70 E-value: 7.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 94 SVLHNLRERYYSGLIYTYSGLFCVVINPYKYLPIYTEEIVEMYK-GKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 172
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 173 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALS-----------HGELEKQLLQANPILEAFGNAKTVKNDNSSRFG 241
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEdnihneentdyQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 242 KFIRINFDvNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYNKYRFLSNGNVTIPGQQDR 321
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 322 ELFAETIDAFRIMGIPEDEQTGLLKVVSAVLQLGNM----SFKKE-----RNSDQASMPDDTAAQKVSH----------- 381
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgKNQCGQNINYETILSELENsedigldenvk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 382 -------LLGMNVTDFTRAILSPRIkVGRDFVQKAQTQEQAEFAVEALAKATYERLFRWLVMRINKALDKTKR--QGASF 452
Cdd:cd14938 321 nlllackLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 453 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgpPGILAL 532
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT--EGSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 533 LDEECWFPKATDKS-FVEKVVQELGNNPKFQKPKKLKDDAD-FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVD 610
Cdd:cd14938 478 LLENVSTKTIFDKSnLHSSIIRKFSRNSKYIKKDDITGNKKtFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 611 KFVSELWKDVDrivgLDKVAGMGE-----SLHGAVKTRKGMFRTVGQ----LYKEQLMNLMTTLRNTNPNFVRCIIPNHE 681
Cdd:cd14938 558 EYMRQFCMFYN----YDNSGNIVEekrrySIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 682 KKA-GKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACVLMVKALELDSNLYRI 760
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 319655760 761 GQSKVF 766
Cdd:cd14938 706 GNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
952-1851 |
2.04e-32 |
|
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: 138.27 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 952 LEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHET 1031
Cdd:TIGR02168 216 KELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1032 MITDLEDRLrkeekmrQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIR 1111
Cdd:TIGR02168 296 EISRLEQQK-------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1112 EMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKRETEVTQLKKTLEDEAraheqml 1191
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAE------- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1192 sevRQKHNQAFEELNEQLEQskrskasvdkakqaLESERNELQIELKSLSQSKNDSENRRKKAESQLQELQ--VKHTESE 1269
Cdd:TIGR02168 435 ---LKELQAELEELEEELEE--------------LQEELERLEEALEELREELEEAEQALDAAERELAQLQarLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1270 RQKHELLDKVSKMQAELESLQGTVTKVESKSIK-AAKDCSAVESQL-KDAQALL-EEETRQKLAISTrlrqleDEQNNLK 1346
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAAIEAALgGRLQAVVvENLNAAKKAIAF------LKQNELG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1347 EMLEEEEESKKNVekqlhTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLeernASYDKLDkTKTRLQREL 1426
Cdd:TIGR02168 572 RVTFLPLDSIKGT-----EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGV----LVVDDLD-NALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1427 D---DVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVN 1503
Cdd:TIGR02168 642 RpgyRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1504 KQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDlqsrdeq 1583
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL------- 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1584 gEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIdlankarDEALKQLKKLQAQMKEQMREFEDLRL 1663
Cdd:TIGR02168 795 -KEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL-------EDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1664 SRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQleeele 1743
Cdd:TIGR02168 867 LIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN------ 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1744 eehlsvelVNDRLkkaslqAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELeGAV-----------------K 1806
Cdd:TIGR02168 941 --------LQERL------SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL-GPVnlaaieeyeelkerydfL 1005
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 319655760 1807 SKYKSTITALETKIQQLEEQLDSEMKERQQSTKQvrRVEKKLKEV 1851
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARERFKDTFD--QVNENFQRV 1048
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
978-1802 |
2.59e-31 |
|
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: 134.81 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 978 KKIEEDLMVIEDQNAKLSK---EKKQMEERISEFTTNLaeeEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNR 1054
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKaleELEEVEENIERLDLII---DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1055 RKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAA--------LKNAAQKSIREMEAQISELQEDLEL 1126
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKkikdlgeeEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1127 EKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEarahEQMLSEVRQKHNQAFEELn 1206
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDEL- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1207 eqleqskrskASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAEL 1286
Cdd:TIGR02169 388 ----------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1287 ESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEeeeskknvekqLHTA 1366
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQG-----------VHGT 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1367 QAQLAEMKkkiEQEAQSLESMEDGkkKLQREV-------ESVLQQLEERNAS-YDKLDKTKTRLQRELDDVLVDQGH--- 1435
Cdd:TIGR02169 527 VAQLGSVG---ERYATAIEVAAGN--RLNNVVveddavaKEAIELLKRRKAGrATFLPLNKMRDERRDLSILSEDGVigf 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1436 ------------------LRQT--VQELERKQKKFDQM--------LAEEKSISTKYAEERDRAEAEAREKETKSLTLAR 1487
Cdd:TIGR02169 602 avdlvefdpkyepafkyvFGDTlvVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRE 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1488 ELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQ 1567
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1568 AL---KAQFERDL-QSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQ 1643
Cdd:TIGR02169 762 ELearIEELEEDLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1644 LKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSL 1723
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1724 SSDERRRLEARIAQLEEELEEEHLSVELVNDrLKKASLQAEQVTVELTA-ERSNSQRLEGLRSQLDRQNkDMKQKLQELE 1802
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRAlEPVNMLAIQEYEEVLKRLD-ELKEKRAKLE 999
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
860-1734 |
7.57e-30 |
|
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: 129.79 E-value: 7.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQ---LQAETELCQEAEEMRSRL--------TARMQEMEEVLHELESRL 928
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQlksLERQAEKAERYKELKAELrelelallVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 929 EEEEERVAQFQSEKKKMQQNIGDLE---QQLDEEEAARQKLQLEKVtmdAKLKKIEEDLMVIEDQNAKLSKEKKQMEERI 1005
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRlevSELEEEIEELQKELYALA---NEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1006 SEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKK 1085
Cdd:TIGR02168 326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1086 EEELQAALARIEEEAALKNAAQKSIRemEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEdtldstAAQQEL 1165
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1166 RAKRETevtqlkktlEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERN-ELQIELkSLSQSK 1244
Cdd:TIGR02168 478 DAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEA-ALGGRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1245 NDSENRRKKAESQLQELQVKHtesERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEE 1324
Cdd:TIGR02168 548 QAVVVENLNAAKKAIAFLKQN---ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1325 TR--QKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVL 1402
Cdd:TIGR02168 625 VLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELR 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1403 QQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKS 1482
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1483 LTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEeledelqltedaklRL 1562
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE--------------EL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1563 EVNMQALKAQFErdlqsrdeqgeekrkQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALK 1642
Cdd:TIGR02168 851 SEDIESLAAEIE---------------ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1643 QLKKLQAQMKEQMREFEDLRLSRDESLNQAKENErkikSMEAEIMQLHEDLAAADRAKrqIQQERDELQDEINSQNAKNS 1722
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEY----SLTLEEAEALENKIEDDEEE--ARRRLKRLENKIKELGPVNL 989
|
890
....*....|..
gi 319655760 1723 LSSDERRRLEAR 1734
Cdd:TIGR02168 990 AAIEEYEELKER 1001
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
99-709 |
1.13e-29 |
|
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: 128.71 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 99 LRERYYSGLIYTYSGLFCV-VINPYKYL------PIYTEEIVEMYKGKKRHE--MPPHIYAI------------------ 151
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 152 --TDTAYRSMMQDReDQSILCTGESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALS--------------------- 208
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEETCKVSgstrqpkiklftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 209 ------------------------------------------------------------HGELEKQL------------ 216
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekleHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 217 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVNGY---IVGANIETYLLEKSRAIRQA------KDERAFHI 281
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 282 FYYLLTGAG-----DKLRSELCLE--DYNKYRFLSNGNVTIPG--------QQDRELFAETIDAFRIMGIPEDEQTGLLK 346
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 347 VVSAVLQLGNMSFKKERNSDQASMPDD---TAAQKVSHLLGM-NVTDFTRAILSPRIKVGRDFVQKAQTQE--QAEFAVE 420
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 421 ALAKATYERLFRWLVMRINKAL-------DKTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQl 484
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 485 fnhtmfileqEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATD----------KSFVEKVVQE 554
Cdd:cd14894 565 ----------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 555 lgNNPKFQKPKKLKDDAD-----------FCIIHYAGKVDYKANEWLMKNMDPLNDNVATLLNQSVDKFVSELWKDVDRi 623
Cdd:cd14894 635 --NSSRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 624 vgLDKVAGMGESLHGAVKTR-KGMFRTVGQLYKEqlMNLMTTLRNTN-PNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGV 701
Cdd:cd14894 712 --LGWSPNTNRSMLGSAESRlSGTKSFVGQFRSH--VNVLTSQDDKNmPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRL 787
|
....*...
gi 319655760 702 LEGIRICR 709
Cdd:cd14894 788 IRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1168-1925 |
2.09e-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: 125.17 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1168 KRETEvTQLKKTLEDEARAhEQMLSEVRQKHN---------QAFEELNEQLEQSKRSKASVDKakqaleserNELQIELK 1238
Cdd:TIGR02168 174 RKETE-RKLERTRENLDRL-EDILNELERQLKslerqaekaERYKELKAELRELELALLVLRL---------EELREELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1239 SLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQ 1318
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1319 ALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREV 1398
Cdd:TIGR02168 323 AQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1399 ESVLQQLEERNASYDKLDKTKTRLQRELDDVLVD--QGHLRQTVQELERKQKKFDQMLAEEKSIStkyaEERDRAEAEAR 1476
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKelQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1477 EKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGkSVHELERAKRGMEQQLEEMktqleeledelqlte 1556
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG-VLSELISVDEGYEAAIEAA--------------- 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1557 daklrLEVNMQAL---KAQFERDLQSRDEQGEEKR-----------KQLVKQVREMEMELEDERKQRAQAVSVRKKLELD 1622
Cdd:TIGR02168 543 -----LGGRLQAVvveNLNAAKKAIAFLKQNELGRvtflpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1623 LSELAAQIDLANKArDEALKQLKKLQAQMK----------------EQMREFEDLRLSRDESLnqaKENERKIKSMEAEI 1686
Cdd:TIGR02168 618 LSYLLGGVLVVDDL-DNALELAKKLRPGYRivtldgdlvrpggvitGGSAKTNSSILERRREI---EELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1687 MQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQV 1766
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1767 TVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSkYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEK 1846
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1847 KLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKL 1925
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1686 |
5.31e-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: 124.01 E-value: 5.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 864 RQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKK 943
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 944 KMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQ 1023
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1024 KLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELhdQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALK 1103
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1104 NAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAlKTELEDTLDSTAAQQELRAKRETEVtqlkktledE 1183
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN-QSGLSGILGVLSELISVDEGYEAAI---------E 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1184 ARAHEQMLSEVRQKHNQAFEELnEQLEQSKRSKASV----DKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQ 1259
Cdd:TIGR02168 541 AALGGRLQAVVVENLNAAKKAI-AFLKQNELGRVTFlpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 EL--QVKHTESERQKHELLDKVSK------MQAELESLQGTVTKvesKSIKAAKDCSAVESQLKDAQALLEEETRQKLAI 1331
Cdd:TIGR02168 620 YLlgGVLVVDDLDNALELAKKLRPgyrivtLDGDLVRPGGVITG---GSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1332 STRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNAs 1411
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1412 ydkldktktrlqrelddvlvdqgHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEA 1491
Cdd:TIGR02168 776 -----------------------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1492 MTDLKNELERVNKQLKTEMEDLVSSKddagksvHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKa 1571
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR- 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1572 QFERDLQSRDEQGEEKRKQLVKQVREMEmELEDERKQRAQAVSVRKKLELDlsELAAQIDLANKARDEALKQLKKLQAQM 1651
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLE-GLEVRIDNLQERLSEEYSLTLE--EAEALENKIEDDEEEARRRLKRLENKI 981
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 319655760 1652 KE-------QMREFEDLR------LSRDESLNQAKEN-ERKIKSMEAEI 1686
Cdd:TIGR02168 982 KElgpvnlaAIEEYEELKerydflTAQKEDLTEAKETlEEAIEEIDREA 1030
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
976-1603 |
5.60e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 976 KLKKIEEDLMVIEDqnakLSKE-KKQMEErisefttnLAEEEEKSKSLQKLKTKHEtmITDLEDRLRKEEKMRQELEKNR 1054
Cdd:COG1196 180 KLEATEENLERLED----ILGElERQLEP--------LERQAEKAERYRELKEELK--ELEAELLLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1055 RKLEGDSTELHDQIAELQAQiaelRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKA 1134
Cdd:COG1196 246 AELEELEAELEELEAELAEL----EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1135 EKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKR 1214
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1215 sKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVT 1294
Cdd:COG1196 402 -LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1295 KVESKSIKAAkdcsavesQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMK 1374
Cdd:COG1196 481 ELLEELAEAA--------ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1375 KKIEQEAQSLESmEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELErkqKKFDQML 1454
Cdd:COG1196 553 VEDDEVAAAAIE-YLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT---LLGRTLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1455 AEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGM 1534
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERE 708
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1535 EQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELE 1603
Cdd:COG1196 709 LAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1047-1883 |
8.03e-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: 113.61 E-value: 8.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1047 RQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQ--LAKKEEELQAALARIEEE--AALKNAAQKSIREMEAQISELQE 1122
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQaeKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1123 DLELEKAARNKAEKQRrdlgEELEALKTELEDTLDstAAQQELRakretEVTQLKKTLEDEARAHEQMLSEVRQKhnqaF 1202
Cdd:TIGR02168 254 ELEELTAELQELEEKL----EELRLEVSELEEEIE--ELQKELY-----ALANEISRLEQQKQILRERLANLERQ----L 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1203 EELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKM 1282
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1283 QAELESLQGTVTKVES-----KSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKK 1357
Cdd:TIGR02168 399 NNEIERLEARLERLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1358 NVEKQLHTAQAQLAemkkkieqeaqSLESMEDGKKKLQREVESVLQQLEERNASYDKL-DKTKTRLQRELDDVLVDQGHL 1436
Cdd:TIGR02168 479 AAERELAQLQARLD-----------SLERLQENLEGFSEGVKALLKNQSGLSGILGVLsELISVDEGYEAAIEAALGGRL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1437 RQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTlarELEAMTDLKNELERVNKQLKTEMEDL--- 1513
Cdd:TIGR02168 548 QAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK---NIEGFLGVAKDLVKFDPKLRKALSYLlgg 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1514 ---VSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAkLRLEVNMQALKAQFERdLQSRDEQGEEKRKQ 1590
Cdd:TIGR02168 625 vlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSI-LERRREIEELEEKIEE-LEEKIAELEKALAE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1591 LVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLsrdesln 1670
Cdd:TIGR02168 703 LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE------- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1671 QAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVE 1750
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1751 LVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKskykstitALETKIQQLEEQLdSE 1830
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS--------ELRRELEELREKL-AQ 926
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1831 MKERQQSTKQ-VRRVEKKLKEVL-LQVEDERRNADQSKTETEKANIRLKQMKRQL 1883
Cdd:TIGR02168 927 LELRLEGLEVrIDNLQERLSEEYsLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
868-1513 |
1.46e-23 |
|
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: 109.39 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 868 AEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQ 947
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 948 NIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKT 1027
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELY 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1028 KHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIA---ELRAQLAKKEEELQAALarieeEAALKN 1104
Cdd:TIGR02169 473 DLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGSVGERYATAI-----EVAAGN 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1105 AAQKSIREMEAQISELQEDLELEKAAR------NKAEKQRRDLGEELE-------------------ALKTELEDTL--D 1157
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKAGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLvvE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1158 STAAQQELRAK-----RETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAfEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:TIGR02169 628 DIEAARRLMGKyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL-QRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1233 LQIELKSLSQSKNDSENRR--------------KKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVE- 1297
Cdd:TIGR02169 707 LSQELSDASRKIGEIEKEIeqleqeeeklkerlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEa 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1298 ----SKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEM 1373
Cdd:TIGR02169 787 rlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1374 KKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQM 1453
Cdd:TIGR02169 867 EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1454 LAEEKSIStKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDL 1513
Cdd:TIGR02169 947 PEEELSLE-DVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1203-1834 |
2.13e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1203 EELNEQLEQSKRSKAsvdKAK--QALESERNELQIEL-----KSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHEL 1275
Cdd:COG1196 196 GELERQLEPLERQAE---KAEryRELKEELKELEAELlllklRELEAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1276 LDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEES 1355
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1356 KKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGH 1435
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1436 LRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAmtdlknelERVNKQLKTEMEDLVS 1515
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--------AAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1516 SKDDAGKSVHELERAKRGmEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQV 1595
Cdd:COG1196 505 GFLEGVKAALLLAGLRGL-AGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1596 REMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKEN 1675
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1676 ERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDR 1755
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1756 LKKASLQAEQVTVELTAERSNSQ-RLEGLRSQLDR-----------------QNKDMKQKLQELEGAvkskykstITALE 1817
Cdd:COG1196 744 EEELLEEEALEELPEPPDLEELErELERLEREIEAlgpvnllaieeyeeleeRYDFLSEQREDLEEA--------RETLE 815
|
650
....*....|....*..
gi 319655760 1818 TKIqqleEQLDSEMKER 1834
Cdd:COG1196 816 EAI----EEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
913-1532 |
3.43e-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: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 913 RMQEMEE-------VLHELESRLEEEEErvaqfQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEkvtmdAKLKKIEEDLM 985
Cdd:COG1196 180 KLEATEEnlerledILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRELE-----AELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 986 VIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELH 1065
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEEL 1145
Cdd:COG1196 330 EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1146 EALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAfEELNEQLEQSKRSKASVDKAKQA 1225
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL-AELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1226 LESERNELQIELKSLSQSKNDSENRRKKAESQL--------------QELQVKHTESERQKHELLDKVSKMQAELESLQ- 1290
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaaYEAALEAALAAALQNIVVEDDEVAAAAIEYLKa 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1291 ---GTVTKVESKSIKAAKDCSAVESQLK--DAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHT 1365
Cdd:COG1196 569 akaGRATFLPLDKIRARAALAAALARGAigAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1366 AqaqLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELER 1445
Cdd:COG1196 649 V---TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1446 KQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVN--------------KQLKTEME 1511
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNllaieeyeeleeryDFLSEQRE 805
|
650 660
....*....|....*....|.
gi 319655760 1512 DLVSSKDDAGKSVHELERAKR 1532
Cdd:COG1196 806 DLEEARETLEEAIEEIDRETR 826
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
858-1446 |
4.11e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVL-------HELESRLEE 930
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarleerrRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 931 EEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTT 1010
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1011 NLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQ 1090
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1091 AALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARN---------KAEKQRRDLGEELEALKTEL--EDTLDST 1159
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLagavavligVEAAYEAALEAALAAALQNIvvEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1160 AAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKS 1239
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1240 LsqskndSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKdcsAVESQLKDAQA 1319
Cdd:COG1196 641 T------LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL---AEEEEERELAE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1320 LLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDgkkklqreve 1399
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGP---------- 781
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1400 sV----LQQLEERNASYDKLDKTKTRLQRELDDvlvdqghLRQTVQELERK 1446
Cdd:COG1196 782 -VnllaIEEYEELEERYDFLSEQREDLEEARET-------LEEAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1041-1883 |
6.69e-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: 103.99 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1041 RKEEKMRQELEKNRRKLEgdstELHDQIAELQAQIAELRAQLAKKEE--ELQAALARIE--EEAALKNAAQKSIREMEAQ 1116
Cdd:TIGR02169 170 RKKEKALEELEEVEENIE----RLDLIIDEKRQQLERLRREREKAERyqALLKEKREYEgyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1117 ISELQEDLElekaarnKAEKQRRDLGEELEALKTELEDtldstaAQQELRAKRETEVTQLKKTLEdearaheqmlsevrq 1196
Cdd:TIGR02169 246 LASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIG--------------- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1197 khnqafeELNEQLEQSKRSkasVDKAKQALEsernelqielkslsqsknDSENRRKKAESQLQELQVKHTESERQKHELL 1276
Cdd:TIGR02169 298 -------ELEAEIASLERS---IAEKERELE------------------DAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1277 DKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESK 1356
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1357 KNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQrevesvlQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHL 1436
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE-------QELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1437 RQTVQELERKQKKFDqmlaeeKSISTKYAEERDRAEAEAReketksLTLARELEAMTDLKNelervnkqlktemedLVSS 1516
Cdd:TIGR02169 503 EERVRGGRAVEEVLK------ASIQGVHGTVAQLGSVGER------YATAIEVAAGNRLNN---------------VVVE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1517 KDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFE-------------RDLQSRDEQ 1583
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEpafkyvfgdtlvvEDIEAARRL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1584 GEEKR-----------------------------KQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLAN 1634
Cdd:TIGR02169 636 MGKYRmvtlegelfeksgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDAS 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1635 KARDEALKQLKKLQAQMKEQMREFEDLRlSRDESLNQAKEN-ERKIKSMEAEIMQLHEDLAAADRAKRQIqqERDELQDE 1713
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELE-EDLSSLEQEIENvKSELKELEARIEELEEDLHKLEEALNDL--EARLSHSR 792
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1714 INSQNAKNSLSSDERRRLEARIAQleeeleeehlsvelVNDRLKKASLQAEQvtveltaERSNSQRLEGLRSQLDRQNKD 1793
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLRE--------------IEQKLNRLTLEKEY-------LEKEIQELQEQRIDLKEQIKS 851
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1794 MKQKLQELEGAvKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKAN 1873
Cdd:TIGR02169 852 IEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE 930
|
890
....*....|
gi 319655760 1874 IRLKQMKRQL 1883
Cdd:TIGR02169 931 EELSEIEDPK 940
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1675 |
1.26e-20 |
|
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: 99.76 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 864 RQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEvlheleSRLEEEEERVAQFQSEKK 943
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGE------EEQLRVKEKIGELEAEIA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 944 KMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDlmvIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQ 1023
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1024 KLKTKHETMITDLEDRLRKeekmRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEE-EAAL 1102
Cdd:TIGR02169 382 ETRDELKDYREKLEKLKRE----INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKqEWKL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1103 KNAAQKSIREmEAQISELQEDLelekaarNKAEKQRRDLGEELEALKTEL----EDTLDSTAAQQELRAKRETEVTQLKK 1178
Cdd:TIGR02169 458 EQLAADLSKY-EQELYDLKEEY-------DRVEKELSKLQRELAEAEAQAraseERVRGGRAVEEVLKASIQGVHGTVAQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1179 tledearaheqmLSEVRQKHNQAFEelneqLEQSKRSKASV----DKAKQALESER------------NELQIELKSLSQ 1242
Cdd:TIGR02169 530 ------------LGSVGERYATAIE-----VAAGNRLNNVVveddAVAKEAIELLKrrkagratflplNKMRDERRDLSI 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1243 SKNDS-----------ENRRKKAESQL--QELQVKHTESERqkhELLDKVS--KMQAELESLQGTVTKVESKSIKAAKDC 1307
Cdd:TIGR02169 593 LSEDGvigfavdlvefDPKYEPAFKYVfgDTLVVEDIEAAR---RLMGKYRmvTLEGELFEKSGAMTGGSRAPRGGILFS 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1308 SAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEEskknvekQLHTAQAQLAEMKKKIEQEAQSLESM 1387
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR-------KIGEIEKEIEQLEQEEEKLKERLEEL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1388 EDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLR-QTVQELERKQKkfdqmlaeeksistkyaE 1466
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLE-----------------E 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1467 ERDRAEAEAREKEtksltlaRELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLE 1546
Cdd:TIGR02169 806 EVSRIEARLREIE-------QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1547 ELEDELQ------LTEDAKLR-LEVNMQALKAQFER------DLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRaQAV 1613
Cdd:TIGR02169 879 DLESRLGdlkkerDELEAQLReLERKIEELEAQIEKkrkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE-DVQ 957
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1614 SVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLsRDESLNQAKEN 1675
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE-RIEEYEKKKRE 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1313-1850 |
1.94e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.86 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1313 QLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKK 1392
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1393 KLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAE 1472
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1473 AEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDEL 1552
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1553 QLTEDAKLRLEVNMQALKAQFERDLQ-SRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQID 1631
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1632 LANkarDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQ 1711
Cdd:COG1196 553 VED---DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1712 DEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQN 1791
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1792 KDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQL----------DSEMKERQQSTKQVRRVEKKLKE 1850
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleeealeeLPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
863-1481 |
6.03e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQLKESEAKQKQ--LNAEKLALQEQLQaETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQS 940
Cdd:PTZ00121 1167 EEARKAEDAKKAEAARKAEevRKAEELRKAEDAR-KAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKA 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQNIGDLEQQLDEEEAARQK-LQLEKVTMDAKLKKIEEdlmVIEDQNAKLSKEKKQMEE-RISEFTTNLAEE--- 1015
Cdd:PTZ00121 1246 EEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEE---KKKADEAKKAEEKKKADEaKKKAEEAKKADEakk 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1016 --EEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDstELHDQIAELQAQIAELRAQLAKKEEELQAAL 1093
Cdd:PTZ00121 1323 kaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA--EKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1094 ARIE---EEAALKNAAQKSIREMEAQISELQEDLELEKaarnKAEKQRRdlgeeLEALKTELEDTLDSTAAQQELRAKRE 1170
Cdd:PTZ00121 1401 EEDKkkaDELKKAAAAKKKADEAKKKAEEKKKADEAKK----KAEEAKK-----ADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1171 TEvtQLKKTLEDEARAHE--QMLSEVRQKHNQA--FEELNEQLEQSKRS--KASVDKAKQALESERNElqiELKSLSQSK 1244
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEakKKAEEAKKKADEAkkAAEAKKKADEAKKAeeAKKADEAKKAEEAKKAD---EAKKAEEKK 1546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1245 NDSENRR----KKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQAL 1320
Cdd:PTZ00121 1547 KADELKKaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELK 1626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1321 LEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQE----AQSLESMEDGKKKLQ- 1395
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAEEAKKAEe 1706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1396 ---------REVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAE 1466
Cdd:PTZ00121 1707 lkkkeaeekKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
650
....*....|....*
gi 319655760 1467 ERDRAEAEAREKETK 1481
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1720 |
9.11e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 859 VKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQA-ETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQ 937
Cdd:PTZ00121 1127 ARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 FQSEKKKMQQnigdlEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNaklSKEKKQMEERISEFTTNLAEEEE 1017
Cdd:PTZ00121 1207 KAEEERKAEE-----ARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR---KFEEARMAHFARRQAAIKAEEAR 1278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKTKHETmitdleDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAElrAQLAKKEEELQAALARIE 1097
Cdd:PTZ00121 1279 KADELKKAEEKKKA------DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD--AAKKKAEEAKKAAEAAKA 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1098 EEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRR--DLGEELEALKTELEDTLDSTAAQQ---ELRAKRE-- 1170
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKkadEAKKKAEek 1430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1171 TEVTQLKKTLEDEARAHEqmlSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNElqielKSLSQSKNDSENR 1250
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADE---AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAK-----KKAEEAKKKADEA 1502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1251 RKKAESQLQELQVKHTESERQKHELLDKVSKMQAelESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQ-KL 1329
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKA--DEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNmAL 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1330 AISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERN 1409
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1410 ASYDKLDKtktrlqrelddvlvdqghlrqtvQELERKQKKFDQMLAEEksistkyaEERDRAEAEAREKETKsltlaREL 1489
Cdd:PTZ00121 1661 IKAAEEAK-----------------------KAEEDKKKAEEAKKAEE--------DEKKAAEALKKEAEEA-----KKA 1704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1490 EAMTDLKNELERVNKQLKTEMEdlvsskdDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQAL 1569
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEE-------ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1570 KAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKklELDLSELAAQIDLANKARDEAlkqlkklqa 1649
Cdd:PTZ00121 1778 EAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK--EMEDSAIKEVADSKNMQLEEA--------- 1846
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1650 qmkeqmREFEDLRLSRDeslNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAK 1720
Cdd:PTZ00121 1847 ------DAFEKHKFNKN---NENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1014-1866 |
9.11e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.05 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1014 EEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQElEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEEL-QAA 1092
Cdd:PTZ00121 1089 ADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA-EDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1093 LARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARnKAEKQRRdlgeELEALKTELEDTLDSTAAQQELRAKRETE 1172
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAAR-KAEEERK----AEEARKAEDAKKAEAVKKAEEAKKDAEEA 1242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1173 VTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRK 1252
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK 1322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1253 KAESQLQELQVKHTESERQKHEllDKVSKMQAELESlqgtvTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAIS 1332
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKA--AEAAKAEAEAAA-----DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1333 TRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKlqREVESVLQQLEERNASY 1412
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA--KKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1413 DKldKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSltlARELEAM 1492
Cdd:PTZ00121 1474 EA--KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK---AEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1493 TDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMktqleeledELQLTEDAKLRLEvnmQALKAQ 1572
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV---------MKLYEEEKKMKAE---EAKKAE 1616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1573 FERDLQSRDEQGEEKRKQLvkqvrEMEMELEDERKQRAQavSVRKKLEldlselaaqidlANKARDEALKQLKKLQAQMK 1652
Cdd:PTZ00121 1617 EAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAE--ELKKAEE------------ENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1653 EQMREFEDLRLSRDESLNQAKENERKIKsmeaeimQLHEDLAAADRAKRQIQQERDElqDEINSQNAKNSLSSDERRRLE 1732
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAE-------ELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEEDKKKAEE 1748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1733 ARIAQLEEELeeehlsvelVNDRLKKASLQAEQVTVELTA--ERSNSQRLEGLRSQLDRQNKDMKQKLQEL-EGAVKSKy 1809
Cdd:PTZ00121 1749 AKKDEEEKKK---------IAHLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDNFANIiEGGKEGN- 1818
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1810 kstitaleTKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQV-----EDERRNADQSK 1866
Cdd:PTZ00121 1819 --------LVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKnnengEDGNKEADFNK 1872
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
858-1721 |
1.58e-18 |
|
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: 92.73 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 L-----VKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEE 932
Cdd:pfam02463 175 LkklieETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 933 ERVAQFQSEKKKMQQNigdlEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNL 1012
Cdd:pfam02463 255 SSKQEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1013 AEEEEKSKSLQKLKTKHEtmiTDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAA 1092
Cdd:pfam02463 331 KKEKEEIEELEKELKELE---IKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1093 LARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAarnkAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETE 1172
Cdd:pfam02463 408 QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQG----KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1173 VTQLKKTLEDEARAHEQMLSEVRQKHNqAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQS---KNDSEN 1249
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLK-VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVsatADEVEE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1250 RRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALL-EEETRQK 1328
Cdd:pfam02463 563 RQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELtKLKESAK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1329 LAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEER 1408
Cdd:pfam02463 643 AKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1409 NASYDKLDKTKtrlqrelddvlvdqghlrQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARE 1488
Cdd:pfam02463 723 LADRVQEAQDK------------------INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1489 LEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQA 1568
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1569 LKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQ 1648
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEE 944
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1649 AQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQ-IQQERDELQDEINSQNAKN 1721
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKErLEEEKKKLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
977-1879 |
2.10e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.90 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 977 LKKIEEdlMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEK--NR 1054
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKaeEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1055 RKLEGDSTELHDQIAELQAQIAELR--AQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARn 1132
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARkaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAAR- 1182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1133 KAEKQRRdlGEELEalKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQS 1212
Cdd:PTZ00121 1183 KAEEVRK--AEELR--KAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1213 KRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQvKHTESERQKHELLDKVSKMQAELESLQGT 1292
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1293 VTKVESKSIKAAKDCSAVESQLKDAQ-----ALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQ 1367
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEekaeaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAK 1417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1368 AQLAEMKKKIEQ---------EAQSLESMEDGKKKLQ--REVESVLQQLEERNASYDKldKTKTRLQRELDDVLVDQGHL 1436
Cdd:PTZ00121 1418 KKADEAKKKAEEkkkadeakkKAEEAKKADEAKKKAEeaKKAEEAKKKAEEAKKADEA--KKKAEEAKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1437 RQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSltlARELEAMTDLKNELERVNKQLKTEMEDLVSS 1516
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK---AEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1517 KDDAGKSVHELERAKRGMEQQLEEMktQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVR 1596
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1597 EMEMElEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQlKKLQAQMKEQMREFEDLRLSRDESLNQAKEnE 1676
Cdd:PTZ00121 1651 ELKKA-EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEE-E 1727
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1677 RKIKSMEA-----EIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSL-------SSDERRRLEA-RIAQLEEELE 1743
Cdd:PTZ00121 1728 NKIKAEEAkkeaeEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieeeldEEDEKRRMEVdKKIKDIFDNF 1807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1744 EEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEglrSQLDRQNKDMKQKLQELEGAVKSKYKSTITALETKIQQL 1823
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE---ADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI 1884
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1824 EE-----QLDSEMKERQQSTKQVRRVEKKLKEVLLQVeDERRNADQSKTETEKANIRLKQM 1879
Cdd:PTZ00121 1885 EEadeieKIDKDDIEREIPNNNMAGKNNDIIDDKLDK-DEYIKRDAEETREEIIKISKKDM 1944
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
996-1871 |
3.39e-18 |
|
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: 91.96 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 996 KEKKQMEERISEFTTNLAEEEEKSKSLQKL--KTKHETMITDLEDRLRKEEKMRQELEKNRRK-----LEGDSTELHDQI 1068
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETenLAELIIDLEELKLQELKLKEQAKKALEYYQLkekleLEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1069 AELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1149 KTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHnqafEELNEQLEQSKRSKASVDKAKQALES 1228
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE----KLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1229 ERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCS 1308
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1309 AVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESME 1388
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1389 DGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEER 1468
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1469 DRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEEL 1548
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1549 EDELQLTEDaklrLEVNMQALKAQFERDLQSRDEQgEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAA 1628
Cdd:pfam02463 709 KEELKKLKL----EAEELLADRVQEAQDKINEELK-LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1629 QIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERD 1708
Cdd:pfam02463 784 EKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1709 ELQDEINSQNAKNSLSSDERRRLEARIAQLEEEleeehlsvelvndRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLD 1788
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEK-------------EEKKELEEESQKLNLLEEKENEIEERIKEEAEIL 930
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1789 RQNKDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTE 1868
Cdd:pfam02463 931 LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
|
...
gi 319655760 1869 TEK 1871
Cdd:pfam02463 1011 IIE 1013
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
880-1535 |
9.84e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 90.12 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 880 KQLNAEKLALQEQLQAEtelcqeaEEMRSRLTARMQEMEEVLHelesrleeeeervaqfqsEKKKMQQNIGDLEQQLDEE 959
Cdd:PRK03918 172 KEIKRRIERLEKFIKRT-------ENIEELIKEKEKELEEVLR------------------EINEISSELPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 960 EAARQKLQLEKVTMDAKLKKIEEdlmvIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITdLEDR 1039
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELES----LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1040 LRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRaQLAKKEEELQAALARIEEEAALKNAAQKSIREMEaQISE 1119
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELE-RLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1120 LQEDLELEKAARnkaekqrrdLGEELEALKTELEDTLDSTAAQqelRAKRETEVTQLKKTLEDEARAHE------QMLSE 1193
Cdd:PRK03918 380 RLTGLTPEKLEK---------ELEELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKGkcpvcgRELTE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1194 VRQKhnQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKslsqskndsENRRKKAESQLQElQVKHTESERQKH 1273
Cdd:PRK03918 448 EHRK--ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK---------KESELIKLKELAE-QLKELEEKLKKY 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1274 ElLDKVSKMQAELEslqgtvtKVESKSIKAAKDCSAVESQLKDAQALleeetrqklaiSTRLRQLEDEqnnlkemleeee 1353
Cdd:PRK03918 516 N-LEELEKKAEEYE-------KLKEKLIKLKGEIKSLKKELEKLEEL-----------KKKLAELEKK------------ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1354 eskknvekqLHTAQAQLAEMKKKIEQEAqsLESMEdgkkklqrEVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQ 1433
Cdd:PRK03918 565 ---------LDELEEELAELLKELEELG--FESVE--------ELEERLKELEPFYNEYLELKDAEKELEREEKELKKLE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1434 GHLRQTVQELERKQKKFDQMLAEEKSISTKYAEErdraeaEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDL 1513
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKL 699
|
650 660
....*....|....*....|..
gi 319655760 1514 VSSKDDAGKSVHELERAKRGME 1535
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALE 721
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
937-1818 |
4.48e-17 |
|
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: 88.18 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 937 QFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDL---MVIEDQNAKLSKEKKQMEERISEFTTNLA 1013
Cdd:TIGR00606 214 QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLskiMKLDNEIKALKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1014 EEEEKS-KSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAA 1092
Cdd:TIGR00606 294 KVFQGTdEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1093 LARIE---------EEAALKNAAQKSIREMEAQ-------ISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTl 1156
Cdd:TIGR00606 374 ATRLEldgfergpfSERQIKNFHTLVIERQEDEaktaaqlCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1157 dstaaQQELRAKREtEVTQLKKTLEDEARAHEQMLSEVRQ----KHNQAFEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:TIGR00606 453 -----QEELKFVIK-ELQQLEGSSDRILELDQELRKAERElskaEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1233 LQIELKSLSQSKNDSENRRKKAEsQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVES 1312
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1313 QLKDAQALLEEETRQKLAISTRLRQL---EDEQNNLKEMLEEEEESKKNVEKqLHTAQAQLAEMKKKIEQEAQSLESMED 1389
Cdd:TIGR00606 606 NKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIEKSSKQRAM-LAGATAVYSQFITQLTDENQSCCPVCQ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1390 GKKKLQREVESVLQQLEERNASY-DKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEER 1468
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1469 DRAEAEAREKET--KSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKD--DAGKSVHELERAKRGMEQQLEEMKTQ 1544
Cdd:TIGR00606 765 NDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1545 LEELEDELQLTEDAKLRLEVNMQALKA---QFERDLQSRdEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLEL 1621
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRR-QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQ 923
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1622 DLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDlrlsrdeSLNQAKENERKIKsmEAEIMQLHEDLAAADRAKR 1701
Cdd:TIGR00606 924 EKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIEN-------KIQDGKDDYLKQK--ETELNTVNAQLEECEKHQE 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1702 QIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLE 1781
Cdd:TIGR00606 995 KINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLAL 1074
|
890 900 910
....*....|....*....|....*....|....*...
gi 319655760 1782 GLRSQLDRQNKDMKQKLQELE-GAVKSKYKSTITALET 1818
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMRT 1112
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1107-1851 |
7.91e-17 |
|
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: 87.10 E-value: 7.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1107 QKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDtldSTAAQQELRAKRETEVTQLKKTLedeaRA 1186
Cdd:pfam15921 109 RQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEA---AKCLKEDMLEDSNTQIEQLRKMM----LS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 HEQMLSEVRQKHNQaFEELNEQ--LEQSKRSKASVDKAKQALESERNELQIELKSLsqskndsENRRKKAESQLQELQvk 1264
Cdd:pfam15921 182 HEGVLQEIRSILVD-FEEASGKkiYEHDSMSTMHFRSLGSAISKILRELDTEISYL-------KGRIFPVEDQLEALK-- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1265 hTESERQKHELL----DKVSKMQAELESlqgTVTKVESKSIKAAKDCSAVESQLKdaqaLLEEETRQKLAISTR-LRQLE 1339
Cdd:pfam15921 252 -SESQNKIELLLqqhqDRIEQLISEHEV---EITGLTEKASSARSQANSIQSQLE----IIQEQARNQNSMYMRqLSDLE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1340 DE----QNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESvlqqlEERNASYDKl 1415
Cdd:pfam15921 324 STvsqlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK-----REKELSLEK- 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1416 DKTKTRLQREL-DDVLVDqgHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTD 1494
Cdd:pfam15921 398 EQNKRLWDRDTgNSITID--HLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKE 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1495 LkneLERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMktqleeledelqltedAKLRLEVNMQAlkaqfe 1574
Cdd:pfam15921 476 M---LRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI----------------TKLRSRVDLKL------ 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1575 RDLQSRDEQGEekrkqlvkQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQ 1654
Cdd:pfam15921 531 QELQHLKNEGD--------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDR 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1655 MREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEI-NSQNAKNSLSSDerrrlea 1733
Cdd:pfam15921 603 RLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVkTSRNELNSLSED------- 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1734 riaqLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGavkskyksTI 1813
Cdd:pfam15921 676 ----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRG--------QI 743
|
730 740 750
....*....|....*....|....*....|....*...
gi 319655760 1814 TALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEV 1851
Cdd:pfam15921 744 DALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTV 781
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
939-1525 |
8.05e-17 |
|
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: 87.00 E-value: 8.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEK 1018
Cdd:TIGR04523 46 KNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDLEDRLRKEEKM-------RQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQA 1091
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKEleklnnkYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1092 ALARIEEEAALK---NAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAK 1168
Cdd:TIGR04523 206 LKKKIQKNKSLEsqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1169 RETEVTQLKKTLED-----EARAHEQMLSEVRQK-------------HNQAFEELNEQLEQSKRSKASVDKAKQALESER 1230
Cdd:TIGR04523 286 LEKQLNQLKSEISDlnnqkEQDWNKELKSELKNQekkleeiqnqisqNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1231 NELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAV 1310
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1311 ESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKI---EQEAQSLESM 1387
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVkdlTKKISSLKEK 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1388 EDGKKKLQREVESVLQQLEERNASyDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEeksistkYAEE 1467
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNK-DDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ-------KEKE 597
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1468 RDRAEAEAREKETKSLTLARELEamtdlknELERVNKQLKTEMEDLVSSKDDAGKSVH 1525
Cdd:TIGR04523 598 KKDLIKEIEEKEKKISSLEKELE-------KAKKENEKLSSIIKNIKSKKNKLKQEVK 648
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
860-1735 |
1.04e-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: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEdQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLheleSRLEEEEERVAQFQ 939
Cdd:TIGR00606 201 KVQEHQMELK-YLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL----SKIMKLDNEIKALK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLDEE-EAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEK 1018
Cdd:TIGR00606 276 SRKKQMEKDNSELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDLEDRLR---------KEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEEL 1089
Cdd:TIGR00606 356 ADRHQEHIRARDSLIQSLATRLEldgfergpfSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1090 QAALARIEEEAALKNAAQKSIREMEAQISE--------LQEDLELEKAARNKAEKQRRDLGE----ELEALKTELEDTLD 1157
Cdd:TIGR00606 436 KGLGRTIELKKEILEKKQEELKFVIKELQQlegssdriLELDQELRKAERELSKAEKNSLTEtlkkEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1158 STAAQQELRAKRETEVTQLKKTL---EDEARAHEQmlseVRQKHNQAFEELNEQL------EQSKRSKASVDKAKQALES 1228
Cdd:TIGR00606 516 KLRKLDQEMEQLNHHTTTRTQMEmltKDKMDKDEQ----IRKIKSRHSDELTSLLgyfpnkKQLEDWLHSKSKEINQTRD 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1229 ERNELQIELKSLSQSKNDSENRRKKAESQLQEL----------QVKHTESERQKHElLDKVSKMQAELESLQGTVTKVES 1298
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYedklfdvcgsQDEESDLERLKEE-IEKSSKQRAMLAGATAVYSQFIT 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1299 KSIKAAKDCSAVESQLKDAQALLEEETRQklaISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIE 1378
Cdd:TIGR00606 671 QLTDENQSCCPVCQRVFQTEAELQEFISD---LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1379 QEAQSLESMEDGKKKLQREVESVLQQLEERNASydkldktktrlQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEK 1458
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE-----------EESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQ 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1459 SISTKYAEERDRAEAEarEKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHEleraKRGMEQQL 1538
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQL 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1539 EEMKTQLEELEDELQLTEDAKLRLEvnmqalkaQFERDLQSRDEQGEEKRKQLVKQVremEMELEDERKQRAQAVSVRKK 1618
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLE--------TFLEKDQQEKEELISSKETSNKKA---QDKVNDIKEKVKNIHGYMKD 959
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1619 LELDLSElaAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRdESLNQAKENERKIKS------MEAEIMQLHED 1692
Cdd:TIGR00606 960 IENKIQD--GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-QDIDTQKIQERWLQDnltlrkRENELKEVEEE 1036
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 319655760 1693 LAAADRAKRQIQ-----QERDELQDEINSQNAKNSLSSDERRRLEARI 1735
Cdd:TIGR00606 1037 LKQHLKEMGQMQvlqmkQEHQKLEENIDLIKRNHVLALGRQKGYEKEI 1084
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
913-1796 |
1.34e-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: 86.56 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 913 RMQEMEEVLHELESRLEEEeervaqfQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNA 992
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKK-------EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 993 KLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMItDLEDRLRKEEKMRQELEKNRRKLegdsteLHDQIAELQ 1072
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-AQVLKENKEEEKEKKLQEEELKL------LAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1073 AQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTEL 1152
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1153 EDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1233 LQIELKSLSQSKNDsENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVES 1312
Cdd:pfam02463 460 LLKDELELKKSEDL-LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1313 QLKDAQALLEEETRqklaiSTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESmeDGKK 1392
Cdd:pfam02463 539 ENYKVAISTAVIVE-----VSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--LDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1393 KLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQG--HLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDR 1470
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSleEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1471 AEAEAREKETKSLTLARELEaMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKR-GMEQQLEEMKTQLEELE 1549
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEE-LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEeKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1550 DELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQ 1629
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1630 IDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKiKSMEAEIMQLHEDLAAADRAKRQIQQERDE 1709
Cdd:pfam02463 851 LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEK-KELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1710 LQDEINSQ-----NAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLR 1784
Cdd:pfam02463 930 LLKYEEEPeelllEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
890
....*....|..
gi 319655760 1785 SQLDRQNKDMKQ 1796
Cdd:pfam02463 1010 AIIEETCQRLKE 1021
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
946-1503 |
1.78e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.86 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 946 QQNIGDLeQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKlsKEKKQMEERISEFTTNLAEEEEKSKSLQKL 1025
Cdd:PRK02224 152 QDMIDDL-LQLGKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1026 KTKHETMITDLEDRLRKEEKMRQE---LEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAAL 1102
Cdd:PRK02224 229 REQARETRDEADEVLEEHEERREEletLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1103 KNAAQKSIREMEAQISELQEDLELE----KAARNKAEKQRRD----------LGEELEALKTELEDTldstaaqQELRAK 1168
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECrvaaQAHNEEAESLREDaddleeraeeLREEAAELESELEEA-------REAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1169 RETEVTQLKKTLEdEARAheqmlsevrqkhnqAFEELNEQLEQskrskasVDKAKQALESERNELQIELKSLSQSKNDSE 1248
Cdd:PRK02224 382 RREEIEELEEEIE-ELRE--------------RFGDAPVDLGN-------AEDFLEELREERDELREREAELEATLRTAR 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1249 NRRKKAESQLQE-------LQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKsIKAAKDCSAVESQL------- 1314
Cdd:PRK02224 440 ERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER-LERAEDLVEAEDRIerleerr 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1315 KDAQALLE------EETRQKLA-ISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQE---AQSL 1384
Cdd:PRK02224 519 EDLEELIAerretiEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLeriRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1385 ESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRlQRELDDVLVDqghlrQTVQELERKQKKFDQMLAEEKSISTKY 1464
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRER-KRELEAEFDE-----ARIEEAREDKERAEEYLEQVEEKLDEL 672
|
570 580 590
....*....|....*....|....*....|....*....
gi 319655760 1465 AEERDRAEAEAREKEtksltlaRELEAMTDLKNELERVN 1503
Cdd:PRK02224 673 REERDDLQAEIGAVE-------NELEELEELRERREALE 704
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1101-1883 |
2.17e-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: 85.79 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1101 ALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDlgEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTL 1180
Cdd:pfam02463 146 IIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENL--AELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1181 EDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKND-SENRRKKAESQLQ 1259
Cdd:pfam02463 224 EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 ELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKvESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLE 1339
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1340 DEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLEsmEDGKKKLQREVESVLQQLEERNASYDKLDKTK 1419
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEE--LEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1420 TRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNEL 1499
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1500 ERVNKQLKTEMED--LVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQA-LKAQFERD 1576
Cdd:pfam02463 541 YKVAISTAVIVEVsaTADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAtLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1577 LQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLeldlselaaqidlaNKARDEALKQLKKLQAQMKEQMR 1656
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSE--------------VKASLSELTKELLEIQELQEKAE 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1657 EFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADR-AKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARI 1735
Cdd:pfam02463 687 SELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQeAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1736 AQLEEELEEEHLSVelvnDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEgavKSKYKSTITA 1815
Cdd:pfam02463 767 SELSLKEKELAEER----EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEK---IKEEELEELA 839
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1816 LETKIQQLEEQLDSEMKERQQ--STKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQL 1883
Cdd:pfam02463 840 LELKEEQKLEKLAEEELERLEeeITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL 909
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1167-1882 |
2.28e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1167 AKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKND 1246
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1247 SENRR----KKAESQLQELQVKHTESERQKHELLDKVSKMQAEleslqgtvtkvESKSIKAAKDCSAvESQLKDAQALLE 1322
Cdd:PTZ00121 1155 EIARKaedaRKAEEARKAEDAKKAEAARKAEEVRKAEELRKAE-----------DARKAEAARKAEE-ERKAEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1323 EETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQlAEMKKKIEQEAQSLESMEDGKKKLQREVESVL 1402
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ-AAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1403 QQLEERnasydkldKTKTRLQRELDDVLVDQGHLRQTVQELERKqkkfdqmlAEEKsistKYAEERDRAEAEAREKETKS 1482
Cdd:PTZ00121 1302 KKADEA--------KKKAEEAKKADEAKKKAEEAKKKADAAKKK--------AEEA----KKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1483 ltlareleamTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRL 1562
Cdd:PTZ00121 1362 ----------AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1563 EVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEalk 1642
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA--- 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1643 QLKKLQAQMKEQMREFEDLRlsRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNS 1722
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1723 lssdeRRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVElTAERSNSQRLEGLRSQLDRQNKDMKqKLQELE 1802
Cdd:PTZ00121 1587 -----KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELK-KAEEEN 1659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1803 GAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRvEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQ 1882
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
873-1247 |
2.38e-16 |
|
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: 85.89 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 873 KESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDL 952
Cdd:TIGR02169 670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 953 EQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAklskekkqmEERISEFTTNLAEEEEKSKSLqklktkhETM 1032
Cdd:TIGR02169 750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS---------HSRIPEIQAELSKLEEEVSRI-------EAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1033 ITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIRE 1112
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1113 MEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELedtldstaAQQELRAKRETEVTQLKKTLEDEARAHEQMLS 1192
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1193 EVRqkhnqAFEELN----EQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDS 1247
Cdd:TIGR02169 966 EIR-----ALEPVNmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
987-1653 |
6.92e-16 |
|
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: 83.92 E-value: 6.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 987 IEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHD 1066
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1067 QIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLelekaarNKAEKQRRDLGEELE 1146
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENEL-------NLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1147 ALKTELedtldstaaqqelrakretevtqlkktledeaRAHEQMLSeVRQKHNQAFEELNEQLEQSKRSKASVDKAKQAL 1226
Cdd:TIGR04523 191 KIKNKL--------------------------------LKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1227 ESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLqgtvtkvesKSIKAAKD 1306
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL---------NNQKEQDW 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1307 CSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLES 1386
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1387 MEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAE 1466
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1467 ERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLE 1546
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELN 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1547 ELEDELQLTEDAKLRLEVNMQALKAQFERD-LQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSE 1625
Cdd:TIGR04523 549 KDDFELKKENLEKEIDEKNKEIEELKQTQKsLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
650 660
....*....|....*....|....*...
gi 319655760 1626 LAAQIDLANKARDEALKQLKKLQAQMKE 1653
Cdd:TIGR04523 629 LSSIIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1066-1287 |
7.95e-16 |
|
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: 81.73 E-value: 7.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEEL 1145
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1146 EALKTELEDTLDstAAQQELRAKRETEVTQLKKTLEDEARAheQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQA 1225
Cdd:COG4942 100 EAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1226 LESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELE 1287
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1010-1734 |
1.25e-15 |
|
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: 83.35 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1010 TNLAEEEEKSKSLQ-KLKTKHETmITDLEDRLRKEEKMRQELEKNRR-KLEGDSTELHDQIAELQAQIAELRAQLAKKEE 1087
Cdd:pfam12128 244 TKLQQEFNTLESAElRLSHLHFG-YKSDETLIASRQEERQETSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1088 ELQA--ALARIEEEAALKNAAQKSIRE--MEAQISELQEDLELEKAARNK--AEKQRRDLGEELEaLKTELEDTLDSTAA 1161
Cdd:pfam12128 323 ELEAleDQHGAFLDADIETAAADQEQLpsWQSELENLEERLKALTGKHQDvtAKYNRRRSKIKEQ-NNRDIAGIKDKLAK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1162 QQELRAKRETEVTQLKKTLEDEARA-HEQMLSEVRQKHNQ---AFEELN----------EQLEQSKRSKASVDKAKQALE 1227
Cdd:pfam12128 402 IREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRlksRLGELKlrlnqatatpELLLQLENFDERIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1228 S---ERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQ----KHELLDKVSKMQAELESLQGTVTKVEsKS 1300
Cdd:pfam12128 482 AanaEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqAGTLLHFLRKEAPDWEQSIGKVISPE-LL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1301 IKAAKDCSAVESQLKDAQAL----LEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKK 1376
Cdd:pfam12128 561 HRTDLDPEVWDGSVGGELNLygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1377 IEQEAQSLESMEDGKKKLQREVESVLQQLEERNASydKLDKTKTRLQRelddvlvdqghLRQTVQELERKQKKFDQMLAE 1456
Cdd:pfam12128 641 ETFARTALKNARLDLRRLFDEKQSEKDKKNKALAE--RKDSANERLNS-----------LEAQLKQLDKKHQAWLEEQKE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1457 EKSistkyaEERDRAEAEARE-KETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGME 1535
Cdd:pfam12128 708 QKR------EARTEKQAYWQVvEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLE 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1536 QQLEemktqleeledelqltedaklRLEVNMQALkAQFERDLQSRDEQgeeKRKQLVKQVREMEMELEDERKQRAQAVSv 1615
Cdd:pfam12128 782 RKIE---------------------RIAVRRQEV-LRYFDWYQETWLQ---RRPRLATQLSNIERAISELQQQLARLIA- 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1616 rkKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFED-----LRLSRDESLNQAKENERKIKSMEAEIMQLH 1690
Cdd:pfam12128 836 --DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDanseqAQGSIGERLAQLEDLKLKRDYLSESVKKYV 913
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 319655760 1691 EDLAAADRAKRQIQQER--DELQDEINSQNAKNSLSSDERRRLEAR 1734
Cdd:pfam12128 914 EHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1076-1685 |
1.37e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1076 AELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDL---GEELEALKTEL 1152
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1153 EDTLDSTAAQQELRAKRETEVTQLKKTLEdEARAHEQMLSEVRQKhNQAFEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1233 LQIELKSLSqsknDSENRRKKAESQLQELQVKHTESErQKHELLDKVSKMQAELESLqgtvtkvesksiKAAKDCSAVEs 1312
Cdd:PRK03918 326 IEERIKELE----EKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERL------------KKRLTGLTPE- 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1313 qlkDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEeeeeskknvekQLHTAQAQLAEMKKKIEQEAQSLEsmEDGKK 1392
Cdd:PRK03918 388 ---KLEKELEELEKAKEEIEEEISKITARIGELKKEIK-----------ELKKAIEELKKAKGKCPVCGRELT--EEHRK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1393 KLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQghlrqtvQELERKQKKFDQMLAEEKSISTKYAEERDRAE 1472
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-------SELIKLKELAEQLKELEEKLKKYNLEELEKKA 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1473 AEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDEL 1552
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1553 QLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKR--KQLVKQVREMEMELEDERKQRAQAVSVrkKLELDLSELAAQI 1630
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKYSEEEYEELREEYL--ELSRELAGLRAEL 682
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1631 DLANKARDEALKQLKKLQAQ---MKEQMREFEDLRLSRDEsLNQAKENERKIKSMEAE 1685
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEEleeREKAKKELEKLEKALER-VEELREKVKKYKALLKE 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1134-1873 |
2.87e-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: 81.94 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1134 AEKQRRDLGEELEALKTELEDTLDSTAAQQElrakretEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSK 1213
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPD-------TYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1214 RSKASvdkakQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKhelldkvskMQAELESLQGTV 1293
Cdd:TIGR00618 258 KQQLL-----KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR---------IHTELQSKMRSR 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1294 TKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKlaistrlrqledEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEM 1373
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR------------DAHEVATSIREISCQQHTLTQHIHTLQQQKTTL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1374 KKKIEQEAQSLEsmedgkkKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQEL---ERKQKKF 1450
Cdd:TIGR00618 392 TQKLQSLCKELD-------ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEkleKIHLQES 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1451 DQMLAEEKSistkyaEERDRAEAEAREKETKSLTLAReLEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGK------SV 1524
Cdd:TIGR00618 465 AQSLKEREQ------QLQTKEQIHLQETRKKAVVLAR-LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqrgeqTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1525 HELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFErdlqsrdeqGEEKRKQLVKQVREMEMELED 1604
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP---------NLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1605 ERKQRAQAVSVRKKLELDLSELAAQidLANKARDEALKQLKKLQAQMK-EQMREFEDLRLSRDESLNQAKENERKIKSME 1683
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQDLQDVRLH--LQQCSQELALKLTALHALQLTlTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1684 AEIMQLH---EDLAAADRAKRQIQQERDELQDEINS-QNAKNSLSSDERRRLEAriaqleeELEEEHLSVELVNDRLKKA 1759
Cdd:TIGR00618 687 SEKEQLTywkEMLAQCQTLLRELETHIEEYDREFNEiENASSSLGSDLAAREDA-------LNQSLKELMHQARTVLKAR 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1760 SLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMK---QKLQELEGAVKSKYKSTITALET---KIQQLEEQLDSEMKE 1833
Cdd:TIGR00618 760 TEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREedtHLLKTLEAEIGQEIPSDEDILNLqceTLVQEEEQFLSRLEE 839
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 319655760 1834 RQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKAN 1873
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1047-1911 |
3.50e-15 |
|
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: 81.92 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1047 RQELEKNRRKLegdsTELHDQIAELQAQIAELRAQLAKKEEELQAA---LARIEEeaALKnaAQKSIREMEAQISELQED 1123
Cdd:COG3096 291 RRELFGARRQL----AEEQYRLVEMARELEELSARESDLEQDYQAAsdhLNLVQT--ALR--QQEKIERYQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1124 LELEKAARNKAEKQRRDLGEELEA-------LKTELED---TLDS--TAA---QQELRAKRETE---------VTQLKKT 1179
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAaeeevdsLKSQLADyqqALDVqqTRAiqyQQAVQALEKARalcglpdltPENAEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1180 LEdEARAHEQMLSEV--------------RQKHNQAFEELNEQLEQSKRSKASvDKAKQALESER---------NELQIE 1236
Cdd:COG3096 443 LA-AFRAKEQQATEEvleleqklsvadaaRRQFEKAYELVCKIAGEVERSQAW-QTARELLRRYRsqqalaqrlQQLRAQ 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1237 LKSLSQSkndsENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKvesksikAAKDCSAVESQLKD 1316
Cdd:COG3096 521 LAELEQR----LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAE-------AVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1317 AQALLEEETRQK---LAISTRLRQLEDEQNnlkemleeeeeskknveKQLHTAQAQLAEMKKKIEQEAQsLESMEDGKKK 1393
Cdd:COG3096 590 LRARIKELAARApawLAAQDALERLREQSG-----------------EALADSQEVTAAMQQLLERERE-ATVERDELAA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1394 LQREVESVLQQLEERNASYD-KLDKTKTRLQREL-----DDVLVDQ--------GHLRQ--TVQELERKQKKFDQMlaeE 1457
Cdd:COG3096 652 RKQALESQIERLSQPGGAEDpRLLALAERLGGVLlseiyDDVTLEDapyfsalyGPARHaiVVPDLSAVKEQLAGL---E 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1458 KSISTKYAEERDRAEAEAREKETKSLTLAreleamtdlknelervnkqlktemeDLVSSKDDAGK-----SVHELERAKR 1532
Cdd:COG3096 729 DCPEDLYLIEGDPDSFDDSVFDAEELEDA-------------------------VVVKLSDRQWRysrfpEVPLFGRAAR 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1533 gmEQQLEEMKTQLEELEDELqltedAKLRLEVN-MQALKAQFERDLQSR-----DEQGEEKRKQLVKQVREMEMELED-- 1604
Cdd:COG3096 784 --EKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEAELAALRQRRSELERELAQhr 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1605 --ERKQRAQAVSVRKKLELdlseLAAQIDLANKARDEALKQLkklqaqmkeqmreFEDLRlsrdESLNQAKENERKIKSM 1682
Cdd:COG3096 857 aqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADETLADR-------------LEELR----EELDAAQEAQAFIQQH 915
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1683 EAEIMQLhEDLAAADRAK----RQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSvelVNDRLKK 1758
Cdd:COG3096 916 GKALAQL-EPLVAVLQSDpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD---LNEKLRA 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1759 ASLQAEQvtveltaERSNS-QRLEGLRSQLDRQNkdmkQKLQELEGAVKSKYKsTITALETKIQQLEEQLDSEMKERQQS 1837
Cdd:COG3096 992 RLEQAEE-------ARREArEQLRQAQAQYSQYN----QVLASLKSSRDAKQQ-TLQELEQELEELGVQADAEAEERARI 1059
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1838 TKQvrrvekklkevllQVEDERRNADQSKTETEKANIRLKQMKRQLEETeeeaaranasCRKLRRELEDATESA 1911
Cdd:COG3096 1060 RRD-------------ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKR----------LRKAERDYKQEREQV 1110
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
995-1921 |
3.50e-15 |
|
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: 81.70 E-value: 3.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 995 SKEKKQMEERISEftTNLAEEEEK----------SKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTEL 1064
Cdd:pfam15921 84 SHQVKDLQRRLNE--SNELHEKQKfylrqsvidlQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1065 HDQIAELQAQIAELRAQLAKKE---EELQAALARIEEEAALKNAAQKSI-----REMEAQISELQEDLELEKAArnkAEK 1136
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISY---LKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1137 QRRDLGEELEALKTELEDTLDSTAAQQELRakreteVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSK 1216
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDR------IEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1217 ASVDKAKQALESERNELQIELKslsQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKV 1296
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1297 EsksikaaKDCSAVESQLKdaqALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKK 1376
Cdd:pfam15921 390 E-------KELSLEKEQNK---RLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1377 IEQEAQSLESMEDGKKKLQREVEsvlqQLEERNASYDKLDKTKTRLQRELDDvlvDQGHLRQTVQELERKQKKFDQMLAE 1456
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVE----ELTAKKMTLESSERTVSDLTASLQE---KERAIEATNAEITKLRSRVDLKLQE 532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1457 EKSISTKYAEERD-RAEAEA-----REKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERA 1530
Cdd:pfam15921 533 LQHLKNEGDHLRNvQTECEAlklqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1531 KRGMEQQLEEMKTQLeeledelqltedAKLRLEvNMQALKAQFERDLQSRDEQGEekRKQLVKQVREMEMEL----EDER 1606
Cdd:pfam15921 613 KDKKDAKIRELEARV------------SDLELE-KVKLVNAGSERLRAVKDIKQE--RDQLLNEVKTSRNELnslsEDYE 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1607 KQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRlsrdeslNQAKENERKIKSMEAEI 1686
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ-------KQITAKRGQIDALQSKI 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1687 MQLHEDLAAADRAKRQIQQERDELQDEINS-QNAKNSLSSD------ERRRLEARIAQLEEEleeehlsvelvndrLKKA 1759
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKMAGElevlrsQERRLKEKVANMEVA--------------LDKA 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1760 SLQAEQVTVELTAERSNSQRLEgLRSQLD---------RQNKDMKQKLqeLEGAVKSKYKSTITALETKIQQLEEQLDSE 1830
Cdd:pfam15921 817 SLQFAECQDIIQRQEQESVRLK-LQHTLDvkelqgpgyTSNSSMKPRL--LQPASFTRTHSNVPSSQSTASFLSHHSRKT 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1831 MKERQQSTKQVRRVEKKLKEVLlqveDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELE-DATE 1909
Cdd:pfam15921 894 NALKEDPTRDLKQLLQELRSVI----NEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQtEGSK 969
|
970
....*....|..
gi 319655760 1910 SASAMNREVSTL 1921
Cdd:pfam15921 970 SSETCSREPVLL 981
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
863-1424 |
3.55e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 3.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVlhelesrleeeEERVAQFQSEK 942
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDL-----------RETIAETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 943 KKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTT-------NLAEE 1015
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEeaeslreDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1016 EEKSKSLQK----LKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEG---DSTELHDQIAELQAQIAELRAQLAKKEEE 1088
Cdd:PRK02224 355 EERAEELREeaaeLESELEEAREAVEDRREEIEELEEEIEELRERFGDapvDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1089 LQAALARIEEEAALKNAAQ--------------KSIREMEAQISELQEDLELEKAARNKAEKqRRDLGEELEALKTELED 1154
Cdd:PRK02224 435 LRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEVEEVEE-RLERAEDLVEAEDRIER 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1155 TLDSTAAQQELRAKRETEVTqlkktlEDEARAheqmlsevrqkhnqafEELNEQLEQSKRSKASVDKAKQALESERNELQ 1234
Cdd:PRK02224 514 LEERREDLEELIAERRETIE------EKRERA----------------EELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1235 IELKSLSQSKNDSENRRkkaesqlqelqvkhtESERQKHELLDKVSKMQAELESLQgtvtkvesksikaakdcsavesQL 1314
Cdd:PRK02224 572 EEVAELNSKLAELKERI---------------ESLERIRTLLAAIADAEDEIERLR----------------------EK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1315 KDAQALLEEETRQKLA-ISTRLRQLEDEQNnlkemleeeeeskknvEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKK 1393
Cdd:PRK02224 615 REALAELNDERRERLAeKRERKRELEAEFD----------------EARIEEAREDKERAEEYLEQVEEKLDELREERDD 678
|
570 580 590
....*....|....*....|....*....|.
gi 319655760 1394 LQREVESVLQQLEERNASYDKLDKTKTRLQR 1424
Cdd:PRK02224 679 LQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1595-1913 |
8.89e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1595 VREMEMELEDERKQRAQAvsvRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKE 1674
Cdd:COG1196 195 LGELERQLEPLERQAEKA---ERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1675 NERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSqnaknslSSDERRRLEARIAQLEEELEEEHLSVELVND 1754
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE-------LEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1755 RLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEgavkskykSTITALETKIQQLEEQLDSEMKER 1834
Cdd:COG1196 345 ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL--------RAAAELAAQLEELEEAEEALLERL 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1835 QQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASA 1913
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
997-1481 |
1.03e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 80.34 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 997 EKKQMEERI----SEFTT------NLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEE-KMRQELEKNRRKLEgdstELH 1065
Cdd:COG4913 219 EEPDTFEAAdalvEHFDDleraheALEDAREQIELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRLE----LLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALARIEE-EAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLG-- 1142
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlp 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1143 -----EELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHN-------QAFEELNEQLE 1210
Cdd:COG4913 375 lpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniparllALRDALAEALG 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1211 QSKR-----------------------------------SKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAE 1255
Cdd:COG4913 455 LDEAelpfvgelievrpeeerwrgaiervlggfaltllvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPD 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1256 SQLQELQVK-HTESERQKHELLDKVSKMQAE-LESLQGTVTKV-------ESKSIKAAKDCSAVES----------QLKD 1316
Cdd:COG4913 535 SLAGKLDFKpHPFRAWLEAELGRRFDYVCVDsPEELRRHPRAItragqvkGNGTRHEKDDRRRIRSryvlgfdnraKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1317 AQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQ--LAEmkkkIEQEAQSLESMEDGKKKL 1394
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEreIAE----LEAELERLDASSDDLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1395 QREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKK-----FDQMLAE------EKSISTK 1463
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLelralLEERFAAalgdavERELREN 770
|
570
....*....|....*...
gi 319655760 1464 YAEERDRAEAEAREKETK 1481
Cdd:COG4913 771 LEERIDALRARLNRAEEE 788
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1193-1816 |
1.23e-14 |
|
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: 80.27 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1193 EVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQK 1272
Cdd:pfam12128 266 GYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAAD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1273 HELLDKV----SKMQAELESLQGTVTKVESKS----IKAAKDCSAVESQLKDAQA-LLEEETRQKLAISTRLRQLEDEqn 1343
Cdd:pfam12128 346 QEQLPSWqselENLEERLKALTGKHQDVTAKYnrrrSKIKEQNNRDIAGIKDKLAkIREARDRQLAVAEDDLQALESE-- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1344 nLKEMLEEEEESKKNVEKQLHTAqaqLAEMKKKIEQEAQSLESMEDgKKKLQREVESVLQQLEERNASYDKLDKTKTRLQ 1423
Cdd:pfam12128 424 -LREQLEAGKLEFNEEEYRLKSR---LGELKLRLNQATATPELLLQ-LENFDERIERAREEQEAANAEVERLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1424 RELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAeerdRAEAeAREKETKSLTLARELEAMTDLKNE----- 1498
Cdd:pfam12128 499 KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFL----RKEA-PDWEQSIGKVISPELLHRTDLDPEvwdgs 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1499 -------------LERV--------NKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTED 1557
Cdd:pfam12128 574 vggelnlygvkldLKRIdvpewaasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1558 AKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMEL--------EDERKQRAQAVSVRKKLELDLSELAAQ 1629
Cdd:pfam12128 654 DLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqawleeqkEQKREARTEKQAYWQVVEGALDAQLAL 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1630 IDLANKARDEALK-QLKKLQAQMKEQMRefedlrlSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQ---- 1704
Cdd:pfam12128 734 LKAAIAARRSGAKaELKALETWYKRDLA-------SLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQetwl 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1705 QERDELQDEINSQNAKNSLSSDERRRLEA----RIAQLEEELEEEHLSVELVNDRLKKasLQAEQVTVELTAERSNSQRL 1780
Cdd:pfam12128 807 QRRPRLATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRG--LRCEMSKLATLKEDANSEQA 884
|
650 660 670
....*....|....*....|....*....|....*....
gi 319655760 1781 EGLRSQLDRQNKDMKQKLQELEGAVKSK---YKSTITAL 1816
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKRDYLSESVKKYvehFKNVIADH 923
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1401 |
2.18e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 871 QLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELEsrleeeeervaqfqsEKKKMQQNIG 950
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK---------------ELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 951 DLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAK---LSKEKKQMEERISEFTTNlAEEEEKSKSLQKLKT 1027
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERleeLKKKLKELEKRLEELEER-HELYEEAKAKKEELE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1028 KHETMITDLEdrLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLakkeEELQAA------LARIEEEAA 1101
Cdd:PRK03918 376 RLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI----EELKKAkgkcpvCGRELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1102 LKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKteLEDTLDstaaqqELRAKRETEVTQLKKTLE 1181
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK--LKELAE------QLKELEEKLKKYNLEELE 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1182 DEARAHEQMLSEVR--QKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKaesQLQ 1259
Cdd:PRK03918 522 KKAEEYEKLKEKLIklKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK---ELE 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 ELQVKHTESERQKHELLDKvskmQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKlaISTRLRQLE 1339
Cdd:PRK03918 599 PFYNEYLELKDAEKELERE----EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELS 672
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1340 DEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQeaqsLESMEDGKKKLQREVESV 1401
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE----LEKLEKALERVEELREKV 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
798-1120 |
2.20e-14 |
|
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: 79.33 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 798 VARRAFAKRQQQLTAMRVIQRNCAAYLKLRNWQWWRLFTKVKPLLQ-VTRQEEEMVAKEEELVKMKERQQQAEDQLKESE 876
Cdd:TIGR02168 702 ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEErIAQLSKELTELEAEIEELEERLEEAEEELAEAE 781
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 877 AKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQL 956
Cdd:TIGR02168 782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 957 DEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDL 1036
Cdd:TIGR02168 862 EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1037 EDRLRKEEKMR-QELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEA 1115
Cdd:TIGR02168 942 QERLSEEYSLTlEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
....*
gi 319655760 1116 QISEL 1120
Cdd:TIGR02168 1022 AIEEI 1026
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
917-1689 |
3.96e-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: 78.24 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 917 MEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLdeeeaarQKLQLEKVTMdAKLKKIEEDLMviEDQNAKLSK 996
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKL-------QEMQMERDAM-ADIRRRESQSQ--EDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 997 EKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHE-------TMITDLEDRLRKeeKMRQELEKNRRKLEGDSTELHDQIA 1069
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlqeirSILVDFEEASGK--KIYEHDSMSTMHFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1070 ELQAQIAELRAQLAKKEEELQAALAriEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALK 1149
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1150 telEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNE---QLEQSKRSKASVDKAKQAL 1226
Cdd:pfam15921 306 ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEartERDQFSQESGNLDDQLQKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1227 ESERNELQIELkSLSQSKNDSENRRKKAESQL-----QELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSI 1301
Cdd:pfam15921 383 LADLHKREKEL-SLEKEQNKRLWDRDTGNSITidhlrRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1302 KAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEeeeskknvekqLHTAQAQLAEMKKKIE--- 1378
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERA-----------IEATNAEITKLRSRVDlkl 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1379 QEAQSLESMEDGKKKLQREVESVLQQLEERnasydklDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEK 1458
Cdd:pfam15921 531 QELQHLKNEGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1459 SISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLV----SSKDDAGKSVHELERAKRGM 1534
Cdd:pfam15921 604 LELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1535 EQQLEEMKtqlEELEDELQLTEDAKLRLEVNMQALKAQFERDLQS------RDEQGEEKRKQ---LVKQVREMEMELEDE 1605
Cdd:pfam15921 684 RNKSEEME---TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAmkvamgMQKQITAKRGQidaLQSKIQFLEEAMTNA 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1606 RKQRAQAVSVRKKLELDLSELAAQidlANKARDEaLKQLKKLQAQMKEQMREFEdlrLSRDESLNQAKENERKIKSMEAE 1685
Cdd:pfam15921 761 NKEKHFLKEEKNKLSQELSTVATE---KNKMAGE-LEVLRSQERRLKEKVANME---VALDKASLQFAECQDIIQRQEQE 833
|
....
gi 319655760 1686 IMQL 1689
Cdd:pfam15921 834 SVRL 837
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1155 |
6.69e-14 |
|
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: 77.80 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEdQLKESEAKQKQLNAEKLALQEQLQAETElcqEAEEMRSRLTARMQEMEEVLHELESR-----LEEEEER 934
Cdd:TIGR02169 717 KIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEIE---NVKSELKELEARIEELEEDLHKLEEAlndleARLSHSR 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 935 VAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFttnLAE 1014
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL---EEE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1015 EEEKSKSLQKLKTKHEtmitDLE-DRLRKEEKMRqELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAAL 1093
Cdd:TIGR02169 870 LEELEAALRDLESRLG----DLKkERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1094 ARIEEEAALKNaAQKSIREMEAQISELQ-------EDLELEKAARNKAEKQRRDLGEELEALKTELEDT 1155
Cdd:TIGR02169 945 EIPEEELSLED-VQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1008-1232 |
1.06e-13 |
|
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: 75.19 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1008 FTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLA---K 1084
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAeleK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1085 KEEELQAALARIEEE-AALKNAAQKSIREMEAQISELQED-LELEKAAR--NKAEKQRRDLGEELEALKTELEDTLDSTA 1160
Cdd:COG4942 91 EIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1161 AQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
867-1472 |
1.17e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 867 QAEDQLKESEAKQKQLnAEKLALQEQLQAETELCQEAEEMRSRLTA-----RMQEMEEVLHELESRLEEEEERVAQFQSE 941
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLwfaqrRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEAAR-QKLQLEKVTMDAKLKKIEEDLMVIEDQ----NAKLSKEKKQMEERISEFTTNLAEEE 1016
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALlaalGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1017 EKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAE-LQAQIAELRA-----QLAKKEEELQ 1090
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFvgeliEVRPEEERWR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1091 AALarieeEAALKNAAQkSI---REMEAQISE------LQEDLELEKAARNKAEKQRRDLG-----EELEALKTELEDTL 1156
Cdd:COG4913 478 GAI-----ERVLGGFAL-TLlvpPEHYAAALRwvnrlhLRGRLVYERVRTGLPDPERPRLDpdslaGKLDFKPHPFRAWL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1157 DSTAAQQELRAKRETEvtqlkKTLEDEARAheqmLSEVRQ-KHNQAFEELNEQleQSKRSK----ASVDKAKQALESERN 1231
Cdd:COG4913 552 EAELGRRFDYVCVDSP-----EELRRHPRA----ITRAGQvKGNGTRHEKDDR--RRIRSRyvlgFDNRAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1232 ELQIELKSLSQSKNDSENRRKKAESQLQELQ--VKHTESERQKHELLDKVSKMQAELESLQgtvtkvesksiKAAKDCSA 1309
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLD-----------ASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1310 VESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEE-EEESKKNVEKQLHTAQAQLAEMKKKI---EQEAQSLE 1385
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDElQDRLEAAEDLARLELRALLEERFAAAlgdAVERELRE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1386 SMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTR-LQRELDDVLVDQGHLRQTVQE-LERKQKKFDQMLAEE-----K 1458
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETAdLDADLESLPEYLALLDRLEEDgLPEYEERFKELLNENsiefvA 849
|
650
....*....|....
gi 319655760 1459 SISTKYAEERDRAE 1472
Cdd:COG4913 850 DLLSKLRRAIREIK 863
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
874-1728 |
1.30e-13 |
|
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: 76.55 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 874 ESEAKQKQLNAEKLALQEQLQAETelcQEAEEMRSRLTARMQEMEEvlhelesrleeeeeRVAQFQSEKKKMQQNIGDLe 953
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLT---LCTPCMPDTYHERKQVLEK--------------ELKHLREALQQTQQSHAYL- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 954 QQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQmeerisefttnlAEEEEKSKSLQKLKTKHETMI 1033
Cdd:TIGR00618 246 TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA------------APLAAHIKAVTQIEQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1034 TDLEDRLRKEEKMRQeleknrrklegdstelhdQIAELQAQIAELRAQlakkeEELQAALARIEEEAALKNAAQKSIREM 1113
Cdd:TIGR00618 314 TELQSKMRSRAKLLM------------------KRAAHVKQQSSIEEQ-----RRLLQTLHSQEIHIRDAHEVATSIREI 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1114 EAQISELQEDLelekaarnKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQlkktleDEARAHEQMlse 1193
Cdd:TIGR00618 371 SCQQHTLTQHI--------HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG------QLAHAKKQQ--- 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1194 vrqkhnQAFEELNEQLEQSKRSKASVDKAKQAlesERNELQIELKSLSQskndsenrrkkaesQLQELQVKHtESERQKH 1273
Cdd:TIGR00618 434 ------ELQQRYAELCAAAITCTAQCEKLEKI---HLQESAQSLKEREQ--------------QLQTKEQIH-LQETRKK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1274 ELLDKVSKMQAELESLqgtvtkvesksikAAKDCSAVESQLKDAqALLEEETRQKLAISTRLRQLEDEQNNLkemleeee 1353
Cdd:TIGR00618 490 AVVLARLLELQEEPCP-------------LCGSCIHPNPARQDI-DNPGPLTRRMQRGEQTYAQLETSEEDV-------- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1354 eskknvEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVdQ 1433
Cdd:TIGR00618 548 ------YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR-K 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1434 GHLRQTVQELERKQKKFDQMLAEEKSISTKYAEE---RDRAEAEAREKETKSLTLARELEAMTDLKNELERVnkqlkTEM 1510
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQL-----TYW 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1511 EDLVSSKDDAGKSVHELERAKRGMEQQLEemktqleeledelqltedaklrlevnmQALKAQfERDLQSRDEQGEEKRKQ 1590
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIE---------------------------NASSSL-GSDLAAREDALNQSLKE 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1591 LVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLN 1670
Cdd:TIGR00618 748 LMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV 827
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1671 QAKENE----RKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDER 1728
Cdd:TIGR00618 828 QEEEQFlsrlEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFD 889
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1310 |
4.17e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 843 QVTRQEEEMVAKEEElvkmKERQQQAEDQLKESEAKQKQLNAEKLAlqEQLQAETELCQEAEEMRSR---LTARMQEMEE 919
Cdd:PTZ00121 1346 EAAKAEAEAAADEAE----AAEEKAEAAEKKKEEAKKKADAAKKKA--EEKKKADEAKKKAEEDKKKadeLKKAAAAKKK 1419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 920 VLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLK-----KIEEDLMVIEDQNAKL 994
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKaeeakKADEAKKKAEEAKKKA 1499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 995 SKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEknRRKLEGDSTELHDQIAELQAQ 1074
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEE--LKKAEEKKKAEEAKKAEEDKN 1577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1075 IAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISelQEDLELEKAARNKAEKQRRDLGEEL---EALKTE 1151
Cdd:PTZ00121 1578 MALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKA 1655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1152 LEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKhnQAFEELNEQLEQSKRSKASVDKAKQALESERN 1231
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEA--KKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1232 ELQielKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAV 1310
Cdd:PTZ00121 1734 EAK---KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
860-1500 |
1.00e-12 |
|
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: 73.52 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQ 939
Cdd:TIGR04523 79 ILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKS 1019
Cdd:TIGR04523 159 NKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQ 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDST---ELHDQIAELQAQIAEL------------RAQLAK 1084
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEKQLNQLKSEISDLnnqkeqdwnkelKSELKN 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1085 KEEELQAALARIEEEAALKNAAQKSIREMEAQI-------SELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLD 1157
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELtnsesenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1158 STAAQQELRAKRETEVTQLKKTLEDEARAHEQmLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIEL 1237
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1238 KSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKda 1317
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-- 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1318 QALLEEETRQKlaiSTRLRQLEDEQNNLKEMLEEEEESKKNVekqlhtaQAQLAEMKKKIEQEAQSLESMEDGKKKLQRE 1397
Cdd:TIGR04523 556 KENLEKEIDEK---NKEIEELKQTQKSLKKKQEEKQELIDQK-------EKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1398 VESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLA---EEKSISTKYAEERDRAEAE 1474
Cdd:TIGR04523 626 NEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKdwlKELSLHYKKYITRMIRIKD 705
|
650 660
....*....|....*....|....*.
gi 319655760 1475 AREKETKSLTLARELEAMTDLKNELE 1500
Cdd:TIGR04523 706 LPKLEEKYKEIEKELKKLDEFSKELE 731
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1531 |
2.93e-12 |
|
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: 72.06 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETelcQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQ 937
Cdd:pfam05483 196 ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEI---NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 FQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMeerisefttnlAEEEE 1017
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ-----------MEELN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLK-TKHETMITDLEDRLRKEEkmrQELEKNRRKLEGDSTELHDQIAELQ----------AQIAELRAQLAKKE 1086
Cdd:pfam05483 342 KAKAAHSFVvTEFEATTCSLEELLRTEQ---QRLEKNEDQLKIITMELQKKSSELEemtkfknnkeVELEELKKILAEDE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1087 EEL--QAALARIEEEaaLKNAAQKSIREMEAQISELQeDLELEKAARNKAEKQrrdLGEELEALKTELEDtldstaaqqe 1164
Cdd:pfam05483 419 KLLdeKKQFEKIAEE--LKGKEQELIFLLQAREKEIH-DLEIQLTAIKTSEEH---YLKEVEDLKTELEK---------- 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1165 lRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSK 1244
Cdd:pfam05483 483 -EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1245 NDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAvesqlkdaqalleeE 1324
Cdd:pfam05483 562 DEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA--------------E 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1325 TRQKLAISTRLRQLEDEqnnlkemleeeeeskknvekqLHTAQAQLAEMKKKIEQEAQSLESMEdgkkklqrevESVLQQ 1404
Cdd:pfam05483 628 NKQLNAYEIKVNKLELE---------------------LASAKQKFEEIIDNYQKEIEDKKISE----------EKLLEE 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1405 LEERNASYDKldktKTRLQRELDdvLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYaeerdraeaEAREKETKSLT 1484
Cdd:pfam05483 677 VEKAKAIADE----AVKLQKEID--KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY---------KNKEQEQSSAK 741
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 319655760 1485 LARELEaMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAK 1531
Cdd:pfam05483 742 AALEIE-LSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
866-1444 |
3.80e-12 |
|
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: 71.79 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 866 QQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAE-EMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKkk 944
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSaELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSEL-- 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 945 mqqnigdleQQLDEEEAARQKLQLEKVTMDAklkkieedlmvieDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSL-Q 1023
Cdd:pfam12128 325 ---------EALEDQHGAFLDADIETAAADQ-------------EQLPSWQSELENLEERLKALTGKHQDVTAKYNRRrS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1024 KLKTKHETMITDLEDRL--RKEEKMRQeLEKNRRKLEGDSTELHDQI--AELQAQIAELRAQLAKKEEELQAALARIEEE 1099
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLakIREARDRQ-LAVAEDDLQALESELREQLeaGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1100 AALK--------NAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELE------------------ 1153
Cdd:pfam12128 462 LLLQlenfderiERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDelelqlfpqagtllhflr 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1154 -------------------------------------------------DTLDSTAAQQELRAKREtevtQLKKTLEDEA 1184
Cdd:pfam12128 542 keapdweqsigkvispellhrtdldpevwdgsvggelnlygvkldlkriDVPEWAASEEELRERLD----KAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1185 RAHEQMLSEVRQKhNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIEL-KSLSQSKNDSENRRKKAESQLQELQV 1263
Cdd:pfam12128 618 EKQAAAEEQLVQA-NGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1264 KHTE-SERQKHELLDKVSKMQAELESLQGTvTKVESKSIKAAKDcsAVESQLKDAQALLEEETRQKLA--------ISTR 1334
Cdd:pfam12128 697 KHQAwLEEQKEQKREARTEKQAYWQVVEGA-LDAQLALLKAAIA--ARRSGAKAELKALETWYKRDLAslgvdpdvIAKL 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1335 LRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDK 1414
Cdd:pfam12128 774 KREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEK 853
|
650 660 670
....*....|....*....|....*....|..
gi 319655760 1415 LDKTKTRLQRELDDVL--VDQGHLRQTVQELE 1444
Cdd:pfam12128 854 QQVRLSENLRGLRCEMskLATLKEDANSEQAQ 885
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
835-1542 |
4.39e-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: 71.93 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 835 FTKVKPLLQVTRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARM 914
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 915 QEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDE----EEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQ 990
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEaqllLELARQLEDLLKEEKKEELEILEEEEESIELK 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 991 NAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNR-----------RKLEG 1059
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARsglkvllalikDGVGG 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRR 1139
Cdd:pfam02463 523 RIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPI 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1140 DLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASV 1219
Cdd:pfam02463 603 LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQ 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1220 DKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQgtvtKVESK 1299
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEE----KSRLK 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1300 SIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQ 1379
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1380 EAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKS 1459
Cdd:pfam02463 839 ALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1460 ISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLE 1539
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
...
gi 319655760 1540 EMK 1542
Cdd:pfam02463 999 RLE 1001
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
27-70 |
4.99e-12 |
|
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: 62.06 E-value: 4.99e-12
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 319655760 27 KKLVWVPSEKLGFEAGSIKEETGDECLVELaDSGKKIKVNKDDI 70
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
936-1162 |
5.60e-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: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 936 AQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEE 1015
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1016 EEkskslqklktkhetmitDLEDRLRKEEKMRQ--------------ELEKNRRKLEGDSTELHDQIAELQAQIAELRAQ 1081
Cdd:COG4942 103 KE-----------------ELAELLRALYRLGRqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1082 LAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAA 1161
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 319655760 1162 Q 1162
Cdd:COG4942 246 A 246
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1367-1917 |
6.46e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1367 QAQLAEMKKKIEQEAQSLESMEdgkkkLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVlvdQGHLRQTVQELERK 1446
Cdd:COG1196 208 QAEKAERYRELKEELKELEAEL-----LLLKLRELEAELEELEAELEELEAELEELEAELAEL---EAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1447 QKKFDQMLAEEKSISTKYAE-ERDRAEAEAREKEtksltLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVH 1525
Cdd:COG1196 280 ELELEEAQAEEYELLAELARlEQDIARLEERRRE-----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1526 ELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRkqlvkqvrememELEDE 1605
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------------RLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1606 RKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAE 1685
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1686 imqlHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQ 1765
Cdd:COG1196 503 ----YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1766 VTVELTAERSNSQRLEGLRSQL------DRQNKDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTK 1839
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAvdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1840 QVRRVEKKLKEVLLQVEDERRNADQsktETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASAMNRE 1917
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEE---LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1047-1856 |
6.96e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1047 RQELEKNRRKLEgDSTELHDQIAELQAQIAELRAQLakkEEELQAALARIeeeaALKNAA---QKSIREMEAQISELQED 1123
Cdd:PRK04863 292 RRELYTSRRQLA-AEQYRLVEMARELAELNEAESDL---EQDYQAASDHL----NLVQTAlrqQEKIERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1124 LELEKAARNKAEKQRrdlgEELEALKTELEDTLDSTAAQQ-------ELRAKRETEVTQLKKTLEdEARA---------- 1186
Cdd:PRK04863 364 LEEQNEVVEEADEQQ----EENEARAEAAEEEVDELKSQLadyqqalDVQQTRAIQYQQAVQALE-RAKQlcglpdltad 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 -HEQMLSEVRQKHNQAFEELNE---QLEQSKRSKASVDKAKQAL-----ESERNELQIELKSLSQsknDSENRRKKAEsQ 1257
Cdd:PRK04863 439 nAEDWLEEFQAKEQEATEELLSleqKLSVAQAAHSQFEQAYQLVrkiagEVSRSEAWDVARELLR---RLREQRHLAE-Q 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1258 LQELQVKHTESERQKHElldkvskmQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQ 1337
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQ--------QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQ 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1338 LEDEqnnlkemLEEEEESKKNVEKQLHTAQAQLAEMkkkieqEAQSLESMEDGkkklqREVESVLQQLEERNASydkldk 1417
Cdd:PRK04863 587 QLEQ-------LQARIQRLAARAPAWLAAQDALARL------REQSGEEFEDS-----QDVTEYMQQLLERERE------ 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1418 tktrLQRELDdvlvdqgHLRQTVQELERKQKKFDQMLAEEKSISTKYAEeRDRAEAEAREKETKSLTLARELEAMTD--- 1494
Cdd:PRK04863 643 ----LTVERD-------ELAARKQALDEEIERLSQPGGSEDPRLNALAE-RFGGVLLSEIYDDVSLEDAPYFSALYGpar 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1495 ---LKNELERVNKQLKTE---MEDL------VSSKDDAGKSVHELERA----------------------KRGMEQQLEE 1540
Cdd:PRK04863 711 haiVVPDLSDAAEQLAGLedcPEDLyliegdPDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQ 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1541 MKTQLEELEDELqltedAKLRLEVN-MQALKAQFERDLQSR-----DEQGEEKRKQLVKQVREMEMELEDERKQRAQAVS 1614
Cdd:PRK04863 791 LRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1615 VRKKLELDLSELAAQIDLANKARDEALKQlkklqaqmkeqmrEFEDLRlsrdESLNQAKENERKIKSMEAEIMQ------ 1688
Cdd:PRK04863 866 QLEQAKEGLSALNRLLPRLNLLADETLAD-------------RVEEIR----EQLDEAEEAKRFVQQHGNALAQlepivs 928
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1689 -LHEDLAAADRAKRQIQQERDELQdeiNSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVT 1767
Cdd:PRK04863 929 vLQSDPEQFEQLKQDYQQAQQTQR---DAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAR 1005
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1768 VELTAERS----NSQRLEGLRSQLDRQN---KDMKQKLQEL-----EGAV------KSKYKSTITALETKIQQLEEQLDS 1829
Cdd:PRK04863 1006 EQLRQAQAqlaqYNQVLASLKSSYDAKRqmlQELKQELQDLgvpadSGAEerararRDELHARLSANRSRRNQLEKQLTF 1085
|
890 900
....*....|....*....|....*..
gi 319655760 1830 EMKERQQSTKQVRRVEKKLKEVLLQVE 1856
Cdd:PRK04863 1086 CEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1586-1926 |
1.70e-11 |
|
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: 69.70 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1586 EKRKQLVKQVREMEMELEderkqRAQAVsvRKKLELDLSELAAQIDLANKARdEALKQLKKLQAQMkeQMREFEDLRLSR 1665
Cdd:TIGR02168 172 ERRKETERKLERTRENLD-----RLEDI--LNELERQLKSLERQAEKAERYK-ELKAELRELELAL--LVLRLEELREEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1666 DESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSlssderrRLEARIAQLEEELEEE 1745
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS-------RLEQQKQILRERLANL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1746 HLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKStITALETKIQQLEE 1825
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-LETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1826 QLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADqsKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELE 1905
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340
....*....|....*....|.
gi 319655760 1906 DATESASAMNREVSTLKNKLR 1926
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLD 492
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1035-1209 |
1.80e-11 |
|
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: 66.10 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEE-EAALKNAaqKSIREM 1113
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNV--RNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1114 EAqiseLQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTldstaaqQELRAKRETEVTQLKKTLEDEARAHEQMLSE 1193
Cdd:COG1579 92 EA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEE 160
|
170
....*....|....*.
gi 319655760 1194 VRQKHNQAFEELNEQL 1209
Cdd:COG1579 161 LEAEREELAAKIPPEL 176
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
860-1470 |
1.85e-11 |
|
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: 69.76 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLqaeTELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQ 939
Cdd:pfam15921 286 KASSARSQANSIQSQLEIIQEQARNQNSMYMRQL---SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEAR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLdeeeaarQKLQlekvtmdAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLaeeEEKS 1019
Cdd:pfam15921 363 TERDQFSQESGNLDDQL-------QKLL-------ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRREL---DDRN 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHETMITDLEDrlrkeekmrqELEKNRRKLEGDSTELhDQIAELQAQIAELRAQLAKKEEELQAALARIEee 1099
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQG----------QMERQMAAIQGKNESL-EKVSSLTAQLESTKEMLRKVVEELTAKKMTLE-- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1100 aalknAAQKSIREMEAQISELQEDLELEKAARNKAeKQRRDLG-EELEALKTElEDTLDStaaqqelrAKRETEVTQLKK 1178
Cdd:pfam15921 493 -----SSERTVSDLTASLQEKERAIEATNAEITKL-RSRVDLKlQELQHLKNE-GDHLRN--------VQTECEALKLQM 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1179 TLEDearaheqmlsEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQL 1258
Cdd:pfam15921 558 AEKD----------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1259 QELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQ-KLAISTRLRQ 1337
Cdd:pfam15921 628 SDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSE 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1338 LEDEQNNLKEMLEE---EEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEernasydK 1414
Cdd:pfam15921 708 LEQTRNTLKSMEGSdghAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS-------T 780
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1415 LDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDR 1470
Cdd:pfam15921 781 VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1011-1450 |
2.56e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1011 NLAEEEEKSKSLQKLKTKHETmITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIA--ELQAQIAELRAQLAKKEEE 1088
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1089 LQAALARIEEEAALknaaQKSIREMEAQISELQEDL-ELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRA 1167
Cdd:COG4717 148 LEELEERLEELREL----EEELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1168 KRETEVTQLKKTLEDEARAHEQ-----------MLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIE 1236
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1237 LKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDcsaveSQLKD 1316
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-----ALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1317 AQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEkqlhtAQAQLAEMKKKIEQEAQSLESMEDGKKKLQR 1396
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1397 EVESVLQQLE--ERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKF 1450
Cdd:COG4717 454 ELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1310-1870 |
2.69e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1310 VESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEkQLHTAQAQLAEMKKKIEQEAQSLESMED 1389
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1390 GKKKLQREVESV---LQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAE 1466
Cdd:PRK03918 270 ELKKEIEELEEKvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1467 -ERDRAEAEAReketksltlARELEAMTDLKNELERVNKQLKT-EMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQ 1544
Cdd:PRK03918 350 lEKRLEELEER---------HELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1545 LEELEDELQLTEDAKLRLEVNMQALKAQFERDLQsrdeqgEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDlS 1624
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELL------EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE-S 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1625 ELAAQIDLANKARdEALKQLKKLQAQ-MKEQMREFEDLRlsrdESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQI 1703
Cdd:PRK03918 494 ELIKLKELAEQLK-ELEEKLKKYNLEeLEKKAEEYEKLK----EKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1704 QQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSnsqRLEGL 1783
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK---RLEEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1784 RSQLDRQNKDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQLDS------EMKERQQSTKQVRRVEKKLKEVLLQVED 1857
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEikktleKLKEELEEREKAKKELEKLEKALERVEE 725
|
570
....*....|...
gi 319655760 1858 ERRNADQSKTETE 1870
Cdd:PRK03918 726 LREKVKKYKALLK 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
738-1484 |
3.80e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 738 MDGKQACVLMVKALELDSnlyrIGQSKVFFRAGVLahleEERDM--KITDVIINFQAWCRgyvARRAFAKRQQQLTAMRV 815
Cdd:COG4913 188 IGSEKALRLLHKTQSFKP----IGDLDDFVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 816 IQRNCAAYLKLRNWQwwRLFTKVKPLLQVTRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQL-- 893
Cdd:COG4913 257 IRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIrg 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 894 ---QAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEK 970
Cdd:COG4913 335 nggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 971 VTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEfTTNLAEEE-----EksksLQKLKTKHE--------------- 1030
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSNIPARLLALRDALAE-ALGLDEAElpfvgE----LIEVRPEEErwrgaiervlggfal 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1031 TMI---------------TDLEDRLRKEEKMRQELEKNRRKLEGDS------TELHDQIAELQAQIAElRAQLAKKE--E 1087
Cdd:COG4913 490 TLLvppehyaaalrwvnrLHLRGRLVYERVRTGLPDPERPRLDPDSlagkldFKPHPFRAWLEAELGR-RFDYVCVDspE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1088 ELQAALARIEEEAALKN---AAQKSIREMEAQISELQED----LELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTA 1160
Cdd:COG4913 569 ELRRHPRAITRAGQVKGngtRHEKDDRRRIRSRYVLGFDnrakLAALEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1161 AQQELRAKRETEVTQlkKTLEDEARAHEQMLSEVRqKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSL 1240
Cdd:COG4913 649 ALQRLAEYSWDEIDV--ASAEREIAELEAELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1241 SQSKNDSENRRKKAESQLQELQVKHTEsERQKHELLDKVSK-----MQAELESLQGTVTKVESKSIKAAKD-CSAVESQL 1314
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVERelrenLEERIDALRARLNRAEEELERAMRAfNREWPAET 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1315 KDAQALLE--EETRQklaistRLRQLEDEqnnlkemleeeeeskknvekQLHTAQAQLAEMKKKieqeaQSLESMEDGKK 1392
Cdd:COG4913 805 ADLDADLEslPEYLA------LLDRLEED--------------------GLPEYEERFKELLNE-----NSIEFVADLLS 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1393 KLQREVESVLQQLEERNASYDKLD-KTKTRLQRELDDVLVDQ-GHLRQTVQELERKQKKFDQMLAEEKSISTKYAEER-D 1469
Cdd:COG4913 854 KLRRAIREIKERIDPLNDSLKRIPfGPGRYLRLEARPRPDPEvREFRQELRAVTSGASLFDEELSEARFAALKRLIERlR 933
|
810
....*....|....*
gi 319655760 1470 RAEAEAREKETKSLT 1484
Cdd:COG4913 934 SEEEESDRRWRARVL 948
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1633-1850 |
6.76e-11 |
|
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: 66.33 E-value: 6.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1633 ANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQD 1712
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1713 EINSQNA--KNSLSSDERRRLEARI-----AQLEEELEEEHLSVELVNDRLKKaslQAEQVTVELTAERSNSQRLEGLRS 1785
Cdd:COG4942 98 ELEAQKEelAELLRALYRLGRQPPLalllsPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1786 QLDRQNKDMKQKLQELEGAVKSKyKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKE 1850
Cdd:COG4942 175 ELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
864-1456 |
9.57e-11 |
|
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: 67.30 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 864 RQQQAEDQLKESEAKQKQLN----AEKLAL------QEQLQAETELCQEAEEMRSRLTARMQ---------------EME 918
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINrarkAAPLAAhikavtQIEQQAQRIHTELQSKMRSRAKLLMKraahvkqqssieeqrRLL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 919 EVLHELESRLEEEEERVAQFQSEK----------KKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKK---IEEDLM 985
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREIScqqhtltqhiHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrdLQGQLA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 986 VIEDQNAKLSKEKKQMEERISEFTTNL-AEEEEKSKSLQKLKTKHEtMITDLEDRLRKEEKMRQELEKNRRKLEGDSTEL 1064
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQ-QLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1065 HDQIAELQAQiaelrAQLAKKEEELQAALARIEEEAALKNAAQKSIR----EMEAQISELQEDLELEKAARNKAEKQRRD 1140
Cdd:TIGR00618 507 CGSCIHPNPA-----RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1141 LGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEA-----RAHEQMLSEVRQKHNQAFEELNEQLEQSK-R 1214
Cdd:TIGR00618 582 SKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQdlqdvRLHLQQCSQELALKLTALHALQLTLTQERvR 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1215 SKASVDKAKQALESERNELQI-ELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHEL----LDKVSKMQAELESL 1289
Cdd:TIGR00618 662 EHALSIRVLPKELLASRQLALqKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIenasSSLGSDLAAREDAL 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1290 QGTVTKVESKSIKAAKDcSAVESQLKDAQALLEEETRQKLAistrlrQLEDEQNNlkemleeeeeskknVEKQLHTAQAQ 1369
Cdd:TIGR00618 742 NQSLKELMHQARTVLKA-RTEAHFNNNEEVTAALQTGAELS------HLAAEIQF--------------FNRLREEDTHL 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1370 LAEMKKKIEQEAQS-LESMEDGKKKLQREVESVLQQLEErnasydkldktKTRLQRELDDVLVDQGHLRQTVQELERKQK 1448
Cdd:TIGR00618 801 LKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEE-----------KSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
....*...
gi 319655760 1449 KFDQMLAE 1456
Cdd:TIGR00618 870 KIIQLSDK 877
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
963-1737 |
1.09e-10 |
|
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: 67.28 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 963 RQKLQLEKVTMDAKLKKIEEdlmviEDQNAKLSKEKKQMEERISEFTTNLaeeEEKSKSLQKLKT--KHETMIT------ 1034
Cdd:COG3096 285 ERALELRRELFGARRQLAEE-----QYRLVEMARELEELSARESDLEQDY---QAASDHLNLVQTalRQQEKIEryqedl 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 -DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELR---------------AQLAKKEEELQAALARIEE 1098
Cdd:COG3096 357 eELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQqaldvqqtraiqyqqAVQALEKARALCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1099 EAALKNAAQKSIREMEA--QISELQEDLELEKAARNKAEKQRrdlgEELEALKTELEDTLDSTAAQQELRAKREtevtql 1176
Cdd:COG3096 437 ENAEDYLAAFRAKEQQAteEVLELEQKLSVADAARRQFEKAY----ELVCKIAGEVERSQAWQTARELLRRYRS------ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1177 KKTLEDEARAHEQMLSEVRQKHNQAfEELNEQLEQ-SKRSKASVDKAKQaLESERNELQIELKSLSQSKNDSENRRKKAE 1255
Cdd:COG3096 507 QQALAQRLQQLRAQLAELEQRLRQQ-QNAERLLEEfCQRIGQQLDAAEE-LEELLAELEAQLEELEEQAAEAVEQRSELR 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1256 SQLQELQVKHTESERQK---HELLDKVSKMQ----AELESLQGtVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQK 1328
Cdd:COG3096 585 QQLEQLRARIKELAARApawLAAQDALERLReqsgEALADSQE-VTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1329 LAIS----TRLRQLEDEQNNLKEMLEEEEESKKNV---------------EKQLHTAQAQLAEMKKK------IEQEAQS 1383
Cdd:COG3096 664 SQPGgaedPRLLALAERLGGVLLSEIYDDVTLEDApyfsalygparhaivVPDLSAVKEQLAGLEDCpedlylIEGDPDS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1384 L-------ESMEDGkkklqrevesVLQQLEERNASYDKL-----------DKTKTRLQRELDDVLVDQGHLRQTVQELER 1445
Cdd:COG3096 744 FddsvfdaEELEDA----------VVVKLSDRQWRYSRFpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQR 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1446 KQKKFDQMLAEEKSIstkyAEERDrAEAEAREKETKSLTLAREL-----------EAMTDLKNELERVNKQLKTEM---- 1510
Cdd:COG3096 814 LHQAFSQFVGGHLAV----AFAPD-PEAELAALRQRRSELERELaqhraqeqqlrQQLDQLKEQLQLLNKLLPQANllad 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1511 EDLVSSKDDAGKSVHELERAKRGMEQQleemktqleeledelqltEDAKLRLEVNMQALK---AQFERdLQSRDEQGEEK 1587
Cdd:COG3096 889 ETLADRLEELREELDAAQEAQAFIQQH------------------GKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQ 949
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1588 RKQLVKQVREMEmeledERKQRAQAVSVRKKLEL-----DLSE-LAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDL 1661
Cdd:COG3096 950 QRRLKQQIFALS-----EVVQRRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASL 1024
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1662 RLSRDESLNQAKENERKIKSMEaeimqLHEDLAAADRAKrqiqQERDELQDEINSQNAKNSLSSDERRRLEARIAQ 1737
Cdd:COG3096 1025 KSSRDAKQQTLQELEQELEELG-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1036-1462 |
1.16e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1036 LEDRLRKEekmRQELEKNR-RKLEGDSTELHDQIAELQaQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREME 1114
Cdd:COG4717 47 LLERLEKE---ADELFKPQgRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1115 AQISELQEDLELEKAarnkaEKQRRDLGEELEALKTELEDtldstaaqqelRAKRETEVTQLKKTLEDEARAHEQMLSEV 1194
Cdd:COG4717 123 KLLQLLPLYQELEAL-----EAELAELPERLEELEERLEE-----------LRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1195 RQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQ----------------- 1257
Cdd:COG4717 187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglgg 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1258 -----------------------LQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQL 1314
Cdd:COG4717 267 sllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1315 KDAQALLEEETRQKLAIstRLRQLEDEQNNLKEMLEEEEE----SKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDG 1390
Cdd:COG4717 347 EELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1391 --KKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDvLVDQGHLRQTVQELERKQKKFDQMLAEEKSIST 1462
Cdd:COG4717 425 ldEEELEEELEELEEELEELEEELEELREELAELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
946-1177 |
1.33e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.58 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 946 QQNIGDLEQQLDEEEAARQKLqlekvtmdaklkKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKL 1025
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF------------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1026 KTKHETMITDLED--RLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLakkEEELQAALARIEEEAAlk 1103
Cdd:COG3206 249 LGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL---QQEAQRILASLEAELE-- 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1104 nAAQKSIREMEAQISELQEDLelekAARNKAEKQRRDLGEELEALKTELEDTLdstAAQQELRAKRETEVTQLK 1177
Cdd:COG3206 324 -ALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
862-1507 |
1.46e-10 |
|
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: 66.53 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKQKQLNAEKLALQEqlqAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSE 941
Cdd:TIGR00618 247 QKREAQEEQLKKQQLLKQLRARIEELRAQE---AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEAARQKLQLEKvtmdaklkkiEEDLMVIEDQNAKLSKE----KKQMEERISEFTTNLAEEEE 1017
Cdd:TIGR00618 324 AKLLMKRAAHVKQQSSIEEQRRLLQTLHS----------QEIHIRDAHEVATSIREiscqQHTLTQHIHTLQQQKTTLTQ 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIE 1097
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1098 EEAALKNAAQK--SIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQ 1175
Cdd:TIGR00618 474 QLQTKEQIHLQetRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTS 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1176 LKKtledearaHEQMLSEVRQKHNQAFEELNEQLEqskRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAE 1255
Cdd:TIGR00618 554 ERK--------QRASLKEQMQEIQQSFSILTQCDN---RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQ 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1256 SQLQELQVKHTESERQKHELLDKVSKMQAELESLQgtvTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRL 1335
Cdd:TIGR00618 623 PEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQ---ERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1336 RQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQ----LEERNAS 1411
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEevtaALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1412 YDKLDKTKTRLQRELDDvlvDQGHLRQTVQELERKQKKFDQMLAEEKSistKYAEERDRAEAEAREKETKSLTLARELEA 1491
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREE---DTHLLKTLEAEIGQEIPSDEDILNLQCE---TLVQEEEQFLSRLEEKSATLGEITHQLLK 853
|
650
....*....|....*.
gi 319655760 1492 MTDLKNELERVNKQLK 1507
Cdd:TIGR00618 854 YEECSKQLAQLTQEQA 869
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1002-1300 |
1.47e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1002 EERISEFTTNLAEEEEKSKSL----QKLKTKHETM------------ITDLEDRLRKEEKMRQELEKNRRKLEGDSTELH 1065
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLsfdvQKLQRLHQAFsrfigshlavafEADPEAELRQLNRRRVELERALADHESQEQQQR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1066 DQIAELQAQIAELRA-----------QLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQED---LELEKAAR 1131
Cdd:PRK04863 865 SQLEQAKEGLSALNRllprlnlladeTLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDpeqFEQLKQDY 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1132 NKAEKQRRDLGEELEALKteledtldstaaqqELRAKRET-EVTQLKKTLEDEARAHEQMlsevRQKHNQAFEELNEQLE 1210
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALT--------------EVVQRRAHfSYEDAAEMLAKNSDLNEKL----RQRLEQAEQERTRARE 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1211 QSKRSKASVDKAKQ---ALESERNELQIELKSLSQSKND-----SENRRKKAESQLQELQVKHTESERQKHELLDKVSKM 1282
Cdd:PRK04863 1007 QLRQAQAQLAQYNQvlaSLKSSYDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANRSRRNQLEKQLTFC 1086
|
330
....*....|....*...
gi 319655760 1283 QAELESLQGTVTKVESKS 1300
Cdd:PRK04863 1087 EAEMDNLTKKLRKLERDY 1104
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1366-1850 |
1.50e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1366 AQAQLAEMKKKIEQ-EAQSLESMEDGKKKLQREVESVLQQLEE-RNASYDKLDKTKTRLQR------ELDDVLVDQGHLR 1437
Cdd:PRK02224 185 QRGSLDQLKAQIEEkEEKDLHERLNGLESELAELDEEIERYEEqREQARETRDEADEVLEEheerreELETLEAEIEDLR 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1438 QTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSK 1517
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1518 DDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFE------RDLQSRDEQGEEKRKQL 1591
Cdd:PRK02224 345 ESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGdapvdlGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1592 VKQVREMEMELEDERKQRAQAVSV----------------------------RKKLELDLSELAAQIDlANKARDEALKQ 1643
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALleagkcpecgqpvegsphvetieedrerVEELEAELEDLEEEVE-EVEERLERAED 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1644 LKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSL 1723
Cdd:PRK02224 504 LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1724 SSDERRRLEaRIAQLEEELEEEHLSVELVNDRLKKaslQAEQvtveltaersNSQRLEGLRSQLDRQnkdmKQKLQELEG 1803
Cdd:PRK02224 584 LKERIESLE-RIRTLLAAIADAEDEIERLREKREA---LAEL----------NDERRERLAEKRERK----RELEAEFDE 645
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 319655760 1804 AVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKE 1850
Cdd:PRK02224 646 ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1012-1180 |
1.53e-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: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1012 LAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQL--AKKEEEL 1089
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1090 QAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEdtldstAAQQELRAKR 1169
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE------AELEELEAER 165
|
170
....*....|.
gi 319655760 1170 ETEVTQLKKTL 1180
Cdd:COG1579 166 EELAAKIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1367-1917 |
1.99e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 66.32 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1367 QAQLAEMKKKIEQEAQSLE---SMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQ--RELDDVLVDQGHLRQTVQ 1441
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEvrkAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEavKKAEEAKKDAEEAKKAEE 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1442 E---LERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLAReleamtdlKNELERVNKQLKTEMEDlVSSKD 1518
Cdd:PTZ00121 1248 ErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAK--------KAEEKKKADEAKKKAEE-AKKAD 1318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1519 DAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDE---QGEEKRK-QLVKQ 1594
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAakkKAEEKKKaDEAKK 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1595 VREMEMELEDERKQRAQAvsvrKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMK-EQMREFEDLRLSRDESlnqAK 1673
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAA----KKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEA---KK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1674 ENERKIKSMEAEimQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSlsSDERRRLEARIAQLEEELEEEHLSVELVN 1753
Cdd:PTZ00121 1472 ADEAKKKAEEAK--KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1754 -DRLKKAS--LQAEQVTVELTAERSNSQRLEGLRsqldrqnkdmkqKLQELEGAVKSKYKSTITALETKIQQLEEQLDSE 1830
Cdd:PTZ00121 1548 aDELKKAEelKKAEEKKKAEEAKKAEEDKNMALR------------KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1831 MKERQQS--TKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQleeteeeAARANASCRKLRRELEDAT 1908
Cdd:PTZ00121 1616 EEAKIKAeeLKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK-------AEEDKKKAEEAKKAEEDEK 1688
|
....*....
gi 319655760 1909 ESASAMNRE 1917
Cdd:PTZ00121 1689 KAAEALKKE 1697
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1015-1333 |
2.21e-10 |
|
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: 65.92 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1015 EEEKSKSLQKLKTKHETMitdLEDRLR--KEEKMRqELEKnRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQaa 1092
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKM---EQERLRqeKEEKAR-EVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELE-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1093 laRIEEEAALKNAAQKSIREMEAQISELQE--DLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRE 1170
Cdd:pfam17380 352 --RIRQEERKRELERIRQEEIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1171 TEVTQLKKTLEDEARAHE-QMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQ----ALESERNELQIELKSLSQSKN 1245
Cdd:pfam17380 430 EEARQREVRRLEEERAREmERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdrkrAEEQRRKILEKELEERKQAMI 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1246 DSENRRKKAESQLQELQVKHTESERQKHEllDKVSKMQAELESLQgtvtKVESKSIKAAKDCSAVESQLKDAQALLE--- 1322
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRREA--EEERRKQQEMEERR----RIQEQMRKATEERSRLEAMEREREMMRQive 583
|
330
....*....|..
gi 319655760 1323 -EETRQKLAIST 1333
Cdd:pfam17380 584 sEKARAEYEATT 595
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1111-1737 |
2.70e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1111 REMEAQISELQEDLELEKAARN---KAEKQRRDLgEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEArah 1187
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEaleDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1188 eqmLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALES----ERNELQIELKSLSQSKNDSENRRKKAESQLQELQV 1263
Cdd:COG4913 297 ---LEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1264 KHTESERQKHELLDKVSKMQAELESLQgtvtkvesksikaakdcSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQN 1343
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEEL-----------------EALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1344 NLKEmleeeeeskknvekQLHTAQAQLAEMKKKIEQEAQSL-ESME--DGKKKLQREVESVLqqleeRNAsydkldktKT 1420
Cdd:COG4913 437 NIPA--------------RLLALRDALAEALGLDEAELPFVgELIEvrPEEERWRGAIERVL-----GGF--------AL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1421 RL---QRELDDVL--VDQGHLRQTV--QELERKQKKFDQMLAEEKSISTKYAEERDRAEAEareketksltlareleamt 1493
Cdd:COG4913 490 TLlvpPEHYAAALrwVNRLHLRGRLvyERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAW------------------- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1494 dLKNELERVNKQLKTEmedlvsskddagkSVHELERAKRGMEQQLeEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQF 1573
Cdd:COG4913 551 -LEAELGRRFDYVCVD-------------SPEELRRHPRAITRAG-QVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAAL 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1574 ERDLQsrdeQGEEKRKQLVKQVREMEMELE--DERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALK---QLKKLQ 1648
Cdd:COG4913 616 EAELA----ELEEELAEAEERLEALEAELDalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAssdDLAALE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1649 AQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQER-DELQDEINSQNAKNSLS--- 1724
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDAVERELRenl 771
|
650
....*....|...
gi 319655760 1725 SDERRRLEARIAQ 1737
Cdd:COG4913 772 EERIDALRARLNR 784
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
903-1289 |
3.19e-10 |
|
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: 64.92 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 903 AEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEE 982
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 983 DLMVIEDQNAKLSKEKKQMEERISEFttnlaeeEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDST 1062
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIREL-------EEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1063 ELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKqrrdLG 1142
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG----LG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1143 EELEALKTELEDTldstaaQQELRAKReTEVTQLKKTLEDEARAheqmLSEVRQKHNQAFEELNEQLEQSK----RSKAS 1218
Cdd:pfam07888 258 EELSSMAAQRDRT------QAELHQAR-LQAAQLTLQLADASLA----LREGRARWAQERETLQQSAEADKdrieKLSAE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1219 VDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQE----LQVKHTESER---QKHELLDKVSKMQAELESL 1289
Cdd:pfam07888 327 LQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQElkasLRVAQKEKEQlqaEKQELLEYIRQLEQRLETV 404
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1066-1304 |
3.36e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.08 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLElekAARNKAEKQRRDLGEEL 1145
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA---EAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1146 EALKTE------LEDTLDSTAAQQELRakretevtqlkktledeaRAheQMLSEVRQKHNQAFEELNEQLEQSKRSKASV 1219
Cdd:COG3883 93 RALYRSggsvsyLDVLLGSESFSDFLD------------------RL--SALSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1220 DKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESK 1299
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....*
gi 319655760 1300 SIKAA 1304
Cdd:COG3883 233 AAAAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1170-1875 |
4.16e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1170 ETEVTQLKKTLEDEARAHEQMLSEVRQ-KHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKslsqskndsE 1248
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL---------E 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1249 NRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGtvtkvesksikaakdcsaveSQLKDAQALLEEETRQK 1328
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG--------------------DRLEQLEREIERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1329 LAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEER 1408
Cdd:COG4913 355 EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1409 NASYD-KLDKTKTRLQRELDdvlVDQGHLRqtvqelerkqkkfdqMLAEEKSISTKYAEERDRAEAEARekeTKSLTL-- 1485
Cdd:COG4913 435 KSNIPaRLLALRDALAEALG---LDEAELP---------------FVGELIEVRPEEERWRGAIERVLG---GFALTLlv 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1486 -----ARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEmktqleeledelqltedakl 1560
Cdd:COG4913 494 ppehyAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-------------------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1561 RLEVNMQALKAQFERDLQSRD----EQGeekrkqLVKQVREMEmELEDERKQRAQAV---SVRKKLEldlsELAAQIDLA 1633
Cdd:COG4913 554 ELGRRFDYVCVDSPEELRRHPraitRAG------QVKGNGTRH-EKDDRRRIRSRYVlgfDNRAKLA----ALEAELAEL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1634 NKARDEALKQLKKLQAQMkEQMREfedlRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAK---RQIQQERDEL 1710
Cdd:COG4913 623 EEELAEAEERLEALEAEL-DALQE----RREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1711 QDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKA-SLQAEQVTVELTAERSNSQRLEGLRSQLDR 1789
Cdd:COG4913 698 EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElRALLEERFAAALGDAVERELRENLEERIDA 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1790 QNKDMKQKLQELEGAV---KSKYKSTITALETKIQQLEEQLdsEMKERQQSTKQVRRvEKKLKEVLLQVEDERRNADQSK 1866
Cdd:COG4913 778 LRARLNRAEEELERAMrafNREWPAETADLDADLESLPEYL--ALLDRLEEDGLPEY-EERFKELLNENSIEFVADLLSK 854
|
....*....
gi 319655760 1867 TETEKANIR 1875
Cdd:COG4913 855 LRRAIREIK 863
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
862-1329 |
4.64e-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: 65.24 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQF-QS 940
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFlRK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQNIG-----------DLEQQLDEEEAArQKLQLEKVTMDakLKKIEEDLMVIEDQnaklskekkQMEERISEFT 1009
Cdd:pfam12128 543 EAPDWEQSIGkvispellhrtDLDPEVWDGSVG-GELNLYGVKLD--LKRIDVPEWAASEE---------ELRERLDKAE 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1010 TNLAEEEEKSKSLQKlktKHETMITDLEDRLRKEEKMRQELEKNR---RKLEGDSTELHDQIAE--------LQAQIAEL 1078
Cdd:pfam12128 611 EALQSAREKQAAAEE---QLVQANGELEKASREETFARTALKNARldlRRLFDEKQSEKDKKNKalaerkdsANERLNSL 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1079 RAQLAKKEEELQAALARIEEEAA-LKNAAQKSIREMEaqiSELQEDLELEKAARNKAEKQRRdlgEELEALKTELEDTLD 1157
Cdd:pfam12128 688 EAQLKQLDKKHQAWLEEQKEQKReARTEKQAYWQVVE---GALDAQLALLKAAIAARRSGAK---AELKALETWYKRDLA 761
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1158 STAAQQELRAKRETEVTQLKKTLEDEARAheqmlsevRQKHNQAFEELNEQ-LEQSKRSKASVDKAKQALEsernELQIE 1236
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIERIAVR--------RQEVLRYFDWYQETwLQRRPRLATQLSNIERAIS----ELQQQ 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1237 LKSLSQsknDSENRRKKAESQLQelqvkhtESERQKHELLDKVSKMQAELESLQGTVTKVESKSIK-AAKDCSAVESQLK 1315
Cdd:pfam12128 830 LARLIA---DTKLRRAKLEMERK-------ASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQgSIGERLAQLEDLK 899
|
490
....*....|....
gi 319655760 1316 DAQALLEEETRQKL 1329
Cdd:pfam12128 900 LKRDYLSESVKKYV 913
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
951-1119 |
6.39e-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: 61.48 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 951 DLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKtkhe 1030
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1031 tMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAAlknAAQKSI 1110
Cdd:COG1579 90 -EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE---ELEAER 165
|
....*....
gi 319655760 1111 REMEAQISE 1119
Cdd:COG1579 166 EELAAKIPP 174
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1259 |
7.51e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 843 QVTRQEEEMVAKEEELVKMKERQQQAE----DQLKESEAKQKqlnAEKLALQEQLQAETELcQEAEEMRSRLTARMQEME 918
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEakkaDEAKKAEEAKK---ADEAKKAEEKKKADEL-KKAEELKKAEEKKKAEEA 1569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 919 EVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKlqlEKVTMDAKLKKIEEDLMVIEDQNAKLSKEK 998
Cdd:PTZ00121 1570 KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE---EAKIKAEELKKAEEEKKKVEQLKKKEAEEK 1646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 999 KQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNR-----RKLEGDSTELHDQIAElQA 1073
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKK-AE 1725
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1074 QIAELRAQLAKKEEELQaalARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTeLE 1153
Cdd:PTZ00121 1726 EENKIKAEEAKKEAEED---KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IK 1801
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1154 DTLDSTAAQQElRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEE--LNEQLEQSKRSKASVDKAKQALESERN 1231
Cdd:PTZ00121 1802 DIFDNFANIIE-GGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKhkFNKNNENGEDGNKEADFNKEKDLKEDD 1880
|
410 420
....*....|....*....|....*...
gi 319655760 1232 ELQIELKSLSQSKNDSENRRKKAESQLQ 1259
Cdd:PTZ00121 1881 EEEIEEADEIEKIDKDDIEREIPNNNMA 1908
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1152 |
1.06e-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: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 887 LALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLhelesrleeeeervAQFQSEKKKMQQNIGDLEQQLDEEEAARQKL 966
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKEL--------------AALKKEEKALLKQLAALERRIAALARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 967 QLEKVTMDAKLKKIEEDlmvIEDQNAKLSKEKKQMEERIsefttnlaeeeeksKSLQKLKTKHETMI-------TDLEDR 1039
Cdd:COG4942 75 EQELAALEAELAELEKE---IAELRAELEAQKEELAELL--------------RALYRLGRQPPLALllspedfLDAVRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1040 LRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISE 1119
Cdd:COG4942 138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
250 260 270
....*....|....*....|....*....|....*...
gi 319655760 1120 LQEDLE-----LEKAARNKAEKQRRDLGEELEALKTEL 1152
Cdd:COG4942 218 LQQEAEelealIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
843-1234 |
1.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 843 QVTRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAEtELCQEAEEMRSRLTARMQEMEEVLH 922
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-PLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 923 ELESrleeeeerVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKV-TMDAKLKKIEEDLMVIEDQNAKLSKEKKQM 1001
Cdd:COG4717 154 RLEE--------LRELEEELEELEAELAELQEELEELLEQLSLATEEELqDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1002 EERISEFTTNLAEEEEKSK-----------------------------------------------SLQKLKTKHETMIT 1034
Cdd:COG4717 226 EEELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAEL---QAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIR 1111
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELldrIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1112 EMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDstAAQQELRAKRETEVTQLKKTLEDEARAHEQM- 1190
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELe 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1191 -------LSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQ 1234
Cdd:COG4717 464 qleedgeLAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
935-1134 |
1.15e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 62.54 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 935 VAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDlmvIEDQNAKLSKEKKQMEERISEF------ 1008
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE---IAEAEAEIEERREELGERARALyrsggs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1009 ---------TTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELR 1079
Cdd:COG3883 102 vsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1080 AQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKA 1134
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1273-1883 |
1.45e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 63.40 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1273 HELLDKVSKMQAELESLQGTVTKVEsKSIKAAKDCSAVEsQLKDAQALLEEETRQKLAiSTRLRQLEDEQNNLKEmleee 1352
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAE-RYAAARERLAELE-YLRAALRLWFAQRRLELL-EAELEELRAELARLEA----- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1353 eeskknvekQLHTAQAQLAEMKKKIEQ-EAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDvlv 1431
Cdd:COG4913 310 ---------ELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA--- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1432 dqghlrqTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEME 1511
Cdd:COG4913 378 -------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1512 DLVSSKDDAGKSVHEL--------------ERAKRGmeqqleemktqleeledelqltedAKLRLEVNmQALKAQFERDL 1577
Cdd:COG4913 451 EALGLDEAELPFVGELievrpeeerwrgaiERVLGG------------------------FALTLLVP-PEHYAAALRWV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1578 QSRDeqgeeKRKQLVkqVREMEMELEDERKQRAQAVSVRKKLELDLS--------ELAAQIDLANKARDEALKQLKK--- 1646
Cdd:COG4913 506 NRLH-----LRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKPHpfrawleaELGRRFDYVCVDSPEELRRHPRait 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1647 LQAQMKEQMREFE-DLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQdeinsqnaknslss 1725
Cdd:COG4913 579 RAGQVKGNGTRHEkDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ-------------- 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1726 dERRRLEARIAQLEEeleeehlsvelvnDRLKKASLQAE--QVTVELTAERSNSQRLEGLRSQLDRQnkdmKQKLQELEG 1803
Cdd:COG4913 645 -ERREALQRLAEYSW-------------DEIDVASAEREiaELEAELERLDASSDDLAALEEQLEEL----EAELEELEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1804 AVKsKYKSTITALETKIQQLEEQLDS-----EMKERQQSTKQVRRVEKKLKEVLLQvEDERRNADQSKTETEKANIRLKQ 1878
Cdd:COG4913 707 ELD-ELKGEIGRLEKELEQAEEELDElqdrlEAAEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNR 784
|
....*
gi 319655760 1879 MKRQL 1883
Cdd:COG4913 785 AEEEL 789
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1578-1790 |
1.88e-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: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1578 QSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMRE 1657
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1658 FEDLRLSRDESLNQAKENERKIKSME----AEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEA 1733
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1734 RIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQ 1790
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1188-1917 |
1.95e-09 |
|
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: 63.07 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1188 EQMLSEVRQKHNQAFEELNEQLEQSKRSKASvdKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKhtE 1267
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKEAL--KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--E 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1268 SERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKE 1347
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1348 MLEEEEESKKNVEKQLHTAQAQLA----EMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASydkldktktrLQ 1423
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKkaekELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----------EQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1424 RELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVN 1503
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1504 KQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQ 1583
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1584 GEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRL 1663
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1664 SRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELE 1743
Cdd:pfam02463 611 ATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1744 EEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQK-LQELEGAVKSKYKSTITALETKIQQ 1822
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKiDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1823 LEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRR 1902
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK 850
|
730
....*....|....*
gi 319655760 1903 ELEDATESASAMNRE 1917
Cdd:pfam02463 851 LAEEELERLEEEITK 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1105-1319 |
3.22e-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: 60.93 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1105 AAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDT---LDSTAAQQELRAKR----ETEVTQLK 1177
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALarrIRALEQELAALEAElaelEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1178 KTLEDEARAHEQMLSEVRQKHNQAFEEL---NEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKA 1254
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1255 ESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQA 1319
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
863-1261 |
3.38e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQLKESEAKQKQLNAeklaLQEQLQAETELCQEAEEMRSRLTARMQEMEEVL--HELESRLEEEEERVAQFQS 940
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKLLqlLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDlmvIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSK 1020
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA---TEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1021 SLQKLKTKHETMITDLEDRLRKEEKMRQ--------ELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAA 1092
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLlliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1093 LARIEEEAALKNAAQKSIREM-----------EAQISELQEDLELEKAARNKAEKQRRDLgeELEALKTELEDTLDSTAA 1161
Cdd:COG4717 304 AEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1162 QQE----LRAKRETEVTQLKKTLED-EARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIE 1236
Cdd:COG4717 382 EDEeelrAALEQAEEYQELKEELEElEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
410 420
....*....|....*....|....*..
gi 319655760 1237 LKSLSQSKNDSENRRKKAE--SQLQEL 1261
Cdd:COG4717 462 LEQLEEDGELAELLQELEElkAELREL 488
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
943-1246 |
3.62e-09 |
|
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: 61.79 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 943 KKMQQNIGDLEQQLDEeeaarqklqlekvtMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEK-SKS 1021
Cdd:pfam06160 82 KKAKKALDEIEELLDD--------------IEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSyGPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1022 LQKLktkhETMITDLEDRL---------------RKE-EKMRQELEKNRRKLEG-------DSTELHDQIAELQAQIAEL 1078
Cdd:pfam06160 148 IDEL----EKQLAEIEEEFsqfeeltesgdyleaREVlEKLEEETDALEELMEDipplyeeLKTELPDQLEELKEGYREM 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1079 RAQ---LAKK--EEELQAALARIEE-EAALKN----AAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:pfam06160 224 EEEgyaLEHLnvDKEIQQLEEQLEEnLALLENleldEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1149 KTELEDTLDSTA--------AQQELRAKR--ETEVTQLKK---TLEDEARAHEQMLSEVRQKhnqaFEELNEQLEQSKRS 1215
Cdd:pfam06160 304 EEQNKELKEELErvqqsytlNENELERVRglEKQLEELEKrydEIVERLEEKEVAYSELQEE----LEEILEQLEEIEEE 379
|
330 340 350
....*....|....*....|....*....|.
gi 319655760 1216 KASVDKAKQALESERNELQIELKSLSQSKND 1246
Cdd:pfam06160 380 QEEFKESLQSLRKDELEAREKLDEFKLELRE 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1132-1806 |
4.76e-09 |
|
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: 61.57 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1132 NKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEdEARAHEQMLSEVRQKHNQAFEELNEQLEQ 1211
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIK-ILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1212 SKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQG 1291
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1292 TVTKVESKSIKAAKDCSAVESQLKDAQALLEEetrqklaistrLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLA 1371
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ-----------ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1372 EMKkkieqeaqslESMEDGKKKLQREVesvlQQLEERNASYDKLDKTKTRLQRELDDV--LVDQGHLRQTVQELERKQKK 1449
Cdd:TIGR04523 257 QLK----------DEQNKIKKQLSEKQ----KELEQNNKKIKELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1450 FDQM---LAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDagksvhe 1526
Cdd:TIGR04523 323 LEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1527 lerakrgMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFErDLQSRDEQGEEKRKQLVKQVREMEMELEDER 1606
Cdd:TIGR04523 396 -------LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII-KNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1607 KQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEI 1686
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1687 MQLHEDL--AAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAE 1764
Cdd:TIGR04523 548 NKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 319655760 1765 QVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVK 1806
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
945-1306 |
4.98e-09 |
|
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: 61.13 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 945 MQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQK 1024
Cdd:COG5185 171 ELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1025 LKTKHETMITDLED----RLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIaELRAQLAKKEEELQAALARIEEEA 1100
Cdd:COG5185 251 TSDKLEKLVEQNTDlrleKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSI-DIKKATESLEEQLAAAEAEQELEE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1101 AlKNAAQKSIREMEAQISELQEDLElEKAARNKAEKQRRDLGEELEALKTELEDtldstaAQQELRAKREtEVTQLKKTL 1180
Cdd:COG5185 330 S-KRETETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELSKSSEELDS------FKDTIESTKE-SLDEIPQNQ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1181 EDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAE--SQL 1258
Cdd:COG5185 401 RGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSvrSKK 480
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 319655760 1259 QELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKD 1306
Cdd:COG5185 481 EDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKD 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1199-1408 |
5.38e-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: 60.55 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1199 NQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDK 1278
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1279 VSKMQAELESLQGTVTKVESKSI-----------KAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKE 1347
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1348 MLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEER 1408
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1331-1925 |
6.19e-09 |
|
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: 61.19 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1331 ISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNA 1410
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1411 SYDKLDKTKTRLQRELDDVLVdqghlrqtvqELERKQKkfdqmlaEEKSISTKYAEERDRAEAEAREKETKSLTLARELE 1490
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLT----------EIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1491 AMTDLKNELERVNKQLkTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALK 1570
Cdd:TIGR04523 188 NIDKIKNKLLKLELLL-SNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1571 AQFErDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLEL-----DLSELAAQIDLANKARDE---ALK 1642
Cdd:TIGR04523 267 KQLS-EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELknqekKLEEIQNQISQNNKIISQlneQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1643 QLKK-----------LQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQ 1711
Cdd:TIGR04523 346 QLKKeltnsesenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1712 DEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQN 1791
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1792 KDMKQKLQELEGAVKSkYKSTITALETKIQQLEEQLDSEMKE--RQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTET 1869
Cdd:TIGR04523 506 KELEEKVKDLTKKISS-LKEKIEKLESEKKEKESKISDLEDElnKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1870 EKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKL 1925
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1083 |
6.41e-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: 60.16 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 847 QEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELES 926
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 927 RLEEEEERVAQF--QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVT--MDAKLKKIEEDLMVIEDQNAKLSKEKKQME 1002
Cdd:COG4942 98 ELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLApaRREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1003 ERisefttnLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEgdstelhDQIAELQAQIAELRAQL 1082
Cdd:COG4942 178 AL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE-------ALIARLEAEAAAAAERT 243
|
.
gi 319655760 1083 A 1083
Cdd:COG4942 244 P 244
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1103 |
8.19e-09 |
|
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: 60.85 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSR------------LTARMQEMEEVLHELESRLE 929
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeiqaelskLEEEVSRIEARLREIEQKLN 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 930 EEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFT 1009
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1010 TNL----AEEEEKSKSLQKLKTKHETM---ITDLEDRLRKEE-------------KMRQELEKNRRKLEGDSTELHDQIA 1069
Cdd:TIGR02169 903 RKIeeleAQIEKKRKRLSELKAKLEALeeeLSEIEDPKGEDEeipeeelsledvqAELQRVEEEIRALEPVNMLAIQEYE 982
|
250 260 270
....*....|....*....|....*....|....
gi 319655760 1070 ELQAQIAELRAQLAKKEEELQAALARIEEEAALK 1103
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
839-1223 |
9.90e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 839 KPLLQVTRQEEEMVAKEEELVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELcqeaEEMRSRLTAR-MQEM 917
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL----ERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 918 EEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMD------------AKLKKIEEDLM 985
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkelleeytAELKRIEKELK 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 986 VIEDQNAKLSKEKKQMEERISEFTT---------------------NLAEEEEKSKSLQKLKTKHETM---ITDLEDRLR 1041
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESEliklkelaeqlkeleeklkkyNLEELEKKAEEYEKLKEKLIKLkgeIKSLKKELE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1042 KE---EKMRQELEKNRRKLEGDSTELHDQIA--------ELQAQIAELR-------------AQLAKKEEELQAALARIE 1097
Cdd:PRK03918 550 KLeelKKKLAELEKKLDELEEELAELLKELEelgfesveELEERLKELEpfyneylelkdaeKELEREEKELKKLEEELD 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1098 EEAALKNAAQKSIREMEAQISELQE--DLELEKAARNKAEKQRRDLG------EELEALKTELEDTLDSTAAQQELRAKR 1169
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKkySEEEYEELREEYLELSRELAglraelEELEKRREEIKKTLEKLKEELEEREKA 709
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1170 ETEVTQLKKTLED-----------EARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAK 1223
Cdd:PRK03918 710 KKELEKLEKALERveelrekvkkyKALLKERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
940-1883 |
1.73e-08 |
|
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: 60.06 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLeQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKS 1019
Cdd:TIGR00606 166 SEGKALKQKFDEI-FSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHE------TMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEElqaAL 1093
Cdd:TIGR00606 245 NELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER---EL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1094 ARIEEEAALKNAAQKSIREMEAQISELQEDLELeKAARNKAEKQRRDLgeELEALKTELEdtLDSTAAQQELRAKRETEV 1173
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQL-QADRHQEHIRARDS--LIQSLATRLE--LDGFERGPFSERQIKNFH 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1174 TQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKK 1253
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1254 AEsqlqelQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKdcsavesqlKDAQALLEEETRQKLAIST 1333
Cdd:TIGR00606 477 DQ------ELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQ---------EMEQLNHHTTTRTQMEMLT 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1334 RLRQLEDEQnnlkemleeeEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYD 1413
Cdd:TIGR00606 542 KDKMDKDEQ----------IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1414 KLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAmt 1493
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT-- 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1494 dlKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQF 1573
Cdd:TIGR00606 690 --EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1574 ERD--LQSRDEQGEEKRKQLVKQVREME---MELEDERKQRAQAVSvrkklELDLSELAAQIDLANKARDEALKQLKKLq 1648
Cdd:TIGR00606 768 EEQetLLGTIMPEEESAKVCLTDVTIMErfqMELKDVERKIAQQAA-----KLQGSDLDRTVQQVNQEKQEKQHELDTV- 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1649 aqmkeqMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINS-QNAKNSLSSDE 1727
Cdd:TIGR00606 842 ------VSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREiKDAKEQDSPLE 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1728 rrrleariaqleeeleeehlsvelvndrlkkaslQAEQVTVELTAERSNSQRLEGLRSQLDRQnkDMKQKLQELEGAVKS 1807
Cdd:TIGR00606 916 ----------------------------------TFLEKDQQEKEELISSKETSNKKAQDKVN--DIKEKVKNIHGYMKD 959
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1808 KYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDE--RRNADQSKTETEKANIRLKQMKRQL 1883
Cdd:TIGR00606 960 IENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQkiQERWLQDNLTLRKRENELKEVEEEL 1037
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1067-1229 |
2.31e-08 |
|
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: 56.86 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1067 QIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQrrdLGE--- 1143
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvrn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1144 --ELEALKTELEdtldSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDK 1221
Cdd:COG1579 88 nkEYEALQKEIE----SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
....*...
gi 319655760 1222 AKQALESE 1229
Cdd:COG1579 164 EREELAAK 171
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
841-1374 |
2.50e-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: 59.35 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 841 LLQVTRQEEEMVAKEEELVKMKERQQQAEDQ-------LKESEAKQKQLNAE--------------KLALQEQLQAETE- 898
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKtklqdenLKELIEKKDHLTKEledikmslqrsmstQKALEEDLQIATKt 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 899 LCQEAEEMRsrltARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLD--EEEAARQKLQLEKVTMDAK 976
Cdd:pfam05483 326 ICQLTEEKE----AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEEMTKFKN 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 977 LKKIE-EDLMVIEDQNAKLSKEKKQMEERISEFTTNLAE----EEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELE 1051
Cdd:pfam05483 402 NKEVElEELKKILAEDEKLLDEKKQFEKIAEELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1052 KNRRK---LEGDSTELHDQIAELQAQIAELRAQLAKKEEELqaalarieeeaalkNAAQKSIREMEAQISELQEDlelEK 1128
Cdd:pfam05483 482 KEKLKnieLTAHCDKLLLENKELTQEASDMTLELKKHQEDI--------------INCKKQEERMLKQIENLEEK---EM 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1129 AARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDearaheqmLSEVRQKHNQAFEELNEQ 1208
Cdd:pfam05483 545 NLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNN--------LKKQIENKNKNIEELHQE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1209 LEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELE- 1287
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDk 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1288 ----SLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQL 1363
Cdd:pfam05483 697 rcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
570
....*....|.
gi 319655760 1364 HTAQAQLAEMK 1374
Cdd:pfam05483 777 KENTAILKDKK 787
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
870-1486 |
2.52e-08 |
|
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: 59.07 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 870 DQLKESEAKQKQLNAEKLALQEQLQAETEL-------CQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEK 942
Cdd:pfam10174 60 EQYRVTQEENQHLQLTIQALQDELRAQRDLnqllqqdFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 943 KKMQQNIGDLEQQLDEEEAARQKLqLEKVTMDAKLKKIEED-------LMVIEDQNAKL-----SKEKKQMEERISEFTT 1010
Cdd:pfam10174 140 EEMELRIETQKQTLGARDESIKKL-LEMLQSKGLPKKSGEEdwertrrIAEAEMQLGHLevlldQKEKENIHLREELHRR 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1011 N-LAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEkmrQELEKNRRKLEGDSTELHDQIAELQA----------QIAELR 1079
Cdd:pfam10174 219 NqLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1080 AQLAKKEEELQAALARIEeeaALKNaaqksiremeaQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTldst 1159
Cdd:pfam10174 296 QELSKKESELLALQTKLE---TLTN-----------QNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEK---- 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1160 aaQQELRAKRE--TEVTQLKKTLEDEARAHEQMLSEVRQKHN---QAFEELNEQLEQSKRSKASVDKAKQALESERNELQ 1234
Cdd:pfam10174 358 --ESFLNKKTKqlQDLTEEKSTLAGEIRDLKDMLDVKERKINvlqKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1235 IELKSLSQSKNDS----ENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAEL--------------ESLQGTVTKV 1296
Cdd:pfam10174 436 TALTTLEEALSEKeriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELtekesslidlkehaSSLASSGLKK 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1297 ES--KSIKAA-----KDCSAVESQLKDAQAlLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQ 1369
Cdd:pfam10174 516 DSklKSLEIAveqkkEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENE 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1370 LAEMKKKIEQeaqsLESMEDGKKKLQREVESVLQ--QLEERNASYDKLDKTKTRLQRELDDVLVDQ-----GHLRQTVQE 1442
Cdd:pfam10174 595 KNDKDKKIAE----LESLTLRQMKEQNKKVANIKhgQQEMKKKGAQLLEEARRREDNLADNSQQLQleelmGALEKTRQE 670
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 319655760 1443 LERKQKKF---DQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLA 1486
Cdd:pfam10174 671 LDATKARLsstQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA 717
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
949-1174 |
2.89e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 949 IGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSL------ 1022
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1023 QKLKTKHETMI---TDLEDRLRKEEKMRQELEKNRRKLEgdstelhdQIAELQAQIAELRAQLAKKEEELQAALARIEEE 1099
Cdd:COG3883 98 SGGSVSYLDVLlgsESFSDFLDRLSALSKIADADADLLE--------ELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 319655760 1100 aalKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRdlgEELEALKTELEDTLDSTAAQQELRAKRETEVT 1174
Cdd:COG3883 170 ---KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELA---AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
868-1133 |
3.96e-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: 57.85 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 868 AEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLhelesrleeeeervaqfqsekKKMQQ 947
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI---------------------RALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 948 NIGDLEQQLDEEEAARQKLQlekvtmdAKLKKIEEDLmviEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKT 1027
Cdd:COG4942 77 ELAALEAELAELEKEIAELR-------AELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1028 KHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQ 1107
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250 260
....*....|....*....|....*.
gi 319655760 1108 KSIREMEAQISELQEDLELEKAARNK 1133
Cdd:COG4942 227 ALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
858-1325 |
5.11e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 58.27 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAET---------ELCQEAEEMR----------SRLTARMQEME 918
Cdd:PRK10246 235 LLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEEkaqpqlaalSLAQPARQLRphweriqeqsAALAHTRQQIE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 919 EVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQlEKVTMDAKLKKIEEDLMVIEDQNAKLSKEK 998
Cdd:PRK10246 315 EVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLTHAE 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 999 KQMEErISEFTTNLAEEEEKSKSLQKLKTKhetmitDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAEL 1078
Cdd:PRK10246 394 QKLNA-LPAITLTLTADEVAAALAQHAEQR------PLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEM 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1079 RAQLAKKEEELQAALARIEEEAalknaaqkSIREMEAQISELQ-------------------EDLEL--EKAARNKAEKQ 1137
Cdd:PRK10246 467 RQRYKEKTQQLADVKTICEQEA--------RIKDLEAQRAQLQagqpcplcgstshpaveayQALEPgvNQSRLDALEKE 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1138 RRDLGEE-------LEALKTELEDtlDSTAAQ------QELRAKRETEVTQLKKTLE---------DEARAHEQMLSEVR 1195
Cdd:PRK10246 539 VKKLGEEgaalrgqLDALTKQLQR--DESEAQslrqeeQALTQQWQAVCASLNITLQpqddiqpwlDAQEEHERQLRLLS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1196 QKHN-QAfeELNEQLEQSKRSKASVDKAKQALESernelQIELKSLSQSKNDSENRRKKA-ESQLQELQVKHTESERqkh 1273
Cdd:PRK10246 617 QRHElQG--QIAAHNQQIIQYQQQIEQRQQQLLT-----ALAGYALTLPQEDEEASWLATrQQEAQSWQQRQNELTA--- 686
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1274 eLLDKVSKMQAELESL-QGTVTKVESKSI------KAAKDCSAVESQLKDAQALLEEET 1325
Cdd:PRK10246 687 -LQNRIQQLTPLLETLpQSDDLPHSEETValdnwrQVHEQCLSLHSQLQTLQQQDVLEA 744
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
943-1155 |
5.94e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 57.72 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 943 KKMQQNIGDLEQQLD---EEEAARQKLQLEkvtMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEK- 1018
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqQQIKTYNKNIEE---QRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDp 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDLEdRLRKEEKMRQEleknrrklEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEE 1098
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIE-QFQKVIKMYEK--------GGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1099 EAALKN---AAQKSIREMEAQISELQEDLELE-------KAARNKAEKQRRDLGEELEALKTELEDT 1155
Cdd:PHA02562 325 LEEIMDefnEQSKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
939-1456 |
6.24e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLS---KEKKQMEERISEFTTNLAEE 1015
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSsleDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1016 EEKSKSLQKLKTKHETMITDL----EDRLRKEEKMRQELEKNRRKLEGDSTEL------HDQIAELQAQIAELrAQLAKK 1085
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDIENKKQILSNIDAEInkyhaiIKKLSVLQKDYNDY-IKKKSR 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1086 EEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAA---- 1161
Cdd:PRK01156 348 YDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSkvss 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1162 -QQELRAKRETEvtqlkktleDEARAHEQMLS------------------EVRQKHNQAFEELNEQLEQSKRSKASVDKA 1222
Cdd:PRK01156 428 lNQRIRALRENL---------DELSRNMEMLNgqsvcpvcgttlgeeksnHIINHYNEKKSRLEEKIREIEIEVKDIDEK 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1223 KQALESERNELQI-ELKSLSQSKNDSENRR---KKAESQLQELQVKHTESERQKHEL----LDKVSKMQAELESLQGTVT 1294
Cdd:PRK01156 499 IVDLKKRKEYLESeEINKSINEYNKIESARadlEDIKIKINELKDKHDKYEEIKNRYkslkLEDLDSKRTSWLNALAVIS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1295 KVESKSIKAAKDcsAVESQLKDAQALLEEETRQ----KLAISTRLRQLEDEQNNLKEMLEeeeeskknvekQLHTAQAQL 1370
Cdd:PRK01156 579 LIDIETNRSRSN--EIKKQLNDLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKYN-----------EIQENKILI 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1371 AEMKKKIEQEAQSLESMeDGKKKLQREVESVLQQLEERnasYDKLDKtktrlqrELDDVLVDQGHLRQTVQELERKQKKF 1450
Cdd:PRK01156 646 EKLRGKIDNYKKQIAEI-DSIIPDLKEITSRINDIEDN---LKKSRK-------ALDDAKANRARLESTIEILRTRINEL 714
|
....*.
gi 319655760 1451 DQMLAE 1456
Cdd:PRK01156 715 SDRIND 720
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1207-1883 |
6.42e-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: 58.06 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1207 EQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHtESERQKHELLDKVSKMQAEL 1286
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH-AYLTQKREAQEEQLKKQQLL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1287 ESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEEtrqklaistRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTA 1366
Cdd:TIGR00618 263 KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK---------AVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1367 QAQLAEmkkkIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTrLQRELDDVLVDQGHLRQTVQELERK 1446
Cdd:TIGR00618 334 VKQQSS----IEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT-LQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1447 QKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKddagkSVHE 1526
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE-----QIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1527 LERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALkaqferdlQSRDEQGEEKRKQLVKQVREMEMELEDER 1606
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL--------TRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1607 KQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQaKENERKIKSMEAEI 1686
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRK-LQPEQDLQDVRLHL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1687 MQLHEDLAAADRAKRQIQQERdeLQDEINSQNAknSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQV 1766
Cdd:TIGR00618 635 QQCSQELALKLTALHALQLTL--TQERVREHAL--SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1767 TVELTAER---SNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKSTITALETKIQQL--EEQLDSEMKERQQSTKQV 1841
Cdd:TIGR00618 711 THIEEYDRefnEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVtaALQTGAELSHLAAEIQFF 790
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 319655760 1842 RRV----EKKLKEVLLQVEDERRNADQSKT-ETEKANIRLKQMKRQL 1883
Cdd:TIGR00618 791 NRLreedTHLLKTLEAEIGQEIPSDEDILNlQCETLVQEEEQFLSRL 837
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1366-1575 |
1.01e-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: 56.31 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1366 AQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQtvqELER 1445
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1446 KQKKFDQMLAEEKSISTKYAEE-----RDRAEAEAREKETKSLTLAR--ELEAMTDLKNELERVNKQLKTEMEDLVSSKD 1518
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARreQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1519 DAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFER 1575
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1022-1511 |
1.04e-07 |
|
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: 57.06 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1022 LQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAA 1101
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1102 LKNAAQKSIREMEAQ---ISELQEDLELEKAARnKAEKQRRDLgeELEALKTELEDTLDstaaQQELRAKRETEVTQLKK 1178
Cdd:pfam05557 84 YLEALNKKLNEKESQladAREVISCLKNELSEL-RRQIQRAEL--ELQSTNSELEELQE----RLDLLKAKASEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1179 TLedearaheQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESeRNELQIELKSL-SQSKNDSENRRKKA--E 1255
Cdd:pfam05557 157 NL--------EKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELERLrEHNKHLNENIENKLllK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1256 SQLQELQVKhteserqkhelLDKVSKMQAELESLQGTVTKVESKsikaakdcsaVESQLKDAQAlLEEETRQKLAISTRL 1335
Cdd:pfam05557 228 EEVEDLKRK-----------LEREEKYREEAATLELEKEKLEQE----------LQSWVKLAQD-TGLNLRSPEDLSRRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1336 RQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREV--------------ESV 1401
Cdd:pfam05557 286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerdgyrailESY 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1402 LQQLEERNASYDKLDKTKTrLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETK 1481
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEE-AEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVD 444
|
490 500 510
....*....|....*....|....*....|
gi 319655760 1482 SLTlaRELEAMTDLKNELERVNKQLKTEME 1511
Cdd:pfam05557 445 SLR--RKLETLELERQRLREQKNELEMELE 472
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
866-1216 |
1.21e-07 |
|
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: 57.05 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 866 QQAEDQLKESEAKQKQLNAE-KLALQE--QLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEK 942
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRvDLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTA 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 943 KKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLskekkqmeerisefttnLAEEEEKSKSL 1022
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKL-----------------VNAGSERLRAV 648
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1023 QKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAAL 1102
Cdd:pfam15921 649 KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKV 728
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1103 KNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELedtldSTAAQQELRAKRETEVTQLK-KTLE 1181
Cdd:pfam15921 729 AMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQEL-----STVATEKNKMAGELEVLRSQeRRLK 803
|
330 340 350
....*....|....*....|....*....|....*
gi 319655760 1182 DEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSK 1216
Cdd:pfam15921 804 EKVANMEVALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
863-1103 |
1.37e-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: 56.67 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQLKESEAKQKQLNAEK---LALQEQLQAETELCQEAEEMRSRLTARMQEMEEvlhelesrleeeeERVAQFQ 939
Cdd:pfam17380 386 ERQQKNERVRQELEAARKVKILEEerqRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA-------------REMERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQldEEEAARQKLQLEKVTMDAKLKKiEEDLMVIEdqnaklskekKQMEERisefTTNLAEEEEKS 1019
Cdd:pfam17380 453 LEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRAE-EQRRKILE----------KELEER----KQAMIEEERKR 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKlegdstelhdQIAELQAQIAELRAQLAKKEEELQAALARIEEE 1099
Cdd:pfam17380 516 KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR----------RIQEQMRKATEERSRLEAMEREREMMRQIVESE 585
|
....
gi 319655760 1100 AALK 1103
Cdd:pfam17380 586 KARA 589
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1060-1696 |
1.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRA--QLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISEL-----QEDLELEKAARN 1132
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERahEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrlwfaQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1133 KAEKQRRDLGEELEALKTELEDTldsTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQaFEELNEQLEqs 1212
Cdd:COG4913 299 ELRAELARLEAELERLEARLDAL---REELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR-LEALLAALG-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1213 krskASVDKAKQALESERNELQielkslsQSKNDSENRRKKAESQLQELQVKHTESERQKHELldkvskmQAELESLQGT 1292
Cdd:COG4913 373 ----LPLPASAEEFAALRAEAA-------ALLEALEEELEALEEALAEAEAALRDLRRELREL-------EAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1293 VTKVESKSIKA----AKDCSAVESQLKDAQALLE---EETRQKLAI-----STRLRQLEDEQnnlkemleeeeeskknve 1360
Cdd:COG4913 435 KSNIPARLLALrdalAEALGLDEAELPFVGELIEvrpEEERWRGAIervlgGFALTLLVPPE------------------ 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1361 kqlHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVE--SVLQQLE-ERNASYDKLdktKTRLQRELDDVLVD-QGHL 1436
Cdd:COG4913 497 ---HYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdSLAGKLDfKPHPFRAWL---EAELGRRFDYVCVDsPEEL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1437 R----------QTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVnKQL 1506
Cdd:COG4913 571 RrhpraitragQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQER-REA 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1507 KTEMEDLVSSKDDAGKSVHELERAkrgmEQQLEemktqleeledelqltedaklRLEVNMQALKaqferdlqsrdeqgee 1586
Cdd:COG4913 650 LQRLAEYSWDEIDVASAEREIAEL----EAELE---------------------RLDASSDDLA---------------- 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1587 krkQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREfedlRLSRD 1666
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA----AALGD 761
|
650 660 670
....*....|....*....|....*....|.
gi 319655760 1667 ESLNQAKEN-ERKIKSMEAEIMQLHEDLAAA 1696
Cdd:COG4913 762 AVERELRENlEERIDALRARLNRAEEELERA 792
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1224-1449 |
2.32e-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: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1224 QALESERNELQIELKSLSQskndsenRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKA 1303
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQ-------EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1304 AKDCSAVESQLKDAQALLEEETR--QKLAISTRLRQLEDEQNNLKEMLEEE-----EESKKNVEKQLHTAQAQLAEMKKK 1376
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRalYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319655760 1377 IEQEAQSLESMEDGKKKLQREVEsvlQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKK 1449
Cdd:COG4942 169 LEAERAELEALLAELEEERAALE---ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1317-1561 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1317 AQALLEEETRQKLAistrlrQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQR 1396
Cdd:COG4942 17 AQADAAAEAEAELE------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1397 EVESVLQQLEERNASYDKLDKTKTRL-QRELDDVLVDQghlrQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEA 1475
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLgRQPPLALLLSP----EDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1476 REKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLT 1555
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
....*.
gi 319655760 1556 EDAKLR 1561
Cdd:COG4942 247 GFAALK 252
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1049-1345 |
3.25e-07 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 55.63 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1049 ELEKNRRKLEGDSTElhdqIAELQAQIAELRAQLAKKEEElqaalARIEEEAALKNAAQKSIREMEAQISE------LQE 1122
Cdd:PLN03229 416 ERKVNMKKREAVKTP----VRELEGEVEKLKEQILKAKES-----SSKPSELALNEMIEKLKKEIDLEYTEaviamgLQE 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1123 DLELEKAARNKAEKQ----RRDLGEELEALKTELEDTLDSTAAQQELRAKRE--TEVTQLKKTLEDEARAhEQMLSEVRQ 1196
Cdd:PLN03229 487 RLENLREEFSKANSQdqlmHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKA-EKLKAEINK 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1197 KHNQAF---------EELNEQLEQSKRSKASV--DKAKQALESERNELQIELKSLSQSKN-DSENRRKKAESQLQELQVk 1264
Cdd:PLN03229 566 KFKEVMdrpeikekmEALKAEVASSGASSGDEldDDLKEKVEKMKKEIELELAGVLKSMGlEVIGVTKKNKDTAEQTPP- 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1265 htESERQKHELLDK-VSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQN 1343
Cdd:PLN03229 645 --PNLQEKIESLNEeINKKIERVIRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFE 722
|
..
gi 319655760 1344 NL 1345
Cdd:PLN03229 723 EL 724
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1041-1720 |
3.30e-07 |
|
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: 55.53 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1041 RKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEA-ALKNAAQKSIREMEAQISE 1119
Cdd:pfam07111 23 RRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAELISRQLQELRRLEEEVrLLRETSLQQKMRLEAQAME 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1120 LQEDLELEKAARNKAEKQRRDLgeelealkteledtldstaAQQELRAKRETEVTQlkKTLEDEARAHEQMLSEVRQKHN 1199
Cdd:pfam07111 103 LDALAVAEKAGQAEAEGLRAAL-------------------AGAEMVRKNLEEGSQ--RELEEIQRLHQEQLSSLTQAHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1200 QAFEELNEQLEQSKRSKASVD-----KAKQALESERnELQIELKSLSQSKNDSEN--------RRKKAESQLQELQVKHT 1266
Cdd:pfam07111 162 EALSSLTSKAEGLEKSLNSLEtkragEAKQLAEAQK-EAELLRKQLSKTQEELEAqvtlveslRKYVGEQVPPEVHSQTW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1267 ESERQkhELLDKVSKMQAELESLQGTV----TKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAIstrLRQLEDEQ 1342
Cdd:pfam07111 241 ELERQ--ELLDTMQHLQEDRADLQATVellqVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL---LNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1343 NNLKEMLEEEEESKKNVEKQLhtaQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRL 1422
Cdd:pfam07111 316 FALMVQLKAQDLEHRDSVKQL---RGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1423 QRELDDVlvdQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELeAMTDLKNELERV 1502
Cdd:pfam07111 393 QQQTASA---EEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKV-ALAQLRQESCPP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1503 NKQLKTEMEDLvsskddagksvhELErakrgMEQQLEEmktqleeledelqltedaKLRLEVNMQALKAQFERDLQSRDE 1582
Cdd:pfam07111 469 PPPAPPVDADL------------SLE-----LEQLREE------------------RNRLDAELQLSAHLIQQEVGRARE 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1583 QGEEKRKQLVKQVREMEMELederkQRAQA--VSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFED 1660
Cdd:pfam07111 514 QGEAERQQLSEVAQQLEQEL-----QRAQEslASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVET 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1661 lRLSRDESLNQAKENERKIKSMEAeIMQLHEDLAAADRAKRQIQQERdELQDEINSQNAK 1720
Cdd:pfam07111 589 -RLREQLSDTKRRLNEARREQAKA-VVSLRQIQHRATQEKERNQELR-RLQDEARKEEGQ 645
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1384-1945 |
3.40e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1384 LESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKfdqmLAEEKSISTK 1463
Cdd:PRK01156 140 MDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQ----IADDEKSHSI 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1464 YAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKR----------- 1532
Cdd:PRK01156 216 TLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrn 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1533 ------GMEQQLEEMKTQLEELEDELQLTEDAKLRLEVnMQALKAQFERDLQSRDE---------QGEEKRKQLVKQVRE 1597
Cdd:PRK01156 296 yindyfKYKNDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDlnnqileleGYEMDYNSYLKSIES 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1598 MEMELEDERKQR----AQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLR----------- 1662
Cdd:PRK01156 375 LKKKIEEYSKNIermsAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSrnmemlngqsv 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1663 -------LSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQ-DEINSQNAKNSLSSDERRRLEaR 1734
Cdd:PRK01156 455 cpvcgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLEsEEINKSINEYNKIESARADLE-D 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1735 IAQLEEELEEEHLSVELVNDRLKKASL----QAEQVTVELTAERSNSQrLEGLRSQLDRQNK---DMKQKLQELEGA--- 1804
Cdd:PRK01156 534 IKIKINELKDKHDKYEEIKNRYKSLKLedldSKRTSWLNALAVISLID-IETNRSRSNEIKKqlnDLESRLQEIEIGfpd 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1805 VKSKYKSTITALETKIQQLEEQLDsEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLE 1884
Cdd:PRK01156 613 DKSYIDKSIREIENEANNLNNKYN-EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1885 ETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKLRRGDFTGNVRRAIGRTGVES 1945
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPA 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1247-1485 |
3.41e-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: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1247 SENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQ----ALLE 1322
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEkeiaELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1323 EETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVL 1402
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1403 QQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAeekSISTKYAEERDRAEAEAREKETKS 1482
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA---RLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 319655760 1483 LTL 1485
Cdd:COG4942 255 LPW 257
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
936-1719 |
3.47e-07 |
|
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: 55.50 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 936 AQFQSEKKKMQQNIGDLEQQldeeEAARQKLQLEKVTMDAKLKK-IEEDLMVIEDQNAK--LSKEKKQMEERISEFTTNL 1012
Cdd:pfam05483 99 AELKQKENKLQENRKIIEAQ----RKAIQELQFENEKVSLKLEEeIQENKDLIKENNATrhLCNLLKETCARSAEKTKKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1013 AEEEEKSKSL-QKLKTKHETMITDLEDrlrkeekMRQELEKNRRKLEGDSTELHDQIAELQAqiaELRAQLAKKEEELQA 1091
Cdd:pfam05483 175 EYEREETRQVyMDLNNNIEKMILAFEE-------LRVQAENARLEMHFKLKEDHEKIQHLEE---EYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1092 ALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDStaaqqelrakret 1171
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST------------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1172 evtqlKKTLEDEARAHEQMLSEVRQKHNQAFEELNeqleqskrskasvdKAKQALESERNELQIELKSLSQSKNDSENRR 1251
Cdd:pfam05483 312 -----QKALEEDLQIATKTICQLTEEKEAQMEELN--------------KAKAAHSFVVTEFEATTCSLEELLRTEQQRL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1252 KKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESksikaakdcsaVESQLKDAQALLEEETRQKLAI 1331
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEK-----------LLDEKKQFEKIAEELKGKEQEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1332 STRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNAS 1411
Cdd:pfam05483 442 IFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1412 YDKLDKTKTRLQRELDDVLVDQGHLRQtvqELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKsltlarelea 1491
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRD---ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ---------- 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1492 MTDLKNELERVNKQLktemedlvsskDDAGKSVHELErakrgmeQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKA 1571
Cdd:pfam05483 589 MKILENKCNNLKKQI-----------ENKNKNIEELH-------QENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1572 QFERDLQSRDEQGEekrkqlVKQVREMEMELEDERKQRAQAVSVRKKLELDLselaaqidlankardEALKQLKKLQAQM 1651
Cdd:pfam05483 651 KFEEIIDNYQKEIE------DKKISEEKLLEEVEKAKAIADEAVKLQKEIDK---------------RCQHKIAEMVALM 709
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1652 KEQMREFEDLRLSRDESLNQAKENERKIKS----MEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNA 1719
Cdd:pfam05483 710 EKHKHQYDKIIEERDSELGLYKNKEQEQSSakaaLEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
862-1329 |
3.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKQKQLnaeklalqEQLQAETELCQEAEEMRSRLTARMQEMEEvlhelesrleeeeeRVAQFQSE 941
Cdd:COG4717 60 KPQGRKPELNLKELKELEEEL--------KEAEEKEEEYAELQEELEELEEELEELEA--------------ELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIgDLEQQLDEEEAARQKLQLEKV---TMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEE-EE 1017
Cdd:COG4717 118 LEKLEKLL-QLLPLYQELEALEAELAELPErleELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIE 1097
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1098 EEAALKNAA--------QKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKR 1169
Cdd:COG4717 277 GVLFLVLGLlallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1170 ETEVTQLKktLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSK----- 1244
Cdd:COG4717 357 EELEEELQ--LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleeel 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1245 NDSENRRKKAESQLQELQVKHTESERQKHELL--DKVSKMQAELESLQgtvTKVESKSIKAAKDCSAVESqLKDAQALLE 1322
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEedGELAELLQELEELK---AELRELAEEWAALKLALEL-LEEAREEYR 510
|
....*..
gi 319655760 1323 EETRQKL 1329
Cdd:COG4717 511 EERLPPV 517
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
858-1165 |
3.82e-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: 55.13 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQlNAEKLALQEQLQAEtelcQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQ 937
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDR-QAAIYAEQERMAME----RERELERIRQEERKRELERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 FQSEKKKMQQNIgdlEQQLdeEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEE 1017
Cdd:pfam17380 383 LQMERQQKNERV---RQEL--EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKtkhetmitdledrlrkeekmRQELEKNRRKLEGDSTElhdqiaELQAQIAELRAQLAkkEEELQAALARIE 1097
Cdd:pfam17380 458 RQQQVERLR--------------------QQEEERKRKKLELEKEK------RDRKRAEEQRRKIL--EKELEERKQAMI 509
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1098 EEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQEL 1165
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1443-1907 |
5.87e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1443 LERKQKKFDQMLAEEKSISTKyaEERDRAEAEAREKETKSLTLARELeaMTDLKNELERVNKQLKTEMEDLVSSKDDAGK 1522
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSE--LPELREELEKLEKEVKELEELKEE--IEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1523 SVHELE--RAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFE---------RDLQSRDEQGEEKRKQL 1591
Cdd:PRK03918 271 LKKEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieerikelEEKEERLEELKKKLKEL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1592 VKQVREME---MELEDERKQRAQAVSVRKKLE-LDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDE 1667
Cdd:PRK03918 351 EKRLEELEerhELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1668 sLNQAK-----------ENERK--IKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSS--DERRRLE 1732
Cdd:PRK03918 431 -LKKAKgkcpvcgreltEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1733 ARIAQLEEeleeehlsvelvnDRLKKASLQAEQVtveltaersnSQRLEGLRSQLDRQNKDMKqKLQELegavkskyKST 1812
Cdd:PRK03918 510 EKLKKYNL-------------EELEKKAEEYEKL----------KEKLIKLKGEIKSLKKELE-KLEEL--------KKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1813 ITALETKIQQLEEQLDSEMKE-RQQSTKQVRRVEKKLKEvLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAA 1891
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKElEELGFESVEELEERLKE-LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELA 636
|
490
....*....|....*.
gi 319655760 1892 RANASCRKLRRELEDA 1907
Cdd:PRK03918 637 ETEKRLEELRKELEEL 652
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1014-1219 |
6.20e-07 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 54.94 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1014 EEEEKSKSLQKLK-TKHETMITDLEDRLRKE--------EKMRQELEKNRRKLEgDSTELHDQIAELQAQIAELRAQLAK 1084
Cdd:PLN03188 1043 ESPEKKLEQERLRwTEAESKWISLAEELRTEldasralaEKQKHELDTEKRCAE-ELKEAMQMAMEGHARMLEQYADLEE 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1085 KEEELQAALARIEE----------EAALKNAAQKSIREMEAQISELqedleleKAARnkaEKQRRDLGEELEALKTELED 1154
Cdd:PLN03188 1122 KHIQLLARHRRIQEgiddvkkaaaRAGVRGAESKFINALAAEISAL-------KVER---EKERRYLRDENKSLQAQLRD 1191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1155 TLDSTAAQQEL--RAKRETE--VTQLKKTLEDEARAHE--QMLSEVRQKHNQAFEELNEQLEQSKRSKASV 1219
Cdd:PLN03188 1192 TAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEayKQIDKLKRKHENEISTLNQLVAESRLPKEAI 1262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
987-1201 |
6.43e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 987 IEDQNAKLSKEKKQMEERISEFTTNLAEEEEKsksLQKLKTKHETM------------ITDLEDRLRKEEKMRQELEKNR 1054
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNGLVdlseeaklllqqLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1055 RKLEGDSTELHDQIAELQA--QIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQI-SELQEDLELEKAAR 1131
Cdd:COG3206 243 AALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAEL 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1132 NKAEKQRRDLGEELEALKTELEDTldstaaqqelrAKRETEVTQlkktLEDEARAHEQMLSEVRQKHNQA 1201
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAEL-----------PELEAELRR----LEREVEVARELYESLLQRLEEA 377
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1035-1299 |
6.84e-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: 54.57 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRA-----------QLAKKEEELQAALARIEEEAALK 1103
Cdd:COG3096 833 DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladeTLADRLEELREELDAAQEAQAFI 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1104 NAAQKSIREMEAQISELQEDLELE---KAARNKAEKQRRDLGEELEALkTEL---------EDTLDSTAAQQELrakret 1171
Cdd:COG3096 913 QQHGKALAQLEPLVAVLQSDPEQFeqlQADYLQAKEQQRRLKQQIFAL-SEVvqrrphfsyEDAVGLLGENSDL------ 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1172 eVTQLKKTLEDEarahEQMLSEVRQKHNQAfeelNEQLEQSKRSKASVDKAKQALESERNELQIELKSLS-QSKNDSENR 1250
Cdd:COG3096 986 -NEKLRARLEQA----EEARREAREQLRQA----QAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGvQADAEAEER 1056
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 319655760 1251 rkkAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESK 1299
Cdd:COG3096 1057 ---ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERD 1102
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
981-1242 |
6.90e-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: 54.57 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 981 EEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKL--------KTKHETMITDLEDRLRKEEKMRQELEK 1052
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLlpqanllaDETLADRLEELREELDAAQEAQAFIQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1053 NRRKLEgdstELHDQIAELQ---AQIAELRAQLAKKEEELQAALARIEeeaALKNAAQKSIR-------EMEAQISELQE 1122
Cdd:COG3096 915 HGKALA----QLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIF---ALSEVVQRRPHfsyedavGLLGENSDLNE 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1123 DLeleKAARNKAEKQRRDLGEELEALKTELED------TLDST--AAQQELRA-KRETEVTQLKKTLEDEARAHEQMlse 1193
Cdd:COG3096 988 KL---RARLEQAEEARREAREQLRQAQAQYSQynqvlaSLKSSrdAKQQTLQElEQELEELGVQADAEAEERARIRR--- 1061
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 319655760 1194 vrqkhnqafEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQ 1242
Cdd:COG3096 1062 ---------DELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1069-1345 |
7.22e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.53 E-value: 7.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1069 AELQAQIAELraqlaKKEEELQAalarieEEAALKNAAQKSIrEMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:PRK11281 39 ADVQAQLDAL-----NKQKLLEA------EDKLVQQDLEQTL-ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1149 KTELEDTLD---STAAQQELRAKRETEVTQLKKTLEDEARAHEQMLS-EVRQKHNQAfeELNE---QLEQSKRSKASVDK 1221
Cdd:PRK11281 107 KDDNDEETRetlSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSlQTQPERAQA--ALYAnsqRLQQIRNLLKGGKV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1222 AKQAL-ESERNELQIELKSLSQSkndSENRRKKAE--SQLQELqvkhteSERQKHELLDKVSKMQAELESLQGTV-TKVE 1297
Cdd:PRK11281 185 GGKALrPSQRVLLQAEQALLNAQ---NDLQRKSLEgnTQLQDL------LQKQRDYLTARIQRLEHQLQLLQEAInSKRL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 319655760 1298 SKSIKAAKDC-SAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNL 1345
Cdd:PRK11281 256 TLSEKTVQEAqSQDEAARIQANPLVAQELEINLQLSQRLLKATEKLNTL 304
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1120-1343 |
7.30e-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: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1120 LQEDLELEKAArnkAEKQRRDLGEELEALKTELEdtldstAAQQELRA-KRETEVTQLkktlEDEARAHEQMLSEVRQKH 1198
Cdd:COG3206 162 LEQNLELRREE---ARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1199 NQA----------FEELNEQLEQSKRSKASV--DKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVK-H 1265
Cdd:COG3206 229 AEAraelaeaearLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1266 TESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAakdcSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQN 1343
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1133-1850 |
8.68e-07 |
|
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: 54.34 E-value: 8.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1133 KAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSE---VRQKHNQAFEELNEQL 1209
Cdd:pfam05483 89 KIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnaTRHLCNLLKETCARSA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1210 EQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQE--LQVKHTESERQKhelldKVSKMQAELE 1287
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEdhEKIQHLEEEYKK-----EINDKEKQVS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1288 SLQGTVTKVESKsikaAKDCSAVESQLKDAQALLEEETRQKlaiSTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQ 1367
Cdd:pfam05483 244 LLLIQITEKENK----MKDLTFLLEESRDKANQLEEKTKLQ---DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1368 AQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKT-KTRLQRELDDVLVDQGHLRQTVQELERK 1446
Cdd:pfam05483 317 EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1447 QKKFDQMLAEEKSISTKYAEERDRAEaEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHE 1526
Cdd:pfam05483 397 TKFKNNKEVELEELKKILAEDEKLLD-EKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1527 LErakrgMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDER 1606
Cdd:pfam05483 476 LK-----TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDEL 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1607 KqraqavSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRlsrdeslNQAKENERKIKSMEAEI 1686
Cdd:pfam05483 551 E------SVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLK-------KQIENKNKNIEELHQEN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1687 MQLHEDLAAADRAKRQIQQERDELQDEINSQNAK-NSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLK---KASLQ 1762
Cdd:pfam05483 618 KALKKKGSAENKQLNAYEIKVNKLELELASAKQKfEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKlqkEIDKR 697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1763 AEQVTVELTA-ERSNSQRLEGLRSQLDRQNKDMKQKLQElEGAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQV 1841
Cdd:pfam05483 698 CQHKIAEMVAlMEKHKHQYDKIIEERDSELGLYKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
....*....
gi 319655760 1842 RRVEKKLKE 1850
Cdd:pfam05483 777 KENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1249-1927 |
9.01e-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: 9.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1249 NRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTK-VESKSIKAAKDCSAVESQLKDAQALLEeetrq 1327
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELE----- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1328 klAISTRLRQLEDEQnnlkemleeeeeskknvEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEE 1407
Cdd:pfam12128 326 --ALEDQHGAFLDAD-----------------IETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1408 RNASYDKLDKTKTRLQRELDDVL--VDQGHLRQTVQEL-ERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKsLT 1484
Cdd:pfam12128 387 QNNRDIAGIKDKLAKIREARDRQlaVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELL-LQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1485 LARELEAMTDLKNELERVNKqlktEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTED---AKLR 1561
Cdd:pfam12128 466 LENFDERIERAREEQEAANA----EVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGtllHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1562 LEVNM--QALKAQFERDLQSRDEQGEEKRKQLVKQVREM-EMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARD 1638
Cdd:pfam12128 542 KEAPDweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLyGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1639 EALKQLKKLQAQMKEQMREFEDLRlsrdESLNQAKENERKIKS-MEAEIMQLHEDLAaadRAKRQIQQERDELQDEINSQ 1717
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFAR----TALKNARLDLRRLFDeKQSEKDKKNKALA---ERKDSANERLNSLEAQLKQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1718 NAKNSLSSDERRR--LEARIAQLEEELEEEHLSvelvndrlkkaSLQAEQVTVELTAERSnsqrleGLRSQLDRQNKDMK 1795
Cdd:pfam12128 695 DKKHQAWLEEQKEqkREARTEKQAYWQVVEGAL-----------DAQLALLKAAIAARRS------GAKAELKALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1796 QKLQEL--EGAVKSKYKSTITALETKIQQLE--EQLDSEMKERQQSTKQVRRveKKLKEVLLQVEDE-RRNADQSKTETE 1870
Cdd:pfam12128 758 RDLASLgvDPDVIAKLKREIRTLERKIERIAvrRQEVLRYFDWYQETWLQRR--PRLATQLSNIERAiSELQQQLARLIA 835
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1871 KANIRLKQMKRQLEETEEEAARANASCRKLRREL------------EDATESASAMNREVSTLKNKLRR 1927
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMsklatlkedansEQAQGSIGERLAQLEDLKLKRDY 904
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1566-1872 |
9.41e-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: 53.97 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1566 MQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEME----LEDERKQRAQAVSVRKKLELDLSELAAQID-----LANKA 1636
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVErrrkLEEAEKARQAEMDRQAAIYAEQERMAMERErelerIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1637 RDEALKQLKKLQAQMK-EQMREFEDLRLSR---DESLNQAKENERKIKSMEAEimqlhedlaaadRAKRQIQQERDELQD 1712
Cdd:pfam17380 358 RKRELERIRQEEIAMEiSRMRELERLQMERqqkNERVRQELEAARKVKILEEE------------RQRKIQQQKVEMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1713 EINSQNAKNslssDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQ-LDRQN 1791
Cdd:pfam17380 426 RAEQEEARQ----REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1792 KDMKQKLQE-------LEGAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKlKEVLLQVEDERRNADQ 1864
Cdd:pfam17380 502 EERKQAMIEeerkrklLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMMRQ 580
|
....*...
gi 319655760 1865 SKtETEKA 1872
Cdd:pfam17380 581 IV-ESEKA 587
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1063-1243 |
1.13e-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: 51.85 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1063 ELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRrdlg 1142
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1143 eELEALKTELEdtldstaaQQELRakretevtqlKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKA 1222
Cdd:COG1579 90 -EYEALQKEIE--------SLKRR----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|.
gi 319655760 1223 KQALESERNELQIELKSLSQS 1243
Cdd:COG1579 151 LAELEAELEELEAEREELAAK 171
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
858-1178 |
1.24e-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: 53.36 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEevlhelesrleeeeervaq 937
Cdd:pfam07888 89 LRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE------------------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 fqSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEE 1017
Cdd:pfam07888 150 --TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHD---QIAELQAQIAELRaqLAKKEEELQAAla 1094
Cdd:pfam07888 228 KEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADAS--LALREGRARWA-- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1095 riEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEdtlDSTAAQQELRA-----KR 1169
Cdd:pfam07888 304 --QERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS---ESRRELQELKAslrvaQK 378
|
....*....
gi 319655760 1170 ETEVTQLKK 1178
Cdd:pfam07888 379 EKEQLQAEK 387
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1038-1240 |
1.47e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1038 DRLRKEEKMRQELEKNRRKlegdstelhdqIAELQAQIAELRAqlakkEEELQAALARIEEEAAL---KNAAQKSIrEME 1114
Cdd:COG2268 220 NREAEEAELEQEREIETAR-----------IAEAEAELAKKKA-----EERREAETARAEAEAAYeiaEANAEREV-QRQ 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1115 AQISELQEDLELEKAARNKAEKQ-RRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLK----KTLEDEARAHE- 1188
Cdd:COG2268 283 LEIAEREREIELQEKEAEREEAElEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALaeawNKLGDAAILLMl 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1189 -QMLSEVRQKHNQAFEEL------NEQLEQSKRSKASVDKAKQALESERNELQIELKSL 1240
Cdd:COG2268 363 iEKLPEIAEAAAKPLEKIdkitiiDGGNGGNGAGSAVAEALAPLLESLLEETGLDLPGL 421
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
978-1444 |
1.51e-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: 53.21 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 978 KKIEEDLMVIEDQNAKLSKEKKQMEERI------SEFTTNLAEEEEKSKSLQKlktkhetMITDLEDRL-RKEEKMRQEL 1050
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIelekkaSALKRQLDRESDRNQELQK-------RIRLLEKREaEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1051 EKNRRKLEGDST-------------ELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQI 1117
Cdd:pfam05557 76 ELNRLKKKYLEAlnkklnekesqlaDAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1118 SELQEDLELEKAARNKAE------KQRRDLGEELEALKTELED--TLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQ 1189
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKelefeiQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1190 MLSEVRQKHNQA--FEELNEQLEQSKRSKASVDKAK-------QALESERNELQIELKSLSQSKNDSENRRKKAESQLQE 1260
Cdd:pfam05557 236 KLEREEKYREEAatLELEKEKLEQELQSWVKLAQDTglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1261 LQVKhteserqKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQA-LLEEETRQKLaiSTRLRQLE 1339
Cdd:pfam05557 316 LEQE-------LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKeLTMSNYSPQL--LERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1340 DEQNNLkemleeeeeskknvekqlhtaQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTK 1419
Cdd:pfam05557 387 DMTQKM---------------------QAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDS 445
|
490 500
....*....|....*....|....*
gi 319655760 1420 trLQRELDDVLVDQGHLRQTVQELE 1444
Cdd:pfam05557 446 --LRRKLETLELERQRLREQKNELE 468
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1002-1720 |
1.51e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1002 EERISEFTTNLAEEEEKSKSLqklktkhETMITDLEDRL----------RKEEKMRQELEKNRRKLEGD---STELHDQI 1068
Cdd:PRK04863 306 QYRLVEMARELAELNEAESDL-------EQDYQAASDHLnlvqtalrqqEKIERYQADLEELEERLEEQnevVEEADEQQ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1069 AELQAQ-------IAELRAQLAKKEEEL----------QAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAAR 1131
Cdd:PRK04863 379 EENEARaeaaeeeVDELKSQLADYQQALdvqqtraiqyQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1132 NKAEKQRRDLGEELEA------LKTELEDTLDSTAAQQELRAKRETEVTQlkKTLEDEARAHEQMLSEVRQKHNQAfEEL 1205
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQfeqayqLVRKIAGEVSRSEAWDVARELLRRLREQ--RHLAEQLQQLRMRLSELEQRLRQQ-QRA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1206 NEQLEQ-SKRSKASVDKAKQaLESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLdkvskmqa 1284
Cdd:PRK04863 536 ERLLAEfCKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL-------- 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1285 eleSLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQ-- 1362
Cdd:PRK04863 607 ---AAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERfg 683
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1363 ----------------------------------LHTAQAQLAEMKK------KIEQEAQSLEsmeDGKKKLQREVESVL 1402
Cdd:PRK04863 684 gvllseiyddvsledapyfsalygparhaivvpdLSDAAEQLAGLEDcpedlyLIEGDPDSFD---DSVFSVEELEKAVV 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1403 QQLEERNASYDKL-----------DKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSIS---------T 1462
Cdd:PRK04863 761 VKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeaelR 840
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1463 KYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKT-EMEDLVSSKDDAGKSVHELERAKRGMEQQ---L 1538
Cdd:PRK04863 841 QLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLlADETLADRVEEIREQLDEAEEAKRFVQQHgnaL 920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1539 EEMKtqleeledelqltedaklRLEVNMQALKAQFERdLQSRDEQGEEKRKQLVKQVREmemeLEDERKQRA-----QAV 1613
Cdd:PRK04863 921 AQLE------------------PIVSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFA----LTEVVQRRAhfsyeDAA 977
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1614 SVRKKlELDLSE-LAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSM------EAEI 1686
Cdd:PRK04863 978 EMLAK-NSDLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsGAEE 1056
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 319655760 1687 M------QLHEDLAAADRAKRQIQQERDELQDEINSQNAK 1720
Cdd:PRK04863 1057 RararrdELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1224-1713 |
1.55e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1224 QALESERNELqieLKSLSQSKNDSENRRKKAESQLQELQvkhtESERQKHELLDKVSKMQAELESLQGTVTKVESK--SI 1301
Cdd:COG4717 49 ERLEKEADEL---FKPQGRKPELNLKELKELEEELKEAE----EKEEEYAELQEELEELEEELEELEAELEELREEleKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1302 KAAKDCSAVESQLKDAQALLEEETRqklaistRLRQLEDEQnnlkemleeeeeskknveKQLHTAQAQLAEMKKKIEQEA 1381
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPE-------RLEELEERL------------------EELRELEEELEELEAELAELQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1382 QSLEsmedgkKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFD--QMLAEEKS 1459
Cdd:COG4717 177 EELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAleERLKEARL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1460 IST------------------------------------KYAEERDRAEAEAREKETKSLTLARELEAMtdlknELERVN 1503
Cdd:COG4717 251 LLLiaaallallglggsllsliltiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEE-----ELEELL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1504 KQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKtqleeledelqlTEDAKLRLEVNMQALKAQFERDLQSRDEQ 1583
Cdd:COG4717 326 AALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ------------LEELEQEIAALLAEAGVEDEEELRAALEQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1584 GEEkRKQLVKQVREMEMELEDERKQRAQAVSVRKK--LELDLSELAAQIDLANKARDEALKQLKKLQAQMKEqmrefedl 1661
Cdd:COG4717 394 AEE-YQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQ-------- 464
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1662 rLSRDESLNQAKEnerKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDE 1713
Cdd:COG4717 465 -LEEDGELAELLQ---ELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1370-1924 |
1.91e-06 |
|
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: 53.19 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1370 LAEMKKKIEQEAqslESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKK 1449
Cdd:pfam05483 76 LSRLYSKLYKEA---EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1450 FDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEdlVSSKDDAGKSVHELER 1529
Cdd:pfam05483 153 TRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1530 AKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKaqferDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQR 1609
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN-----QLEEKTKLQDENLKELIEKKDHLTKELEDIKMSL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1610 AQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKE----NERKIKSMEAE 1685
Cdd:pfam05483 306 QRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNEDQLKIITME 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1686 IMQLHEDLAAADRAKRQIQQERDELQDEInsqnAKNSLSSDERRRLEaRIAQleEELEEEHLSVELVNDRLKKASLQAEQ 1765
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVELEELKKIL----AEDEKLLDEKKQFE-KIAE--ELKGKEQELIFLLQAREKEIHDLEIQ 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1766 VTVELTAERSNSQRLEGLRSQLDRQ---NKDMKQKLQELEGAVKSKYKSTiTALETKIQQLEEQLDSEMKERQQSTKQVR 1842
Cdd:pfam05483 459 LTAIKTSEEHYLKEVEDLKTELEKEklkNIELTAHCDKLLLENKELTQEA-SDMTLELKKHQEDIINCKKQEERMLKQIE 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1843 RVEKK---LKEVLLQVEDE-RRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASAMNREV 1918
Cdd:pfam05483 538 NLEEKemnLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN 617
|
....*.
gi 319655760 1919 STLKNK 1924
Cdd:pfam05483 618 KALKKK 623
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
867-1132 |
1.97e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 867 QAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEvlhelesrleeeeeRVAQFQSEKKKMQ 946
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA--------------EIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 947 QNIGDLEQQLDEEEAARQKLQLEKVTMDAklkkieedLMVIEDQNAKLSKEkkQMEERISEFTTNLAEEeeksksLQKLK 1026
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDV--------LLGSESFSDFLDRL--SALSKIADADADLLEE------LKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1027 TKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAA 1106
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
250 260
....*....|....*....|....*.
gi 319655760 1107 QKSIREMEAQISELQEDLELEKAARN 1132
Cdd:COG3883 223 AAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
998-1133 |
2.85e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 51.51 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 998 KKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLrkeekmrQELEKNRRKLEGDSTELHDQIAELQAQIAE 1077
Cdd:PRK09039 76 NQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSARALAQVELLNQQIAA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1078 LRAQLAKkeeeLQAALarieeeaalkNAAQKSIREMEAQISELQEDLELEKAARNK 1133
Cdd:PRK09039 149 LRRQLAA----LEAAL----------DASEKRDRESQAKIADLGRRLNVALAQRVQ 190
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1604-1927 |
2.97e-06 |
|
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: 52.76 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1604 DERKQRAQAvsvrkklelDLSELAAQIDLANKARDEALKQLKKLQAQmKEQMREFEDLRLSRDESlnQAKENERKIKSME 1683
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRRE-REKAERYQALLKEKREY--EGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1684 AEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNaknslssDERRRLEARIaqleeeleeehlsvelvndrlkKASLQA 1763
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIE-------QLLEELNKKI----------------------KDLGEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1764 EQVTVELTAERsnsqrLEGLRSQLDRQNKDMKQKLQELEGAVKsKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRR 1843
Cdd:TIGR02169 288 EQLRVKEKIGE-----LEAEIASLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1844 VEKKLKEVLLQVEDERRNADQSKTETekanirlkqmkrqleeteeeaaranascRKLRRELEDATESASAMNREVSTLKN 1923
Cdd:TIGR02169 362 LKEELEDLRAELEEVDKEFAETRDEL----------------------------KDYREKLEKLKREINELKRELDRLQE 413
|
....
gi 319655760 1924 KLRR 1927
Cdd:TIGR02169 414 ELQR 417
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1035-1344 |
2.98e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.46 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 DLEDRLR-KEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKnaaqksiREM 1113
Cdd:pfam00038 29 LLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLR-------TSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1114 EAQISELQEDLELEKAARNKAEKQRRDLGEELEALKT-------ELEDTLDSTAAQQELRAKRETEVTQlkkTLEDEARA 1186
Cdd:pfam00038 102 ENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKnheeevrELQAQVSDTQVNVEMDAARKLDLTS---ALAEIRAQ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 HEQMLSEVRQkhnQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLsqskndsenrrkkaESQLQELQVKHT 1266
Cdd:pfam00038 179 YEEIAAKNRE---EAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSL--------------EIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1267 ESERQKHELLDkvsKMQAELESLQGTVTKVESKSIKAAKDcsaVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNN 1344
Cdd:pfam00038 242 SLERQLAETEE---RYELQLADYQELISELEAELQETRQE---MARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
869-1139 |
3.01e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 869 EDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQN 948
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 949 IGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMviEDQNAKLSKEK-KQMEERISEfttnLAEEEEKSKSLQKLKT 1027
Cdd:COG1340 87 LNELREELDELRKELAELNKAGGSIDKLRKEIERLEW--RQQTEVLSPEEeKELVEKIKE----LEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1028 KhetmITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQ 1107
Cdd:COG1340 161 K----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|..
gi 319655760 1108 KSIREMEAQISELQEDLELEKAARNKAEKQRR 1139
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1030-1170 |
3.11e-06 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 51.77 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1030 ETMITDLEDRLRkEEKMR---QELEKNRRKLEGDSTELHD------------QIAELQAQIAELRAQLAKKEEELQAALA 1094
Cdd:COG3524 164 EELVNQLSERAR-EDAVRfaeEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRS 242
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1095 RIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQrrdlgEELEALKTEL---EDTLDSTAAQQElRAKRE 1170
Cdd:COG3524 243 YLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSLASLL-----AEYERLELERefaEKAYTSALAALE-QARIE 315
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
974-1408 |
3.28e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 974 DAKLKKIEEDLMVIEDQNAK--LSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHEtmitdledRLRKE-EKMRQEL 1050
Cdd:PRK04778 78 TNSLPDIEEQLFEAEELNDKfrFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEE--------KNREEvEQLKDLY 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1051 EKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEE------LQAA--LARIEEEAalkNAAQKSIREMEAQISELQE 1122
Cdd:PRK04778 150 RELRKSLLANRFSFGPALDELEKQLENLEEEFSQFVELtesgdyVEAReiLDQLEEEL---AALEQIMEEIPELLKELQT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1123 DL-----ELEKAAR-----------NKAEKQRRDLGEELEALKTELEDtLDSTAAQQELRaKRETEVTQLKKTLEDEARA 1186
Cdd:PRK04778 227 ELpdqlqELKAGYRelveegyhldhLDIEKEIQDLKEQIDENLALLEE-LDLDEAEEKNE-EIQERIDQLYDILEREVKA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 heqmlsevRQKHNQAFEELNEQLEQSKRSKasvdkakqaleserNELQIELKSLSQSkndsenrrkkaesqlqeLQVKHT 1266
Cdd:PRK04778 305 --------RKYVEKNSDTLPDFLEHAKEQN--------------KELKEEIDRVKQS-----------------YTLNES 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1267 ESERQKhelldkvsKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNlk 1346
Cdd:PRK04778 346 ELESVR--------QLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELE-- 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1347 emleeeeeskknvekqlhtAQAQLAEMKKKIEQ-----EAQSL----ESMEDGKKKLQREVESVLQQLEER 1408
Cdd:PRK04778 416 -------------------AREKLERYRNKLHEikrylEKSNLpglpEDYLEMFFEVSDEIEALAEELEEK 467
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
935-1099 |
3.34e-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: 50.31 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 935 VAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMviedqNAKLSKEKKQMEERISefttnlae 1014
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-----NVRNNKEYEALQKEIE-------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1015 eeekskSLQKLKTKHETMITDLEDRLrkeEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALA 1094
Cdd:COG1579 100 ------SLKRRISDLEDEILELMERI---EELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
....*
gi 319655760 1095 RIEEE 1099
Cdd:COG1579 171 KIPPE 175
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
862-1262 |
3.53e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQ-LKESEAKQKQLNAEKLALQEQLQA---------ETELCQEAEEMRS----RLTARMQEMEEVLHELESR 927
Cdd:PRK04863 298 SRRQLAAEQYrLVEMARELAELNEAESDLEQDYQAasdhlnlvqTALRQQEKIERYQadleELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 928 LEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEE----AARQKLQLekvtmdakLKKIEE--DLMVIEDQNAklskekkqm 1001
Cdd:PRK04863 378 QEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiQYQQAVQA--------LERAKQlcGLPDLTADNA--------- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1002 EERISEFTtnlAEEEEKSKSLQKLKTKhetmITDLEDRLRKEEKMRQELeknrRKLEG--DSTELHDQIAELQAQIAELR 1079
Cdd:PRK04863 441 EDWLEEFQ---AKEQEATEELLSLEQK----LSVAQAAHSQFEQAYQLV----RKIAGevSRSEAWDVARELLRRLREQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1080 AQlAKKEEELQAALARIEEEAALKNAAQKSIREMEaQISELQEDLElekaarnkaekqrrdlgEELEALKTELEDTLDST 1159
Cdd:PRK04863 510 HL-AEQLQQLRMRLSELEQRLRQQQRAERLLAEFC-KRLGKNLDDE-----------------DELEQLQEELEARLESL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1160 AAQQELRAKRETEVTQLKKTLEDEARAHEQmLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQalesernELQIELKS 1239
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAA-RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQ-------QLLERERE 642
|
410 420
....*....|....*....|...
gi 319655760 1240 LSQSKNDSENRRKKAESQLQELQ 1262
Cdd:PRK04863 643 LTVERDELAARKQALDEEIERLS 665
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
869-1881 |
3.69e-06 |
|
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: 52.36 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 869 EDQLKESEAKQKQLNA-EKLALQEQLQAETELcQEAEEMRSRLTARMQEMEEVLHELESRLEEEEerVAQFQSEKKKMQQ 947
Cdd:TIGR01612 693 EDKAKLDDLKSKIDKEyDKIQNMETATVELHL-SNIENKKNELLDIIVEIKKHIHGEINKDLNKI--LEDFKNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 948 NIGDLEQQLDEEEAARQKLqlekvtmdAKLKKIEEDLMVIEdqNAKlSKEKKQMEERISEFTTNLA-EEEEKSKSLQKLK 1026
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKI--------SEIKNHYNDQINID--NIK-DEDAKQNYDKSKEYIKTISiKEDEIFKIINEMK 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1027 TKHETMITDLEDRLRKEEKMRQELEKNrrklegdstelHDQIAELQAQIaelRAQLAkkEEELQAALARIEEEAALKNAA 1106
Cdd:TIGR01612 839 FMKDDFLNKVDKFINFENNCKEKIDSE-----------HEQFAELTNKI---KAEIS--DDKLNDYEKKFNDSKSLINEI 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1107 QKSIREMEAQISELQEDLELEKAARNKAE--KQRRDLGEEL-EALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDE 1183
Cdd:TIGR01612 903 NKSIEEEYQNINTLKKVDEYIKICENTKEsiEKFHNKQNILkEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1184 ARahEQMLSEVRQKHN---QAFEELNEQLEQSK----------RSKASVDKAKQALESERNELQIELKSLSQSKNDSENR 1250
Cdd:TIGR01612 983 FK--DASLNDYEAKNNeliKYFNDLKANLGKNKenmlyhqfdeKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEI 1060
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1251 RKKAESQLQELqvkHTESERQKHELLDKVSKMQAELEsLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLE------EE 1324
Cdd:TIGR01612 1061 EKEIGKNIELL---NKEILEEAEINITNFNEIKEKLK-HYNFDDFGKEENIKYADEINKIKDDIKNLDQKIDhhikalEE 1136
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1325 TRQKLA-----ISTRLRQLEDEQNNLKEMLEEEEESKKNVE--KQLHTAQAQLAEMKK------KIEQEAQSLESMEDGK 1391
Cdd:TIGR01612 1137 IKKKSEnyideIKAQINDLEDVADKAISNDDPEEIEKKIENivTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVKGIN 1216
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1392 KKLQREVESV-LQQLEERNASYDKLDKTKTRLQRELDDVlVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKY---AEE 1467
Cdd:TIGR01612 1217 LSYGKNLGKLfLEKIDEEKKKSEHMIKAMEAYIEDLDEI-KEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhiiSKK 1295
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1468 RDRAEAEAREKETKSLTLARELEAMTDLKNELER--VNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQL 1545
Cdd:TIGR01612 1296 HDENISDIREKSLKIIEDFSEESDINDIKKELQKnlLDAQKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEYTKEIE 1375
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1546 EELEDELQLTEDA-----KLRLEVNMQALKAQFERDLQSRDEQGeekrkqLVKQVREMEMELEDERKQRAQAVSVRKKLE 1620
Cdd:TIGR01612 1376 ENNKNIKDELDKSeklikKIKDDINLEECKSKIESTLDDKDIDE------CIKKIKELKNHILSEESNIDTYFKNADENN 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1621 LDLSELAAQIDLANKardealkqlkKLQAQMKEQMREFEDlrlSRDESLNQAKENERKIKSMEAEimqlhedlaaADRAK 1700
Cdd:TIGR01612 1450 ENVLLLFKNIEMADN----------KSQHILKIKKDNATN---DHDFNINELKEHIDKSKGCKDE----------ADKNA 1506
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1701 RQIqqERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSvelVNDRLKKASLQAEQVTVELTAERSNSQRL 1780
Cdd:TIGR01612 1507 KAI--EKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKE---IKDAHKKFILEAEKSEQKIKEIKKEKFRI 1581
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1781 EGLRSQLDRQNK---DMKQKLQELEGA------VKSKYKSTIT---ALETKIQQLE-EQLDSEMKERQQSTKQVRRVEKK 1847
Cdd:TIGR01612 1582 EDDAAKNDKSNKaaiDIQLSLENFENKflkisdIKKKINDCLKeteSIEKKISSFSiDSQDTELKENGDNLNSLQEFLES 1661
|
1050 1060 1070
....*....|....*....|....*....|....
gi 319655760 1848 LKEVLLQVEDERRNADQSKTETEKANIRLKQMKR 1881
Cdd:TIGR01612 1662 LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKK 1695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1014-1225 |
4.71e-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: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1014 EEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEgdstELHDQIAELQAQIAELRAQLAKKEEELQAAL 1093
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1094 ARIEEE----------------------AALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTE 1151
Cdd:COG3883 93 RALYRSggsvsyldvllgsesfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1152 LEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQA 1225
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
889-1116 |
4.88e-06 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 51.23 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 889 LQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEA--ARQkl 966
Cdd:PRK11637 52 IQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQERllAAQ-- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 967 qlekvtMDAKLKKIEED-LMVIedqnakLSKEKKQMEERISEFTTNLAEEEEKS---------------KSLQKLKTKHE 1030
Cdd:PRK11637 130 ------LDAAFRQGEHTgLQLI------LSGEESQRGERILAYFGYLNQARQETiaelkqtreelaaqkAELEEKQSQQK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1031 TMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEElqaALARIEEEAalKNAAQKSI 1110
Cdd:PRK11637 198 TLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAERE---AKARAEREA--REAARVRD 272
|
....*.
gi 319655760 1111 REMEAQ 1116
Cdd:PRK11637 273 KQKQAK 278
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1173-1434 |
4.94e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 51.55 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1173 VTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSkrskasVDKAKQaLESERNELQIELKSLSQSKNDSENRRK 1252
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDEL------VEEAKT-IKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1253 KaesqlqelqvkhteserqkheLLDKVSKMQAELESLQGtvtkvESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAIS 1332
Cdd:PHA02562 259 K---------------------LNTAAAKIKSKIEQFQK-----VIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1333 TRLRQLEDEQNNLKEMLEeeeeskknvekQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQ-------L 1405
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMD-----------EFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnaeeL 381
|
250 260 270
....*....|....*....|....*....|....*
gi 319655760 1406 EERNASYDKLDKTKTRLQRELD------DVLVDQG 1434
Cdd:PHA02562 382 AKLQDELDKIVKTKSELVKEKYhrgivtDLLKDSG 416
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1060-1182 |
5.04e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 50.82 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRAQLAK------KEEELQAALARIEE-EAALKNAAQ--KSIREMEAQ--ISelQEDLELEK 1128
Cdd:COG1566 77 DPTDLQAALAQAEAQLAAAEAQLARleaelgAEAEIAAAEAQLAAaQAQLDLAQRelERYQALYKKgaVS--QQELDEAR 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1129 AARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKREtEVTQLKKTLED 1182
Cdd:COG1566 155 AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEA-ALAQAELNLAR 207
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1015-1150 |
5.07e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.40 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1015 EEEKSKSLQKLKTKHETMITDLEdrlRKEEKMRQELEKNRRKLEgdstELHDQIAELQAQIAELRAQLAKKEEELqaALA 1094
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEE---RELTEEEEEIRRLEEQVE----RLEAEVEELEAELEEKDERIERLEREL--SEA 453
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1095 RIEEEAALKnaAQKSIREMEAQISELQEDLElekaarnKAEKQRRDLGEELEALKT 1150
Cdd:COG2433 454 RSEERREIR--KDREISRLDREIERLERELE-------EERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1471-1699 |
5.57e-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: 50.92 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1471 AEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELED 1550
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1551 ELQLTEDAKLRLEVNMQALKAQFERD--LQSRDEQGEEKRKQLVKQV-REMEMELEDERKQRAQAVSVRKKLELDLSELA 1627
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAllLSPEDFLDAVRRLQYLKYLaPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1628 AQidlankaRDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRA 1699
Cdd:COG4942 178 AL-------LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1048-1261 |
5.68e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 51.23 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1048 QELEKNRRKLEGDSTELHDQIAELQAQIAEL-RAQLAKKE-EELQAALARIEEEAALKNAAQKSIREM-------EAQIS 1118
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLEELeAAALQPGEeEELEEERRRLSNAEKLREALQEALEALsggeggaLDLLG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1119 ELQEdlELEKAARnkAEKQRRDLGEELEALKTELEDtldstaAQQELRAKRET---------EVTQLKKTLEDEARAHEQ 1189
Cdd:COG0497 248 QALR--ALERLAE--YDPSLAELAERLESALIELEE------AASELRRYLDSlefdperleEVEERLALLRRLARKYGV 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1190 MLSEVRQKHNQAFEELnEQLEQSkrskasvDKAKQALESERNELQIELKSLSQSKndSENRRKKA-------ESQLQEL 1261
Cdd:COG0497 318 TVEELLAYAEELRAEL-AELENS-------DERLEELEAELAEAEAELLEAAEKL--SAARKKAAkklekavTAELADL 386
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1335-1739 |
9.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1335 LRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLE--ERNASY 1412
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1413 DKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETkslTLARELEAM 1492
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---DLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1493 TDLKNELERVNKQLKTEMEDLVSSKDDAgksvhELERAKRGMEQQLEEMKTQ------------LEELEDELQLTEDAKL 1560
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQL-----ENELEAAALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1561 RLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEA 1640
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1641 LKQLKkLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQI--QQERDELQDEINSQN 1718
Cdd:COG4717 360 EEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELleALDEEELEEELEELE 438
|
410 420
....*....|....*....|.
gi 319655760 1719 AKNSLSSDERRRLEARIAQLE 1739
Cdd:COG4717 439 EELEELEEELEELREELAELE 459
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1624-1878 |
9.97e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.68 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1624 SELAAQIDLANKARDeaLKQLKKLQAQMKEQMREFEDlrlsrdeslnqakenerKIKSMEAEIMQLHEDLAAADRAKRQI 1703
Cdd:PRK11281 39 ADVQAQLDALNKQKL--LEAEDKLVQQDLEQTLALLD-----------------KIDRQKEETEQLKQQLAQAPAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1704 QQERDELQDEINSQnAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAersNSQRLEGL 1783
Cdd:PRK11281 100 QAELEALKDDNDEE-TRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYA---NSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1784 RSQL------------DRQNK----------DMKQKLQELEGAvkskykSTITALETK--------IQQLEEQLD----- 1828
Cdd:PRK11281 176 RNLLkggkvggkalrpSQRVLlqaeqallnaQNDLQRKSLEGN------TQLQDLLQKqrdyltarIQRLEHQLQllqea 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1829 -SEmKERQQSTKQVRRVEKKLKEV------LLQVEDErRNADQSK---TETEKAN------IRLKQ 1878
Cdd:PRK11281 250 iNS-KRLTLSEKTVQEAQSQDEAAriqanpLVAQELE-INLQLSQrllKATEKLNtltqqnLRVKN 313
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1208-1412 |
1.17e-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: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1208 QLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELE 1287
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1288 SLQGTVTKVE----SKSIKAAKD-CSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQ 1362
Cdd:COG3883 97 RSGGSVSYLDvllgSESFSDFLDrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 319655760 1363 LHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASY 1412
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1056-1210 |
1.22e-05 |
|
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: 47.64 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1056 KLEGDSTELHDQIAELQAQIA----ELRAQLAKKEEELQAAL--------ARIEEEAA-LKNAAQKSIREMEAQISELQE 1122
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGpvaqELVDRLEKETEALRERLqkdleevrAKLEPYLEeLQAKLGQNVEELRQRLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1123 dlELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQ-----QELRAKRETEVTQLKKTLEDEARAHE----QMLSE 1193
Cdd:pfam01442 81 --ELRKRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQaqlsQRLQE 158
|
170
....*....|....*..
gi 319655760 1194 VRQKHNQAFEELNEQLE 1210
Cdd:pfam01442 159 LREKLEPQAEDLREKLD 175
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1060-1287 |
1.30e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEeeaALKNAAQK---------SIREMEAQISELQEDLelekaa 1130
Cdd:PRK11281 67 QTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELE---ALKDDNDEetretlstlSLRQLESRLAQTLDQL------ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1131 rNKAEKQRRDLGEELEALKTELEDtldstaAQQELRA--KRETEVTQLKKTLEDEARAheqMLSEVRQKHNQAFEELNEQ 1208
Cdd:PRK11281 138 -QNAQNDLAEYNSQLVSLQTQPER------AQAALYAnsQRLQQIRNLLKGGKVGGKA---LRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1209 LEQSKRSKASVDKAKQALESERNELQIELKSLSQSKND-----SENRRKKAESQLQELQVKHTESERQKHELLdkvskmQ 1283
Cdd:PRK11281 208 NDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLlqeaiNSKRLTLSEKTVQEAQSQDEAARIQANPLV------A 281
|
....
gi 319655760 1284 AELE 1287
Cdd:PRK11281 282 QELE 285
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
888-1129 |
1.31e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.07 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 888 ALQEQLQAETELCQEAEEMRSRLTARMQEMEEVlhelesrlEEEEERVAQFQSEKKKMQ------QNIGDLEQQLDEEE- 960
Cdd:COG0497 169 ALKKELEELRADEAERARELDLLRFQLEELEAA--------ALQPGEEEELEEERRRLSnaeklrEALQEALEALSGGEg 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 961 -------AARQKLQlEKVTMDAKLKKIEEDL----MVIEDQNAKLSKEKKQME---ERisefttnLAEEEEKSKSLQKLK 1026
Cdd:COG0497 241 galdllgQALRALE-RLAEYDPSLAELAERLesalIELEEAASELRRYLDSLEfdpER-------LEEVEERLALLRRLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1027 TKHETMITDLedrLRKEEKMRQELEKnrrkLEGDStelhDQIAELQAQIAELRAQLAKKEEELQAalARieeeaalknaa 1106
Cdd:COG0497 313 RKYGVTVEEL---LAYAEELRAELAE----LENSD----ERLEELEAELAEAEAELLEAAEKLSA--AR----------- 368
|
250 260
....*....|....*....|...
gi 319655760 1107 QKSIREMEAQISELQEDLELEKA 1129
Cdd:COG0497 369 KKAAKKLEKAVTAELADLGMPNA 391
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1188-1407 |
1.31e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1188 EQMLSEVRQKHNQAFEELNEQLEQSKrskASVDKAKQALESERNELQIelkslsqskNDSENRRKKAESQLQELQVKHTE 1267
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELR---KELEEAEAALEEFRQKNGL---------VDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1268 SERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAkdcsaVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKE 1347
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ-----LRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1348 M-LEEEEESKKNVEKQLHTAQAQLAEMKKKIEQ---EAQSLESMEDGKKKLQREVE-------SVLQQLEE 1407
Cdd:COG3206 306 QlQQEAQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVEvarelyeSLLQRLEE 376
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
939-1116 |
1.38e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAarqKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEErISEFTTNLAEEEEK 1018
Cdd:PRK01156 586 RSRSNEIKKQLNDLESRLQEIEI---GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEK-LRGKIDNYKKQIAE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKeEELQAALARIEE 1098
Cdd:PRK01156 662 IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESM-KKIKKAIGDLKR 740
|
170 180
....*....|....*....|
gi 319655760 1099 --EAALKNAAQKSIREMEAQ 1116
Cdd:PRK01156 741 lrEAFDKSGVPAMIRKSASQ 760
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
951-1248 |
1.51e-05 |
|
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: 50.14 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 951 DLEQQLDEEEAARQK-----LQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKL 1025
Cdd:pfam09731 165 SLKEASDTAEISREKatdsaLQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1026 KTK-HETMITDLEDRLRKEEKMRQELEKNRRKLEGDS-TELHDQIAELQAQIAELRAQLA--KKEEELQAALARIEEEAA 1101
Cdd:pfam09731 245 VDQyKELVASERIVFQQELVSIFPDIIPVLKEDNLLSnDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1102 LKNAAQKSIREMEAQIS--ELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEvTQLKKT 1179
Cdd:pfam09731 325 LDKLAEELSARLEEVRAadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEK 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1180 LEDEARAH----EQMLSEVRQKHnQAFEELNEQLEQSKRSKA---SVDKAKQALE-----SERNELQIELKSLSQSKNDS 1247
Cdd:pfam09731 404 VEEERAGRllklNELLANLKGLE-KATSSHSEVEDENRKAQQlwlAVEALRSTLEdgsadSRPRPLVRELKALKELASDD 482
|
.
gi 319655760 1248 E 1248
Cdd:pfam09731 483 E 483
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
877-1182 |
1.77e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.91 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 877 AKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEmeevlhelesrleeeeerVAQFQSEKKKMQQNIGDLEQQL 956
Cdd:PRK11281 49 NKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQ------------------LAQAPAKLRQAQAELEALKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 957 DEEEAAR-QKLQLEkvTMDAKLKKIEEDLMVIEDQ----NAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHET 1031
Cdd:PRK11281 111 DEETRETlSTLSLR--QLESRLAQTLDQLQNAQNDlaeyNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1032 MITDLEDRLRKEEKM-RQELEKNRRKLEGdSTELHDQiaeLQAQIAELRAQLAKKEEELQaalarieeeaALKNA-AQKS 1109
Cdd:PRK11281 189 LRPSQRVLLQAEQALlNAQNDLQRKSLEG-NTQLQDL---LQKQRDYLTARIQRLEHQLQ----------LLQEAiNSKR 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1110 IREMEAQISELQEDLELEKAARN---KAEKQR-RDLGEELeaLK-TELEDTLdstaAQQELRAKRETE-VTQLKKTLED 1182
Cdd:PRK11281 255 LTLSEKTVQEAQSQDEAARIQANplvAQELEInLQLSQRL--LKaTEKLNTL----TQQNLRVKNWLDrLTQSERNIKE 327
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1674-1907 |
1.85e-05 |
|
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: 50.07 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1674 ENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSD------------------ERRRLEARI 1735
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEkreyegyellkekealerQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1736 AQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQR--------LEGLRSQLDRQNKDMKQKLQELEGAVKs 1807
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLrvkekigeLEAEIASLERSIAEKERELEDAEERLA- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1808 KYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETE 1887
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260
....*....|....*....|
gi 319655760 1888 EEAARANASCRKLRRELEDA 1907
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADL 425
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1501 |
1.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 866 QQAEDQLKESEAKQKQLNAEKLALQEQL----QAETELCQEAEEMRSRLTArMQEMEEVLHELESRLEEEEERVAQFQSE 941
Cdd:PRK04863 372 EEADEQQEENEARAEAAEEEVDELKSQLadyqQALDVQQTRAIQYQQAVQA-LERAKQLCGLPDLTADNAEDWLEEFQAK 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEAARQklQLEKVTmdAKLKKIEEDLMVIEDQNAKLSKEKK------------QMEERISEFT 1009
Cdd:PRK04863 451 EQEATEELLSLEQKLSVAQAAHS--QFEQAY--QLVRKIAGEVSRSEAWDVARELLRRlreqrhlaeqlqQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1010 TNLAEEEEKSKSLQKLKTKHETMITD---LEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQlAKKE 1086
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDedeLEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAAR-APAW 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1087 EELQAALARIEEE--AALKNAAQ-----------------------KSIREMEAQI------------------------ 1117
Cdd:PRK04863 606 LAAQDALARLREQsgEEFEDSQDvteymqqllerereltverdelaARKQALDEEIerlsqpggsedprlnalaerfggv 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1118 --SELQEDLELEKAARNKAEKQR-------RDLG---EELEALKTELEDTL----------DSTAAQQEL---------- 1165
Cdd:PRK04863 686 llSEIYDDVSLEDAPYFSALYGParhaivvPDLSdaaEQLAGLEDCPEDLYliegdpdsfdDSVFSVEELekavvvkiad 765
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1166 ---------------RAKRETEVTQLKKTLEDEARAH---------------------------------EQMLSEVRQK 1197
Cdd:PRK04863 766 rqwrysrfpevplfgRAAREKRIEQLRAEREELAERYatlsfdvqklqrlhqafsrfigshlavafeadpEAELRQLNRR 845
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1198 HNQAFEELNEQLEQSKRSKASVDKAKQA------------------LESERNELQIELKSLSQSKNDSeNRRKKAESQLq 1259
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADRVEEIREQLDEAEEAKRFV-QQHGNALAQL- 923
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 ELQVKHTESERQKHELLdkvskmQAELESLQGTVTKVESKsIKAAKDCSAVESQLK--DAQALLEEETRQKLAISTRLRQ 1337
Cdd:PRK04863 924 EPIVSVLQSDPEQFEQL------KQDYQQAQQTQRDAKQQ-AFALTEVVQRRAHFSyeDAAEMLAKNSDLNEKLRQRLEQ 996
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1338 LEDEQNNLkemleeeeeskknvEKQLHTAQAQLAEMKkkieQEAQSLESMEDGKKKLQREVEsvlQQLEERNASYDKLDK 1417
Cdd:PRK04863 997 AEQERTRA--------------REQLRQAQAQLAQYN----QVLASLKSSYDAKRQMLQELK---QELQDLGVPADSGAE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1418 TKTRLQR-ELDDVLV------DQGHLRQTVQELERK--QKKFdqmlaeeKSISTKYAEERdraeaEAREKETKSLTLARE 1488
Cdd:PRK04863 1056 ERARARRdELHARLSanrsrrNQLEKQLTFCEAEMDnlTKKL-------RKLERDYHEMR-----EQVVNAKAGWCAVLR 1123
|
810
....*....|...
gi 319655760 1489 LEAMTDLKNELER 1501
Cdd:PRK04863 1124 LVKDNGVERRLHR 1136
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1064-1711 |
2.20e-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: 49.44 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1064 LHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEA-QISELQEDLELEKAARNKAEKQRRDLG 1142
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAaRISVLKEQYRVTQEENQHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1143 EELEALKTeledtLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHN----QAFEELNEQLEQSKRSKAS 1218
Cdd:pfam10174 81 DELRAQRD-----LNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELfllrKTLEEMELRIETQKQTLGA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1219 VDKAKQALeSERNELQIELKSLSQSKNDSENRRKKAESQLQELQV----KHTESERQKHELLDKVSKMQ--AELESLQGT 1292
Cdd:pfam10174 156 RDESIKKL-LEMLQSKGLPKKSGEEDWERTRRIAEAEMQLGHLEVlldqKEKENIHLREELHRRNQLQPdpAKTKALQTV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1293 VTKVESK--SIKAAKDCSAVESQLKDAQALL-----EEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHT 1365
Cdd:pfam10174 235 IEMKDTKisSLERNIRDLEDEVQMLKTNGLLhtedrEEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLET 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1366 AQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELER 1445
Cdd:pfam10174 315 LTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKER 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1446 K----QKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTD-------LKNELERVNKQLKTEMEDLV 1514
Cdd:pfam10174 395 KinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEkeriierLKEQREREDRERLEELESLK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1515 SSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQF---ERDLQSRDEQGEEKRK-- 1589
Cdd:pfam10174 475 KENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECsklENQLKKAHNAEEAVRTnp 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1590 QLVKQVREMEMELEDERKQraqavSVRKKLELD-LSELAAQIDLANKARDEALKQLKKLQA-QMKEQMREFEDLRLSRDE 1667
Cdd:pfam10174 555 EINDRIRLLEQEVARYKEE-----SGKAQAEVErLLGILREVENEKNDKDKKIAELESLTLrQMKEQNKKVANIKHGQQE 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 319655760 1668 slnqakenERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQ 1711
Cdd:pfam10174 630 --------MKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-1021 |
2.36e-05 |
|
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: 48.99 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETElcQEAEEMR--------------------SRLTARMQEM 917
Cdd:COG4942 64 IAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE--ELAELLRalyrlgrqpplalllspedfLDAVRRLQYL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 918 EEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKE 997
Cdd:COG4942 142 KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
170 180
....*....|....*....|....
gi 319655760 998 KKQMEERISEFTTNLAEEEEKSKS 1021
Cdd:COG4942 222 AEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1187-1479 |
2.72e-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: 49.35 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 HEQMLSEVRQKhnQAFEEL-NEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQV-- 1263
Cdd:pfam17380 280 HQKAVSERQQQ--EKFEKMeQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQee 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1264 KHTESER-QKHELLDKVSKMQaELESLQgtvtkvesksikaakdcsaVESQLKDaqalleEETRQKLAISTRLRQLEDEQ 1342
Cdd:pfam17380 358 RKRELERiRQEEIAMEISRMR-ELERLQ-------------------MERQQKN------ERVRQELEAARKVKILEEER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1343 NNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDgkkklQREVESVLQQLEERNASYDKLDKTKTRL 1422
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1423 QR--ELDDVLVDQ--GHLRQTVQELERKQKKFDQMLaEEKSISTKYAEERDRAEAEAREKE 1479
Cdd:pfam17380 487 KRaeEQRRKILEKelEERKQAMIEEERKRKLLEKEM-EERQKAIYEEERRREAEEERRKQQ 546
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
937-1178 |
2.97e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 937 QFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEE 1016
Cdd:COG1340 33 ELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1017 EKSKSLQKLKTKHETMITDLEDR---LRKEEKMRQELEKNRRKLEGDS--TELHDQIAELQAQIAELRAQLAKKEEELQA 1091
Cdd:COG1340 113 KLRKEIERLEWRQQTEVLSPEEEkelVEKIKELEKELEKAKKALEKNEklKELRAELKELRKEAEEIHKKIKELAEEAQE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1092 ALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLdSTAAQQELRAKRET 1171
Cdd:COG1340 193 LHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEE 271
|
....*..
gi 319655760 1172 EVTQLKK 1178
Cdd:COG1340 272 IFEKLKK 278
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1671-1864 |
3.29e-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: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1671 QAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVE 1750
Cdd:COG3206 169 RREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1751 LVNDRLKKASLQAEQVTVELTAERSN-SQRLEGLRSQLDRQN---KDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQ 1826
Cdd:COG3206 249 LGSGPDALPELLQSPVIQQLRAQLAElEAELAELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|....*...
gi 319655760 1827 LDSEMKERQQSTKQVRRVEKKLKEvLLQVEDERRNADQ 1864
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARE 365
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1336-1926 |
3.49e-05 |
|
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: 48.96 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1336 RQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEE-------- 1407
Cdd:pfam15921 78 RVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvheleaa 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1408 RNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEA-REKET------ 1480
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISKIlRELDTeisylk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1481 -KSLTLARELEAM-TDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRgmeQQLEEMKTQLEELEDELQLTEDA 1558
Cdd:pfam15921 238 gRIFPVEDQLEALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSAR---SQANSIQSQLEIIQEQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1559 KLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARD 1638
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1639 EALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKR-----------QIQQER 1707
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNeslekvssltaQLESTK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1708 DELQDEINSQNAKN-SLSSDER--RRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLR 1784
Cdd:pfam15921 475 EMLRKVVEELTAKKmTLESSERtvSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALK 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1785 SQLDRQNKDMKQKLQELEGAVK--SKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVED---ER 1859
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQlvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEK 634
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1860 RNADQSKTETEKANIRLKQMKRQLEETeeeaaranasCRKLRRELEDATESASAMNR-------EVSTLKNKLR 1926
Cdd:pfam15921 635 VKLVNAGSERLRAVKDIKQERDQLLNE----------VKTSRNELNSLSEDYEVLKRnfrnkseEMETTTNKLK 698
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1029-1180 |
3.93e-05 |
|
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: 47.83 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1029 HETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEelqaalaRIEEEAALKNAAQK 1108
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEE-------QLATERSARREAEA 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1109 SIREMEAQISELQEDLELEKAARnkaEKQRRDLGEELEALKTELEDTLDSTAAQQELrakrETEVTQLKKTL 1180
Cdd:pfam09787 115 ELERLQEELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETL 179
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1024-1147 |
3.98e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.92 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1024 KLKTKHETMITDLEDRLRKEEKMRQELEKNRRklegdstelhDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALK 1103
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAEKELI 470
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 319655760 1104 NAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEA 1147
Cdd:COG0542 471 EEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1107-1245 |
4.00e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1107 QKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEEL---EALKTELEDTLDSTAAQQELRAKRETEvtqLKKTLEDE 1183
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQALLAELAGAGAAAEGRAGE---LAQELDSE 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1184 ARAHEQMLSEVrqkhnqafEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKN 1245
Cdd:PRK09039 129 KQVSARALAQV--------ELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLN 182
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
858-1528 |
4.04e-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: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 858 LVKMKERQQQAEDQLKESEAKQKQLNAEKlalqeqlqaetELCQEAEEMRSRLTARMQEMEeVLHELESRLEeeeervaQ 937
Cdd:TIGR01612 1228 LEKIDEEKKKSEHMIKAMEAYIEDLDEIK-----------EKSPEIENEMGIEMDIKAEME-TFNISHDDDK-------D 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 FQSEKKKMQQNIGDLEQQ--------LDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNA----KLSKEKKQMEErI 1005
Cdd:TIGR01612 1289 HHIISKKHDENISDIREKslkiiedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIynilKLNKIKKIIDE-V 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1006 SEFTTNLaeeEEKSKSLQKLKTKHETMITDLEDRLRKEE-KMRQELEKNRRKLEG---DSTELHDQIAELQAQIAELRAQ 1081
Cdd:TIGR01612 1368 KEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEEcKSKIESTLDDKDIDEcikKIKELKNHILSEESNIDTYFKN 1444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1082 LAKKEEELQAALARIE-----EEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALK------- 1149
Cdd:TIGR01612 1445 ADENNENVLLLFKNIEmadnkSQHILKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEqykkdvt 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1150 --------TELEDTLDSTAAQQELRAKretEVTQLKKTLEDEARAHEQMLSEVRqkhNQAFEELNEQLEQSKRSKASVDk 1221
Cdd:TIGR01612 1525 ellnkysaLAIKNKFAKTKKDSEIIIK---EIKDAHKKFILEAEKSEQKIKEIK---KEKFRIEDDAAKNDKSNKAAID- 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1222 AKQALESERNELqIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQkhELLDKVSKMQAELESLQGTVTKVESKSi 1301
Cdd:TIGR01612 1598 IQLSLENFENKF-LKISDIKKKINDCLKETESIEKKISSFSIDSQDTELK--ENGDNLNSLQEFLESLKDQKKNIEDKK- 1673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1302 kaaKDCSAVESQLKDAQALLEEETRQ-KLAISTRLRQL-EDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQ 1379
Cdd:TIGR01612 1674 ---KELDELDSEIEKIEIDVDQHKKNyEIGIIEKIKEIaIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEE 1750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1380 EAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLvdqghlrqtvqELERKQKKFdqmlaeeks 1459
Cdd:TIGR01612 1751 YNTEIGDIYEEFIELYNIIAGCLETVSKEPITYDEIKNTRINAQNEFLKII-----------EIEKKSKSY--------- 1810
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1460 ISTKYAEERDRAeaeareketksltlareleaMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELE 1528
Cdd:TIGR01612 1811 LDDIEAKEFDRI--------------------INHFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVK 1859
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1030-1287 |
4.32e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1030 ETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKS 1109
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1110 IREMEAQISELQEdlelEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELrAKRETEVTQLKKTLEDEARAHEQ 1189
Cdd:COG1340 87 LNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKEL-VEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1190 M------LSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALES---ERNELQIELKSLSQSKNDSENRRKKAESQLQE 1260
Cdd:COG1340 162 LkelraeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADElrkEADELHKEIVEAQEKADELHEEIIELQKELRE 241
|
250 260
....*....|....*....|....*..
gi 319655760 1261 LQVKHTESERQKHELLDKVSKMQAELE 1287
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1479-1737 |
4.49e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1479 ETKSLTLAREL-EAMTDLK---NELERVNKQLKTeMEDLVSSKDDAGKSVHELERAKRGMEQ-QLEEMKTQLEELEDELQ 1553
Cdd:COG4913 220 EPDTFEAADALvEHFDDLErahEALEDAREQIEL-LEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1554 LTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLEldlsELAAQIDLA 1633
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE----ALLAALGLP 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1634 NKARDEALKQLKKLQAQMKEQmrefedlrlsrdeslnqakenerkiksMEAEIMQLHEDLAAADRAKRQIQQERDELQDE 1713
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEA---------------------------LEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
250 260
....*....|....*....|....
gi 319655760 1714 INSQNAKNSLSSDERRRLEARIAQ 1737
Cdd:COG4913 428 IASLERRKSNIPARLLALRDALAE 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1366-1835 |
5.57e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1366 AQAQLAEMKKKIEQEAQSLESMEDGKKKLQ----REVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQ 1441
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNlkelKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1442 ELERKQKKFDQmlaeeksistkyAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVsskddag 1521
Cdd:COG4717 120 KLEKLLQLLPL------------YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELE------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1522 ksvHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQLVKQ------- 1594
Cdd:COG4717 181 ---ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1595 ---VREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQA-QMKEQMREFEDLRLSRDESLN 1670
Cdd:COG4717 258 llaLLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1671 QAKENERKIKSMEAEIMQLHEDLAAADRAkrQIQQERDELQDEINSQN----AKNSLSSDERRRLEARIAQLEEELEEEH 1746
Cdd:COG4717 338 ELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDeeelRAALEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1747 LSVELVNDRLKKASLQAEQVTVEltaersnsQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKyksTITALETKIQQLEEQ 1826
Cdd:COG4717 416 GELEELLEALDEEELEEELEELE--------EELEELEEELEELREELAELEAELEQLEEDG---ELAELLQELEELKAE 484
|
....*....
gi 319655760 1827 LDSEMKERQ 1835
Cdd:COG4717 485 LRELAEEWA 493
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1586-1881 |
5.58e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1586 EKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSR 1665
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1666 DESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEinsqnaknSLSSDERRRLEARIAQlEEELEEE 1745
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTE--------VLSPEEEKELVEKIKE-LEKELEK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1746 HLSVELVNDRLKKASLQAEQVTVELtaeRSNSQRLEGLRSQLDRQNKDMKQKLQELEgavksKYKSTITALETKIQQLEE 1825
Cdd:COG1340 152 AKKALEKNEKLKELRAELKELRKEA---EEIHKKIKELAEEAQELHEEMIELYKEAD-----ELRKEADELHKEIVEAQE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1826 QLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTEtEKANIRLKQMKR 1881
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE-EKAEEIFEKLKK 278
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
860-1219 |
6.89e-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: 48.30 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQL-QAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEeeervaQF 938
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE------QK 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAA-RQKLQLEKVTMDAKLKKIEED-------LMVIEDQNAKLSKEKKQMEERISEFTT 1010
Cdd:pfam12128 710 REARTEKQAYWQVVEGALDAQLALlKAAIAARRSGAKAELKALETWykrdlasLGVDPDVIAKLKREIRTLERKIERIAV 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1011 NLAEEEEKSKSLQKLKTKHEtmiTDLEDRLRKEEKMRQELEKNRRKLEGDsTELhdQIAELQAQIAELRAQLAKKEEELQ 1090
Cdd:pfam12128 790 RRQEVLRYFDWYQETWLQRR---PRLATQLSNIERAISELQQQLARLIAD-TKL--RRAKLEMERKASEKQQVRLSENLR 863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1091 AALARIEEEAALK-----NAAQKSIREMEAQISELQEDLELEKAARNKaekqrrdlgeELEALKTELEDTLDSTAAQQEL 1165
Cdd:pfam12128 864 GLRCEMSKLATLKedansEQAQGSIGERLAQLEDLKLKRDYLSESVKK----------YVEHFKNVIADHSGSGLAETWE 933
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1166 RAKRETEVTQLKKTLEDEARAHEQMLSEVrqkhnqaFEELNEQLEQSKRSKASV 1219
Cdd:pfam12128 934 SLREEDHYQNDKGIRLLDYRKLVPYLEQW-------FDVRVPQSIMVLREQVSI 980
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1022-1181 |
7.41e-05 |
|
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: 45.33 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1022 LQKLKTKHETMITDLEDRLRKE-----EKMRQELEKNRRKLEGDSTELHDQI--------AELQAQIAELRAQLAKKEEE 1088
Cdd:pfam01442 13 AEELQEQLGPVAQELVDRLEKEtealrERLQKDLEEVRAKLEPYLEELQAKLgqnveelrQRLEPYTEELRKRLNADAEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1089 LQAALARIEEEaaLKNAAQKSIREMEAQISELQEDLelekaaRNKAEKQRRDLGEELEALKTELEDTLDSTAaqQELRAK 1168
Cdd:pfam01442 93 LQEKLAPYGEE--LRERLEQNVDALRARLAPYAEEL------RQKLAERLEELKESLAPYAEEVQAQLSQRL--QELREK 162
|
170
....*....|...
gi 319655760 1169 RETEVTQLKKTLE 1181
Cdd:pfam01442 163 LEPQAEDLREKLD 175
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1016-1152 |
7.71e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 7.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1016 EEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLakkEEELQAALar 1095
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1096 ieeeAALKNAAQKSIREMEAqiselQEDLELEKAARNKAEKQRRDLGEELEALKTEL 1152
Cdd:PRK00409 580 ----KEAKKEADEIIKELRQ-----LQKGGYASVKAHELIEARKRLNKANEKKEKKK 627
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1266-1883 |
7.96e-05 |
|
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: 48.04 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1266 TESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQAlleeETRQKLAISTRLRQLEDEQNNL 1345
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ----QTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1346 KEMLEEEEESKKNVEKQLhtaqAQLAEMKKKIEQEAQslesmedgKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRE 1425
Cdd:TIGR00618 259 QQLLKQLRARIEELRAQE----AVLEETQERINRARK--------AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1426 LDDVlvdQGHLRQTvQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKS--LTLARELEAMTDLKNELERVN 1503
Cdd:TIGR00618 327 LMKR---AAHVKQQ-SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKEL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1504 KQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKA--QFERDLQSRD 1581
Cdd:TIGR00618 403 DILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEreQQLQTKEQIH 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1582 EQGEEKrKQLVKQVREMEMELEDERKQRAqavsvrkkLELDLSELAAQIDLANKARDEALKQlkklqaQMKEQMREFEDL 1661
Cdd:TIGR00618 483 LQETRK-KAVVLARLLELQEEPCPLCGSC--------IHPNPARQDIDNPGPLTRRMQRGEQ------TYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1662 RLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQN-AKNSLSSDERRRLEARIAQLEE 1740
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSeAEDMLACEQHALLRKLQPEQDL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1741 ELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVkSKYKSTITALETKI 1820
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQL-TYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1821 QQLEEQLDSEMKERQQSTKQVRRVEKKLK-------EVLLQVEDERR-------NADQSKTETEKANIRLKQMKRQL 1883
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAaredalnQSLKELMHQARtvlkartEAHFNNNEEVTAALQTGAELSHL 783
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1068-1222 |
8.59e-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: 47.03 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1068 IAELQAQIAELRAQLAKkeeeLQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEA 1147
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1148 LKTEL-------EDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQleQSKRSKASVD 1220
Cdd:pfam00529 129 RRVLApiggisrESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEA--EAELKLAKLD 206
|
..
gi 319655760 1221 KA 1222
Cdd:pfam00529 207 LE 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
942-1239 |
8.79e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKS 1021
Cdd:COG4372 19 RPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1022 LQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAalARIEEEAA 1101
Cdd:COG4372 99 AQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA--LEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1102 LKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRE-TEVTQLKKTL 1180
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEeDKEELLEEVI 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1181 EDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKS 1239
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1452-1804 |
9.14e-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: 47.43 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1452 QMLAEEKSISTKYAEERDRAEAEAREKETKSlTLARELEAmtdlKNELERVNKQLKTEMedlvsskDDAGKSVHELERAK 1531
Cdd:pfam17380 276 HIVQHQKAVSERQQQEKFEKMEQERLRQEKE-EKAREVER----RRKLEEAEKARQAEM-------DRQAAIYAEQERMA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1532 RGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERdlqsrdEQGEEKRKQlvkqvrememELEDERKQRAQ 1611
Cdd:pfam17380 344 MERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMER------QQKNERVRQ----------ELEAARKVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1612 AVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQaKENERKIKSMEAEIMQLHE 1691
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-QEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1692 DLAAADRaKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKaslQAEQVTVELT 1771
Cdd:pfam17380 487 KRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR---RIQEQMRKAT 562
|
330 340 350
....*....|....*....|....*....|...
gi 319655760 1772 AERSNSQRLEGLRSQLdRQNKDMKQKLQELEGA 1804
Cdd:pfam17380 563 EERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1620-1873 |
1.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1620 ELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRA 1699
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1700 KRQIQQERDELQDEINSQNAKNSLSsderrRLEARiaqleeeleeehlsvELVNDRLKKASLQAEQVTVELTAERSnsqR 1779
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLD-----RLSAL---------------SKIADADADLLEELKADKAELEAKKA---E 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1780 LEGLRSQLDRQNKDMKQKLQELEgAVKSKYKSTITALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDER 1859
Cdd:COG3883 152 LEAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
250
....*....|....
gi 319655760 1860 RNADQSKTETEKAN 1873
Cdd:COG3883 231 AAAAAAAAAAAAAA 244
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1072-1285 |
1.08e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.00 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1072 QAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQedlelekaarNKAEKQRRDLGEELEAL--- 1148
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLE----------QQQAAQERLLAAQLDAAfrq 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1149 --KTELEDTLDSTAAQQE---------LRAKRETEVTQLKKTLEDEAraheQMLSEVRQKHNQAFEELNEQLEQskrska 1217
Cdd:PRK11637 137 geHTGLQLILSGEESQRGerilayfgyLNQARQETIAELKQTREELA----AQKAELEEKQSQQKTLLYEQQAQ------ 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1218 svdkaKQALESERNELQIELKSLsqskndsENRRKKAESQLQELqvKHTESerqkhELLDKVSKMQAE 1285
Cdd:PRK11637 207 -----QQKLEQARNERKKTLTGL-------ESSLQKDQQQLSEL--RANES-----RLRDSIARAERE 255
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
871-1149 |
1.08e-04 |
|
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: 47.33 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 871 QLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERvAQFQSEKKKMQQN-- 948
Cdd:pfam05667 234 RLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKG-SRFTHTEKLQFTNea 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 949 ---IGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEErisefttNLAEEEEKSKSLQKL 1025
Cdd:pfam05667 313 paaTSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEE-------ELEELKEQNEELEKQ 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1026 KTKHETMItdledrlrkeeKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNA 1105
Cdd:pfam05667 386 YKVKKKTL-----------DLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLE 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 319655760 1106 aqkSIREMEAQISELQEDlelekaARNKAEKQRRdLGEELEALK 1149
Cdd:pfam05667 455 ---EIKELREKIKEVAEE------AKQKEELYKQ-LVAEYERLP 488
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
962-1132 |
1.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 962 ARQKLQLEKVTMDAKLKKIEEDLMVIEDQnaKLSKEKKQMEERISEFTTNLAEEEEKSKSLQK-LKTKHETmitdLEDRL 1040
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKE--ALLEAKEEIHKLRNEFEKELRERRNELQKLEKrLLQKEEN----LDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1041 RKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAK-----KEEELQAALARIEEEAalKNAAQKSIREMEA 1115
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEEEA--RHEAAVLIKEIEE 180
|
170
....*....|....*..
gi 319655760 1116 QISElqedlELEKAARN 1132
Cdd:PRK12704 181 EAKE-----EADKKAKE 192
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
863-1135 |
1.14e-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: 46.60 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQlkeseaKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQ----- 937
Cdd:pfam19220 124 ERQLAAETE------QNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEltrrl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 --FQSEKKKMQQNIGDLEQQLDEEEAARQKL-----------QLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEER 1004
Cdd:pfam19220 198 aeLETQLDATRARLRALEGQLAAEQAERERAeaqleeaveahRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1005 ISEFTTNLAEEEEKSKSLQKlktKHETMITDLEDRlrkeEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAK 1084
Cdd:pfam19220 278 IRAAERRLKEASIERDTLER---RLAGLEADLERR----TQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIAS 350
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1085 KEEELQAALARIEEEAAlknaaqksirEMEAQISELQEDLELEKAARNKAE 1135
Cdd:pfam19220 351 LSDRIAELTKRFEVERA----------ALEQANRRLKEELQRERAERALAQ 391
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
938-1400 |
1.15e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 938 FQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTtnlAEEEE 1017
Cdd:PRK01156 337 DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK---KELNE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 KSKSLQKLKTKhetmITDLEDRLRKEEKMRQELEKNRRKLEGDS------TELHDQiaelqaQIAELRAQLAKKEEELQA 1091
Cdd:PRK01156 414 INVKLQDISSK----VSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEE------KSNHIINHYNEKKSRLEE 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1092 ALARIEEEAalknaaqKSIREMEAQISELQEDLELEKAARNKAEKQRrdlgeeLEALKTELEDTLDSTAAQQELRAKRET 1171
Cdd:PRK01156 484 KIREIEIEV-------KDIDEKIVDLKKRKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1172 EVTQLKKT-LEDEARAHEQMLSEVRQKHNQAFEELNEQLEQskrskasVDKAKQALESERNELQIELKSLsqsKNDSENR 1250
Cdd:PRK01156 551 IKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETNRSRSNE-------IKKQLNDLESRLQEIEIGFPDD---KSYIDKS 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1251 RKKAESQLQELQVKHTESERQKhelldkvskmqAELESLQGTVTKVESKSikaakdcsaveSQLKDAQALLEEETRQKLA 1330
Cdd:PRK01156 621 IREIENEANNLNNKYNEIQENK-----------ILIEKLRGKIDNYKKQI-----------AEIDSIIPDLKEITSRIND 678
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1331 ISTRLRQLEdeqnnlkemleeeeeskknveKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVES 1400
Cdd:PRK01156 679 IEDNLKKSR---------------------KALDDAKANRARLESTIEILRTRINELSDRINDINETLES 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1693-1933 |
1.26e-04 |
|
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: 46.68 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1693 LAAADRAKRQIQQERDELQDEINSQNAknslssdERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELta 1772
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEK-------ELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1773 eRSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKSTITALE--TKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKE 1850
Cdd:COG4942 86 -AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1851 VLLQVEDERRNADQSKTETEKANIRLKQMKRQ----LEETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKLR 1926
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
....*..
gi 319655760 1927 RGDFTGN 1933
Cdd:COG4942 245 AAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1654 |
1.40e-04 |
|
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: 46.30 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1389 DGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEksistkyaeER 1468
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL---------EK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1469 DRAEAEAREKETKSLtLARELEAMTDLKNElervnkqlkTEMEDLVSSKD--DAGKSVHELERAKRGMEQQLEEMKTQLE 1546
Cdd:COG4942 91 EIAELRAELEAQKEE-LAELLRALYRLGRQ---------PPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1547 eledelqltedaklRLEVNMQALKAQFERDLQSRDEQGEEKRkqlvkqvrememELEDERKQRAQAVsvrKKLELDLSEL 1626
Cdd:COG4942 161 --------------ELAALRAELEAERAELEALLAELEEERA------------ALEALKAERQKLL---ARLEKELAEL 211
|
250 260
....*....|....*....|....*...
gi 319655760 1627 AAQIDLANKARDEALKQLKKLQAQMKEQ 1654
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
860-1149 |
1.44e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQ 939
Cdd:COG4372 35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKS 1019
Cdd:COG4372 115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEE 1099
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 319655760 1100 AALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALK 1149
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1229-1603 |
1.47e-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: 46.43 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1229 ERNELQIELKSLSQSKNDSENRRKKAESQLqelqvkhtesERQKHELLDKVSKMQAELESLQGTVTKVESKSiKAAKDCS 1308
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQW----------ERQRRELESRVAELKEELRQSREKHEELEEKY-KELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1309 AVESQLKDAQALLEEETRQklaistRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESME 1388
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEA------RIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1389 DGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKF---DQMLAEEKSISTKYA 1465
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLnasERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1466 EERDRAEAEAREKETKSLTLARELeamTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQL 1545
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQL---ADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1546 EELEDELQLTEDAKL----RLEVNMQALKAQFeRDLQSRDEQGEEKRKQLVKQVREMEMELE 1603
Cdd:pfam07888 342 EKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1561-1927 |
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 319655760 1561 RLEVNMQALKAQFE--RDLQSRDEQGEEKRKQLVKQVREMEMELE--DERKQRAQAVSVRKKLELDLSELAAQIDLAN-- 1634
Cdd:COG4717 75 ELEEELKEAEEKEEeyAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEer 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1635 -KARDEALKQLKKLQAQMKEQMREFEDL-RLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQD 1712
Cdd:COG4717 155 lEELRELEEELEELEAELAELQEELEELlEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1713 EINSQNAKNSLSSDERRRLEA---------------------------------RIAQLEEELEEEHLSVELVNDRLKKA 1759
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1760 SLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKskyKSTITALETKIQQLEEQLDSEMKE----RQ 1835
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE---ELQLEELEQEIAALLAEAGVEDEEelraAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1836 QSTKQVRRVEKKLKEVLLQVEDER--RNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATES--A 1911
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeL 471
|
410
....*....|....*.
gi 319655760 1912 SAMNREVSTLKNKLRR 1927
Cdd:COG4717 472 AELLQELEELKAELRE 487
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
862-1119 |
1.81e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKqkqlnaeklalqeqlqaetelcqeaeemrsrltarmqemeevlhelesrleeeeerVAQFQSE 941
Cdd:COG3206 181 EEQLPELRKELEEAEAA--------------------------------------------------------LEEFRQK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KK--KMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKL--SKEKKQMEERISEFTTNLAEEee 1017
Cdd:COG3206 205 NGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAELAEL-- 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1018 ksksLQKLKTKHETMItDLEDRLRK-EEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLaKKEEELQAALARI 1096
Cdd:COG3206 283 ----SARYTPNHPDVI-ALRAQIAAlRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRL 356
|
250 260
....*....|....*....|....*
gi 319655760 1097 EEEAALKNAAQKSI--REMEAQISE 1119
Cdd:COG3206 357 EREVEVARELYESLlqRLEEARLAE 381
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1144-1926 |
1.86e-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: 46.58 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1144 ELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEA-----RAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKAS 1218
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMelkylKQYKEKACEIRDQITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1219 VDKAKQALE------SERNELQIELKSLSQSKNDSENRRKK-----------AESQLQELQVKHTESERQKHElldKVSK 1281
Cdd:TIGR00606 247 LDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSElelkmekvfqgTDEQLNDLYHNHQRTVREKER---ELVD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1282 MQAELESLQGTVTKVESKSIKAAKDCS--AVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNV 1359
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGrlQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1360 EKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQT 1439
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1440 VQELERKQKK--FDQMLAEEKSISTKYAE--ERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVS 1515
Cdd:TIGR00606 484 ERELSKAEKNslTETLKKEVKSLQNEKADldRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELT 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1516 S-------KDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKR 1588
Cdd:TIGR00606 564 SllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1589 kqlvkqvreMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQ---AQMKEQMREFEDlRLSR 1665
Cdd:TIGR00606 644 ---------LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQefiSDLQSKLRLAPD-KLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1666 DESLNQAKENERKIKSMEAEIMQlhedlAAADRAKRQIQQERDELQdeinsqnaknslssderrRLEARIAQLEEELEEE 1745
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPGRQ-----SIIDLKEKEIPELRNKLQ------------------KVNRDIQRLKNDIEEQ 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1746 HLSVELVNDRLKKASLQAEQVTVeltaersnsqrLEGLRSQLDRQNKDMKQKLQELEGavkSKYKSTITALETKIQQLEE 1825
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTI-----------MERFQMELKDVERKIAQQAAKLQG---SDLDRTVQQVNQEKQEKQH 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1826 QLDSE----------MKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANA 1895
Cdd:TIGR00606 837 ELDTVvskielnrklIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
810 820 830
....*....|....*....|....*....|....*
gi 319655760 1896 SCRKLRRELEDATESASAMNR----EVSTLKNKLR 1926
Cdd:TIGR00606 917 FLEKDQQEKEELISSKETSNKkaqdKVNDIKEKVK 951
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1428-1927 |
2.19e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1428 DVLVDQ-GHLRQTVQELERKQKK--------FDQMLAEEKSISTKYAEERDRAeAEAREKETKSLTLARE-LEAMTDLKN 1497
Cdd:PRK02224 180 RVLSDQrGSLDQLKAQIEEKEEKdlherlngLESELAELDEEIERYEEQREQA-RETRDEADEVLEEHEErREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1498 ELERVnKQLKTEMEdlvSSKDDAGKSVHELERAKRGMEQQLEEMKtqleeledelqltedAKLRLE-VNMQALKAQFErD 1576
Cdd:PRK02224 259 EIEDL-RETIAETE---REREELAEEVRDLRERLEELEEERDDLL---------------AEAGLDdADAEAVEARRE-E 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1577 LQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMR 1656
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1657 EFEDLRLSRD------ESLNQAKENER-KIKSMEAEIMQLHEDLAAADR--------------AKRQIQQERDELQDEIN 1715
Cdd:PRK02224 399 RFGDAPVDLGnaedflEELREERDELReREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETIEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1716 SQNAKNSLSSDERRRLEARIAQLEEELEEEHLsvelVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQ---LDRQNK 1792
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDR----IERLEERREDLEELIAERRETIEEKRERAEELRERaaeLEAEAE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1793 DMKQKLQELEGAVKSKyKSTITALETKIQQLEEQLDS------EMKERQQSTKQVRRVEKKLKEvLLQVEDERRNADQSK 1866
Cdd:PRK02224 555 EKREAAAEAEEEAEEA-REEVAELNSKLAELKERIESlerirtLLAAIADAEDEIERLREKREA-LAELNDERRERLAEK 632
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1867 TEtEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESASAMNREVSTLKNKLRR 1927
Cdd:PRK02224 633 RE-RKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1066-1139 |
2.21e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.48 E-value: 2.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRR 1139
Cdd:PRK11448 142 NLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1362-1914 |
2.28e-04 |
|
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: 46.25 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1362 QLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQ----LEERNASY---DKLDKTKTRLQRELDDVLVDQG 1434
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlIKENNATRhlcNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1435 HLRQTVQELERKQKK----FDQM--LAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKqlkt 1508
Cdd:pfam05483 180 ETRQVYMDLNNNIEKmilaFEELrvQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK---- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1509 eMEDLVSSKDDAGKSVHELERAKRgmeQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAqFERDLQSrdeqgeeKR 1588
Cdd:pfam05483 256 -MKDLTFLLEESRDKANQLEEKTK---LQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKA-LEEDLQI-------AT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1589 KQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRD-- 1666
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNnk 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1667 ----ESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERD----ELQDEINSQNAKNSLSSDERRRLEARIAQL 1738
Cdd:pfam05483 404 evelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREkeihDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1739 EEELEEEHLSVELVNDRLKKASLQAEQVTVELTAER----SNSQRLEGLRSQLDRQNKDMKQKLQELEgAVKSKYKSTIT 1814
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQediiNCKKQEERMLKQIENLEEKEMNLRDELE-SVREEFIQKGD 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1815 ALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETekanirlKQMKRQLEETEEEAARAN 1894
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN-------KALKKKGSAENKQLNAYE 635
|
570 580
....*....|....*....|
gi 319655760 1895 ASCRKLRRELEDATESASAM 1914
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEI 655
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
654-678 |
2.34e-04 |
|
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: 43.87 E-value: 2.34e-04
10 20
....*....|....*....|....*
gi 319655760 654 YKEQLMNLMTTLRNTNPNFVRCIIP 678
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1035-1255 |
2.50e-04 |
|
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: 46.30 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1035 DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQiAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREME 1114
Cdd:pfam18971 618 DLEKSLRKREHLEKEVEKKLESKSGNKNKMEAK-AQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKIS 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1115 AQISELQEDLELEKAARNKAEKQRRdlgEELEALKTELED----------TLDSTAAQQELRAKRE---TEVTQLKKTLE 1181
Cdd:pfam18971 697 KDLKDFSKSFDEFKNGKNKDFSKAE---ETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNkdfSKVTQAKSDLE 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1182 DEARAheqmlSEVRQKHNQAFEELNEQLEQSKrSKASVDKAKQALESERNELQIELKSLSQsKNDSENRRKKAE 1255
Cdd:pfam18971 774 NSVKD-----VIINQKVTDKVDNLNQAVSVAK-AMGDFSRVEQVLADLKNFSKEQLAQQAQ-KNEDFNTGKNSE 840
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
1067-1181 |
2.55e-04 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 45.04 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1067 QIAELQAQIAELRAQLAKKEEELQAALARIEEEAAlknaaqksIREMEAQISELQEDLELEKAArnKAEKQRRDLGEELE 1146
Cdd:COG4223 1 EIAALEAAVAELPAQLTALEQRLAALEAAPAAAAA--------TAALEARLAALRAALAAAREA--VAAAAAAALEARLA 70
|
90 100 110
....*....|....*....|....*....|....*
gi 319655760 1147 ALKTELEdTLDSTAAQQELRAKRETEVTQLKKTLE 1181
Cdd:COG4223 71 ALEAKAA-APEAEAAAAARAAALALAAAALRAAVE 104
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
971-1186 |
2.59e-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: 45.44 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 971 VTMDAKLKKIEEDLMVIEDQNAKLSKEKKQmeERISEFTTNLAeeeeksKSLQKLKTKHETMITDLEDRLRKEEKMRQEL 1050
Cdd:cd22656 87 GTIDSYYAEILELIDDLADATDDEELEEAK--KTIKALLDDLL------KEAKKYQDKAAKVVDKLTDFENQTEKDQTAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1051 EKNRRKLEG-----DSTELHDQIAELQAQIAELRAQLAKKE----EELQAALARIEEEAALKNAAQKSIREMEAQISELQ 1121
Cdd:cd22656 159 ETLEKALKDlltdeGGAIARKEIKDLQKELEKLNEEYAAKLkakiDELKALIADDEAKLAAALRLIADLTAADTDLDNLL 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1122 EDLELEKAARNKAEKQRRDLGEELEALKTELEDtlDSTAAQQELRAKRETEVTQLK-KTLEDEARA 1186
Cdd:cd22656 239 ALIGPAIPALEKLQGAWQAIATDLDSLKDLLED--DISKIPAAILAKLELEKAIEKwNELAEKADK 302
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1043-1190 |
2.73e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1043 EEKMRQELEKnrrklegdSTEL------HDQIAELQaQIAELRAQLAKKEEELQAALARIEEEAA----LKNAAQ----- 1107
Cdd:PTZ00491 642 DERTRDSLQK--------SVQLaieittKSQEAAAR-HQAELLEQEARGRLERQKMHDKAKAEEQrtklLELQAEsaave 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1108 ---KSIREMEAQISELQEDLELE-KAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQEL---RAKR--ETEVTQLKK 1178
Cdd:PTZ00491 713 ssgQSRAEALAEAEARLIEAEAEvEQAELRAKALRIEAEAELEKLRKRQELELEYEQAQNELeiaKAKElaDIEATKFER 792
|
170 180
....*....|....*....|
gi 319655760 1179 --------TLEDEARAHEQM 1190
Cdd:PTZ00491 793 ivealgreTLIAIARAGPEL 812
|
|
| LegC3_N |
pfam18654 |
LegC3 N-terminal coiled-coil domain; LegC3 is an effector protein secreted by Legionella ... |
1068-1259 |
2.99e-04 |
|
LegC3 N-terminal coiled-coil domain; LegC3 is an effector protein secreted by Legionella pneumophila which is believed to act by inhibiting vacuolar fusion. The N-terminal domain of LegC3 is composed of a long discontinuous coiled-coil capped by an antiparallel four-helix bundle that is rigidly connected to the coiled-coil segment. The features responsible for fusion inhibition are located mainly within the N-terminal domain, as this domain alone was sufficient to inhibit vacuole fusion, and that this domain remains associated with vacuoles.
Pssm-ID: 408436 [Multi-domain] Cd Length: 296 Bit Score: 44.81 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1068 IAELQAQIAELRAQLakKEEELQAALARIEEEAalknaaqksireMEAQISELQEDLELEKAARNKAEKQRRDLGEELEA 1147
Cdd:pfam18654 39 IPWIHSQITSLLSQA--KKSDEAAVKAALEKQA------------YKQQMKEDKKQKERDVEEERKDLLRKERLTRELEH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1148 LKTELEDTldstaaQQELRAKRetevTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALE 1227
Cdd:pfam18654 105 IPVELSEY------ERELRLLE----TKLHRLTESQTPVEVTQHSTPISAKLLSPSNHVASIERARRSSQDIELKIRSLN 174
|
170 180 190
....*....|....*....|....*....|..
gi 319655760 1228 SERNELQIELKSLSQSKNDSENRRKKAESQLQ 1259
Cdd:pfam18654 175 ERIVNIKKELKEIESRNKDREDRRGKREKRLQ 206
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1051-1303 |
3.16e-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: 45.98 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1051 EKNRRKLEGDSTELHDQIAELQAQIaELRAQLAkKEEELQAALARIEEEAalknaaqksiREMEAQISELQEDLELEKAA 1130
Cdd:NF012221 1568 EADRQRLEQEKQQQLAAISGSQSQL-ESTDQNA-LETNGQAQRDAILEES----------RAVTKELTTLAQGLDALDSQ 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1131 RNKAEKqrrdLGEE-----LEALKTELEDTLDST----------------AAQQELR---AKRETEVTQLKKTLEDEARA 1186
Cdd:NF012221 1636 ATYAGE----SGDQwrnpfAGGLLDRVQEQLDDAkkisgkqladakqrhvDNQQKVKdavAKSEAGVAQGEQNQANAEQD 1711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1187 HEQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQ-------ALESERNELQIELKSLSQSKNDSENRRKKAESQL- 1258
Cdd:NF012221 1712 IDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSrgeqdasAAENKANQAQADAKGAKQDESDKPNRQGAAGSGLs 1791
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1259 -QELQVkhtESERQKHELLDKVSKMQA-----------ELESLQGTVTKVESKSIKA 1303
Cdd:NF012221 1792 gKAYSV---EGVAEPGSHINPDSPAAAdgrfseglteqEQEALEGATNAVNRLQINA 1845
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1410-1631 |
3.29e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1410 ASYDKLDKTKTR-LQRELDDVLVDQGHLRQTV---------------QELERKQKKFDQMLAEEKSISTKYAEERDRAEA 1473
Cdd:PHA02562 166 SEMDKLNKDKIReLNQQIQTLDMKIDHIQQQIktynknieeqrkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLN 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1474 EAREKETKSLTLARELEAMTDLKNELERVNKQLK---------TEMEDLvsskDDAGKSVHELERAKRGMEQQLEEMKtq 1544
Cdd:PHA02562 246 LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKmyekggvcpTCTQQI----SEGPDRITKIKDKLKELQHSLEKLD-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1545 leELEDELQLTEDAKLRLEVNMQALKAQFE---RDLQSRDEQGeekrKQLVKQVREMEMELEDERKQRAQAVSVRKKLEL 1621
Cdd:PHA02562 320 --TAIDELEEIMDEFNEQSKKLLELKNKIStnkQSLITLVDKA----KKVKAAIEELQAEFVDNAEELAKLQDELDKIVK 393
|
250
....*....|
gi 319655760 1622 DLSELAAQID 1631
Cdd:PHA02562 394 TKSELVKEKY 403
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
941-1149 |
3.35e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQN-IGDLEQQLDEeeaARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKS 1019
Cdd:PHA02562 195 QQIKTYNKnIEEQRKKNGE---NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHET----------------MITDLEDRLRKEEKMRQELEKNRRKLEgdstELHDQIAELQAQIAELRAQLA 1083
Cdd:PHA02562 272 EQFQKVIKMYEKggvcptctqqisegpdRITKIKDKLKELQHSLEKLDTAIDELE----EIMDEFNEQSKKLLELKNKIS 347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1084 KKEEELQAALARIEE-EAALKNAaQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALK 1149
Cdd:PHA02562 348 TNKQSLITLVDKAKKvKAAIEEL-QAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLLK 413
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1145-1665 |
3.35e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1145 LEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKhNQAFEELNEQLEQSKRSKASVDKAKQ 1224
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEEL-EEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1225 ALEserneLQIELKSLSQSKNDSENRRKKAESQLQELQvkhtESERQKHELLDKVSKMQAELESLQGTVTKVESKSIK-A 1303
Cdd:COG4717 127 LLP-----LYQELEALEAELAELPERLEELEERLEELR----ELEEELEELEAELAELQEELEELLEQLSLATEEELQdL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1304 AKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQnnlkemleeeeeSKKNVEKQLHTAQAQLAemkkkIEQEAQS 1383
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL------------EAAALEERLKEARLLLL-----IAAALLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1384 LESMEDGKKKLQREVESVLQ-QLEERNASYDKLDKTKTRLQRELDDvlVDQGHLRQTVQELERKQKKFDQMLAEEksIST 1462
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLFlVLGLLALLFLLLAREKASLGKEAEE--LQALPALEELEEEELEELLAALGLPPD--LSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1463 KYAEERDRAEAEAREKETKSLTLARELEaMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEEmk 1542
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE-- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1543 tqleeledelqltedaklrlevnmqALKAQFERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELD 1622
Cdd:COG4717 414 -------------------------LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 319655760 1623 --LSELAAQIDLANKARDEALKQ---LKKLQAQMKEQMREFEDLRLSR 1665
Cdd:COG4717 469 geLAELLQELEELKAELRELAEEwaaLKLALELLEEAREEYREERLPP 516
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1512-1925 |
3.57e-04 |
|
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: 45.50 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1512 DLVSSKDDAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRkQL 1591
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNR-LK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1592 VKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQ---MREFEDLRLSRDES 1668
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1669 LNQAKENERKIKSMEAEImQLHEDLAAADRAKRQIQQERDELQDEI----------NSQNAKNSLSSDERRRLEARIAQL 1738
Cdd:pfam05557 162 QSSLAEAEQRIKELEFEI-QSQEQDSEIVKNSKSELARIPELEKELerlrehnkhlNENIENKLLLKEEVEDLKRKLERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1739 EEELEEEhlsvelVNDRLKKASLQAEQVTVELTAERS--NSQRLEGLRS---QLDRQNKDMKQKLQELEGAVKSKyKSTI 1813
Cdd:pfam05557 241 EKYREEA------ATLELEKEKLEQELQSWVKLAQDTglNLRSPEDLSRrieQLQQREIVLKEENSSLTSSARQL-EKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1814 TALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKL----------KEVLLQVEDE--RRNADQSKTE--------TEKAN 1873
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerdgyRAILESYDKEltMSNYSPQLLErieeaedmTQKMQ 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1874 IRLKQMKRQLEETEEEAARANASCRKLRRELE-----DATESASAMNREVSTLKNKL 1925
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQalrqqESLADPSYSKEEVDSLRRKL 450
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1107-1404 |
3.61e-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: 45.50 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1107 QKSIREMEAQisELQEDLELEKAARNKAEK-----QRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKktLE 1181
Cdd:pfam17380 281 QKAVSERQQQ--EKFEKMEQERLRQEKEEKareveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR--QE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1182 DEARAHEQMLSEVRQKHNQAFEELnEQLEQSKRSKAsvDKAKQALESERN----ELQIELKSLSQSKNDSENRRKKAESQ 1257
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMREL-ERLQMERQQKN--ERVRQELEAARKvkilEEERQRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1258 LQELQVKHTESERQKHELLDKVSKMQAELESLQgtvtkvesksikaakdcSAVESQLKDAQALLEEETRQKLAISTRLRQ 1337
Cdd:pfam17380 434 QREVRRLEEERAREMERVRLEEQERQQQVERLR-----------------QQEEERKRKKLELEKEKRDRKRAEEQRRKI 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1338 LEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAE--MKKKIEQEAQSLESMEDgKKKLQREVESVLQQ 1404
Cdd:pfam17380 497 LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEeeRRREAEEERRKQQEMEE-RRRIQEQMRKATEE 564
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
987-1196 |
3.62e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 44.21 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 987 IEDQNAKLSKEKKQMEE---RISEFTTNLAEEEeKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTE 1063
Cdd:pfam12795 32 IDASKQRAAAYQKALDDapaELRELRQELAALQ-AKAEAAPKEILASLSLEELEQRLLQTSAQLQELQNQLAQLNSQLIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1064 LHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEA-ALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLG 1142
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSeAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLLT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1143 EELEALKTELEdtldstAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQ 1196
Cdd:pfam12795 191 LRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1069-1193 |
4.05e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1069 AELQAQIAELRAQLAKKEEE---LQAALARIEEEAAlknaaqksirEMEAQISELQEDLELEKAARNKAEKQRRDLGEEL 1145
Cdd:PRK09039 77 QDLQDSVANLRASLSAAEAErsrLQALLAELAGAGA----------AAEGRAGELAQELDSEKQVSARALAQVELLNQQI 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1146 EALKTEL---EDTLD-STAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSE 1193
Cdd:PRK09039 147 AALRRQLaalEAALDaSEKRDRESQAKIADLGRRLNVALAQRVQELNRYRSE 198
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1419-1883 |
4.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1419 KTRLQRELDDVLVDQghLRQTVQELERKQKKFDQMLAEEksistkyAEERDRAEAEAREKETKSLTLARELEAMTDLKNE 1498
Cdd:COG4717 36 KSTLLAFIRAMLLER--LEKEADELFKPQGRKPELNLKE-------LKELEEELKEAEEKEEEYAELQEELEELEEELEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1499 LERVNKQLKTEMEDLVSSKD--DAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTEdaklRLEVNMQALKAQFERD 1576
Cdd:COG4717 107 LEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELE----ELEAELAELQEELEEL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1577 LQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQidlanKARDEALKQLKKLQaqmkeQMR 1656
Cdd:COG4717 183 LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE-----LEAAALEERLKEAR-----LLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1657 EFEDLRLSRDESLNQAKENERKIKSMEAEIMQLhedLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIA 1736
Cdd:COG4717 253 LIAAALLALLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1737 QLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQR-----------LEGLRSQLDRQNK--DMKQKLQELEG 1803
Cdd:COG4717 330 LPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaallaeagvedEEELRAALEQAEEyqELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1804 AVKSKYKSTI--------TALETKIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIR 1875
Cdd:COG4717 410 QLEELLGELEellealdeEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELA 489
|
....*...
gi 319655760 1876 LKQMKRQL 1883
Cdd:COG4717 490 EEWAALKL 497
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1621-1774 |
4.21e-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: 44.15 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1621 LDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAK 1700
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1701 rqiqqERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAER 1774
Cdd:COG1579 90 -----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1575-1778 |
4.53e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1575 RDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQ 1654
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1655 MR------------EFEDLrLSRDESLNQAKENERKI--------KSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEI 1714
Cdd:COG3883 99 GGsvsyldvllgseSFSDF-LDRLSALSKIADADADLleelkadkAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1715 NSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQ 1778
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
994-1341 |
4.55e-04 |
|
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: 45.44 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 994 LSKEKKQMEERISEFTTNLAEEEEK----SKSLQKLKTKHETMITDLEDRLRKEE--KMRQELEKNRRKLEGDSTELHDQ 1067
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKldaaEANLQKLDKEKEKLEADFLDECWKKIkrKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1068 IAELQAQI---------AELRAQLAKKEEELQAALARIEEEA----ALKNAA--QKSIREMEAQISELQEDLELEKAARN 1132
Cdd:pfam13166 167 LREIEKDNfnagvllsdEDRKAALATVFSDNKPEIAPLTFNVidfdALEKAEilIQKVIGKSSAIEELIKNPDLADWVEQ 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1133 KAEKQRRDL------GEEL-EALKTELEDTLDSTAAQQelrakreteVTQLKKTLEDEARAHEQML------SEVRQKHn 1199
Cdd:pfam13166 247 GLELHKAHLdtcpfcGQPLpAERKAALEAHFDDEFTEF---------QNRLQKLIEKVESAISSLLaqlpavSDLASLL- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1200 QAFEELNEQLEQSKRSKAS-VDKAKQALESERNELQIELkSLSQSKNDSENrRKKAESQLQELQVKHTEserQKHELLDK 1278
Cdd:pfam13166 317 SAFELDVEDIESEAEVLNSqLDGLRRALEAKRKDPFKSI-ELDSVDAKIES-INDLVASINELIAKHNE---ITDNFEEE 391
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 319655760 1279 VSKMQAELEslQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDE 1341
Cdd:pfam13166 392 KNKAKKKLR--LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQ 452
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
959-1090 |
4.97e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.07 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 959 EEAARQKLQLEkvTMDAKLKKIEEDLMVIEDQNAKLSKEKKQ-MEERISEFTTNLAEEEEKskslqklktkhetmITDLE 1037
Cdd:COG0542 397 EAAARVRMEID--SKPEELDELERRLEQLEIEKEALKKEQDEaSFERLAELRDELAELEEE--------------LEALK 460
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 319655760 1038 DRLRKEEKMRQELEKNRRKLEgdstELHDQIAELQAQIAELRAQLAKKEEELQ 1090
Cdd:COG0542 461 ARWEAEKELIEEIQELKEELE----QRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1563-1927 |
5.58e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1563 EVNMQALKAQfERDLQSRDEQgEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLE--LDLSELAAQIDLANKARDEA 1640
Cdd:COG4717 67 ELNLKELKEL-EEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1641 LKQLKKLQAQMKE------------------QMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQ 1702
Cdd:COG4717 145 PERLEELEERLEElreleeeleeleaelaelQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1703 IQQERDELQDEINSQNAKNSLSSDERR-RLEARIAQLEEELEEEHLSVELVNDRLK----KASLQAEQVTVELTAERSNS 1777
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIAGVLFlvlgLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1778 QRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKSTITALEtKIQQLEEQLDSEMKERQQSTKQVRRVEKK--LKEVLLQV 1855
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD-RIEELQELLREAEELEEELQLEELEQEIAalLAEAGVED 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1856 EDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRK--LRRELEDATESASAMNREVSTLKNKLRR 1927
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAE 457
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
937-1334 |
5.62e-04 |
|
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: 44.63 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 937 QFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEkvtMDAKLKKIEEdlmviedqnAKLSKEKKQMEERISEFTTNLAeee 1016
Cdd:pfam05701 39 LVELELEKVQEEIPEYKKQSEAAEAAKAQVLEE---LESTKRLIEE---------LKLNLERAQTEEAQAKQDSELA--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1017 ekskslqklKTKHETMITDLEDRLRKEEKMRQELEKNRRKlegdstelhDQIAELQAQIAEL---RAQLAKKEEELQAAL 1093
Cdd:pfam05701 104 ---------KLRVEEMEQGIADEASVAAKAQLEVAKARHA---------AAVAELKSVKEELeslRKEYASLVSERDIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1094 ARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLG----EELEALKTELEDtldstaAQQELRAKR 1169
Cdd:pfam05701 166 KRAEEAVSASKEIEKTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareQDKLNWEKELKQ------AEEELQRLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1170 ETEVTqlKKTLEDEARAHEQMLSEVRQKHNQAFE-ELNEQLEQSKRSKASVDKAKQALESERNELQiELKSLSQSKNDSE 1248
Cdd:pfam05701 240 QQLLS--AKDLKSKLETASALLLDLKAELAAYMEsKLKEEADGEGNEKKTSTSIQAALASAKKELE-EVKANIEKAKDEV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1249 NRRKKAESQLQelqvkhTESERQKHELLD----------KVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKdaQ 1318
Cdd:pfam05701 317 NCLRVAAASLR------SELEKEKAELASlrqregmasiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQ--Q 388
|
410
....*....|....*.
gi 319655760 1319 ALLEEETRQKLAISTR 1334
Cdd:pfam05701 389 AAQEAEEAKSLAQAAR 404
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
863-1469 |
5.92e-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: 44.94 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 863 ERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQ-EAEEMRSRLT--------------------ARMQEMEEVL 921
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEeEVDSLKSQLAdyqqaldvqqtraiqyqqavQALEKARALC 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 922 HELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAAR----QKLQLEK-----VTMDAKLKKIEEDLMVIEDQNA 992
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARrqfeKAYELVCkiageVERSQAWQTARELLRRYRSQQA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 993 KLSKEKkQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMIT---DLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIA 1069
Cdd:COG3096 510 LAQRLQ-QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1070 ELQAQIAELRAQlAKKEEELQAALARIEEE--AALKNAAQKS-------IREMEAQISE---LQEDLELEKAARN----- 1132
Cdd:COG3096 589 QLRARIKELAAR-APAWLAAQDALERLREQsgEALADSQEVTaamqqllEREREATVERdelAARKQALESQIERlsqpg 667
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1133 KAEKQR-----------------------------------------RDLGEELEALKTeLEDTL--------------D 1157
Cdd:COG3096 668 GAEDPRllalaerlggvllseiyddvtledapyfsalygparhaivvPDLSAVKEQLAG-LEDCPedlyliegdpdsfdD 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1158 STAAQQEL-------------------------RAKRETEVTQLKKTLEDEARAH------------------------- 1187
Cdd:COG3096 747 SVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQYakasfdvqklqrlhqafsqfvgghl 826
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1188 --------EQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESeRNELQIELKSLSQskNDSENRRKKAESQLQ 1259
Cdd:COG3096 827 avafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQL-LNKLLPQANLLAD--ETLADRLEELREELD 903
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 ELQvkhtESER--QKH-----ELLDKVSKMQ---AELESLQGTVTKVESKSIKAAKDCSAVESQLK--------DAQALL 1321
Cdd:COG3096 904 AAQ----EAQAfiQQHgkalaQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQrrphfsyeDAVGLL 979
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1322 EEETRQKLAISTRLRQLEDEQNnlkemleeeeeskkNVEKQLHTAQAQLAEMKkkieQEAQSLESMEDGKKKLQREVESV 1401
Cdd:COG3096 980 GENSDLNEKLRARLEQAEEARR--------------EAREQLRQAQAQYSQYN----QVLASLKSSRDAKQQTLQELEQE 1041
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1402 LQQLEERNASyDKLDKTKTRlQRELDDVLVdqgHLRQTVQELErKQKKFDQmlAEEKSISTKY-AEERD 1469
Cdd:COG3096 1042 LEELGVQADA-EAEERARIR-RDELHEELS---QNRSRRSQLE-KQLTRCE--AEMDSLQKRLrKAERD 1102
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1303-1491 |
6.25e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1303 AAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQ--- 1379
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1380 ----------------EAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQEL 1443
Cdd:COG3883 94 alyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 319655760 1444 ERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEA 1491
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1585-1737 |
6.64e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.28 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1585 EEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQI-DLANKARD-----------EALKQLKKLQAQMK 1652
Cdd:COG1842 22 EDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAeKWEEKARLalekgredlarEALERKAELEAQAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1653 EQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLhedlaaadRAKRQIQQERDELQDEINSQNAKNSLSSDErrRLE 1732
Cdd:COG1842 102 ALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTL--------KARAKAAKAQEKVNEALSGIDSDDATSALE--RME 171
|
....*
gi 319655760 1733 ARIAQ 1737
Cdd:COG1842 172 EKIEE 176
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1036-1303 |
6.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1036 LEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEA 1115
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1116 QISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVR 1195
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1196 QKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHEL 1275
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260
....*....|....*....|....*...
gi 319655760 1276 LDKVSKMQAELESLQGTVTKVESKSIKA 1303
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAA 282
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
860-1054 |
6.73e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQ----------AEDQLK-------ESEAKQKQLNAEKLALQEQLQAETE-LCQEAEEMRSRLTARMQEMEEV- 920
Cdd:PHA02562 175 KIRELNQQiqtldmkidhIQQQIKtynknieEQRKKNGENIARKQNKYDELVEEAKtIKAEIEELTDELLNLVMDIEDPs 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 921 --LHELESRLEEEEERVAQFQSEKKKMQQniGDL----EQQLDEEEAARQKLQLEKVTMDAKLKKIE---EDLMVIEDQN 991
Cdd:PHA02562 255 aaLNKLNTAAAKIKSKIEQFQKVIKMYEK--GGVcptcTQQISEGPDRITKIKDKLKELQHSLEKLDtaiDELEEIMDEF 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 992 AKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTK-------HETMITDLEDRLRKEEKMRQELEKNR 1054
Cdd:PHA02562 333 NEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEElqaefvdNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
995-1149 |
6.90e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 995 SKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEgdstelhdQIAELQAQ 1074
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEE--------QLDARAEK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1075 IAELRAQLAKKEEELQAALARIEEEAA-----LKNAAQKSIREMEAQI-SELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:PRK12705 100 LDNLENQLEEREKALSARELELEELEKqldneLYRVAGLTPEQARKLLlKLLDAELEEEKAQRVKKIEEEADLEAERKAQ 179
|
.
gi 319655760 1149 K 1149
Cdd:PRK12705 180 N 180
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
867-1287 |
6.91e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.79 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 867 QAEDQLKESEAKQKQLnaekLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKmQ 946
Cdd:PRK10246 413 AALAQHAEQRPLRQRL----VALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-E 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 947 QNIGDLEQQLD--------------EEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNA----KLSKEKKQMEERISEF 1008
Cdd:PRK10246 488 ARIKDLEAQRAqlqagqpcplcgstSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAalrgQLDALTKQLQRDESEA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1009 TTNLAEEEEKSKSLQKLKTKHETMIT---DLEDRLRKEEKMRQELEKNRRKLEgdsteLHDQIAELQAQIAELRAQLAKK 1085
Cdd:PRK10246 568 QSLRQEEQALTQQWQAVCASLNITLQpqdDIQPWLDAQEEHERQLRLLSQRHE-----LQGQIAAHNQQIIQYQQQIEQR 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1086 EEELQAALARI-----------------EEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:PRK10246 643 QQQLLTALAGYaltlpqedeeaswlatrQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQV 722
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1149 KTE---LEDTLDSTAAQQELRAKRETEVTQ-----------------LKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQ 1208
Cdd:PRK10246 723 HEQclsLHSQLQTLQQQDVLEAQRLQKAQAqfdtalqasvfddqqafLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQ 802
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1209 LEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQElqvkHTESERQKHELLDKVSKMQAELE 1287
Cdd:PRK10246 803 TAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQ----DADNRQQQQALMQQIAQATQQVE 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1590 |
7.43e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1376 KIEQEAQSLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVlvdQGHLRQTVQELERKQKKFDQMLA 1455
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL---QAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1456 E--EKSISTKYAEE----RDRAEAEAReketkSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELER 1529
Cdd:COG3883 94 AlyRSGGSVSYLDVllgsESFSDFLDR-----LSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1530 AKRGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFERDLQSRDEQGEEKRKQ 1590
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
860-1007 |
7.49e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDQLKESEAKQKQLNAEKLALQEQL-QAETELCQEAEEMR------------------SRLTARMQEMEEV 920
Cdd:COG3883 48 ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeERREELGERARALYrsggsvsyldvllgsesfSDFLDRLSALSKI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 921 LHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQ 1000
Cdd:COG3883 128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
....*..
gi 319655760 1001 MEERISE 1007
Cdd:COG3883 208 AEAAAAA 214
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1060-1163 |
7.97e-04 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 42.13 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKsiREMEAQISELQEDLELEKAARNKAEKQRR 1139
Cdd:COG2825 37 ESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQDLQKRQ 114
|
90 100
....*....|....*....|....
gi 319655760 1140 DlgEELEALKTELEDTLDSTAAQQ 1163
Cdd:COG2825 115 Q--ELLQPILEKIQKAIKEVAKEE 136
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1048-1144 |
8.78e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 42.23 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1048 QELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISE-------L 1120
Cdd:pfam08614 53 QSLEQLLAQLREELAELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREkrklnqdL 132
|
90 100
....*....|....*....|....
gi 319655760 1121 QEDLELEKAARNKAEKQRRDLGEE 1144
Cdd:pfam08614 133 QDELVALQLQLNMAEEKLRKLEKE 156
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
973-1230 |
8.96e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 973 MDAKLKKI-EEDLMVIEDQNAKLSkekkqmEERISEFTTNLAEEEEKSKSLQKLKTKhETMITDLEDRLRKE--EKMRQE 1049
Cdd:PRK05771 18 KDEVLEALhELGVVHIEDLKEELS------NERLRKLRSLLTKLSEALDKLRSYLPK-LNPLREEKKKVSVKslEELIKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1050 LEKNRRKLEGDSTELHDQIAELQAQIAELRAQLA--------KKEEELQAALARIEEEAALKNAAQKSiremEAQISELQ 1121
Cdd:PRK05771 91 VEEELEKIEKEIKELEEEISELENEIKELEQEIErlepwgnfDLDLSLLLGFKYVSVFVGTVPEDKLE----ELKLESDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1122 EDLELEKAARNK-------AEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKrETEVTQLKKTLEDearAHEQmLSEV 1194
Cdd:PRK05771 167 ENVEYISTDKGYvyvvvvvLKELSDEVEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERES---LLEE-LKEL 241
|
250 260 270
....*....|....*....|....*....|....*..
gi 319655760 1195 RQKHNQAFEELNEQLEQ-SKRSKASVdkakQALESER 1230
Cdd:PRK05771 242 AKKYLEELLALYEYLEIeLERAEALS----KFLKTDK 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1214-1575 |
9.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1214 RSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTV 1293
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1294 TKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEM 1373
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1374 KKKIEQEAQSLESMEDGK--KKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFD 1451
Cdd:COG4372 163 QEELAALEQELQALSEAEaeQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1452 QMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAK 1531
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 319655760 1532 RGMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNMQALKAQFER 1575
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAG 366
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1224-1415 |
1.00e-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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1224 QALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHEL---LDKVSKMQAELESLQGTVTKVesks 1300
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLeleIEEVEARIKKYEEQLGNVRNN---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1301 ikaakdcsavesqlKDAQALLEEETRQKLAIStrlrQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQE 1380
Cdd:COG1579 89 --------------KEYEALQKEIESLKRRIS----DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 319655760 1381 AQSLESMEdgkKKLQREVESVLQQLEERN-ASYDKL 1415
Cdd:COG1579 151 LAELEAEL---EELEAEREELAAKIPPELlALYERI 183
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1679-1927 |
1.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1679 IKSMEAEIMQLHEDLAAADRAKRQIQQERD--ELQDEINSQnaknslsSDERRRLEARIAQLeeeleeehlsvelvndRL 1756
Cdd:COG4913 227 ADALVEHFDDLERAHEALEDAREQIELLEPirELAERYAAA-------RERLAELEYLRAAL----------------RL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1757 KKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKSTITALETKIQQLEEQLDSEMKERQQ 1836
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1837 STKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANascRKLRRELEDATESASAMNR 1916
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL---RELEAEIASLERRKSNIPA 440
|
250
....*....|.
gi 319655760 1917 EVSTLKNKLRR 1927
Cdd:COG4913 441 RLLALRDALAE 451
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1130-1334 |
1.30e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 43.85 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1130 ARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQ---LKKTLEDEARAHEQMLSEVRQKHNQAFEELN 1206
Cdd:NF033838 52 GNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKteyLYELNVLKEKSEAELTSKTKKELDAAFEQFK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1207 EQL--------EQSKRSKASVDKAK-QALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESErqkhellD 1277
Cdd:NF033838 132 KDTlepgkkvaEATKKVEEAEKKAKdQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDE-------E 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1278 KVSKMQAELESLQGTVTKVEskSIKAAKDcSAVESQLKDAQALLEEETRQKLAISTR 1334
Cdd:NF033838 205 KIKQAKAKVESKKAEATRLE--KIKTDRE-KAEEEAKRRADAKLKEAVEKNVATSEQ 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1400-1637 |
1.35e-03 |
|
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: 43.21 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1400 SVLQQLEERNASYDKLDKTKTRLQRELDDVLVDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKE 1479
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1480 TKSLTLARELEAMTDLKNELERVNKQLKTEMedLVSSKD--DAGKSVHELERAKRGMEQQLEEMKTQLEELEDELQLTED 1557
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1558 AKLRLEVNMQALKAQfERDLQSRDEQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKAR 1637
Cdd:COG4942 172 ERAELEALLAELEEE-RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1339-1540 |
1.50e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1339 EDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERnasYDKLDKT 1418
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---REELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1419 KTRLQRELD-----DVLVDQghlrQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMT 1493
Cdd:COG3883 92 ARALYRSGGsvsylDVLLGS----ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 319655760 1494 DLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAKRGMEQQLEE 1540
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1452-1708 |
1.50e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1452 QMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEMEDLVSSKDDAGKSVHELERAK 1531
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1532 RGMEQQLEEMKTQLEELEDELQLTEDAKLRLEvNMQALKAQFERDLQSRDeQGEEKRKQLVKQVREMEMELEDERKQ--- 1608
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEV-LSPEEEKELVEKIKELEKELEKAKKAlek 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1609 -------RAQAVSVRKKLE---LDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENERK 1678
Cdd:COG1340 159 neklkelRAELKELRKEAEeihKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250 260 270
....*....|....*....|....*....|
gi 319655760 1679 IKSMEAEIMQLHEDLAAADRAKRQIQQERD 1708
Cdd:COG1340 239 LRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1138-1285 |
1.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1138 RRDLGEELEALKTELEDTLDstAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRSKA 1217
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1218 SVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQE---LQvkhteSERQKHELLDKV-SKMQAE 1285
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgLT-----AEEAKEILLEKVeEEARHE 170
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
941-1158 |
1.57e-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: 42.88 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQNIGDLEQQLDEEEAARQKLQLeKVTMDAKLKKIEEDLMviedqnaKLSKEKKQMEERISEFTTNLAEEEEKSK 1020
Cdd:pfam15905 116 EKTSLSASVASLEKQLLELTRVNELLKA-KFSEDGTQKKMSSLSM-------ELMKLRNKLEAKMKEVMAKQEGMEGKLQ 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1021 SLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELH---DQIAELQAQIAELRAQLAKKEEELQaalarie 1097
Cdd:pfam15905 188 VTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELScvsEQVEKYKLDIAQLEELLKEKNDEIE------- 260
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 319655760 1098 eeaALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDS 1158
Cdd:pfam15905 261 ---SLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTL 318
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
869-1324 |
1.58e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 869 EDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQn 948
Cdd:COG5278 75 ESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDE- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 949 IGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTK 1028
Cdd:COG5278 154 IRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1029 HETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQK 1108
Cdd:COG5278 234 LLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1109 SIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHE 1188
Cdd:COG5278 314 AAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVL 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1189 QMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTES 1268
Cdd:COG5278 394 AIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAA 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1269 ERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEE 1324
Cdd:COG5278 474 LAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAE 529
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
987-1178 |
1.66e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.12 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 987 IEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRK------EEKMRQELEKnRRKLEGD 1060
Cdd:COG1842 21 AEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLalekgrEDLAREALER-KAELEAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1061 STELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAA--QKSIREMEAQISELQEDLELEKAARNKAEKQR 1138
Cdd:COG1842 100 AEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAkaQEKVNEALSGIDSDDATSALERMEEKIEEMEA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 319655760 1139 R-DLGEELEAlktelEDTLDSTAAQQELRAKRETEVTQLKK 1178
Cdd:COG1842 180 RaEAAAELAA-----GDSLDDELAELEADSEVEDELAALKA 215
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
1060-1140 |
1.70e-03 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 42.62 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1060 DSTELHDQIAELQAQIAELRAQLakkeEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRR 1139
Cdd:COG0845 55 DPPDLQAALAQAQAQLAAAQAQL----ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLA 130
|
.
gi 319655760 1140 D 1140
Cdd:COG0845 131 Y 131
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1640-1883 |
1.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1640 ALKQLKKLQAQMKEQMREFEDLRLSRDESLNQAKENE-------RKIKSMEAEIMQLHEDLAAADRAKrqiqQERDELQD 1712
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEkeleevlREINEISSELPELREELEKLEKEV----KELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1713 EINSQNAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVNDR------LKKASLQAEQVTVELTAERSNSQRLEGLRSQ 1786
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkeLKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1787 LDRQNKDMKQKLQELEgavksKYKSTITALETKIQQLEEQLdSEMKERQQSTKQVRRVEKKLKEV--------LLQVEDE 1858
Cdd:PRK03918 319 LEEEINGIEERIKELE-----EKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLkkrltgltPEKLEKE 392
|
250 260
....*....|....*....|....*
gi 319655760 1859 RRNADQSKTETEKANIRLKQMKRQL 1883
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGEL 417
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1217-1423 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1217 ASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKV 1296
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1297 ESKSIKAAKDCSAVESQL--KDAQALLEEETRQKlAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMK 1374
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLgsESFSDFLDRLSALS-KIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 319655760 1375 KKIEQEaqsLESMEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQ 1423
Cdd:COG3883 171 AELEAQ---QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
937-1075 |
1.88e-03 |
|
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: 43.13 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 937 QFQSEKKKMQQNIGDLEQQLDEeeaARQKLqLEKVTMDAKLKKIEedlmVIEDQNAKLSKEKKQMEERIS---EFTTNLA 1013
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDG---LRRAL-EAKRKDPFKSIELD----SVDAKIESINDLVASINELIAkhnEITDNFE 389
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1014 EEEEKSKSL--QKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQI 1075
Cdd:pfam13166 390 EEKNKAKKKlrLHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQL 453
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
942-1301 |
1.89e-03 |
|
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: 43.50 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEE-------------RISEF 1008
Cdd:TIGR01612 1536 KNKFAKTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflKISDI 1615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1009 TTN----LAEEEEKSKSLQKLK-TKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHdqiaELQAQIAELRAQLA 1083
Cdd:TIGR01612 1616 KKKindcLKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVD 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1084 KKEEELQAALARIEEEAALKNAaqksiREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQ 1163
Cdd:TIGR01612 1692 QHKKNYEIGIIEKIKEIAIANK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELY 1766
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1164 ELrakreteVTQLKKTLEDEARAHEQmlseVRQKHNQAFEELNEQLEQSKRSKASVDKAKqALESER--NELQIELKSLS 1241
Cdd:TIGR01612 1767 NI-------IAGCLETVSKEPITYDE----IKNTRINAQNEFLKIIEIEKKSKSYLDDIE-AKEFDRiiNHFKKKLDHVN 1834
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1242 QS-KNDSENRRKKAESQLQELQ-VKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSI 1301
Cdd:TIGR01612 1835 DKfTKEYSKINEGFDDISKSIEnVKNSTDENLLFDILNKTKDAYAGIIGKKYYSYKDEAEKI 1896
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
986-1108 |
1.90e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 986 VIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKlegdstELH 1065
Cdd:PRK00409 503 IIEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEK------EAQ 576
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 319655760 1066 DQIAELQAQIAELRAQLAKKEEELQAALAR---IEEEAALKNAAQK 1108
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQKGGYASVKAhelIEARKRLNKANEK 622
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1167-1328 |
1.96e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1167 AKRETEVTQLKKTLEDEARAHEQmLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKND 1246
Cdd:PRK12704 47 AKKEAEAIKKEALLEAKEEIHKL-RNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1247 SENRRKKAEsqlqelqvkhteserqkhellDKVSKMQAELESLQGtVTKVESKSIKAAKdcsaVESQLK-DAQALL---E 1322
Cdd:PRK12704 126 LEKKEEELE---------------------ELIEEQLQELERISG-LTAEEAKEILLEK----VEEEARhEAAVLIkeiE 179
|
....*.
gi 319655760 1323 EETRQK 1328
Cdd:PRK12704 180 EEAKEE 185
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
945-1269 |
2.02e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 945 MQQNIGDLEQQLDEEEAArqklQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERIS-EFTTNLAE----EEEKS 1019
Cdd:PLN03229 460 LNEMIEKLKKEIDLEYTE----AVIAMGLQERLENLREEFSKANSQDQLMHPVLMEKIEKLKdEFNKRLSRapnyLSLKY 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KsLQKLKTKHETmiTDLEDRLRKEEKMRQELEKnRRKLEGDSTELHDQIAELQAQIAElraQLAKKEEELqaalarieeE 1099
Cdd:PLN03229 536 K-LDMLNEFSRA--KALSEKKSKAEKLKAEINK-KFKEVMDRPEIKEKMEALKAEVAS---SGASSGDEL---------D 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1100 AALKNAAQKSIREMEAQISELQEDLELEKA---ARNKAEKQRR---DLGEELEALKTELEDTLDSTAAQQELRAKreteV 1173
Cdd:PLN03229 600 DDLKEKVEKMKKEIELELAGVLKSMGLEVIgvtKKNKDTAEQTpppNLQEKIESLNEEINKKIERVIRSSDLKSK----I 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1174 TQLKktLEdearaheqmLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKk 1253
Cdd:PLN03229 676 ELLK--LE---------VAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLK- 743
|
330
....*....|....*.
gi 319655760 1254 aESQLQELQVKHTESE 1269
Cdd:PLN03229 744 -NDDDKEEDSKEDGSR 758
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
990-1287 |
2.09e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 990 QNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLE-----DRLRKEEKMRQ----ELEKNRRKLEGD 1060
Cdd:pfam02029 13 RRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeaflDRTAKREERRQkrlqEALERQKEFDPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1061 STELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRD 1140
Cdd:pfam02029 93 IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1141 LGEE----LEALKTELEDTLDSTAAQQELR-------AKRETEVTQLKKT-----------LEDEARAH-----EQMLSE 1193
Cdd:pfam02029 173 NFAKeevkDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTtkrrqgglsqsQEREEEAEvfleaEQKLEE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1194 VRQKHNQAFEELNEQLEQSKRskasvdkakqalesernELQIELKSLsqsKNDSENRRKKAESqlQELQVKHTESERQKH 1273
Cdd:pfam02029 253 LRRRRQEKESEEFEKLRQKQQ-----------------EAELELEEL---KKKREERRKLLEE--EEQRRKQEEAERKLR 310
|
330
....*....|....
gi 319655760 1274 ELLDKvSKMQAELE 1287
Cdd:pfam02029 311 EEEEK-RRMKEEIE 323
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1067-1219 |
2.28e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1067 QIAELQAQIAELRAQLAKKEEELQAAlariEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELE 1146
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLEAK----EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1147 ALKTELEdtldstaaqqelraKRETEVTQLKKTLEDEARAHEQMLSEVRQ-KHNQAFEELNEQLEQSKRSKASV 1219
Cdd:PRK12704 114 KKEKELE--------------QKQQELEKKEEELEELIEEQLQELERISGlTAEEAKEILLEKVEEEARHEAAV 173
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1054-1157 |
2.48e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1054 RRKLEGDST-----ELHDQIAELQAQIAELR----AQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDL 1124
Cdd:COG0542 401 RVRMEIDSKpeeldELERRLEQLEIEKEALKkeqdEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|...
gi 319655760 1125 ELEKAARNKAEKQRRDLGEELEALKTELEDTLD 1157
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEVT 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1257-1408 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1257 QLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEE-ETRQKLAISTR- 1334
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyEEQLGNVRNNKe 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 319655760 1335 LRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEER 1408
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
964-1124 |
2.62e-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: 41.05 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 964 QKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKhetmITDLEDRLRKE 1043
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNLKAR----LKVLEKELKDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1044 EKMRQELEKNRRKLEGDSTELHDQIAE---------------LQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQK 1108
Cdd:pfam13851 105 KWEHEVLEQRFEKVERERDELYDKFEAaiqdvqqktglknllLEKKLQALGETLEKKEAQLNEVLAAANLDPDALQAVTE 184
|
170
....*....|....*.
gi 319655760 1109 SIREMEAQISELQEDL 1124
Cdd:pfam13851 185 KLEDVLESKNQLIKDL 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1582-1883 |
2.70e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1582 EQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQIDLANKARDEALKQLKKLQAQMKEQMREFEDL 1661
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1662 RLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSLSSDERRRLEARIAQLEEE 1741
Cdd:COG4372 114 QEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEAN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1742 LEEEHLSVELVNDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKSKYKSTITALETKIQ 1821
Cdd:COG4372 194 RNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 319655760 1822 QLEEQLDSEMKERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQL 1883
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1572-1924 |
2.77e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1572 QFERDLQSRDEQGEEKRKQLVKQVREMEM-ELEDERKQR---AQAVSVRKKLELDLSELAAQIDLANKARDEALKQLkkl 1647
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETgKAEEARKAEeakKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEI--- 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1648 qAQMKEQMREFEDLRlsRDESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRqiqqerdelqdeinsqnaknslSSDE 1727
Cdd:PTZ00121 1157 -ARKAEDARKAEEAR--KAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK----------------------AEEE 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1728 RRRLEARIAQLEEeleeehlsvelvndrlkkaslQAEQVTvelTAERSNSQRLEGLRSQLDRQNKDMKqKLQELEGAVKS 1807
Cdd:PTZ00121 1212 RKAEEARKAEDAK---------------------KAEAVK---KAEEAKKDAEEAKKAEEERNNEEIR-KFEEARMAHFA 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1808 KYKSTITALET-KIQQLEEQLDSEMKERQQSTKQVRRVEKKLKEVllqveDERRNADQSKTETEKANIRLKQMKRQLEET 1886
Cdd:PTZ00121 1267 RRQAAIKAEEArKADELKKAEEKKKADEAKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350
....*....|....*....|....*....|....*...
gi 319655760 1887 EEEAARANASCRKLRRELEDATESASAMNREVSTLKNK 1924
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
864-1497 |
2.79e-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: 42.82 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 864 RQQQAEDQLKESEAKQK-QLNAEKLALQEQLQAETELCQEAEEMRSRLT-ARM--QEMEEVLHELESRLEEEEERvaQFQ 939
Cdd:pfam07111 77 RLEEEVRLLRETSLQQKmRLEAQAMELDALAVAEKAGQAEAEGLRAALAgAEMvrKNLEEGSQRELEEIQRLHQE--QLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQnakLSKEKKQMEERISefttnLAEEEEKS 1019
Cdd:pfam07111 155 SLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQ---LSKTQEELEAQVT-----LVESLRKY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1020 KSLQKLKTKHEtmitdledrlRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQaalARIEEE 1099
Cdd:pfam07111 227 VGEQVPPEVHS----------QTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELT---RKIQPS 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1100 AALKNAAQKSIREMEAQISELQEDLELEKAARnkaEKQRRDLGEELEALKTELEDTLDSTAAQQELrakretevtqLKKT 1179
Cdd:pfam07111 294 DSLEPEFPKKCRSLLNRWREKVFALMVQLKAQ---DLEHRDSVKQLRGQVAELQEQVTSQSQEQAI----------LQRA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1180 LEDEAraheqmlsevrqkhnqafeelnEQLEQSKRSKASvdkakqaleserneLQIELKSLSQSKNDSENRRKKAESQLQ 1259
Cdd:pfam07111 361 LQDKA----------------------AEVEVERMSAKG--------------LQMELSRAQEARRRQQQQTASAEEQLK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1260 ELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESK--SIKAAKDCSAVESQLKDAQALLEEETRQKLA-ISTRLR 1336
Cdd:pfam07111 405 FVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhTIKGLMARKVALAQLRQESCPPPPPAPPVDAdLSLELE 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1337 QLEDEQNNLKEMLEEE----EESKKNVEKQLHTAQAQLAEMKKKIEQE-----------AQSLESMEDGKKKLQREVESV 1401
Cdd:pfam07111 485 QLREERNRLDAELQLSahliQQEVGRAREQGEAERQQLSEVAQQLEQElqraqeslasvGQQLEVARQGQQESTEEAASL 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1402 LQQLEERNASY-----DKLDKTKTRLQRELDDVlvdqghlRQTVQELERKQKKFDQMLAEEKSISTKYAE---ERDRAEA 1473
Cdd:pfam07111 565 RQELTQQQEIYgqalqEKVAEVETRLREQLSDT-------KRRLNEARREQAKAVVSLRQIQHRATQEKErnqELRRLQD 637
|
650 660
....*....|....*....|....
gi 319655760 1474 EAREKETKSltLARELEAMTDLKN 1497
Cdd:pfam07111 638 EARKEEGQR--LARRVQELERDKN 659
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1585-1859 |
2.80e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1585 EEKRKQLVKQVREM-EMELEDeRKQRAQAVSVRKKLELdLSELAAQIDLANKARdEALKQLKKLQAQMKEQmrEFEDLRL 1663
Cdd:PRK05771 15 KSYKDEVLEALHELgVVHIED-LKEELSNERLRKLRSL-LTKLSEALDKLRSYL-PKLNPLREEKKKVSVK--SLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1664 SRDESLNQAkenERKIKSMEAEIMQLhedlaaaDRAKRQIQQERDELQ-------DEINSQNAKN------SLSSDERRR 1730
Cdd:PRK05771 90 DVEEELEKI---EKEIKELEEEISEL-------ENEIKELEQEIERLEpwgnfdlDLSLLLGFKYvsvfvgTVPEDKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1731 LEARIAQLEEELEEEH------------LSVELVNDRLKKASLQAeqvtVELTAERSNSQRLEGLRSQLDRQNKDMKQKL 1798
Cdd:PRK05771 160 LKLESDVENVEYISTDkgyvyvvvvvlkELSDEVEEELKKLGFER----LELEEEGTPSELIREIKEELEEIEKERESLL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 319655760 1799 QELEgAVKSKYKSTITALETKIQQLEEQLdsEMKERQQSTKQVRRVE--------KKLKEVLLQVEDER 1859
Cdd:PRK05771 236 EELK-ELAKKYLEELLALYEYLEIELERA--EALSKFLKTDKTFAIEgwvpedrvKKLKELIDKATGGS 301
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1074-1408 |
2.90e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1074 QIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIremeaqISELQE-------DLELEKAARNKAEKQRR------D 1140
Cdd:PTZ00108 1000 LLGKLERELARLSNKVRFIKHVINGELVITNAKKKDL------VKELKKlgyvrfkDIIKKKSEKITAEEEEGaeeddeA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1141 LGEELEALKTELED------------TLDSTAAQQELRAKRETEVTQLKKTledearAHEQMLSEVRQKHNQAFEELNEQ 1208
Cdd:PTZ00108 1074 DDEDDEEELGAAVSydyllsmpiwslTKEKVEKLNAELEKKEKELEKLKNT------TPKDMWLEDLDKFEEALEEQEEV 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1209 LEQS--KRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAEL 1286
Cdd:PTZ00108 1148 EEKEiaKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQED 1227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1287 ESLQGTVTKVES----KSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLED---EQNNLKEMLEEEEESKKNV 1359
Cdd:PTZ00108 1228 DEEQKTKPKKSSvkrlKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPpppSKRPDGESNGGSKPSSPTK 1307
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 319655760 1360 EKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEER 1408
Cdd:PTZ00108 1308 KKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQASASQSSRLLRRP 1356
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
862-1209 |
3.06e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 42.63 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 862 KERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEA-EEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQS 940
Cdd:pfam15818 20 REAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAmAVFKKQLQMKMCALEEEKGKYQLATEIKEKEIEGLKE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 941 EKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQ---------------------NAKLSKEKK 999
Cdd:pfam15818 100 TLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQfglvkenhgkleqnvqeaiqlNKRLSALNK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1000 QMEERISEFTTNL---AEEEEKSKSLQKLKTKHETMITDLEDRLRKE--EKMRQELEKNRRKLEGDS---TELHDQIAEL 1071
Cdd:pfam15818 180 KQESEICSLKKELkkvTSDLIKSKVTCQYKMGEENINLTIKEQKFQElqERLNMELELNKKINEEIThiqEEKQDIIISF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1072 QaQIAELRAQLAKKEEELQAALarieeeAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTE 1151
Cdd:pfam15818 260 Q-HMQQLLQQQTQANTEMEAEL------KALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGE 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1152 LEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQKHNQAFEELNEQL 1209
Cdd:pfam15818 333 INEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENSEMSTEKSENL 390
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
935-1306 |
3.28e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 42.40 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 935 VAQFQSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKvtmDAKLKKIEEDLMVIEDQ----NAKLSKEKKQMEERISEFTT 1010
Cdd:pfam03528 10 VAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAK---EEDLKRQNAVLQEAQVEldalQNQLALARAEMENIKAVATV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1011 NlaeEEEKSKSLQKLKTKHETMITDLEDRLRkeEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLA--KKEEE 1088
Cdd:pfam03528 87 S---ENTKQEAIDEVKSQWQEEVASLQAIMK--ETVREYEVQFHRRLEQERAQWNQYRESAEREIADLRRRLSegQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1089 LQAALARIEEEAalkNAAQKSIREMEAQISELQEDL-ELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRA 1167
Cdd:pfam03528 162 LEDEMKKAQEDA---EKLRSVVMPMEKEIAALKAKLtEAEDKIKELEASKMKELNHYLEAEKSCRTDLEMYVAVLNTQKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1168 KRETEVTQLKKTLEDEARAHEQMlsevRQKHNQ---AFEELNEQLEQSKR-SKASVDKAKQALESERNELQIELKSLSQS 1243
Cdd:pfam03528 239 VLQEDAEKLRKELHEVCHLLEQE----RQQHNQlkhTWQKANDQFLESQRlLMRDMQRMESVLTSEQLRQVEEIKKKDQE 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1244 KNDSENRRKKAE---SQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKD 1306
Cdd:pfam03528 315 EHKRARTHKEKEtlkSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLGAGD 380
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
939-1286 |
3.71e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.98 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEE-----------------DLMVIEDQNAKLSKEKKQM 1001
Cdd:pfam05622 6 QEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESgddsgtpggkkylllqkQLEQLQEENFRLETARDDY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1002 EERISEFTTNLAEEEEKSKSLQKLkTKHETMITDLEDRLR----KEEKMRQELEKNRRKLEgDSTELHDQIAELQAQIAE 1077
Cdd:pfam05622 86 RIKCEELEKEVLELQHRNEELTSL-AEEAQALKDEMDILRessdKVKKLEATVETYKKKLE-DLGDLRRQVKLLEERNAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1078 LRAQLAKKEEELQAAlarieeeaalkNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELE---- 1153
Cdd:pfam05622 164 YMQRTLQLEEELKKA-----------NALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKErlii 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1154 --DTLDST-----AAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVRQK------------------HNQAFEELNEQ 1208
Cdd:pfam05622 233 erDTLRETneelrCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKlirlqhenkmlrlgqegsYRERLTELQQL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1209 LEQSKRSKASVD----KAKQ---ALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSK 1281
Cdd:pfam05622 313 LEDANRRKNELEtqnrLANQrilELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPK 392
|
....*
gi 319655760 1282 MQAEL 1286
Cdd:pfam05622 393 QDSNL 397
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
989-1189 |
3.79e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 989 DQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHEtmitdlEDRLRKEEKMRQELEKNRRKLEGDSTELHDQI 1068
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ------EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1069 AELQAQIAELRAQLAKKEEELQAalarIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEAL 1148
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKK----KAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 319655760 1149 KteledtlDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQ 1189
Cdd:PRK09510 223 A-------KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1667-1883 |
3.79e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.13 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1667 ESLNQAKENERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAK--NSLSSDErrrLEARIAQLEEELEE 1744
Cdd:pfam12795 20 QDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEilASLSLEE---LEQRLLQTSAQLQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1745 EHLSVELVNDRLKKASLQAEQVTVELTaerSNSQRLEGLRSQLdrqnKDMKQKLQELEGAVKSKYKSTITALETKIQQLE 1824
Cdd:pfam12795 97 LQNQLAQLNSQLIELQTRPERAQQQLS---EARQRLQQIRNRL----NGPAPPGEPLSEAQRWALQAELAALKAQIDMLE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 319655760 1825 EQLDS-------EMKERQQSTKQVRRVEKKLkEVLLQVEDERRNAdqsktETEKANIRLKQMKRQL 1883
Cdd:pfam12795 170 QELLSnnnrqdlLKARRDLLTLRIQRLEQQL-QALQELLNEKRLQ-----EAEQAVAQTEQLAEEA 229
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1365-1790 |
3.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1365 TAQAQLAEMKKKIEQEAQSLESMEDgKKKLQREVESVLQQleERNASYDKLDKTKTRLQRelddvlvdQGHLRQTVQELE 1444
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMAR-ELAELNEAESDLEQ--DYQAASDHLNLVQTALRQ--------QEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1445 RKQKKfdqmLAEEKSISTKYAEERDRAEAEAREKETksltlareleamtdlknELERVNKQLKTEMEDLVSSKDDAGK-- 1522
Cdd:PRK04863 359 ELEER----LEEQNEVVEEADEQQEENEARAEAAEE-----------------EVDELKSQLADYQQALDVQQTRAIQyq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1523 -SVHELERAKR---GMEQQLEEMKTQLEELEDELQLTEDAKLRLEVNM---QALKAQFERDLQS-RDEQGEEKRKQLVKQ 1594
Cdd:PRK04863 418 qAVQALERAKQlcgLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAYQLvRKIAGEVSRSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1595 VREMEMELEDERKQRAQAVSVRKKLEldlselaaqidlankardeALKQLKKLQAQMKEQMREFEDlRLSRDesLNQAKE 1674
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLS-------------------ELEQRLRQQQRAERLLAEFCK-RLGKN--LDDEDE 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1675 NERKIKSMEAEIMQLHEDLAAADRAKRQIQQERDELQDEInsqnAKNSLSSDERRRLEARIAQLEEELEEEHLSVELVND 1754
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI----QRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
410 420 430
....*....|....*....|....*....|....*.
gi 319655760 1755 RLKKaslQAEQVtVELTAERSnsqRLEGLRSQLDRQ 1790
Cdd:PRK04863 632 YMQQ---LLERE-RELTVERD---ELAARKQALDEE 660
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
860-1124 |
4.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 860 KMKERQQQAEDqLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEvlhelesRLEEEEERVAQFQ 939
Cdd:PRK02224 493 EVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA-------EAEEKREAAAEAE 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 940 SEKKKMQQNIGDLEQQLDEEEAARQKLQlekvtmdaklkKIEEDLMVIEDQNAKLskekkqmeERISEFTTNLAE-EEEK 1018
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIESLE-----------RIRTLLAAIADAEDEI--------ERLREKREALAElNDER 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDL-EDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKE---EELQAALA 1094
Cdd:PRK02224 626 RERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEelrERREALEN 705
|
250 260 270
....*....|....*....|....*....|
gi 319655760 1095 RIEEEAALKNAAqksiREMEAQISELQEDL 1124
Cdd:PRK02224 706 RVEALEALYDEA----EELESMYGDLRAEL 731
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
998-1149 |
4.21e-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: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 998 KKQMEERISEFTTNLAEEEEKSKSLqklkTKHETMITDLEDRLRK-----EEKMRQELEKNRRKLEGDSTEL---HDQIA 1069
Cdd:smart00787 139 MKLLEGLKEGLDENLEGLKEDYKLL----MKELELLNSIKPKLRDrkdalEEELRQLKQLEDELEDCDPTELdraKEKLK 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1070 ELQAQIAELRAQLAKKEEELQAALARIEEEAALKNaaqksirEMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALK 1149
Cdd:smart00787 215 KLLQEIMIKVKKLEELEEELQELESKIEDLTNKKS-------ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
942-1433 |
4.65e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 942 KKKMQQNIGDLEQQLDEEEA-------ARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLsKEKKQMEERISEFTTNLAE 1014
Cdd:PTZ00440 445 KKKYDEKINELKKSINQLKTlisimksFYDLIISEKDSMDSKEKKESSDSNYQEKVDELL-QIINSIKEKNNIVNNNFKN 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1015 EEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQElEKNRRKLEGD-------STELHDQIAELQAQIAELRAQLAKKEE 1087
Cdd:PTZ00440 524 IEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKD-EKLKRSMKNDiknkikyIEENVDHIKDIISLNDEIDNIIQQIEE 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1088 ELQAALARIEEEAALKNAAQKSI---------REMEAQISEL------QEDLELEKAARNKAEKQRRDLGEELEALKTEL 1152
Cdd:PTZ00440 603 LINEALFNKEKFINEKNDLQEKVkyilnkfykGDLQELLDELshflddHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMK 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1153 EDTLDSTAaqqELRAKRETEVTQLKKTLEDEARAH-EQMLSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERN 1231
Cdd:PTZ00440 683 SDNIDNII---KNLKKELQNLLSLKENIIKKQLNNiEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKN 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1232 ELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLQGTVTKVESKSIKaakdcsave 1311
Cdd:PTZ00440 760 EFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEK--------- 830
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1312 sqlKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLEEEEESKKNVEKQLHTAQaQLAEMKKKIEQEAQSLESMEDGK 1391
Cdd:PTZ00440 831 ---NDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKDIENMNKNINIIK-TLNIAINRSNSNKQLVEHLLNNK 906
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 319655760 1392 KKLQREVESVLQQLEERN--ASYDK------LDKTKTRLQRELDDVLVDQ 1433
Cdd:PTZ00440 907 IDLKNKLEQHMKIINTDNiiQKNEKlnllnnLNKEKEKIEKQLSDTKINN 956
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1582-1736 |
5.93e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 5.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1582 EQGEEKRKQLVKQVREMEMELEDERKQRAQAVSVRKKLELDLSELAAQI-DLANKAR-----------DEALKQLKKLQA 1649
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAkKLEEKAQaaltkgneelaREALAEKKSLEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1650 QMKEQMREFEDLRLSRDESLNQAKENERKIKSMEAEIMQLHEDLAAAdRAKRQIQQERDelqdeinsqNAKNSLSSDERR 1729
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA-KAQEAVQTSLG---------SLSTSSATDSFE 167
|
....*..
gi 319655760 1730 RLEARIA 1736
Cdd:pfam04012 168 RIEEKIE 174
|
|
| Cortex-I_coil |
pfam09304 |
Cortexillin I, coiled coil; Members of this family are predominantly found in the ... |
1051-1157 |
6.14e-03 |
|
Cortexillin I, coiled coil; Members of this family are predominantly found in the actin-bundling protein Cortexillin I from Dictyostelium discoideum. They adopt a structure consisting of an 18-heptad-repeat alpha-helical coiled-coil, and are a prerequisite for the assembly of Cortexillin I.
Pssm-ID: 312712 [Multi-domain] Cd Length: 107 Bit Score: 38.45 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1051 EKNRRKLEGDSTELHDQIAELQAQIAE---LRAQLAKKEEELQAALARIEEEAALKNaaqKSIREMEAQISELQEDLELE 1127
Cdd:pfam09304 1 KEEKERLEASKNSLANKLAGLENSLESektSREQLIKQKDELESLLASLEQENAERE---KRLRELEAKLDEALKNLELE 77
|
90 100 110
....*....|....*....|....*....|
gi 319655760 1128 KAARNKAEKQRRDLGEELEALKTELEDTLD 1157
Cdd:pfam09304 78 KLARMELESRLSKTEKDKAILELKLAEALD 107
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1195-1459 |
6.22e-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: 41.55 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1195 RQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESERQKHE 1274
Cdd:pfam05667 246 TKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVET 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1275 LLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKlaistrlRQLEDEQNNlkemleeeee 1354
Cdd:pfam05667 326 EEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQN-------EELEKQYKV---------- 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1355 sKKNVEKQLHTAQAQLAEMKKKIEQEAQSLESMEDGKKKLQREVESVLQQLEERNAsyDKLDKTKTRLQ--RELDDvlvd 1432
Cdd:pfam05667 389 -KKKTLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRALKEAKS--NKEDESQRKLEeiKELRE---- 461
|
250 260
....*....|....*....|....*..
gi 319655760 1433 qgHLRQTVQELERKQKKFDQMLAEEKS 1459
Cdd:pfam05667 462 --KIKEVAEEAKQKEELYKQLVAEYER 486
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
939-1141 |
6.53e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.95 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEdlmviedqNAKLSKEKKQMEErisefttnlaEEEEK 1018
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEE--------AAKQAALKQKQAE----------EAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 SKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQiAELRAQLAKKEEELQAALARIEE 1098
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAA-AEAKKKAEAEAKKKAAAEAKKKA 219
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 319655760 1099 EAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDL 1141
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1219-1399 |
6.59e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1219 VDKAKQALESERNELQIELKSLsqskndsENRRKKAESQLQELQVKHTESERQKHELLDKVSKMQAELESLqgtvtkves 1298
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASL-------EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL--------- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1299 ksikaakdcsaVESQLKDAQALLEEETRQKLAISTRLRQLEDEQnnlkemleeeeeskknvekqlHTAQA--QLAEMKKK 1376
Cdd:PRK00409 568 -----------LEEAEKEAQQAIKEAKKEADEIIKELRQLQKGG---------------------YASVKahELIEARKR 615
|
170 180
....*....|....*....|...
gi 319655760 1377 IEQEAQSLESMEDGKKKLQREVE 1399
Cdd:PRK00409 616 LNKANEKKEKKKKKQKEKQEELK 638
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
859-1215 |
6.63e-03 |
|
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: 41.57 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 859 VKMKERQQQAEDQLKESEAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQF 938
Cdd:TIGR00606 804 VERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRR 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 939 QSEKKKMQQNIGDLEQQLDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEK 1018
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1019 -SKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAelraqLAKKEEELQaalaRIE 1097
Cdd:TIGR00606 964 iQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLT-----LRKRENELK----EVE 1034
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1098 EEAA--LKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQ 1175
Cdd:TIGR00606 1035 EELKqhLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTE 1114
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 319655760 1176 LkkTLEDEARAHEQMLSEVRQKHNQAFEELNEQLEQSKRS 1215
Cdd:TIGR00606 1115 L--VNKDLDIYYKTLDQAIMKFHSMKMEEINKIIRDLWRS 1152
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
1071-1155 |
6.81e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.95 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1071 LQAQIAELRA---QLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKAARNKAEKQRRDLGEELEA 1147
Cdd:pfam05266 90 PQSRINKLLSlkdRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEK 169
|
....*...
gi 319655760 1148 LKTELEDT 1155
Cdd:pfam05266 170 LEQEIQDV 177
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1683-1827 |
7.15e-03 |
|
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: 40.87 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1683 EAEIMQLHEDLAAADRAKRQIQQERDELQDEINSQNAKNSL---SSDERRRLEARIAQLEEELEEEHLSVELVNDRLKKA 1759
Cdd:pfam00529 57 QAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDydgATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIG 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 319655760 1760 SLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVkskyKSTITALETKIQQLEEQL 1827
Cdd:pfam00529 137 GISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEV----RSELSGAQLQIAEAEAEL 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
876-1232 |
7.17e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 876 EAKQKQLNAEKLALQEQLQAETELCQEAEEMRSRLTARMQEMEEVLHELESRLEEEEERVAQFQSEKKKMQQNIGDLEQQ 955
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 956 LDEEEAARQKLQLEKVTMDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITD 1035
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1036 LEDRLRKEEKMRQELEKNRRKLEGDSTELHDQIAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEA 1115
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1116 QISELQEDLELEKAARNKAEKQRRDLGEELEALKTELEDTLDSTAAQQELRAKRETEVTQLKKTLEDEARAHEQMLSEVR 1195
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350
....*....|....*....|....*....|....*..
gi 319655760 1196 QKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNE 1232
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
948-1153 |
7.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 948 NIGDLEQQLDEEEAARQKLQLEKVT-MDAKLKKIEEDLMVIEDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLK 1026
Cdd:PRK05771 51 LLTKLSEALDKLRSYLPKLNPLREEkKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPWG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1027 T--------KHETMITDLEDRLRKEEKMRQELEKNRRKLEGDST-ELHDQIAelqaqIAELRAQLAKKEEELQAALARIE 1097
Cdd:PRK05771 131 NfdldlsllLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTdKGYVYVV-----VVVLKELSDEVEEELKKLGFERL 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 319655760 1098 EEAALKNAAQKsIREMEAQISELQEDLE-LEKAARNKAEKQRRDLGEELEALKTELE 1153
Cdd:PRK05771 206 ELEEEGTPSEL-IREIKEELEEIEKEREsLLEELKELAKKYLEELLALYEYLEIELE 261
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1753-1927 |
7.79e-03 |
|
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: 41.20 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1753 NDRLKKASLQAEQVTVELTAERSNSQRLEGLRSQLDRQNKDMKQKLQELEGAVKskykstitALETKIQQLEEQLDSEMK 1832
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY--------ALANEISRLEQQKQILRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1833 ERQQSTKQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQLEETEEEAARANASCRKLRRELEDATESAS 1912
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170
....*....|....*
gi 319655760 1913 AMNREVSTLKNKLRR 1927
Cdd:TIGR02168 390 QLELQIASLNNEIER 404
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1692-1882 |
8.19e-03 |
|
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: 41.36 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1692 DLAAADRAKRQIQQERDELQDEINSQNAKnsLSSDERRRLEAriaqleeeleeehlsvelvNDRLKKASLQAEQ--VTVE 1769
Cdd:NF012221 1563 DKERAEADRQRLEQEKQQQLAAISGSQSQ--LESTDQNALET-------------------NGQAQRDAILEESraVTKE 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1770 LTaerSNSQRLEGLRSQLDRQNKD-----------MKQKLQELEGAVKSKYKSTITALETKIQQLEEQLDSEMKerqQST 1838
Cdd:NF012221 1622 LT---TLAQGLDALDSQATYAGESgdqwrnpfaggLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVA---KSE 1695
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 319655760 1839 KQVRRVEKKLKEVLLQVEDERRNADQSKTETEKANIRLKQMKRQ 1882
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESD 1739
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
988-1148 |
8.28e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 988 EDQNAKLSKEKKQMEERISEFTTNLAEEEEKSKSLQKLKTKHETMITDLEDRLRKEEKMRQELEKNRRKLEGdSTELHDQ 1067
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAE-IDSIIPD 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1068 IAELQAQIAELRAQLAKKEEELQAALARIEEEAALKNAAQKSIREMEAQISELQEDLELEKaarnKAEKQRRDLGEELEA 1147
Cdd:PRK01156 669 LKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMK----KIKKAIGDLKRLREA 744
|
.
gi 319655760 1148 L 1148
Cdd:PRK01156 745 F 745
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1023-1096 |
8.95e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.82 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1023 QKLKTKHETMITD----LEDRLRKEEKMRQELeKNRRKL-----------EGDSTELHDQIAELQAQIAELRAQLAKKEE 1087
Cdd:PRK05431 16 EALAKRGFPLDVDelleLDEERRELQTELEEL-QAERNAlskeigqakrkGEDAEALIAEVKELKEEIKALEAELDELEA 94
|
....*....
gi 319655760 1088 ELQAALARI 1096
Cdd:PRK05431 95 ELEELLLRI 103
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1191-1514 |
9.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1191 LSEVRQKHNQAFEELNEQLEQSKRSKASVDKAKQALESERNELQIELKSLSQSKNDSENRRKKAESQLQELQVKHTESER 1270
Cdd:COG4372 15 LFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1271 QKHELLDKVSKMQAELESLQGTVTKVESKSIKAAKDCSAVESQLKDAQALLEEETRQKLAISTRLRQLEDEQNNLKEMLE 1350
Cdd:COG4372 95 ELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1351 EEEESKKNVEKQLHTAQAQLAEMKKKIEQEAQSLEsmEDGKKKLQREVESVLQQLEERNASYDKLDKTKTRLQRELDDVL 1430
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI--ESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 319655760 1431 VDQGHLRQTVQELERKQKKFDQMLAEEKSISTKYAEERDRAEAEAREKETKSLTLARELEAMTDLKNELERVNKQLKTEM 1510
Cdd:COG4372 253 EEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELAL 332
|
....
gi 319655760 1511 EDLV 1514
Cdd:COG4372 333 AILL 336
|
|
| |
