|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-786 |
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: 1344.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGLL 356
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 357 PEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 436
Cdd:cd14930 241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 437 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 516
Cdd:cd14930 321 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 517 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLH 596
Cdd:cd14930 401 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 597 YAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 676
Cdd:cd14930 481 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 677 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 756
Cdd:cd14930 561 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 148690794 757 DGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14930 641 DGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-786 |
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: 1291.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETLESLRVLGL 355
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 435
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 436 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 515
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 516 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 595
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 596 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 673
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 674 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 753
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 148690794 754 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
863-1943 |
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: 1280.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 863 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 942
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1022
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1102
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1183 LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR 1262
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1263 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEE 1342
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1343 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1422
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1423 LAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1502
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1503 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1582
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1583 TVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL 1662
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1663 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1742
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1743 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAG 1822
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1823 ARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLE 1902
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 148690794 1903 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1943
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
117-786 |
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: 1276.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQETLESLRVL 353
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 433
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 434 ADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 513
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 514 EEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK-FQRPRNLRDQADF 592
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 593 SVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMFRTVGQLY 672
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 673 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 752
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 148690794 753 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-786 |
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: 1167.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 272
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 273 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLR 351
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 431
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 591
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQ 670
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 671 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 750
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 751 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14932 641 IPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
117-786 |
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: 1131.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 267
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 268 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 346
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 347 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 426
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 427 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 506
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 507 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPrNL 586
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 666
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 148690794 747 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
117-786 |
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: 1114.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGL 355
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 435
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 436 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 515
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 516 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 595
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 596 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYK 673
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 674 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 753
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 148690794 754 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
117-786 |
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: 1099.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVLGL 355
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 435
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 436 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 515
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 516 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 595
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 596 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 673
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 674 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 753
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 148690794 754 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
117-786 |
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: 1096.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG----VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 272
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 273 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLR 351
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 431
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 591
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQL 671
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 672 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 751
Cdd:cd15896 561 YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 640
|
650 660 670
....*....|....*....|....*....|....*
gi 148690794 752 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd15896 641 PKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
106-786 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1069.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 106 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 185
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 186 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGS----GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 266 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELF 343
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiDGiDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 344 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 423
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 424 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 503
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 504 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 583
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 584 RnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGPPGGRPRRG 663
Cdd:pfam00063 475 R-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 664 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 743
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 148690794 744 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
98-798 |
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: 996.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 98 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 177
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 178 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpGELERQLLQANPILEAFGNAKTVKNDNS 257
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 258 SRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 336
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTvD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 337 GQE-RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNT-AAQKLCRLLGLGVTDFSRALL 414
Cdd:smart00242 235 GIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 415 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCIN 494
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 495 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQ 574
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 575 GSHPKFQRPRNlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGdg 654
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS-----NAGSKK-- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 655 ppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:smart00242 543 ---------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 735 LFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 798
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
96-1173 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 96 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 175
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 176 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkEPGVPGELERQLLQANPILEAFGNAKTVKND 255
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-----STVEISSIEKQILATNPILEAFGNAKTVRND 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 256 NSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS 335
Cdd:COG5022 214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 336 PGQ--ERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 413
Cdd:COG5022 294 IDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 414 LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCI 493
Cdd:COG5022 373 VKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 494 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKSFVEKVAQ- 572
Cdd:COG5022 452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQr 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 573 -EQGSHPKFQRPRnLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVgleqvssl 651
Cdd:COG5022 530 lNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 652 gdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP 731
Cdd:COG5022 600 ---------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 732 NRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVS 807
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 808 FQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKVQ--ELQQQ 885
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQktIKREK 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 886 SAREvgelqgrvaQLEEERTRLAEQLRAEAelcSEAEEtrarlaARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ 965
Cdd:COG5022 831 KLRE---------TEEVEFSLKAEVLIQKF---GRSLK------AKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 966 HIQELEShleaeegarQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERRLLEERlaEFSSQAAEEEEKVKSLNKLR 1044
Cdd:COG5022 893 SISSLKL---------VNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLH 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1045 L---KYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK--QRAEELLAQLGRKEDELQAALLRAEEEGG 1119
Cdd:COG5022 961 EvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSASKIISSEST 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1120 ARAQlLKSLREAQAGLAEAQEDLEaervARAKAEKQRRDLGEELEALRGELEDT 1173
Cdd:COG5022 1041 ELSI-LKPLQKLKGLLLLENNQLQ----ARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
117-786 |
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: 839.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RELFQETLES 349
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 350 LRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNT--DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 506
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 507 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 586
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppggrprrgmfr 666
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 tvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd00124 519 -----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 148690794 747 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
117-786 |
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: 773.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 270
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 271 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 348
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 349 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 428
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 429 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 507
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 508 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR-- 584
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 585 -NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRG 663
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 664 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 743
Cdd:cd14927 553 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 148690794 744 EILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14927 633 RILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
118-786 |
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: 758.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 353
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQA 590
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 591 D--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 668
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 669 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd14913 550 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 148690794 749 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14913 630 SAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
117-786 |
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: 739.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 354
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 434
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 435 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 514
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 515 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLR---DQA 590
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 591 DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRRGMFRTVGQ 670
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKGGGFATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 671 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 750
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 751 IpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14909 632 I-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
117-786 |
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: 707.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQETLESLRVLG 354
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 434
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 435 DFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 514
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 515 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD---QA 590
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGkgpEA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 591 DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRRGMFRTVGQ 670
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRGSSFMTVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 671 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 750
Cdd:cd14934 544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 751 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14934 624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
118-786 |
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: 697.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGrkEPGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQETLESLRVLG 354
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 434
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 435 DFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 513
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 514 EEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK--FQRPRnlRDQAD 591
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR--FSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrgmfRTVGQL 671
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------------KTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 672 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 751
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....*
gi 148690794 752 PKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01380 596 WLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
117-786 |
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: 695.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA---LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGL 355
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 435
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 436 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 514
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 515 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD--QAD 591
Cdd:cd14929 396 EYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKkfEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrgmFRTVGQL 671
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS---FQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 672 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 751
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 752 PKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14929 627 PKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
118-786 |
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: 691.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 353
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD-- 588
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGkp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 668
Cdd:cd14917 476 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 669 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd14917 550 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 148690794 749 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14917 630 AAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
118-786 |
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: 673.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 274
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 275 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 352
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 431
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 510
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 511 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNL--R 587
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVkgK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 588 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRprrgmFRT 667
Cdd:cd14916 476 QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-----FQT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 668 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 747
Cdd:cd14916 551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 148690794 748 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14916 631 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
119-786 |
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: 671.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 119 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 198
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 199 GAGKTENTKKVIQYLAHVA-SSPKGRKEPG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAvTGEKKKEESGkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 354
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 433
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 434 ADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 512
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 513 QEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQAD 591
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 --FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRGMFRTVG 669
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 670 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 749
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 148690794 750 AIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
118-786 |
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: 666.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 273
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 274 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 351
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 430
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 431 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 509
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRD 588
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 QAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRGMFR 666
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKGSSFQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14912 553 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 148690794 747 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14912 633 NASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
118-786 |
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: 661.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 273
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 274 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 351
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 430
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 431 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 509
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD 588
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 --QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRRGMFR 666
Cdd:cd14910 476 kvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 148690794 747 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14910 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
118-786 |
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: 660.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGRKE--PG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 274
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 275 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQETL 347
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 348 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 426
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 427 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 505
Cdd:cd14923 316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 506 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPR 584
Cdd:cd14923 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 585 NLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPGGRPRR 662
Cdd:cd14923 471 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 663 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 742
Cdd:cd14923 547 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 148690794 743 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14923 627 YRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
118-786 |
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: 656.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 273
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 274 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 351
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 430
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 431 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 509
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD 588
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 QAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRRGMFR 666
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14915 551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 148690794 747 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14915 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
118-786 |
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: 634.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 274
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 275 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESLRV 352
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDYVQKAQ 429
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 430 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFnhTMF 509
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGSHPKFQRPRNL 586
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggrprrGM 664
Cdd:cd01378 468 FElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK------------KR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 665 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 744
Cdd:cd01378 531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 148690794 745 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
118-786 |
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: 633.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 277
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 278 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVL 353
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKK-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 512
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 513 QEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADF 592
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 593 SVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLY 672
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGKPTVGDTF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 673 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 752
Cdd:cd14883 548 KHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARS 627
|
650 660 670
....*....|....*....|....*....|....
gi 148690794 753 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14883 628 ADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
118-786 |
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: 624.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 277
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 278 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLESLRVLGL 355
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 435
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 436 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 515
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 516 YQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRdqadFSVL 595
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA----FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 596 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKES 675
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 676 LSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGF 755
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SAS 616
|
650 660 670
....*....|....*....|....*....|.
gi 148690794 756 MDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01383 617 QDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
117-786 |
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: 594.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVAsspkGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQHS-----WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQETLESLRVLG 354
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKK--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 510
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 511 LEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlRDQ 589
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS-DLN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 590 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPrrgmfrTVG 669
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP------TLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 670 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 749
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 148690794 750 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01381 612 IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
117-786 |
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: 591.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGRKEPgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQETLESLRVL 353
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGRD-YVQKAQ 429
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTPDgIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 430 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 509
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQ 589
Cdd:cd01384 394 KMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 590 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPRRGM-FRTV 668
Cdd:cd01384 469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTSSSSkFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 669 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 148690794 749 NAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 786
Cdd:cd01384 613 EV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
117-786 |
1.58e-180 |
|
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: 562.64 E-value: 1.58e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETLESLRVLGL 355
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 356 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRIKVGRDYVQ 426
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGGAKGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 427 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 504
Cdd:cd01382 299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 505 NHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPR 584
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 585 --------NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQVSSLGDGPP 656
Cdd:cd01382 452 ksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFESSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 657 GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 736
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 148690794 737 QEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
117-786 |
9.49e-177 |
|
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: 552.84 E-value: 9.49e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 191
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 192 ILCTGESGAGKTENTKKVIQYLAHVAS-----SPKGRKEPGVPGE-----LERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgASGEGEAASEAIEqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 262 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 340
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 341 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 417
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 418 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 497
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 498 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 567
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 568 ------EKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 641
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 642 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 721
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 722 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
117-786 |
1.46e-172 |
|
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: 540.90 E-value: 1.46e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL----------FQET 346
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvddvadFEEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 347 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCR---LLGLGVTDFSRALLTPRIKV-GR 422
Cdd:cd14872 222 VLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 423 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 502
Cdd:cd14872 302 DPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 503 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQR 582
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 583 PRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdgppggrPRR 662
Cdd:cd14872 459 AEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------------DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 663 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 742
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 148690794 743 YEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14872 601 YRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
118-786 |
1.34e-166 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 524.15 E-value: 1.34e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 277
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR--------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 278 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELFQETLESLR 351
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVL----KKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 505
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 506 HTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPkFQRPR 584
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 585 nlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgppggrprrgm 664
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 665 frTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 744
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 148690794 745 ILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 786
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
117-786 |
1.94e-164 |
|
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: 518.48 E-value: 1.94e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE--------RELFQETL 347
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 348 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 503
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 504 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 583
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 584 rnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgppggrprrg 663
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 664 mfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 743
Cdd:cd14897 522 ------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRY 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 148690794 744 EILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 786
Cdd:cd14897 596 KEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
117-786 |
9.50e-164 |
|
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: 517.38 E-value: 9.50e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 276
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQETLESLRVLG 354
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 431
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD 591
Cdd:cd01387 391 EQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--MPLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 592 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRGmfRTVGQL 671
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT--PTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 672 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 751
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 752 PKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 786
Cdd:cd01387 623 PRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
117-786 |
3.80e-163 |
|
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: 515.87 E-value: 3.80e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 353
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 431
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 511
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 512 EQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGSHPKFQR----PRNLR 587
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 588 DQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMfRT 667
Cdd:cd14903 463 TQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT-TT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 668 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 747
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 148690794 748 PNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 786
Cdd:cd14903 620 PEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
117-784 |
1.73e-161 |
|
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: 511.26 E-value: 1.73e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 188
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 189 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 266
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 267 NFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQER------ 340
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCYDRrdgvdd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 341 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI-VLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI 418
Cdd:cd14901 237 sVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLcFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 419 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFEQLCINYTN 497
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 498 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSH 577
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 578 PKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSlgdgppg 657
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 658 grprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 737
Cdd:cd14901 531 ---------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHD 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 148690794 738 EFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 784
Cdd:cd14901 602 AFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
117-786 |
2.53e-159 |
|
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: 506.53 E-value: 2.53e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLahVASSPKGRKEpGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGS-GV----EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQETLESLRVLG 354
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 508
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 509 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnLRD 588
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ-VME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 QAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL----------------- 651
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 652 -GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 712
Cdd:cd01385 541 aGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 713 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
117-748 |
1.08e-157 |
|
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: 501.14 E-value: 1.08e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI----- 270
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 271 ----AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKADLLL-EPCS 323
Cdd:cd14888 155 msgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISIDMSSfEPHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 324 HYRFLT-NGPSSSPG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL--- 398
Cdd:cd14888 235 KFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 399 CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIA 478
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 479 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWF 558
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 559 PKATDKSFVEKVAQEQGSHPKFQRPRNlrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKd 638
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 639 vegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 718
Cdd:cd14888 549 -----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 148690794 719 VLEGIRICRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
117-786 |
1.28e-157 |
|
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: 500.48 E-value: 1.28e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 353
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIvlkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 433
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNI---EFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 434 ADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 513
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 514 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQadFS 593
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNN--FG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 594 VLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMFRTVGQLYK 673
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRRPTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 674 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 753
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|...
gi 148690794 754 GFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14873 621 EDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
117-786 |
2.74e-156 |
|
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: 496.97 E-value: 2.74e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 189
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 190 QSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 266 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQEREL-F 343
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDDATeF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 344 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNivLKKERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLTPRIK 419
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 420 VGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQLNSFE 489
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 490 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDKSFVE 568
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 569 KVAQEQ-GSHPKFQRPRNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleq 647
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 648 vsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 727
Cdd:cd14892 536 -----------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 728 QGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 786
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
117-786 |
8.28e-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: 473.75 E-value: 8.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 187
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 188 EDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE-----------LERQLLQANPILEAFGNAKTVKNDN 256
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 257 SSRFGKFIRINFDI-AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNGPSS 334
Cdd:cd14907 161 SSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 335 SPGQER----ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAA-QKLCRLLGLGVTD 408
Cdd:cd14907 241 CYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 409 FSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIAGFE 481
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 482 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEECWFP 559
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 560 KATDKSFVEKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDV 639
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 640 EGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGV 719
Cdd:cd14907 557 DG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 720 LEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 786
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
119-786 |
3.98e-142 |
|
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: 457.83 E-value: 3.98e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 119 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 194
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 195 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYI 274
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 275 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELFQETLESLR 351
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 352 VLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 430
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEmDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 431 KEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 506
Cdd:cd14889 312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 507 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNl 586
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRS- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 rDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFR 666
Cdd:cd14889 466 -KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRKQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14889 545 SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL 624
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 148690794 747 --TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 786
Cdd:cd14889 625 lcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
118-746 |
3.98e-136 |
|
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: 439.74 E-value: 3.98e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 183
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 184 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSP-KGRKEPGVPGE-LERQLLQANPILEAFGNAKTVKNDNSSR 259
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNlAASVSMGKSTSgIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 260 FGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngpssspgqe 339
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 340 RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAAQKL------CRLLGLGVTDFSRA 412
Cdd:cd14900 218 RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEKA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 413 LLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFEIFQLNSF 488
Cdd:cd14900 298 LSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 489 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVE 568
Cdd:cd14900 378 EQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 569 KVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDplndnvaaLLHQstdrltaeiwkdvegivglEQV 648
Cdd:cd14900 455 KLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ-------------------EAV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 649 SslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 728
Cdd:cd14900 508 D--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARA 572
|
650
....*....|....*...
gi 148690794 729 GFPNRILFQEFRQRYEIL 746
Cdd:cd14900 573 GFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
117-786 |
6.84e-136 |
|
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: 440.15 E-value: 6.84e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAHVASspkGRKEPGVPgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQETLESLRV 352
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEEITAMLRTVSAVLQFGNIVLkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 432
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 433 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 512
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 513 QEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGSHPKFQRPRNLRDQ 589
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 590 adFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPRrgmfRTVG 669
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP----KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 670 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 749
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 148690794 750 AIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 786
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
117-786 |
6.96e-132 |
|
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: 428.69 E-value: 6.96e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 189
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 190 QSILCTGESGAGKTENTKKVIQYLAH------------VASSPKGRKEPGVpgELERQLLQANPILEAFGNAKTVKNDNS 257
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 258 SRFGKFIRINFDIAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSS 335
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 336 PG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK----ERNTDQATMPDNTAAQKLCRLLGLGVTDFS 410
Cdd:cd14891 234 DNiDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 411 RALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSF 488
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 489 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDK 564
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 565 SFVEKVAQEQGSHPKFQRP--RNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegi 642
Cdd:cd14891 465 KLNETLHKTHKRHPCFPRPhpKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 643 vgleqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 722
Cdd:cd14891 528 ---------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 723 IRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14891 581 CEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
117-748 |
4.65e-128 |
|
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: 420.45 E-value: 4.65e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 186
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 187 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPG-ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 266 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPGQER---- 340
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARKRAVadky 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 341 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTP 416
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 417 RIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFEIFQLNSF 488
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 489 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE 568
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 569 KVAQEQGShpkfqrprnlRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQV 648
Cdd:cd14902 478 KFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 649 SSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 725
Cdd:cd14902 539 DSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650 660
....*....|....*....|...
gi 148690794 726 CRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
117-786 |
4.73e-128 |
|
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: 417.64 E-value: 4.73e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 276
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR--------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 354
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRDYVQKAQTK 431
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 432 EQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 509
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 510 VLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrDQ 589
Cdd:cd14896 390 AQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 590 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrprrgmfrTVG 669
Cdd:cd14896 465 PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------------TLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 670 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpN 749
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-S 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 148690794 750 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
115-797 |
7.84e-126 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 417.51 E-value: 7.84e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 115 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 193
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 194 CTGESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 273
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMD----LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 274 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRV 352
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEEITAMLRTVSAVLQFGNI-VLKKERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVeIEGKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 506
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 507 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 586
Cdd:PTZ00014 499 IVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RDQaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdgppggrprrg 663
Cdd:PTZ00014 576 SNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL--------------- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 664 mfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 743
Cdd:PTZ00014 640 ----IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQF 715
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 744 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEER 797
Cdd:PTZ00014 716 KYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
117-786 |
1.66e-125 |
|
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: 411.99 E-value: 1.66e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 186
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 187 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 263
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 264 IRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTNG--PS 333
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGgaPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 334 SSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQK----LCRLLGLGVTDF 409
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 410 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSF 488
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 489 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFV 567
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 568 EKV--------AQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLM-KNMDPLNdnvaallhqstdrLTAEIwkd 638
Cdd:cd14908 477 SRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTADS--- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 639 vegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 718
Cdd:cd14908 541 -------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 719 VLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL----YR 777
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQ 673
|
....*....
gi 148690794 778 VGQSKIFFR 786
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
117-782 |
6.85e-123 |
|
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: 405.52 E-value: 6.85e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 194
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 195 TGESGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 272
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 273 YIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TNGPSSSP 336
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 337 GQEREL---FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQAT--MPDNTAA-QKLCRLLGLGVTDFS 410
Cdd:cd14906 241 NNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 411 RALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFLGILDIA 478
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 479 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWF 558
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 559 PKATDKSFVEKVAQEQGSHPKFQRpRNLrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkd 638
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 639 vegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 718
Cdd:cd14906 549 ---KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 719 VLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 782
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
117-784 |
2.83e-122 |
|
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: 401.29 E-value: 2.83e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 195
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMD----LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 354
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGN--IVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 429
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNvkITGKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 430 TKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 508
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 509 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRD 588
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 589 QaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrprrgmfrtV 668
Cdd:cd14876 469 I-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL----------------I 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 669 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 748
Cdd:cd14876 532 GSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL 611
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 749 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 784
Cdd:cd14876 612 GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
118-747 |
3.24e-118 |
|
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: 391.62 E-value: 3.24e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 185
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 186 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGElerQLLQANPILEAFGNAKTVKNDNSSR 259
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 260 FGKFIRINF-----DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNG- 331
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 332 --PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---------------QATMPDNTA 394
Cdd:cd14895 232 cyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 395 AQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR-----SPR 466
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalNPN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 467 QGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIEr 541
Cdd:cd14895 392 KAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 542 pANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDN 619
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 620 VAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHE 699
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 148690794 700 KRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 747
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
117-786 |
8.51e-118 |
|
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: 390.13 E-value: 8.51e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgelerqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 275
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEK--------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---FQETLESL 350
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaFSKLQAAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 351 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL------------LTPRI 418
Cdd:cd01386 231 KTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 419 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN---------SFE 489
Cdd:cd01386 311 QESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 490 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLALLDEECW 557
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 558 FPKATDKSFVEKV--AQEQGSHPKFQRPRNLRDQA-DFSVLHYAGK--VDYKASEWLMK-NMDPLNDNVAALLHQSTDRL 631
Cdd:cd01386 467 YPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 632 TAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--- 708
Cdd:cd01386 547 AAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStss 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 709 -----------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELD 772
Cdd:cd01386 596 paagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 148690794 773 PNLYRVGQSKIFFR 786
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
117-748 |
1.04e-111 |
|
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: 371.49 E-value: 1.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 192
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 193 LCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 272
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 273 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELFQETLESLRV 352
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCFEVTREAMLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV--QK 427
Cdd:cd14880 238 LGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 507
Cdd:cd14880 318 PCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 508 MFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGSHPKFQRPRnL 586
Cdd:cd14880 398 YLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK-L 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrPRRGMFR 666
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG---------QSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
..
gi 148690794 747 TP 748
Cdd:cd14880 625 RR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
117-786 |
9.98e-110 |
|
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: 365.36 E-value: 9.98e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 190
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 191 SILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 270
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 271 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLE 348
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 349 SLRVLgLLPEEITAMLRTVSAVLQFGNIVLKKERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYV 425
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 426 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 503
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 504 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE----KVAQE-----Q 574
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSscksKIKNNsfipgK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 575 GShpkfqrprnlrdQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdg 654
Cdd:cd14886 466 GS------------QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMK------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 655 ppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 734
Cdd:cd14886 527 ----------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYND 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 735 LFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14886 597 TFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
117-786 |
3.06e-104 |
|
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: 349.88 E-value: 3.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 193
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 194 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKEpgVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 269
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQRS--IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 270 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPSSSPGQERE 341
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 342 LFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLtprIKVG 421
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 422 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQLCINYTNE 498
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 499 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQE-QGSH 577
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 578 PKFQRPRN-LRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgpp 656
Cdd:cd14875 470 PYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 657 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 736
Cdd:cd14875 539 ----------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 737 QEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 786
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
117-743 |
3.63e-99 |
|
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: 337.07 E-value: 3.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 183
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 184 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---------LERQLLQANPILEAFGNAKTVKN 254
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 255 DNSSRFGKFIRINF-DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 328
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 329 TNGPSSSPG---QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL-----KKERNT--DQATMPDNTAA--- 395
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 396 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 465
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 466 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 539
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 540 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPL 616
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 617 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 694
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 148690794 695 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 743
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
118-750 |
2.94e-97 |
|
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: 326.85 E-value: 2.94e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 197
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLA-HVASSPKgrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiaGYIVG 276
Cdd:cd14898 78 SGSGKTENAKLVIKYLVeRTASTTS----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLESLRVLGLL 356
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 357 peEITAMLRTVSAVLQFGNIVLKKERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 436
Cdd:cd14898 220 --NFKSIEDCLLGILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 437 ALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 516
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 517 QREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAqeqgshpKFQRpRNLRDQAD--FSV 594
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIK-------KYLN-GFINTKARdkIKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 595 LHYAGKVDYKASEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKE 674
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL-----------------VKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 675 SLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 750
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
117-786 |
5.71e-96 |
|
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: 328.15 E-value: 5.71e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 188
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 189 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 269 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqerelFQETLE 348
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD------------LRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 349 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA--------AQKLCRLL-------GLGVTDFSRAL 413
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 414 LT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR------- 466
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 467 ------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI---------PWTF-LD 527
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsafPFSFpLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 528 FGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQ--EQGSHPKFQRPRNL 586
Cdd:cd14887 463 STLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKniINSAKYKNITPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 587 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGGRPRRGMFR 666
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 667 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 746
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 148690794 747 TPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 786
Cdd:cd14887 687 LPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
114-785 |
1.08e-91 |
|
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: 312.95 E-value: 1.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 114 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 183
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 184 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGK 262
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 263 FIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-----PSSSPG 337
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgchplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 338 QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI--VLKKERNTDqATMPDNTAA-QKLCRLLGLGVTDFsRALL 414
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 415 TPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEifQL---- 485
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--NRsstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 486 -NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC-WFPKATD 563
Cdd:cd14879 384 gNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 564 KSFVEKVAQEQGSHPKFQRPRNLRDQAD---FSVLHYAGKVDYKASEWLMKNMDPLndnvaallhqSTDRLTaeiwkdve 640
Cdd:cd14879 461 EQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 641 givgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVL 720
Cdd:cd14879 523 -----------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 721 EGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 785
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
117-786 |
2.41e-90 |
|
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: 309.44 E-value: 2.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 193
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 194 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DIAG 272
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 273 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELFQETL---- 347
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLNREKLavlk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 348 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 504
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 505 NHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----FPKATdKSF 566
Cdd:cd14878 393 NEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnLPKKL-QSL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 567 VEKVAQEQGSHPKFQRPRN--LRDQ-ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegiv 643
Cdd:cd14878 460 LESSNTNAVYSPMKDGNGNvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 644 gleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 723
Cdd:cd14878 534 -----SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 724 RICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 786
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
117-786 |
1.32e-86 |
|
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: 297.70 E-value: 1.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG----PSSSPGQERELFQETLESLRV 352
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKnvviPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 353 LGLLPEeitaMLRTVSAVLQFGNIV---LKKERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd14937 228 HDMKDD----LFLTLSGLLLLGNVEyqeIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 507
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 508 MFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlR 587
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--K 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 588 D-QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppggRPRRGMF 665
Cdd:cd14937 457 DiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG------RKNLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 666 RtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEI 745
Cdd:cd14937 524 K-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEY 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 148690794 746 LTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 786
Cdd:cd14937 598 LDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
117-738 |
1.39e-78 |
|
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: 275.63 E-value: 1.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 188
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 189 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 268
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-------ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 269 D---------IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL---------- 328
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 329 ----------TNGPSSSPGQEREL-FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKkerntdqatmpdntAAqk 397
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK--------------AA-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 398 lCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-----------DRSPR 466
Cdd:cd14884 298 -AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdnEDIYS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 467 QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDLIERpanpp 546
Cdd:cd14884 377 INEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 547 gLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGSH------PKFQRPRNLRDQAD---FSVLHYAGKVDYKASE 607
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADGTAKKQNIKkniFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 608 WLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRLMATLSNTN 687
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 688 PSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 738
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
118-785 |
3.00e-72 |
|
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: 255.42 E-value: 3.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 190
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 191 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDi 270
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 271 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQEREL-FQETL 347
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAArFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 348 ESLRVLGLlpeEITAMLRTVSAVLQFGNIVLKkERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 427
Cdd:cd14881 222 ACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 428 AQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQLCINYTNEK 499
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 500 LQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKVAQEQGSHP 578
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 579 KFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSSLGdgppgg 658
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCNFG------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 659 rprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 738
Cdd:cd14881 503 ------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 739 FRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 785
Cdd:cd14881 577 FNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
118-746 |
2.85e-69 |
|
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: 246.96 E-value: 2.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 197
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 198 SGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 277
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--------GNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 278 NIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER----------ELFQE 345
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 346 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 425
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 426 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 503
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 504 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQGSHPKfqr 582
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 583 prnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdgppggrprr 662
Cdd:cd14882 462 ---KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 663 gmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 738
Cdd:cd14882 521 ---RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
....*...
gi 148690794 739 FRQRYEIL 746
Cdd:cd14882 598 FLRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
118-786 |
1.90e-66 |
|
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: 239.61 E-value: 1.90e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 276
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSK-----YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 277 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQETLESLRVLG 354
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 355 LLPEEITAMLRTVSAVLQFGNIVLKKERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAqtkeqa 434
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 435 dfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 514
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 515 EYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrdqaDFS 593
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPN-----KFG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 594 VLHYAGKVDYKASEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGMFRTVGQLYK 673
Cdd:cd14905 446 IEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 674 ESLS--RLMATLSNTNPS-----------------------------------------------FVRCIVPNHEKRAGK 704
Cdd:cd14905 513 SPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIKPNSKKTHLT 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 705 LEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALELDPNLYRVG 779
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVG 666
|
....*..
gi 148690794 780 QSKIFFR 786
Cdd:cd14905 667 NTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
117-751 |
6.96e-65 |
|
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: 233.61 E-value: 6.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 117 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 195
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 196 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIV 275
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVT-------TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 276 GANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVL 353
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 354 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKVGrdyvqKA 428
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSEDG-----TT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 429 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 508
Cdd:cd14874 293 IDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 509 FVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlR 587
Cdd:cd14874 371 FHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-K 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 588 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggrprrgmfrt 667
Cdd:cd14874 448 ERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS------------------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 668 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 747
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 148690794 748 PNAI 751
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
120-744 |
2.63e-62 |
|
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: 228.70 E-value: 2.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 120 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 189
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 190 QSILCTGESGAGKTENTKKVIQYLAHVASS----PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 265
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 266 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSPGQER 340
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 341 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL------KKERNTDQATMPDNTAAqklCRLLGLGVTDFSRALL 414
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGGANSTTVSDAQS---CALKDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 415 TPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQG----AS 470
Cdd:cd14893 321 EVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 471 FLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQPCIDLIER 541
Cdd:cd14893 401 GVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 542 PanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD------------FSVLHYAGKVDYKASEWL 609
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 610 MKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYKESLS------- 677
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSARESKNitdsaat 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 678 -------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 744
Cdd:cd14893 631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
139-273 |
1.78e-58 |
|
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: 199.49 E-value: 1.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 139 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 217
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 218 SS--PKGRKEPGVP-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 273
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 ... |
118-784 |
9.45e-53 |
|
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: 199.29 E-value: 9.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 118 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 196
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 197 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPG-----------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFG 261
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEednihneentdYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 262 KFIRINFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNgpSSSPGQERE 341
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNN--EKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 342 LFQETLESLRVLGLL---PEEITAMLRTVSAVLQFGNI----------VLKKER----------------NTDQATMPDN 392
Cdd:cd14938 239 YSGKILELLKSLNYIfddDKEIDFIFSVLSALLLLGNTeivkafrkksLLMGKNqcgqninyetilseleNSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 393 TAAQKL-CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 469
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 470 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 549
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 550 ALLDEECwFPKATDKS-FVEKVAQEQGSHPKFQRPRN-LRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQS 627
Cdd:cd14938 477 SLLENVS-TKTIFDKSnLHSSIIRKFSRNSKYIKKDDiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 628 TDRLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNH 698
Cdd:cd14938 556 ENEYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 699 EKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYR 777
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 148690794 778 VGQSKIF 784
Cdd:cd14938 705 IGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1034-1686 |
8.59e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.20 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1034 EEKVKSLNKLRlkyeatisDMEDRLKKEEKGRQELEklkRRLDgessELQEQmVEQKQRAEELLAQLgrKEDELQAALLR 1113
Cdd:COG1196 172 ERKEEAERKLE--------ATEENLERLEDILGELE---RQLE----PLERQ-AEKAERYRELKEEL--KELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1114 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELedtldstnaqQELRSKREQevte 1193
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----------YELLAELAR---- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1194 lkkalEEESRAHEvsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1273
Cdd:COG1196 300 -----LEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1274 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1353
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1354 RALEAEAAGLREQMEEEvvARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1433
Cdd:COG1196 452 AELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1434 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdqlLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEA 1513
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAA-----IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1514 REELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQA--ASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH 1591
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLreVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1592 ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1671
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650
....*....|....*
gi 148690794 1672 LWREVEETRSSRDEM 1686
Cdd:COG1196 765 LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
922-1531 |
1.17e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 922 EETRARLAarkqELELVVTELEARVGEEEEcsrqlQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtteAKMKKFEED 1001
Cdd:COG1196 182 EATEENLE----RLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRELE-----AELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1002 LLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQEL----EKLKRRLDg 1077
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELA- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1078 essELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1157
Cdd:COG1196 327 ---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1158 DLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEvsmqELRQRHSQALVEMAEQLEQARRGKGVW 1237
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA----ELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1238 EKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ--RAQAELESVSTALSEAE 1315
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1316 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1395
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1396 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1475
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1476 KAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA----LRAELEAL 1531
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERelerLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1149-1745 |
5.32e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.51 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1149 RAKAEKQ----RRDLgEELEALRGELEDTLDSTnaqqelrsKREQEVTELKKALEEESRAHEVSMQELRQRHSQA-LVEM 1223
Cdd:COG1196 174 KEEAERKleatEENL-ERLEDILGELERQLEPL--------ERQAEKAERYRELKEELKELEAELLLLKLRELEAeLEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1224 AEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE 1303
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1304 LESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQS 1383
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1384 TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEK 1463
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1464 KQRKfdqllAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddVGKNVH 1543
Cdd:COG1196 485 ELAE-----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL-----QNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1544 ELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEE 1623
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1624 RKQRALAMAARKKLELELEELKAQT-SAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEmfTLSRENEKKLKGLEA 1702
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEA 712
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 148690794 1703 EVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEE 1745
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
869-1397 |
5.37e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 123.51 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 869 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 948
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 949 EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLEERLAEFSS 1028
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE---ALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1029 QAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1108
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1109 AALLRAEEEGGARAQLLKSLREAQAGL-AEAQEDLEAERVARAKAEKQRRDLGEELEALR--GELEDTLDSTNAQQELRS 1185
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgvEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1186 KREQEVTELKKALEE-----ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1260
Cdd:COG1196 551 IVVEDDEVAAAAIEYlkaakAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1261 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA----ESQLHDTQ 1336
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAllaeEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1337 ELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1397
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1615 |
2.72e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 121.70 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 864 RQDEVLQARAQELQKVQELQQQ-SAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 942
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1022
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgr 1102
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 kedELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:TIGR02168 434 ---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1183 LRSKREQE------VTELKKALEEESRAHEVSMQELRQ----RHSQALVEMAEQLEQARRGKGVW----EKTRLSLEAEV 1248
Cdd:TIGR02168 511 LLKNQSGLsgilgvLSELISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1249 SELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA 1328
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1329 ESQLHDTQELlqEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEE 1407
Cdd:TIGR02168 670 SSILERRREI--EELEEKIEeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1408 ARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRE 1487
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1488 RIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELE 1567
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 148690794 1568 DELTAAEDAKLRLevtvQALKAQHERDLQGrddaGEERRRQLAKQLRD 1615
Cdd:TIGR02168 908 SKRSELRRELEEL----REKLAQLELRLEG----LEVRIDNLQERLSE 947
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
236-727 |
1.24e-25 |
|
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: 115.61 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 236 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDIAGY---IVGANIETYLLEKSRAIRQA------KDECSFHIFYQ 304
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 305 LLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGLLPEEITAMLRTVS 368
Cdd:cd14894 329 MVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 369 AVLQFGNIVLKKERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALEALA 442
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 443 KATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQqlfnh 506
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 507 tmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQEQGS 576
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 577 HPKfQRPRNLRDQA----------DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVG 644
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlGWSP 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 645 LEQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIR 724
Cdd:cd14894 717 NTNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 148690794 725 ICR 727
Cdd:cd14894 793 ICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1146-1945 |
1.85e-24 |
|
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: 112.46 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1146 RVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKALEEeSRAHEVSMQ 1210
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1211 ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR 1290
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1291 SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEE 1370
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1371 VVARERAGRELQS-----TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELD 1445
Cdd:TIGR02168 413 EDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1446 DATVDLGQQKQL---LSTLEKKQRKFDQLL----------AEEKAAVLRAV-EDRERIEAEGREREARALS-LTRALEEE 1510
Cdd:TIGR02168 493 SLERLQENLEGFsegVKALLKNQSGLSGILgvlselisvdEGYEAAIEAALgGRLQAVVVENLNAAKKAIAfLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1511 QEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE----VTVQA 1586
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyriVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1587 LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1666
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1667 VQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNlskaatlEEK 1746
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EAL 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1747 RQLEGRLsqleeeleeeqnnsELLKDHYRKLVLQVESLTTELSAersfsakAESGRQQLERQIQELRARLgEEDAGARAR 1826
Cdd:TIGR02168 806 DELRAEL--------------TLLNEEAANLRERLESLERRIAA-------TERRLEDLEEQIEELSEDI-ESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1827 QKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAee 1906
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL-- 941
|
810 820 830
....*....|....*....|....*....|....*....
gi 148690794 1907 easrAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1945
Cdd:TIGR02168 942 ----QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1287-1878 |
2.79e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.57 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1287 ERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQ 1366
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1367 MEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDD 1446
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1447 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRA 1526
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1527 ELEALLSSKDDVGKnvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERR 1606
Cdd:COG1196 464 LLAELLEEAALLEA---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1607 RQLAKQLRDAEVERDEER--------KQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1678
Cdd:COG1196 541 EAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1679 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1758
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1759 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSfsakAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKL 1838
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAERE----ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 148690794 1839 AQ-------AEEQL-EQESRERILSGKL--VRRAEKRLKEVVLQVDEERR 1878
Cdd:COG1196 777 EAlgpvnllAIEEYeELEERYDFLSEQRedLEEARETLEEAIEEIDRETR 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1527 |
4.50e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.39 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 872 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQElELVVTELEARVGEEE 950
Cdd:PTZ00121 1171 KAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 951 ECSRQLQSEKKRLQQHIQELESHLEAEEgARQKLQLEKvtteAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQA 1030
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1031 AEEEEKvkSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRldGESSELQEQmvEQKQRAEELL--AQLGRKEDELQ 1108
Cdd:PTZ00121 1324 AEEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKE--EAKKKADAAKkkAEEKKKADEAK 1397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1109 aallRAEEEGGARAQLLKSLREAQAGLAEAQEdlEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKRE 1188
Cdd:PTZ00121 1398 ----KKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1189 QEvtELKKALEEESRAHEVsmqelrQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE--LKAELSSLQTSRQEGE 1266
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAKKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1267 QKRRRLEsqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAK 1346
Cdd:PTZ00121 1544 EKKKADE--LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1347 LALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAE- 1425
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEa 1701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1426 -KTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRKFDQLLAEEkaavlravEDRERIEAEGREREARALSL 1503
Cdd:PTZ00121 1702 kKAEELKKKEAEEKKKAEELKKAeEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEI 1773
|
650 660
....*....|....*....|....
gi 148690794 1504 TRALEEEQEAREELERQNRALRAE 1527
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
922-1734 |
1.46e-23 |
|
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: 109.38 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 922 EETRARLAARKQELELV---VTELEARVGeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteaKMKKF 998
Cdd:TIGR02168 175 KETERKLERTRENLDRLediLNELERQLK-----SLERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 999 EEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrQELEKLKRRLDGE 1078
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1079 SSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1158
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1159 LGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALeEESRAHEVSMQelrqrhsqaLVEMAEQLEQarrgkgvwe 1238
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKL-EEAELKELQAE---------LEELEEELEE--------- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1239 ktrlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserarseaAEKLQRAQAELESVSTALSEAESKA 1318
Cdd:TIGR02168 452 -----LQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----------LDSLERLQENLEGFSEGVKALLKNQ 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1319 IRLGKELSSAESQLHDTQELlqeETRAKLALGSRVRAL----EAEAAGLREQMEEEVVAR-------ERAGRELQSTQAQ 1387
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGY---EAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRvtflpldSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1388 LSEWrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQEL-------------------DDAT 1448
Cdd:TIGR02168 593 ILKN---IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1449 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRaleeeqeareelerQNRALRAEL 1528
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1529 EALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH---ERDLQG-RDDAGEE 1604
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDElRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1605 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTS--AAGQGKEEAVKQLKKMQVQMKELWREVEETRSS 1682
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1683 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1734
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
843-1390 |
1.62e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.46 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 843 KLRNWQWWRLFIKVKPLLQVTRQ-----------DEVLQA----------RAQELQKVQELQQQS--AREVGELQGRVaq 899
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaikaeearkaDELKKAeekkkadeakKAEEKKKADEAKKKAeeAKKADEAKKKA-- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 900 leEERTRLAEQLRAEAELCSEAEET-RARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 978
Cdd:PTZ00121 1325 --EEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 979 GARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRL 1058
Cdd:PTZ00121 1403 DKKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK---KAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1059 KKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL-AQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAE 1137
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE----LKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1138 AQEDLEAERVARA----KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEvtELKKALEEESRAHEV-SMQEL 1212
Cdd:PTZ00121 1554 AEELKKAEEKKKAeeakKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELkKAEEE 1631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1213 RQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE 1292
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1293 A-----AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEaaGLREQM 1367
Cdd:PTZ00121 1712 AeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEED 1789
|
570 580
....*....|....*....|...
gi 148690794 1368 EEEVVARERAGRELQSTQAQLSE 1390
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
864-1497 |
7.88e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.53 E-value: 7.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 864 RQDEVLQARAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQELELVVTEL 942
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 ----EARVGEE----EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--LLEDQNSKL 1012
Cdd:PTZ00121 1194 rkaeDARKAEAarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMahFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1013 SKERRLLEE-RLAEFSSQAAE--EEEKVKSLNKLRLKYEATisdmedrlKKEEKGRQELEKLKRRLDgessELQEQMVEQ 1089
Cdd:PTZ00121 1274 AEEARKADElKKAEEKKKADEakKAEEKKKADEAKKKAEEA--------KKADEAKKKAEEAKKKAD----AAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1090 KQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLK----SLREAQAGLAEAQED-LEAERVARAKAEKQRRD 1158
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEaaekkkEEAKKKADAAKkkaeEKKKADEAKKKAEEDkKKADELKKAAAAKKKAD 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1159 lgeelealrgELEDTLDSTNAQQELRSKREQ--EVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGV 1236
Cdd:PTZ00121 1422 ----------EAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1237 WEKTRlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-------EAAEKLQRAQaELESVST 1309
Cdd:PTZ00121 1492 AEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkadelKKAEELKKAE-EKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1310 ALSEAESK--AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ 1387
Cdd:PTZ00121 1569 AKKAEEDKnmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1388 LSEWRRRQEEEAAVLEAGEEARRRAAReaetltqrlaEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRK 1467
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDK----------KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
650 660 670
....*....|....*....|....*....|
gi 148690794 1468 FDQLLAEEKAAVLRAVEDRERIEAEGRERE 1497
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1498 |
1.65e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.91 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 940
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 941 ELEARVgeeeecsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEedlllLEDQNSKLSKERRLLE 1020
Cdd:TIGR02168 383 TLRSKV-------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1021 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdrlkkEEKGRQE-LEKLKRRLDGESSELQEQMVEQKQRAEEL--L 1097
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELA-----QLQARLDsLERLQENLEGFSEGVKALLKNQSGLSGILgvL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1098 AQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAGLA-EAQEDLEAERVA-----RAKAEKQRRDLGEELEALRGELE 1171
Cdd:TIGR02168 526 SELISVDEGYEAAI---EAALGGRLQAVVVENLNAAKKAiAFLKQNELGRVTflpldSIKGTEIQGNDREILKNIEGFLG 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1172 --------------------------DTLDSTNAQQEL-------------------------------RSKREQEVTEL 1194
Cdd:TIGR02168 603 vakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1195 KKALEE-ESRAHEVSMQelRQRHSQALVEMAEQLEQARRGKgvwektrLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1273
Cdd:TIGR02168 683 EEKIEElEEKIAELEKA--LAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1274 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1353
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1354 RALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1433
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1434 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVED-----RERIEAEGREREA 1498
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
865-1738 |
5.84e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQElelvvtelEA 944
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE--------DA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 945 RVGEEeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERRLLEERLA 1024
Cdd:PTZ00121 1140 RKAEE---ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1025 EfSSQAAEEEEKVKSLNKLRlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM-VEQKQRAEELL-AQLGR 1102
Cdd:PTZ00121 1215 E-EARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKkAEEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 KEDEL-QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQ 1181
Cdd:PTZ00121 1291 KADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1182 ELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRlslEAEVSELKAELS-SLQ 1259
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAkKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1260 TSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAirlgKELSSAESQLHDTQELL 1339
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-------EAKKKA----DEAKKAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1340 QEEtRAKLALGSRvRALEAEAAGLREQMEEEVVARE-RAGREL-QSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAE 1417
Cdd:PTZ00121 1517 KAE-EAKKADEAK-KAEEAKKADEAKKAEEKKKADElKKAEELkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1418 TLTQRLAEKTEAVERLERARRRLQ----QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEG 1493
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1494 REREAralslTRALEEEQEAREELERQNRALRAELEALlssKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAA 1573
Cdd:PTZ00121 1675 KKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEEL---KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1574 EDAKLRLEvtvQALKAQHERdlQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA--LAMAARKKLELELEELKAQTSAA 1651
Cdd:PTZ00121 1747 EEAKKDEE---EKKKIAHLK--KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVI 1821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1652 GQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEE 1731
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
....*..
gi 148690794 1732 VASGNLS 1738
Cdd:PTZ00121 1902 IPNNNMA 1908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
879-1397 |
1.62e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.45 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 879 VQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEEECSRQLQS 958
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 959 EKKRLQQHIQELESHlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVK 1038
Cdd:PRK03918 267 RIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1039 SLNKLRLKYEAtisdMEDRLKKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQKQRAEEllaQLGRKEDELQAALLRAE 1115
Cdd:PRK03918 346 KLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1116 EEGGARAQLLKSLREAQAGL----AEAQEDLEAERVARAKAE-----KQRRDLGEELEALRGELEDTLDSTNAQQELRsk 1186
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEEKERKLRKELRELEKVLKKESELI-- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1187 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLE--------QARRGKGVwEKTRLSLEAEVSELKAELSSL 1258
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkELEKLEEL-KKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1259 QTS-RQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQE 1337
Cdd:PRK03918 576 LKElEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1338 LLQEETRAKLAlgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1397
Cdd:PRK03918 655 KYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
950-1745 |
2.25e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.53 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 950 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RRLLEERLAE 1025
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1026 FSSQA-----AEEEEKVKSLNKlrlkyeatisdMEDRLKKEEKGRQELEklkRRLDGESSELQEQMVEQKQRAEELlaql 1100
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRK-----------AEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEA---- 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1101 grKEDELQAAllRAEEEggaraqllkSLREAQAGLAEAQEDLEAERVARAKAEKQRRdlgeelealRGELEDTLDSTNAQ 1180
Cdd:PTZ00121 1236 --KKDAEEAK--KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1181 QELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSlEAEVSELKAELSSLQ 1259
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1260 TSrqEGEQKRRRLESQLQEVqgRSSDSERARSE----AAEKLQRAQAELESVSTALSEAESKaiRLGKELSSAESQLHDT 1335
Cdd:PTZ00121 1373 KE--EAKKKADAAKKKAEEK--KKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1336 QELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEaavleageearrraarE 1415
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK----------------K 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1416 AETLTQRLAEKTEAVERLERARRRLQQELDDAtvdlgqqkqllstleKKQRKFDQLlaeEKAAVLRAVEDRERIEAEGRE 1495
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKA---------------EEKKKADEL---KKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1496 REARALSLTRALeeeqeareelerqnralraELEALLSSKDDVGKNVHELERARKAaeqaasdlrtqvteleDELTAAED 1575
Cdd:PTZ00121 1573 EEDKNMALRKAE-------------------EAKKAEEARIEEVMKLYEEEKKMKA----------------EEAKKAEE 1617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1576 AKLRLEvtvQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVE---RDEERKQRALAMAARKKLELELEELKAQTSAAG 1652
Cdd:PTZ00121 1618 AKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1653 QGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1732
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
810
....*....|...
gi 148690794 1733 ASGNLSKAATLEE 1745
Cdd:PTZ00121 1771 EEIRKEKEAVIEE 1783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
860-1579 |
2.21e-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: 98.99 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 860 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 939
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 940 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLL 1019
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1020 EERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAE---EL 1096
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1097 LAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglAEAQEDLEAERVARA------KAEKQRRDLGEELEAlrGEL 1170
Cdd:TIGR02169 527 VAQLGSVGERYATAI---EVAAGNRLNNVVVEDDAVA--KEAIELLKRRKAGRAtflplnKMRDERRDLSILSED--GVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1171 EDTLDSTNAQQELRSKREQEV--TELKKALEEESRAhevsMQELRqrhsqaLVEMAEQLEQ--------ARRGKGVWEKT 1240
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYVFgdTLVVEDIEAARRL----MGKYR------MVTLEGELFEksgamtggSRAPRGGILFS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1241 RlSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIR 1320
Cdd:TIGR02169 670 R-SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1321 LGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAglREQMEEevvarerAGRELQSTQAQLSEWRRRQEEeaa 1400
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPE-------IQAELSKLEEEVSRIEARLRE--- 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1401 vleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVL 1480
Cdd:TIGR02169 817 ------------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1481 RAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERArKAAEQAASDLR 1560
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQ 957
|
730
....*....|....*....
gi 148690794 1561 TQVTELEDELTAAEDAKLR 1579
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
868-1214 |
1.57e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.81 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 868 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARLAARKQELElvvtELEARVG 947
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLA----RLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 948 EEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1027
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1028 SQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEklkrrldGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1107
Cdd:TIGR02168 824 ERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1108 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEEL-EALRGELEDTLDSTNAQQELRSK 1186
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|....*...
gi 148690794 1187 REQEVTELKKALEEESRAHEVSMQELRQ 1214
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
944-1826 |
1.49e-17 |
|
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: 89.74 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 944 ARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteAKMKKFEEDLLLLED-QNSKLSKERRLLEER 1022
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREyEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqeleKLKRRLDGESSELQEQMveqkqraEELLAQLGR 1102
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEKI-------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAK-------AEKQRRDLGEELEALRGELedtld 1175
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyaeLKEELEDLRAELEEVDKEF----- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1176 stnaqQELRSKREQEVTELKKALEE--ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKA 1253
Cdd:TIGR02169 381 -----AETRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1254 ELSSLQTSRQEGEQKRRRLESQLQEVqgrssdsERARSEAAEKLQRAQAELESVSTalSEAESKAIRlgKELSSAESQLH 1333
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRV-------EKELSKLQRELAEAEAQARASEE--RVRGGRAVE--EVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1334 DT-QELLQEETRAKLALGSrvraleaeAAGLREQ---MEEEVVA--------RERAGR-------ELQSTQAQLSEWRRR 1394
Cdd:TIGR02169 525 GTvAQLGSVGERYATAIEV--------AAGNRLNnvvVEDDAVAkeaiellkRRKAGRatflplnKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1395 -------------QEEEAAVL----------EAGEEARRRAAREAETLTQRLAEKTEAV-------ERLERARRRLQQEL 1444
Cdd:TIGR02169 597 gvigfavdlvefdPKYEPAFKyvfgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGAMtggsrapRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1445 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARAlsltraleeeqeareeleRQNRAL 1524
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE------------------EKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1525 RAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvQALKAQHERDLQGRDDAGEE 1604
Cdd:TIGR02169 739 LEELEEDLS----------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1605 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVeetrssrd 1684
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------- 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1685 emftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQ 1764
Cdd:TIGR02169 878 ------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1765 NnsellkdhYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL---RARLGEEDAGARAR 1826
Cdd:TIGR02169 952 S--------LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELkekRAKLEEERKAILER 1008
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
859-1390 |
4.48e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 938
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 939 VtELEARVGEEEECSRQLQSEKKRLQQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1015
Cdd:PRK03918 296 I-KLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1016 RRlLEERLAEFSSQAAEE-----EEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL--------DGESSEL 1082
Cdd:PRK03918 375 ER-LKKRLTGLTPEKLEKeleelEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1083 QEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKsLREAQAGLAEAQEDLEAERVARAKAE-KQRRDLGE 1161
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1162 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTR 1241
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL----KELEELGFESVEELEERLKELEPFYNEYLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1242 lSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEaaEKLQRAQAELESVSTALSEAESKAIRL 1321
Cdd:PRK03918 609 -DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEEL 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1322 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEaEAAGLREQMEE-EVVARERAGRELQSTQAQLSE 1390
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKyKALLKERALSKVGEIASEIFE 754
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
864-1196 |
4.68e-17 |
|
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: 88.20 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 864 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELE 943
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 944 ARVGEEEECSRQLqsEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1023
Cdd:TIGR02169 772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1024 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1103
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1104 EDELqAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRrdlgEELEALRGELEDTLDSTNAQQEL 1183
Cdd:TIGR02169 930 EEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY----EEVLKRLDELKEKRAKLEEERKA 1004
|
330
....*....|...
gi 148690794 1184 RSKREQEVTELKK 1196
Cdd:TIGR02169 1005 ILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
921-1304 |
8.36e-17 |
|
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: 87.42 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 921 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL---QLEKVTTEAKMKK 997
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 998 FEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDG 1077
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1078 ESSELQEqmveqkqRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1157
Cdd:TIGR02168 818 EAANLRE-------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1158 DLGEELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAhEVSMQELRQR---HSQALVEMAEQLEQARrgk 1234
Cdd:TIGR02168 891 LLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGL-EVRIDNLQERlseEYSLTLEEAEALENKI--- 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1235 gvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARseaaEKLQRAQAEL 1304
Cdd:TIGR02168 964 ---EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK----ETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
889-1721 |
6.76e-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: 84.35 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 889 EVGELQGRVAQLEEERTRLAEQLRAEAElcsEAEETRArLAARKQELElvVTELEARVGEEEECSRQLQSEKKRLQQHIQ 968
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRERE---KAERYQA-LLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 969 ELESHLE--AEEGARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1046
Cdd:TIGR02169 255 KLTEEISelEKRLEEIEQLLEELNKKI-KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1047 YEATISDMEDRLKKEEKGR-----------QELEKLKRRLDGESSELQEQMVEQKQRAEEL------LAQLGRKEDELQA 1109
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRdklteeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1110 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE-RVARAKAEKQRRDLG---EELEALRGELEDTldstnaqQELRS 1185
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSkyeQELYDLKEEYDRV-------EKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1186 KREQEVTELKKaleeesrahEVSMQELRQRHSQALVEMAEQLEQARRGK-----GVWEKTRLSLE-AEVSELKAELSSLQ 1259
Cdd:TIGR02169 487 KLQRELAEAEA---------QARASEERVRGGRAVEEVLKASIQGVHGTvaqlgSVGERYATAIEvAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1260 TSRQEGEQ--KRRRLESQ----LQEVQGRSSDSERARSEA----AEKLQRAQAELESV------STALSEAESKAIRLGK 1323
Cdd:TIGR02169 558 AVAKEAIEllKRRKAGRAtflpLNKMRDERRDLSILSEDGvigfAVDLVEFDPKYEPAfkyvfgDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1324 E--LSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAV 1401
Cdd:TIGR02169 638 KyrMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1402 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLR 1481
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1482 AveDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRT 1561
Cdd:TIGR02169 798 A--ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1562 QVTELEDELTAAEDAKLRLEVTVQALkaqherdlqgrddagEERRRQLAKQLRDAEvERDEERKQRALAMAARKKLELEL 1641
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLREL---------------ERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1642 EELKAQTSAAGQGKEEAVKQLKKMQVQMKELW-------REVEETRSSRDEMftlsrenEKKLKGLEAEVLRLQEELAAS 1714
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDEL-------KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 148690794 1715 DRARRQA 1721
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1185-1959 |
7.42e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 7.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1185 SKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKgvwEKTRLSLEAEVSElkaelsslqtSRQE 1264
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA---EDARKAEEARKAE----------DARK 1141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1265 GEQKRRRLESQLQEVQGRSSDSERAR-SEAAEKLQRAqaelESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEET 1343
Cdd:PTZ00121 1142 AEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKA----EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEA 1217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1344 RaklalgsrvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQlsEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRL 1423
Cdd:PTZ00121 1218 R---------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1424 AEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLL--AEEK---AAVLRAVEDRERIEAEGREREA 1498
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAkkaAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1499 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDlrtqvtelEDELTAAEDAKL 1578
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--------AEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1579 RLEVTVQA----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRAlamaarkkleLELEELKAQTSAAGQG 1654
Cdd:PTZ00121 1439 KAEEAKKAdeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA----------EEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1655 KEEAVKQLKKMQVQMKELWREVEETRSSRDemftLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1734
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1735 GNLSKAATLEEKRQLEgrlSQLEEELEEEQNNSELLKDHYRKLvlQVESLTTElSAERSFSAKAESGRQQLERQIQELRA 1814
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEE---VMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1815 RlgEEDAGARARQKMLIAALESKlaQAEEQLEQESRERILSGKLVRRAE--KRLKEVVLQVDEERRVADQVRDQLEKSNL 1892
Cdd:PTZ00121 1655 A--EEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1893 RLKQLKR----------QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1959
Cdd:PTZ00121 1731 KAEEAKKeaeedkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
861-1166 |
8.26e-16 |
|
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: 83.95 E-value: 8.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 940
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 941 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1020
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1021 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1100
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1101 grkedelqaallraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVA-RAKAEKQRRDLGEELEAL 1166
Cdd:TIGR02168 939 ---------------------DNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1290-1945 |
1.83e-15 |
|
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: 82.80 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1290 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAEsqlhDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQME 1368
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1369 EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1448
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1449 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1528
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1529 EALLSSKDDVGKNVHELERARKAA------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERdLQ 1596
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-LQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1597 GRDDAGEERRRQ------------------------------------------LAKQLRDAEVERDEERKQ-------- 1626
Cdd:TIGR02168 489 ARLDSLERLQENlegfsegvkallknqsglsgilgvlselisvdegyeaaieaaLGGRLQAVVVENLNAAKKaiaflkqn 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1627 ---RALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKK---------------------------MQVQMKELWREV 1676
Cdd:TIGR02168 569 elgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddldnaleLAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1677 EET------------RSSRDEMFTLSRENEkkLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLE 1744
Cdd:TIGR02168 649 TLDgdlvrpggvitgGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1745 EKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGAR 1824
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1825 ARQKMLiAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEerrvadqVRDQLEKSNLRLKQLKRQLEEA 1904
Cdd:TIGR02168 807 ELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEAL 878
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 148690794 1905 EEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1945
Cdd:TIGR02168 879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
943-1878 |
7.53e-15 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.79 E-value: 7.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1022
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1102
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1183 LRSKREQEVTELKKALEEEsrahevsMQELRQRHSQALVEMAEQleqarrgkgvwEKTRLSLEAEVSELKAELSSLQTSR 1262
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQL-------EDLLKEEKKEELEILEEE-----------EESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1263 QEGEQKRRRLESQLQEVQGRSSdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEe 1342
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKL-------QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1343 tRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1422
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1423 LAEKTEAVERLERARRRLQQELDDATVDLGqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1502
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESA--KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1503 LTRALEEEQEAREELErqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1582
Cdd:pfam02463 690 AKEEILRRQLEIKKKE-----QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1583 TVQALKAQHERDlqgrddagEERRRQLAKQLRDAEVERDEERKQRALAMAarkkleleleelkaqtsaagqgKEEAVKQL 1662
Cdd:pfam02463 765 EKSELSLKEKEL--------AEEREKTEKLKVEEEKEEKLKAQEEELRAL----------------------EEELKEEA 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1663 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1742
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1743 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAErsfsAKAESGRQQLERQIQELRARLGEEdag 1822
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE----EADEKEKEENNKEEEEERNKRLLL--- 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1823 ararQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERR 1878
Cdd:pfam02463 968 ----AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1073-1852 |
9.34e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1073 RRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARAKA 1152
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEA-----------RKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1153 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR 1232
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK-----AEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1233 GkgvwEKTRLSLEAEVSElkaELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERArsEAAEKLQRAQAELESVSTALS 1312
Cdd:PTZ00121 1214 A----EEARKAEDAKKAE---AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA--HFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1313 EAESKaiRLGKELSSAEsQLHDTQELLQEETRAKLALGSRVRALEA--EAAGLREQMEEEVVARERAGRELQSTQAQLSe 1390
Cdd:PTZ00121 1285 KAEEK--KKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAE- 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1391 wRRRQEEEAAVLEAGEEARRRAAREAETLTQRlaeKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdq 1470
Cdd:PTZ00121 1361 -AAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK---- 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1471 llAEEkaAVLRAVEDRERIEAEGREREAR-ALSLTRALEEEQEAREELERQNRALRAelEALLSSKDDVGKNVHELERAR 1549
Cdd:PTZ00121 1433 --ADE--AKKKAEEAKKADEAKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1550 KAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvqALKAQHERDLQGRDDAGEERRRQLAKQLRDAevERDEERKQRAL 1629
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEA--KKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1630 AMA--ARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETRSSRDEMFTLSRENEKKlkgleAEVLRL 1707
Cdd:PTZ00121 1581 RKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKKEAEEKKK-----AEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1708 QEElaasDRARRQAQQDRDEMAEEVASGNLSKAAtlEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKlvlqVESLTTE 1787
Cdd:PTZ00121 1655 AEE----ENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK----AEELKKA 1724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1788 LSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALE---SKLAQAEEQLEQESRER 1852
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEirkEKEAVIEEELDEEDEKR 1792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
892-1490 |
3.19e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 892 ELQGRVAQLEEERTRLaEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELE 971
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 972 SHLEAEEGARQKLQlekvttEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAeeeekvkslnKLRLKYEATI 1051
Cdd:COG4913 316 ARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA----------ALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1052 SDMEDRlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRA----EEEGGARAQLLKS 1127
Cdd:COG4913 380 EEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1128 LREAQAGL---AEAQEDLEAERVARAKAEK----QRRDL----GEELEALRgeledTLDSTNAQQELRSKR--EQEVTEL 1194
Cdd:COG4913 453 LGLDEAELpfvGELIEVRPEEERWRGAIERvlggFALTLlvppEHYAAALR-----WVNRLHLRGRLVYERvrTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1195 KKALEEESRAHEVS----------MQELRQRHSQALVEMAEQLEQARRG----------KGVWEK--------------- 1239
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEELRRHPRAitragqvkgnGTRHEKddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1240 --TRL-SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRS--SDSERARSEAAEKLQRAQAELESVSTALSEa 1314
Cdd:COG4913 608 nrAKLaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERLDASSDD- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1315 eskairlgkeLSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1394
Cdd:COG4913 687 ----------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1395 QEEEAAVLEAGEEARRRAAREAETLTQRLAEK-TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLE-----KKQRKF 1468
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEedglpEYEERF 836
|
650 660 670
....*....|....*....|....*....|.
gi 148690794 1469 DQLLAE----EKAAVLRAVED-----RERIE 1490
Cdd:COG4913 837 KELLNEnsieFVADLLSKLRRaireiKERID 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
926-1398 |
7.36e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 926 ARLAAR--KQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1003
Cdd:PRK02224 174 ARLGVErvLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1004 LLEDqnskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQ 1083
Cdd:PRK02224 252 ELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1084 EQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggaraqllksLREAQaglAEAQEDLEAERVARAKAEKQRRDLGEEL 1163
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-----------LREEA---AELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1164 EALRGELEDTLDSTNAQQELRskreQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR----GKGVWEK 1239
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFL----EELREERDELREREAELEATLRTARER-----VEEAEALLEAGKcpecGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1240 TRLSL----EAEVSELKAELSSLQTSRQEGEQKRRRLESqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAE 1315
Cdd:PRK02224 465 PHVETieedRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1316 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLrEQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1395
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELN 622
|
...
gi 148690794 1396 EEE 1398
Cdd:PRK02224 623 DER 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1489-1932 |
1.23e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.90 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1489 IEAEGREREARALSLTRALEEEQEAREELERQnrALRAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELED 1568
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELE--ELEAELEELEA----------ELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1569 ELTAAEDAKLRLEVTVQALKAQHER--DLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKA 1646
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1647 QTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRD 1726
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1727 EMAEEVAsgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLE 1806
Cdd:COG1196 446 EAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1807 RQIQELRARLGEEDAGAR----ARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQ 1882
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 148690794 1883 VRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESM 1932
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1222-1939 |
1.66e-13 |
|
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: 76.26 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1222 EMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEqKRRRLESQLQEVQG-----RSSDSERARSEAAEK 1296
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1297 LQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARE 1375
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1376 RAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQK 1455
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1456 QLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSK 1535
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1536 DDVGKNVHELERARKAAEQAASDLRTQVTELEDEL-----TAAEDAKLRlEVTVQALKAQHERDLQG---RDDAGEERRR 1607
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgTVAQLGSVG-ERYATAIEVAAGNRLNNvvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1608 QLAKQLRDAEVE-------RDEERKQRALAM-----------------------------------AARKKLEL------ 1639
Cdd:TIGR02169 565 ELLKRRKAGRATflplnkmRDERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvvedieAARRLMGKyrmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1640 ---------------ELEELKAQTSAAGQGKEEAVK-QLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAE 1703
Cdd:TIGR02169 645 egelfeksgamtggsRAPRGGILFSRSEPAELQRLReRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1704 VLRLQEELAAS--------------DRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSel 1769
Cdd:TIGR02169 725 IEQLEQEEEKLkerleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK-- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1770 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEdagaRARQKMLIAALESKLAQAEeqlEQES 1849
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI----EKEIENLNGKKEELEEELE---ELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1850 RERILSGKLVRRAEKRlKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRE------LE 1923
Cdd:TIGR02169 876 ALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLE 954
|
810
....*....|....*.
gi 148690794 1924 DVTESAESMNREVTTL 1939
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL 970
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
927-1559 |
2.48e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 927 RLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ---HIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdll 1003
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVKELEELKEEIEE--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1004 lLEDQNSKLSKERRLLEERLAEFSSQAAEE-------EEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRRLD 1076
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1077 GESSELQEQMVEQKQRAEELlAQLGRKEDELQAALLRAEEeggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKqr 1156
Cdd:PRK03918 321 EEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1157 rdlgEELEALRGELEDTLDSTNAQqelRSKREQEVTELKKALEEESRAHE---VSMQELRQRHSQALveMAEQLEQARRg 1233
Cdd:PRK03918 394 ----EELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKEL--LEEYTAELKR- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1234 kgvWEKTRLSLEAEVSELKAELSSLQTSRqEGEQKRRRLESQLQEVQgrsSDSERARSEAAEKLQRAQAELESVstalse 1313
Cdd:PRK03918 464 ---IEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLK---ELEEKLKKYNLEELEKKAEEYEKL------ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1314 aESKAIRLGKELSSAESQLHDTQELLQEetraKLALGSRVRALEAEAAGLREQMEEEVVARERagrELQSTQAQLSEWRR 1393
Cdd:PRK03918 531 -KEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESVE---ELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1394 RQEEeaavleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLgqqKQLLSTLEKKQRKFDQlla 1473
Cdd:PRK03918 603 EYLE------------------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSE--- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1474 eekaavlravEDRERIEAEGREREaRALSltraleeeqeareelerqnrALRAELEALLSSKDDVGKNVHELERARKAAE 1553
Cdd:PRK03918 659 ----------EEYEELREEYLELS-RELA--------------------GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
....*.
gi 148690794 1554 QAASDL 1559
Cdd:PRK03918 708 KAKKEL 713
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1064-1874 |
3.32e-13 |
|
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: 75.54 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1064 GRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKslREAQAglaeaQEDLE 1143
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRR--RESQS-----QEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1144 aervarakaeKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKALeeesRAHEVSMQELRQrhsqALVEM 1223
Cdd:pfam15921 145 ----------NQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMM----LSHEGVLQEIRS----ILVDF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1224 AEQleqarRGKGVWEKTRLSlEAEVSELKAELSSLQtsrqegeqkrRRLESQLQEVQGR----SSDSERARSEAAEK--- 1296
Cdd:pfam15921 197 EEA-----SGKKIYEHDSMS-TMHFRSLGSAISKIL----------RELDTEISYLKGRifpvEDQLEALKSESQNKiel 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1297 -LQRAQAELESVstaLSEAESKAIRLGKELSSAESQLHDTQ---ELLQEETRAKLALGSR-VRALEAEAAGLREQMEEEV 1371
Cdd:pfam15921 261 lLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1372 VARERAGRELqstqaqlsewrrrqeEEAAVLEAGEearrraareaetLTQRLAEKTEAVERLERARRRLQQELddatVDL 1451
Cdd:pfam15921 338 RMYEDKIEEL---------------EKQLVLANSE------------LTEARTERDQFSQESGNLDDQLQKLL----ADL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1452 GQQKQLLStLEKKQRK--FDQLLAEEKAA--VLRAVEDR----ERIEAEGREREARALSLTRALEEEQEAREELERQNRA 1523
Cdd:pfam15921 387 HKREKELS-LEKEQNKrlWDRDTGNSITIdhLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1524 LRAELEallSSKDDVGKNVHELERAR---KAAEQAASDLRTQVTELED--ELTAAEDAKLRLEVTVQALKAQHerdLQGR 1598
Cdd:pfam15921 466 LTAQLE---STKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELQH---LKNE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1599 DDageerrrqlakQLRDAEVERDEERKQRAlamAARKKLELELEELKAQTSAAGQGKEEAvkqlKKMQVQMKELWREVEE 1678
Cdd:pfam15921 540 GD-----------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQLVGQHGRTA----GAMQVEKAQLEKEIND 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1679 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEEL-----AASDRAR--RQAQQDRDEMAEEVASGNLSKAATLEEKRQLEG 1751
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnAGSERLRavKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1752 RLSQLEEEleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRARLG------- 1817
Cdd:pfam15921 682 NFRNKSEE----------METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDalqskiq 751
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1818 --EEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVD 1874
Cdd:pfam15921 752 flEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
861-1474 |
3.74e-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: 75.39 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------TRLAEQLRAEAELCSEAEETRARLAAR 931
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 932 KQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIqelESHLEAEEGARQKLQLEKVTTEAK-MKKFEEDLLLLEDQ-- 1008
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQhIHTLQQQKTTLTQKlq 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1009 --NSKLSKERRLLEERLAEFSSQAAEEEEKV--KSLNKLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRLDGESSELQ 1083
Cdd:TIGR00618 397 slCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1084 --EQMVEQKQRAEELLAQLGRKEDELQ----------AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE------ 1145
Cdd:TIGR00618 477 tkEQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQltserk 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1146 RVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMA 1224
Cdd:TIGR00618 557 QRASLKEQMQEiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1225 EQLEQARrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAEL 1304
Cdd:TIGR00618 637 CSQELAL------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1305 ESVSTA---LSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLalgsrvraleAEAAGLREQMEEEVVARERAGREL 1381
Cdd:TIGR00618 711 THIEEYdreFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL----------KARTEAHFNNNEEVTAALQTGAEL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1382 QSTQAQLSEWRRRQEE---EAAVLEAGEEARRRAAREAETLTQ-RLAEKTEAVERLERARRRLQQELDDATVDLGQQKQL 1457
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthLLKTLEAEIGQEIPSDEDILNLQCeTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
650
....*....|....*..
gi 148690794 1458 LSTLEKKQRKFDQLLAE 1474
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDK 877
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1140-1630 |
3.81e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.34 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1140 EDLEAERVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQQELRSK-----REQEVTELKKALEEESRAHEVSMQELRQ 1214
Cdd:COG4913 235 DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1215 RHSQ--ALVEMAEQLEQARRGKGVwektrlsleAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSE----R 1288
Cdd:COG4913 314 LEARldALREELDELEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1289 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeetraklALGSRVRALEAEAAGLREQME 1368
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--------------SLERRKSNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1369 EEVVARERAGR---ELQSTQAQLSEWRR---------------RQEEEAAVL-----------------EAGEEARRRAA 1413
Cdd:COG4913 451 EALGLDEAELPfvgELIEVRPEEERWRGaiervlggfaltllvPPEHYAAALrwvnrlhlrgrlvyervRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1414 REAETLTQRLAEKTEAVERLERARRRLQ---------QELDDA----TVDlGQQKQLLSTLEKKQRK------------- 1467
Cdd:COG4913 531 LDPDSLAGKLDFKPHPFRAWLEAELGRRfdyvcvdspEELRRHpraiTRA-GQVKGNGTRHEKDDRRrirsryvlgfdnr 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1468 -----FDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--ALRAELEALLSSKDDVGk 1540
Cdd:COG4913 610 aklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1541 nvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDlqgRDDAGEERRRQLAKQLRDAEVER 1620
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALLEERFAAALGDA 762
|
570
....*....|
gi 148690794 1621 DEERKQRALA 1630
Cdd:COG4913 763 VERELRENLE 772
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1240-1935 |
3.82e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1240 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQ--GRSSDSERARSEAAEKLQRAQAELESVSTALSEAESK 1317
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGkaEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1318 AIRLGKELSSAESQLHDTQELLQEETRaklalgsrvRALEAEAAGLREQMEEEVVARE--RAGRELQSTQAQLSEWRRRQ 1395
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDAR---------KAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1396 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1475
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1476 --KAAVLRAVEDRERI-EAEGREREARalsltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAA 1552
Cdd:PTZ00121 1289 kkKADEAKKAEEKKKAdEAKKKAEEAK--------------------------------------------KADEAKKKA 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1553 EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMA 1632
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1633 ARKKLELELEELKAQTSAAGQGKEEAVK--QLKKMQVQMK---ELWREVEETRSSRDemftLSRENEKKLKGLEAEvlRL 1707
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkadEAKKKAEEAKKAEE----AKKKAEEAKKADEAK--KK 1478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1708 QEELAASDRARRQAQQDRDEmAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1787
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1788 LSAERSfsAKAESGRQQLERQIQELRaRLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAE--KR 1865
Cdd:PTZ00121 1558 KKAEEK--KKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekKK 1634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1866 LKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAqagrrrlQRELEDVTESAESMNRE 1935
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-------KKAEEDEKKAAEALKKE 1697
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
874-1390 |
8.49e-13 |
|
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: 73.99 E-value: 8.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 874 QELQKVQELQQQSAREVGELQGRVAQL------------------EEERTR---LAEQLRAEAELCSEAEETRARLAark 932
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLliqitekenkmkdltfllEESRDKanqLEEKTKLQDENLKELIEKKDHLT--- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKL 1012
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1013 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDG-------ES 1079
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFllqarekEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1080 SELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG-------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1152
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1153 EKQRRDLGE-------ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR--HSQALVEM 1223
Cdd:pfam05483 533 LKQIENLEEkemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1224 AEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS--------LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAA 1294
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAyEIKVNKLELELASakqkfeeiIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1295 EKLQRAQAELESVSTALSEAESKAIRLGKELSSaESQLHDTQEllQEETRAKLALGSRVRALEAEAAGLREQMEEEVVAR 1374
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
570
....*....|....*.
gi 148690794 1375 ERAGRELQSTQAQLSE 1390
Cdd:pfam05483 770 EKLKMEAKENTAILKD 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
867-1389 |
3.12e-12 |
|
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: 71.78 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARAQELQKVQELQQQSAR------EVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarkqeLELVVT 940
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA--------LQTVIE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 941 ELEARVGEEEECSRQLQSEKKRL-----------QQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1006
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1007 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNkLRLKYEATIsdmedrLKKEEKGRQELEKLKRRLDGESSELQeQM 1086
Cdd:pfam10174 317 NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALR-LRLEEKESF------LNKKTKQLQDLTEEKSTLAGEIRDLK-DM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1087 VEQKQRA--------EELLAQLGRKE---DELQAALLRAEEEGGARAQLLKSLREAqagLAEAQEDLEAERVARAKAEKQ 1155
Cdd:pfam10174 389 LDVKERKinvlqkkiENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDTALTTLEEA---LSEKERIIERLKEQREREDRE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1156 RRdlgEELEALRGELEDTLDSTNAQQELRSKREQEVTELKkaleEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKG 1235
Cdd:pfam10174 466 RL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1236 VWEKTRLSleAEVSELKAELSSlqtsrqegeqKRRRLEsqlQEVQGRSSDSERARSEAA---EKLQRAQAELESVSTALS 1312
Cdd:pfam10174 539 QLKKAHNA--EEAVRTNPEIND----------RIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIA 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1313 EAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLS 1389
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
855-1280 |
3.52e-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: 71.59 E-value: 3.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 855 KVKPLLQVTRQDEVLQARAQELQ-KVQELQQQSAREV-GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 932
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1012
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1013 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEkgrQELEKLKRRLDGESSELqEQMVEQKQR 1092
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKEL-KKLNEEKKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1093 AEELLAQLGRKEDELQaallraeeeggaraqllkslreaqaglaEAQEDLEAERvarAKAEKQRRDLGEELEalrgELED 1172
Cdd:TIGR04523 508 LEEKVKDLTKKISSLK----------------------------EKIEKLESEK---KEKESKISDLEDELN----KDDF 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1173 TLDSTNAQQELRSKrEQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQarrgkgvWEKTRLSLEAEVSELK 1252
Cdd:TIGR04523 553 ELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEE-------KEKKISSLEKELEKAK 623
|
410 420
....*....|....*....|....*...
gi 148690794 1253 AELSSLQTSRQEGEQKRRRLESQLQEVQ 1280
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
869-1230 |
8.13e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.14 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 869 LQARAQELQKVQELQQQsarevgelQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 948
Cdd:COG3096 329 YQAASDHLNLVQTALRQ--------QEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 949 EEECSRQLQSEKKRLQQHIQELEShleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERRLLEERLAEFSS 1028
Cdd:COG3096 401 YQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVADA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1029 QAAEEEEKVKSLNKlrlkyeatISDMEDRLKKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQKQRAEELLAQL 1100
Cdd:COG3096 470 ARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEEF 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1101 GRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT 1173
Cdd:COG3096 542 CQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEA 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1174 LDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQA 1230
Cdd:COG3096 622 LADS-----------QEVTAAMQQLLEREREATVERDELAAR-KQALESQIERLSQP 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
790-1278 |
9.32e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 790 LAQLEEERdlkvtdiivsfqaaargylarrafqrrqqqqsalrvmqrncaaylklrnwqwwrlfikvkpLLQVTRQDEVL 869
Cdd:COG1196 360 LAEAEEAL-------------------------------------------------------------LEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 870 QARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEE 949
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 950 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQ 1029
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1030 AAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQE---LEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1106
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1107 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDtldstnAQQELRSK 1186
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE------LAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1187 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELsslqtSRQEGE 1266
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP-----DLEELE 766
|
490
....*....|..
gi 148690794 1267 QKRRRLESQLQE 1278
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
897-1931 |
1.12e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 897 VAQLEEERTRLAEQLRAEAELCSEAEEtraRLAARKQELELVVTELEARVGEE--------EECSRQLQSEKKRLQQHIQ 968
Cdd:NF041483 246 AAESDQARRQAAELSRAAEQRMQEAEE---ALREARAEAEKVVAEAKEAAAKQlasaesanEQRTRTAKEEIARLVGEAT 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 969 ELESHLEAEEG---ARQKLQLEKVTTEAKMKKfeeDLLLLEDQNSKLSKERRLLEERLAEfSSQAAEEEEKVKSLNKLRL 1045
Cdd:NF041483 323 KEAEALKAEAEqalADARAEAEKLVAEAAEKA---RTVAAEDTAAQLAKAARTAEEVLTK-ASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1046 KYEATISdmEDRLKKEekGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL--AQLGRKEDELQAALLRAEEEGGARAQ 1123
Cdd:NF041483 399 RREAEAE--ADRLRGE--AADQAEQLKGAAKDDTKEYRAKTVELQEEARRLRgeAEQLRAEAVAEGERIRGEARREAVQQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1124 LLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRSKREQEVTELKKALEEE 1201
Cdd:NF041483 475 IEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERA 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1202 SRahevsmqELRqrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEvSELKAELSSLQTSRQEGEQKRRRlesqlqevqg 1281
Cdd:NF041483 555 AR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEAERIRRE---------- 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1282 RSSDSERARSEAAEKLQ--RAQAELES----------VSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL 1349
Cdd:NF041483 609 AAEETERLRTEAAERIRtlQAQAEQEAerlrteaaadASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1350 GSRVRALEAeAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAReaeTLTQRLAEKTEA 1429
Cdd:NF041483 689 AAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEAQ---AEAQRLVEEADR 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1430 -VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAVLRAVEDRERIEAEGRE 1495
Cdd:NF041483 765 rATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAERERASEDANRLRREAQE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1496 REARALSLtraleeeqeareelerqnralraeleallsSKDDVGKNVHELERARKAAEQAASDLRTqvtELEDELTAAED 1575
Cdd:NF041483 845 ETEAAKAL------------------------------AERTVSEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQ 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1576 AKLRLEVtvqalkaqherdlQGRDDAgeERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGK 1655
Cdd:NF041483 892 DAARTRA-------------DAREDA--NRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAA 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1656 EEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSR-ENEKKLKGLEAEVLRLQEELAAS-----DRARRQAQQDRDEMA 1729
Cdd:NF041483 957 AQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRtEAERVKAEAAAEAERLRTEAREEadrtlDEARKDANKRRSEAA 1036
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1730 EEV---ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----------KLVLQVESLTTEL--SAERSF 1794
Cdd:NF041483 1037 EQAdtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERivaeatvegnSLVEKARTDADELlvGARRDA 1116
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1795 SA---KAESGRQQLERQIQELRARLGEEDA----GARARQKMLIAALESKLAQAEEQLEQ--------ESRERILSgklV 1859
Cdd:NF041483 1117 TAireRAEELRDRITGEIEELHERARRESAeqmkSAGERCDALVKAAEEQLAEAEAKAKElvsdanseASKVRIAA---V 1193
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1860 RRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL-KQLKRQLEEAEEEASRAQAGRRRLQreleDVTESAES 1931
Cdd:NF041483 1194 KKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQ----DVLEALES 1262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
861-1277 |
1.82e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAeAELCSEAEETRARLA----------A 930
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-LPLYQELEALEAELAelperleeleE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 931 RKQELELVVTELEARVGEEEECSRQLQSEKKRL----QQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1006
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1007 DQNSKLSKERRLLEER--------LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEE----KGRQELEKLKRR 1074
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaslgKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1075 LDGESSELQEQMVEQ---KQRAEELLAQLGRKEDELQAALLRAEEEgGARAQLLKSLREAQAGLAEAQEDLEAERVARAK 1151
Cdd:COG4717 314 EELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEEL-EEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1152 AEKQRRDLGEELEALRGELEdtldstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE---QLE 1228
Cdd:COG4717 393 QAEEYQELKEELEELEEQLE---------ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEleaELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1229 QARRGKGVWEKT--RLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQ 1277
Cdd:COG4717 464 QLEEDGELAELLqeLEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1120-1332 |
3.35e-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: 67.48 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1120 ARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALE 1199
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1200 EESRA---HEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQL 1276
Cdd:COG4942 101 AQKEElaeLLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1277 QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQL 1332
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1263-1945 |
6.09e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 67.89 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1263 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQrAQAELesvstaLSEAESKAIRLGKELSSAESQLHDTQELLQEE 1342
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETEL------CAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1343 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrRRQEEEAAVLEageearrraareaetltqr 1422
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI----KKLEEDILLLE------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1423 laektEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEekaavlraVEDRERIEAEGRErearals 1502
Cdd:pfam01576 145 -----DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--------LEERLKKEEKGRQ------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1503 ltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1582
Cdd:pfam01576 205 -----------------------------------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1583 TVQALKAQHErDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQ------TSAAGQ--- 1653
Cdd:pfam01576 244 ELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldTTAAQQelr 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1654 -GKEEAVKQLKKMQVqmkelwrevEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1732
Cdd:pfam01576 323 sKREQEVTELKKALE---------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1733 ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL 1812
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1813 RARLGEEdagarARQKMLIA----ALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLE 1888
Cdd:pfam01576 474 QELLQEE-----TRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1889 KSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1945
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
909-1394 |
8.11e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.56 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 909 EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsrQLQSEKKRLQQHIQELESHLEAeegARQKLQLEK 988
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE---ERQETSAELNQLLRTLDDQWKE---KRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 989 VTTEAKMKKFEEDLLLLEDQNSKLSKER----RLLEERLAEFSSQAAEEEEKVKSL----NKLRLKYEATISDMEDRLKK 1060
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKALtgkhQDVTAKYNRRRSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1061 EEKG-RQELEKLK----RRLDGESSELQEQmvEQKQRaEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSlREAQAGL 1135
Cdd:pfam12128 391 DIAGiKDKLAKIReardRQLAVAEDDLQAL--ESELR-EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1136 AEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRA--HEVSMQELR 1213
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTllHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1214 QRHSQALVEMAEQLEQARRGKGVWEKT----------RLSLE--------AEVSELKAELSSLQTSRQEGEQKRRRLESQ 1275
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLDPEVWDGSvggelnlygvKLDLKridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1276 L-------QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL-GKELSSAESQL----HDTQELLQEET 1343
Cdd:pfam12128 627 LvqangelEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLkqldKKHQAWLEEQK 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1344 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRE-LQSTQAQLSEWRRR 1394
Cdd:pfam12128 707 EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgAKAELKALETWYKR 758
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1060-1924 |
8.97e-11 |
|
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: 67.40 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1060 KEEKGRQELEKLKRRLD------GESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqLLKSLREAQA 1133
Cdd:TIGR02169 171 KKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1134 GLAEAQEDLEaervaraKAEKQRRDLGEELEALRGELEDtldstnAQQELRSKREQEVTELKKALeeesraHEVSMQELR 1213
Cdd:TIGR02169 245 QLASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKI------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1214 QRHSQALVEMAEQLEQARRGKGVWEKTRL-----SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSER 1288
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLlaeieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1289 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1368
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1369 EEvvarERAGRELQSTQAQLSEWRRRQEEEAAVleageearrraareaetltqrlAEKTEAVERLERARRRLQQELDDAT 1448
Cdd:TIGR02169 466 KY----EQELYDLKEEYDRVEKELSKLQRELAE----------------------AEAQARASEERVRGGRAVEEVLKAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1449 VD--LGQQKQLLSTLEKKQrkfdqlLAEEKAAVLRA----VED----RERIEAEGREREARALSLTRALEEEQEAREELE 1518
Cdd:TIGR02169 520 IQgvHGTVAQLGSVGERYA------TAIEVAAGNRLnnvvVEDdavaKEAIELLKRRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1519 RQNRALRAELEalLSSKDDVGKN-----------VHELERARKAAEQA-ASDLRTQVTELEDELTAAEDAKLRLEVTVQA 1586
Cdd:TIGR02169 594 SEDGVIGFAVD--LVEFDPKYEPafkyvfgdtlvVEDIEAARRLMGKYrMVTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1587 LKAQHERdLQGRDDAGEERRRQLAKQLRDAEVERDEerkqralAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1666
Cdd:TIGR02169 672 EPAELQR-LRERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1667 VQMKELWREVEETRSSRDEmftlsreNEKKLKGLEAEVLRLQEELAA-----SDRARRQAQQDRDEMAEEVASGNLSKAA 1741
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-------LEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1742 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHyrklvlqveslttelsaersfsakaesgRQQLERQIQELRARLGEEDA 1821
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----------------------------IKSIEKEIENLNGKKEELEE 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1822 gararqkmLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQL 1901
Cdd:TIGR02169 869 --------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900
....*....|....*....|....*....
gi 148690794 1902 EEAEEEAS------RAQAGRRRLQRELED 1924
Cdd:TIGR02169 941 GEDEEIPEeelsleDVQAELQRVEEEIRA 969
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
859-1488 |
1.20e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.07 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQQQSARE-VGELQGRVAQLEEERTRLAEQLRAEaelcSEAEETRarlaarKQELEL 937
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQEMQMERDAMADIRRRE----SQSQEDL------RNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 938 VVTELEArvgeeEECSRQLQSEKKRLQqhIQELESHLEAEEGARQKLQLEKVT-TEAKMKKFEE----DLLLLEDQNSKL 1012
Cdd:pfam15921 150 TVHELEA-----AKCLKEDMLEDSNTQ--IEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEhdsmSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1013 SKERRLLEERLAEFSSQAAEEEEKVKSL-----NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1087
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALksesqNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1088 EQKQRAEELLAQLGRKEDELQAALlraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1167
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTV----------SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1168 GELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQrhsqalvEMAEQLEQARRgkgvwektrlsLEAE 1247
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR-------ELDDRNMEVQR-----------LEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1248 VSELKAELSSlqtsrqegeqkrrRLESQLQEVQGRSsdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1327
Cdd:pfam15921 435 LKAMKSECQG-------------QMERQMAAIQGKN--------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1328 AESQLHDTQELLQEETRAklalgsrVRALEAEAAGLREQME---EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLea 1404
Cdd:pfam15921 494 SERTVSDLTASLQEKERA-------IEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVI-- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1405 geearRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAE---EKAAVLR 1481
Cdd:pfam15921 565 -----EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLVN 639
|
....*..
gi 148690794 1482 AVEDRER 1488
Cdd:pfam15921 640 AGSERLR 646
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1007-1215 |
1.41e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.56 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1007 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM 1086
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1087 VEQKQRAEELLAQLGRKEDELQAALLRAEEEGG--------------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1152
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1153 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR 1215
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
872-1183 |
1.50e-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: 66.30 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 872 RAQELQKVQELQQQSAREVGElQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAARKQELELVVTELEARVGEEEE 951
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAME--RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 952 CSRQLQSEKKRLQQHIQEleshlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAA 1031
Cdd:pfam17380 379 ELERLQMERQQKNERVRQ-----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1032 EEEEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRR-LDGESSELQEQMVEQKQRAEELLAQLgrkeDELQAA 1110
Cdd:pfam17380 454 EEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEM----EERQKA 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1111 LLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARA--KAEKQRRDLgEELEALRGELEDTLDSTNAQQEL 1183
Cdd:pfam17380 529 IYEEERR-----------REAEEERRKQQEMEERRRIQEQmrKATEERSRL-EAMEREREMMRQIVESEKARAEY 591
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1243-1901 |
1.51e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1243 SLEAEVSELKAELSSLQTSRQEGEQKRRRLEsQLQEVQgrssdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLG 1322
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIR-----------ELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1323 KELssAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMeeevvaRERAGRELQSTQAQLSEWRRRQEEeaavl 1402
Cdd:COG4913 290 LEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEE----- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1403 eageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDAtvdLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRA 1482
Cdd:COG4913 357 ----------------RERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1483 VEDRERIEAEGREREARALSLTRALEeeqeareelerqnrALRAELEALLSSKDD----VGK--NVHELERA-RKAAEQA 1555
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLL--------------ALRDALAEALGLDEAelpfVGEliEVRPEEERwRGAIERV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1556 asdLRTQVTEL--EDELTAA-----EDAKLRLEVTVQALKAQHERDLQGRDDAG--------------EERRRQLAKQLR 1614
Cdd:COG4913 484 ---LGGFALTLlvPPEHYAAalrwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrAWLEAELGRRFD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1615 DAEVERDEERKQRALAMaarkkleleleelkaqtSAAGQGKEEAVKQLKKMQVQMKELWReveetrssrdemftLSRENE 1694
Cdd:COG4913 561 YVCVDSPEELRRHPRAI-----------------TRAGQVKGNGTRHEKDDRRRIRSRYV--------------LGFDNR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1695 KKLKGLEAEVLRLQEELAASDRARRQAQQDRDemaeevasgnlskaaTLEEKRQLEGRLSQLEEELEEEQNnsellkdhy 1774
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEIDVAS--------- 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1775 rkLVLQVESLTTELSAERSFSAKAEsgrqQLERQIQELRARLgEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ES 1849
Cdd:COG4913 666 --AEREIAELEAELERLDASSDDLA----ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdrlEA 738
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1850 RERILSGKLVRRAEKRLKEVVLQvDEERRVADQVRDQLEKSNLRLKQLKRQL 1901
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
962-1500 |
1.72e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.48 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 962 RLQQHIQELES-HLEAEEGARQKLQLEKVTTEA-KMKKFEEDLLLLEDQNSKL-----SKERRLLEERLAEFSSQAAEEE 1034
Cdd:COG4913 229 ALVEHFDDLERaHEALEDAREQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1035 EKVkslnklrlkyeatisdmeDRLKKEEKG-RQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1113
Cdd:COG4913 309 AEL------------------ERLEARLDAlREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1114 AEEEG-GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQ 1189
Cdd:COG4913 371 LGLPLpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1190 EVTELKKALEEESRAHEVSMQ------ELRQR------------HSQA---LVEmAEQLEQARR--------GKGVWEKT 1240
Cdd:COG4913 441 RLLALRDALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFAltlLVP-PEHYAAALRwvnrlhlrGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1241 RLSLEAEVSE---------------------LKAELSSLQ-----TSRQEGEQKRRRLESQLQEVQGRSS----DSERAR 1290
Cdd:COG4913 520 RTGLPDPERPrldpdslagkldfkphpfrawLEAELGRRFdyvcvDSPEELRRHPRAITRAGQVKGNGTRhekdDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1291 SE------AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKlalgsRVRALEAEAAGLR 1364
Cdd:COG4913 600 SRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1365 EQMEEEvvarERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVERLerarrrlQQEL 1444
Cdd:COG4913 675 AELERL----DASSDDLAALEEQLEELEAELEE---------------------LEEELDELKGEIGRL-------EKEL 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1445 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEK--AAVLRAVEDRERIEAEGREREARA 1500
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRA 780
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
891-1749 |
1.79e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 891 GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTelearvgeeeecSRQLQSEKKRLQQHIQEL 970
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT------------ALRQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 971 ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFsSQAAEEEEKVKSLNKLRLKYEAT 1050
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1051 ISDMEDRLK-KEEKGRQELEKLKRRLDgesseLQEQMVEQKQRAEELLAQLGRKEDELQA-----ALLRAEEEGGARAQL 1124
Cdd:PRK04863 440 AEDWLEEFQaKEQEATEELLSLEQKLS-----VAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1125 LKSLReaqAGLAEAQEDLEAERVA-RAKAEKQRR-----DLGEELEALRGELEDTLDSTNAQQElrskreqEVTELKKAL 1198
Cdd:PRK04863 515 LQQLR---MRLSELEQRLRQQQRAeRLLAEFCKRlgknlDDEDELEQLQEELEARLESLSESVS-------EARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1199 EEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQE 1278
Cdd:PRK04863 585 RQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1279 VQGRSSDSerarseaAEKLQRAQAELESVSTA-------LSEAESKAIRLG--------KELSSAESQL----------- 1332
Cdd:PRK04863 664 LSQPGGSE-------DPRLNALAERFGGVLLSeiyddvsLEDAPYFSALYGparhaivvPDLSDAAEQLagledcpedly 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1333 -------------HDTQEL----LQEETRAKLALgSRV--------RALEAEAAGLREQMEEEVVARERAGRELQSTQ-- 1385
Cdd:PRK04863 737 liegdpdsfddsvFSVEELekavVVKIADRQWRY-SRFpevplfgrAAREKRIEQLRAEREELAERYATLSFDVQKLQrl 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1386 ---------------------AQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR------------------LAEK 1426
Cdd:PRK04863 816 hqafsrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1427 TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLlaeeKAAVLRAVEDRERIEAegrerEARALSltra 1506
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQ-----QAFALT---- 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1507 leeeqeareeLERQNRALRAELEA--LLSSKDDvgkNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTV 1584
Cdd:PRK04863 963 ----------EVVQRRAHFSYEDAaeMLAKNSD---LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1585 QALKAQH---ERDLQG---RDDAGEE-----RRRQLAKQLRDAEVERDEERKQRALAMAARkkleleleelkaqtsaagq 1653
Cdd:PRK04863 1030 DAKRQMLqelKQELQDlgvPADSGAEeraraRRDELHARLSANRSRRNQLEKQLTFCEAEM------------------- 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1654 gkEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSREN--EKKLKGLEAEVLRLQEELAASDRAR---RQAQQDRDEM 1728
Cdd:PRK04863 1091 --DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKALgalRLAVADNEHL 1168
|
970 980
....*....|....*....|.
gi 148690794 1729 AEEVASgnLSKAATLEEKRQL 1749
Cdd:PRK04863 1169 RDVLRL--SEDPKRPERKVQF 1187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
869-1340 |
3.55e-10 |
|
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: 65.15 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 869 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLA-EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 947
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 948 EEEECSRQLQSEKKRLQQH---IQELESHLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLskerrlleERLA 1024
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAeqlRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSEL--------ARIP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1025 EFSSQAAEEEEKVKSLNKLR---LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQE-----QMVEQKQRAEEL 1096
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaQDTGLNLRSPED 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1097 LAqlGRKEDELQAALLRAEEEGGARAQLL---KSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL-------GEELEAL 1166
Cdd:pfam05557 281 LS--RRIEQLQQREIVLKEENSSLTSSARqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvlllTKERDGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1167 RGELED-----TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQaLVEMAEQLEQARRGKGVWEKTR 1241
Cdd:pfam05557 359 RAILESydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQ-QAQTLERELQALRQQESLADPS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1242 LSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQL--QEVQGRS---------------SDSERARSEAAEKLQ------ 1298
Cdd:pfam05557 438 YSKE-EVDSLRRKLETLELERQRLREQKNELEMELerRCLQGDYdpkktkvlhlsmnpaAEAYQQRKNQLEKLQaeierl 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1299 -----RAQAELESV----STALSEAESKAIRLGKELSSAESQLHDTQELLQ 1340
Cdd:pfam05557 517 krllkKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1014-1873 |
5.83e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 5.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1014 KERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRA 1093
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDL-------EQDYQAASDHLNLVQTALRQQEKIER-YQADLEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1094 EELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDLGEELEALRGELEDT 1173
Cdd:PRK04863 372 EEADEQQ----EENEARAEAAEEE----------VDELKSQLADYQQALDVQQ-TRAIQYQQAVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1174 LDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQAL---------VEMAEQLEQARRGKGVWEKTRLsL 1244
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQAYqlvrkiageVSRSEAWDVARELLRRLREQRH-L 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1245 EAEVSELKAELSSLQTSRQEgeqkRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAirlgke 1324
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR------ 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1325 lssaeSQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ---LSEWRRRQEEEAAV 1401
Cdd:PRK04863 582 -----MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERereLTVERDELAARKQA 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1402 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRlqqELDDA---------------TVDLGQQKQLLSTL----- 1461
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIYDDV---SLEDApyfsalygparhaivVPDLSDAAEQLAGLedcpe 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1462 -----EKKQRKFDQ--LLAEE-KAAVLRAVEDRE----RIEAE---GRE-REARALsltraleeeqeareelerqnrALR 1525
Cdd:PRK04863 734 dlyliEGDPDSFDDsvFSVEElEKAVVVKIADRQwrysRFPEVplfGRAaREKRIE---------------------QLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1526 AELEALLSSKDDVGKNVHELERARKAA----------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA 1589
Cdd:PRK04863 793 AEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1590 QHE--RDLQGR-----DDAGEERRRQLAKQLRDAEV-ERDEERKQRALAMAARKKleleleelkaqtsAAGQGKEEAVKQ 1661
Cdd:PRK04863 873 GLSalNRLLPRlnllaDETLADRVEEIREQLDEAEEaKRFVQQHGNALAQLEPIV-------------SVLQSDPEQFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1662 LKKMQVQMKELWREVeetrssRDEMFTLSRENEKKLK-GLEAEVLRLQEELAASDRAR---RQAQQDRDEMAEEVasgnl 1737
Cdd:PRK04863 940 LKQDYQQAQQTQRDA------KQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRAREQL----- 1008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1738 skaatleekRQLEGRLsqleeeleeeqnnsellkDHYRKLVLQVESlttelsaerSFSAKAESgRQQLERQIQEL--RAR 1815
Cdd:PRK04863 1009 ---------RQAQAQL------------------AQYNQVLASLKS---------SYDAKRQM-LQELKQELQDLgvPAD 1051
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1816 LGEEDAgARARQKMLIAAL---ESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQV 1873
Cdd:PRK04863 1052 SGAEER-ARARRDELHARLsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
892-1494 |
7.28e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 7.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 892 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTE----------LEARVGEEEECSRQLQSEKK 961
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 962 RLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSL 1040
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1041 NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSE----LQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEE 1116
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1117 EGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQ---------------- 1180
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveleelkkilaedek 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1181 ------------QELRSKrEQEVTELKKALEEESRAHEVSMQELR---QRHSQALVEMAEQLEQ---------ARRGKGV 1236
Cdd:pfam05483 420 lldekkqfekiaEELKGK-EQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKeklknieltAHCDKLL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1237 WEKTRLSLEAE--VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEA 1314
Cdd:pfam05483 499 LENKELTQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1315 ESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1394
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1395 QEEEAAVleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATvdlgQQK--QLLSTLEKKQRKFDQLL 1472
Cdd:pfam05483 659 YQKEIED--------------KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC----QHKiaEMVALMEKHKHQYDKII 720
|
650 660
....*....|....*....|..
gi 148690794 1473 aEEKAAVLRAVEDRERIEAEGR 1494
Cdd:pfam05483 721 -EERDSELGLYKNKEQEQSSAK 741
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
865-1257 |
7.51e-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: 63.76 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 944
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 945 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLA 1024
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1025 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELqeqmveqkqraEELLAQLGRKE 1104
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-----------SSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1105 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDL------EAERVARAKAEKQRRD--LGEEL---EALRGELEDT 1173
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALREGRARWAQERETLqqsaeaDKDRIEKLSAELQRLEerLQEERmerEKLEVELGRE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1174 LDSTNAQqelRSKREQEVTELKKALEEESRAhevsmQELRQRHSQALVEMAEQLEQaRRGKGVWEKTRLSLEAEVSELKA 1253
Cdd:pfam07888 352 KDCNRVQ---LSESRRELQELKASLRVAQKE-----KEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDS 422
|
....
gi 148690794 1254 ELSS 1257
Cdd:pfam07888 423 PLSD 426
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1524-1945 |
1.64e-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: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1524 LRAELEALLSSKDDVGKNVHELERAR-KAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAG 1602
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1603 EERRRQLAKQLRDAEVERDeERKQRALAMAarkkleleleelkAQTSAAGQGKEEAVKQLKKMQVQMKELwreVEETRSS 1682
Cdd:COG4913 337 GDRLEQLEREIERLERELE-ERERRRARLE-------------ALLAALGLPLPASAEEFAALRAEAAAL---LEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1683 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRAR----RQAQQDRDEMAEE--------------------------- 1731
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEAlgldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1732 -------------VASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDH--YRKLVLQVESLTTELSAE--RSF 1794
Cdd:COG4913 480 iervlggfaltllVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1795 S-AKAESGrQQLER---------QIQELRARlGEEDA----------GARARQKmlIAALESKLAQAEEQLEQ-ESRERI 1853
Cdd:COG4913 560 DyVCVDSP-EELRRhpraitragQVKGNGTR-HEKDDrrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1854 LSGKL-----VRRAEKRLKEV------VLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQREL 1922
Cdd:COG4913 636 LEAELdalqeRREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500
....*....|....*....|...
gi 148690794 1923 EDVTESAESMNREVTTLRNRLRR 1945
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEA 738
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1000-1836 |
3.45e-09 |
|
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: 62.28 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1000 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDgES 1079
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1080 SELQEQMVEQKQRAEELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDL 1159
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEE----------VDSLKSQLADYQQALDVQQ-TRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1160 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEeesraHEVSM-QELRQRHSQA---LVEMAEQLEQARrgkg 1235
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE-----QKLSVaDAARRQFEKAyelVCKIAGEVERSQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1236 VWEKTRLSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQ------LQEVQGRSSDSERARSEAAEKLQRAQAELESVST 1309
Cdd:COG3096 493 AWQTARELLR-RYRSQQALAQRLQQLRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1310 ALSEAESKAIRLGKELSSAESQ-------------LHDTQELLQEETRAKLAlgsrvraleaEAAGLREQMEEeVVARER 1376
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALA----------DSQEVTAAMQQ-LLERER 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1377 agrELQSTQAQLSEWRRRQEEEAAVLEAGEEARRraareaeTLTQRLAEKTEAVERLERARRRLqqeLDDATV------- 1449
Cdd:COG3096 641 ---EATVERDELAARKQALESQIERLSQPGGAED-------PRLLALAERLGGVLLSEIYDDVT---LEDAPYfsalygp 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1450 --------DLGQQKQLLSTL----------EKKQRKFDQLL---AEEKAAVLRAVEDRE----RIEAE---GRE-REARA 1500
Cdd:COG3096 708 arhaivvpDLSAVKEQLAGLedcpedlyliEGDPDSFDDSVfdaEELEDAVVVKLSDRQwrysRFPEVplfGRAaREKRL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1501 lsltraleeeqeareelerqnRALRAELEALLSSKDDVGKNVHELERARKAAEQ----------------AASDLRTQVT 1564
Cdd:COG3096 788 ---------------------EELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1565 ELEDELTAAEDAKLRLEVTVQALKAQHE--RDLQGR-----DDAGEERRRQLAKQLRDAEVERDEERKQRAlAMAARKKL 1637
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGK-ALAQLEPL 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1638 ELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETR-----SSRDEMFTLSRE-NEKklkgLEAEVLRLQEEL 1711
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRphfsyEDAVGLLGENSDlNEK----LRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1712 AASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKdhyrklvlqVESLTTELSAE 1791
Cdd:COG3096 1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIR---------RDELHEELSQN 1071
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 148690794 1792 RSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALES 1836
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1088-1328 |
4.10e-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: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1088 EQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1167
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1168 GELEDTLDSTnAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQarrgkgvwekTRLSLEAE 1247
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----------DLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1248 VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1327
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 148690794 1328 A 1328
Cdd:COG4942 246 A 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1156-1958 |
6.07e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.47 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1156 RRDLGEELEALRGELeDTLDStnAQQELRSKREQevtelKKALEEESRAHEvSMQELRQRHS--QALVEMAeQLEQARRG 1233
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLER--AHEALEDAREQ-----IELLEPIRELAE-RYAAARERLAelEYLRAAL-RLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1234 KGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserARSEAAEKLQRAQAELESVSTALSE 1313
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1314 AESKAIRLGKELSSAESQLHDTQELLQEetraklalgsRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRR 1393
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1394 RQ----EEEAAVLEAgeearrraareaetLTQRLAEKTEAVERLErarrrlqqELDDatVDLGQQK------QLLSTLek 1463
Cdd:COG4913 434 RKsnipARLLALRDA--------------LAEALGLDEAELPFVG--------ELIE--VRPEEERwrgaieRVLGGF-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1464 kqrKFDqLLAEEK--AAVLRAVEDR--------ERIEAEGREREARAL---SLTRALEEEQEareelerqnrALRAELEA 1530
Cdd:COG4913 488 ---ALT-LLVPPEhyAAALRWVNRLhlrgrlvyERVRTGLPDPERPRLdpdSLAGKLDFKPH----------PFRAWLEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1531 LLSSKDDVGK--NVHELERARKAaeqaasdlrtqvteledeltaaedaklrleVTVQALkAQHERDLQGRDDAGEERRRQ 1608
Cdd:COG4913 554 ELGRRFDYVCvdSPEELRRHPRA------------------------------ITRAGQ-VKGNGTRHEKDDRRRIRSRY 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1609 L-----AKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAgqgkeEAVKQLKKMQVQMKELWREVEETRSSR 1683
Cdd:COG4913 603 VlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAELEAEL 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1684 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEE 1763
Cdd:COG4913 678 ERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1764 QNNSELLKDHYRKLvlqVESLTTELSAERsfsAKAESGRQQLERQIQELRAR-------LGEEDAGARARQKMLIAALES 1836
Cdd:COG4913 754 RFAAALGDAVEREL---RENLEERIDALR---ARLNRAEEELERAMRAFNREwpaetadLDADLESLPEYLALLDRLEED 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1837 KLAQAEEQLEQEsrerilsgkLVRRAEKRLKEVVLQVDEERRvadQVRDQLEKSNLRLKQLK----RQLEEAEEEASRAQ 1912
Cdd:COG4913 828 GLPEYEERFKEL---------LNENSIEFVADLLSKLRRAIR---EIKERIDPLNDSLKRIPfgpgRYLRLEARPRPDPE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1913 AgrRRLQRELEDVTESAESMNRE--------VTTLRNRLRRGPLTFTTRTVRQV 1958
Cdd:COG4913 896 V--REFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEEESDRRWRARV 947
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
898-1127 |
6.36e-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: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 898 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEae 977
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 978 egaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL--LEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDME 1055
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1056 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRaeelLAQLGRKEDELQAALLRAEEEGGARAQLLKS 1127
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
865-1093 |
7.07e-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: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 944
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 945 RVGE-EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1023
Cdd:COG4942 98 ELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1024 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRA 1093
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
967-1345 |
7.26e-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: 60.74 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 967 IQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1046
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1047 YEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK--EDELQAALLRAEEEG------ 1118
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKiaEYTKSIDIKKATESLeeqlaa 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1119 -GARAQLLKSLREAQAGLAEAQEDLeaervarakaEKQRRDLGEELEALRGELE---DTLDSTNAQQELRSKrEQEVTEL 1194
Cdd:COG5185 321 aEAEQELEESKRETETGIQNLTAEI----------EQGQESLTENLEAIKEEIEnivGEVELSKSSEELDSF-KDTIEST 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1195 KKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQkrrrlES 1274
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---IEQATSSNEEVSKLLNELISELNKVMREADE-----ES 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1275 QLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRA 1345
Cdd:COG5185 462 QSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1105-1505 |
1.30e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1105 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNA 1179
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1180 QQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQ 1259
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1260 TSRQEGEQKRR--------RLESQLQEVQGRSSDSERARSEAAE--------------KLQRAQAELESVSTALSEAESK 1317
Cdd:COG4717 234 NELEAAALEERlkearlllLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1318 AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQlsewrrrQEE 1397
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVE-------DEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1398 EAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQ--QELDDATVDL----GQQKQLLSTLEKKQRKFDQL 1471
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELeeleEELEELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|....
gi 148690794 1472 LAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1505
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1023-1232 |
1.83e-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: 58.62 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQrAEELLAQLGR 1102
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 KEDELQAALLRAEEEGGARAQLL--KSLREAQAGLAEAQEDLEAERVAR--AKAEKQRRDLGEELEALRGELEDTLDSTN 1178
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1179 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1232
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
954-1398 |
1.90e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 954 RQLQSEKKRLQQhIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLED--QNSKLSKERRLLEERLAEFSSQAA 1031
Cdd:COG4717 71 KELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1032 EEEEKVKSLNKLRlkyeatiSDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1111
Cdd:COG4717 150 ELEERLEELRELE-------EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1112 LRAEEE------GGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLG-------------EELEALRGELED 1172
Cdd:COG4717 223 EELEEEleqlenELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1173 TLDSTNAQQELRSKREQEVTELKKA--LEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE 1250
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1251 LKAELSSLQTSRQEGEQKRRRLESQLQEVqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAES 1330
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQL--EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1331 QLHDtqellqeetrakLALGSRVRALEAEAAGLREQMEEEvvarERAGRELQSTQAQLSEWRRRQEEE 1398
Cdd:COG4717 461 ELEQ------------LEEDGELAELLQELEELKAELREL----AEEWAALKLALELLEEAREEYREE 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
860-1341 |
1.97e-08 |
|
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: 59.75 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 860 LQVTRQDEVLQARAQELQKVQELQ-------QQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 932
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELVVtelearvgeeEECSRQLQSEKKRLQQHIQELEsHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1012
Cdd:pfam15921 506 QEKERAI----------EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1013 SKerrLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE--ATISDMEDRLKKEEKGR-QELEKLKRRLDGESSELQEQMVEQ 1089
Cdd:pfam15921 575 TQ---LVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAKIRELEARvSDLELEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1090 KQRAEELLAQLGRKEDELQA------ALLR-----AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1158
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSlsedyeVLKRnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1159 LGEELEALRGELEDTLDSTNAQQELRSKREQEvtelKKALEEESrahevsmQELRQRHSQALVE---MAEQLEQARRGKG 1235
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKE----KHFLKEEK-------NKLSQELSTVATEknkMAGELEVLRSQER 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1236 VWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ----LQEVQG---RSSDSERARSEAAEKLQRAQAEL---E 1305
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhtldVKELQGpgyTSNSSMKPRLLQPASFTRTHSNVpssQ 880
|
490 500 510
....*....|....*....|....*....|....*.
gi 148690794 1306 SVSTALSEAESKAIRLgkelssAESQLHDTQELLQE 1341
Cdd:pfam15921 881 STASFLSHHSRKTNAL------KEDPTRDLKQLLQE 910
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
871-1622 |
3.31e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 871 ARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAE-LCSEAEEtrarlaarkqelelvvtelEARVGEE 949
Cdd:NF041483 299 AESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEkLVAEAAE-------------------KARTVAA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 950 EECSRQLQSEKKrlqqhiqeleshlEAEEGARQKLQLEKVTTEAKMKKFEedlllledqnsklsKERRLLEERLAEFSSQ 1029
Cdd:NF041483 360 EDTAAQLAKAAR-------------TAEEVLTKASEDAKATTRAAAEEAE--------------RIRREAEAEADRLRGE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1030 AAEEEEKVKSLNKlrlkyeatisdmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRaeellaqlgrkedelqa 1109
Cdd:NF041483 413 AADQAEQLKGAAK-------------DDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGER----------------- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1110 alLRAEEEGGARAQLLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRSKR 1187
Cdd:NF041483 463 --IRGEARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1188 EQEVTELKKALEEESRahevsmqELRqrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEvSELKAELSSLQTSRQEGEQ 1267
Cdd:NF041483 541 EEQAEEVRAAAERAAR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEAER 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1268 KRRRlesqlqevqgRSSDSERARSEAAEKLQ--RAQAELES----------VSTALSEAESKAIRLGKELSSAESQLHDT 1335
Cdd:NF041483 605 IRRE----------AAEETERLRTEAAERIRtlQAQAEQEAerlrteaaadASAARAEGENVAVRLRSEAAAEAERLKSE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1336 QELLQEETRAKLALGSRVRALEAeAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLeagEEARRRAARE 1415
Cdd:NF041483 675 AQESADRVRAEAAAAAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEL---LASARKRVEE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1416 AETLTQRLAEKTEA-VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAVLR 1481
Cdd:NF041483 751 AQAEAQRLVEEADRrATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAERER 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1482 AVEDRERIEAEGREREARALSL---TRALEEEQEAREELERQNRALRAELEAllssKDDVGKNVHELERARKAAEQAASD 1558
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaerTVSEAIAEAERLRSDASEYAQRVRTEA----SDTLASAEQDAARTRADAREDANR 906
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1559 LRTQVTELEDEL---TAAEDAKLRLEVTVQALKAQHERDLQG---RDDAGEERRRQLAKQLRDAEVERDE 1622
Cdd:NF041483 907 IRSDAAAQADRLigeATSEAERLTAEARAEAERLRDEARAEAervRADAAAQAEQLIAEATGEAERLRAE 976
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
862-1400 |
5.16e-08 |
|
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: 58.21 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 862 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRvaQLEEERTRLAeQLRaeaelcSEAEETRARLAARKQELELVVTE 941
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR--QLSDLESTVS-QLR------SELREAKRMYEDKIEELEKQLVL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 942 LEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEgarQKLQLEKvttEAKMKKFEEDL----------LLLEDQNSK 1011
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE---KELSLEK---EQNKRLWDRDTgnsitidhlrRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1012 LSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgESSElqeqmveqkQ 1091
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL--ESSE---------R 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1092 RAEELLAQLGRKEDELQAA---LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1168
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATnaeITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1169 ELEDTLDSTNAQQELRSKREQEVTELKKALEE---ESRAHEVSMQELRQRHSQALVEMAEQL----EQARRGKGVwEKTR 1241
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLELEKVKLVnagsERLRAVKDI-KQER 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1242 LSLEAEVSELKAELSSLQtsrQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1321
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLS---EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1322 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQlsewRRRQEEEAA 1400
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ----ERRLKEKVA 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1055-1307 |
5.37e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 5.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1055 EDRLKKEEKGRQELEKLKRRLDGESSELQEQ-----MVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLR 1129
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1130 EAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSM 1209
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1210 QELRQRHSQALVEMAEQLEQARRgkgVWEKTRLSLEAEVSEL---KAELSSLQTS---RQEGEQKRRRLESQLQEVQGRS 1283
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNR---EWPAETADLDADLESLpeyLALLDRLEEDglpEYEERFKELLNENSIEFVADLL 852
|
250 260
....*....|....*....|....
gi 148690794 1284 SDSERARSEAAEKLQRAQAELESV 1307
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRI 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
866-1230 |
8.54e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 866 DEVLQARAQ------ELQKVQELQQQSAREVGELQGRVAQLEEER-------------TRLAEQL-RAEAELcseaEETR 925
Cdd:PRK04863 286 EEALELRRElytsrrQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIeRYQADL----EELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 926 ARLAARKQELELV---VTELEARVGEEEECSRQLQSEKKRLQQHIQELESH-------LEAEEGARQKLQLEKVTTEakm 995
Cdd:PRK04863 362 ERLEEQNEVVEEAdeqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaVQALERAKQLCGLPDLTAD--- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 996 kKFEEDLLLLEDQNSKLSKERRLLEERLAeFSSQAAEEEEKVKSLNKlrlkyeaTISDMEDRLKKEEKGRQELEKLK--R 1073
Cdd:PRK04863 439 -NAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLVR-------KIAGEVSRSEAWDVARELLRRLReqR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1074 RLDGESSELQ------EQMVEQKQRAEELLAQLGRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1140
Cdd:PRK04863 510 HLAEQLQQLRmrlselEQRLRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1141 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQAL 1220
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-----------QDVTEYMQQLLERERELTVERDELAAR-KQAL 657
|
410
....*....|
gi 148690794 1221 VEMAEQLEQA 1230
Cdd:PRK04863 658 DEEIERLSQP 667
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
908-1627 |
1.04e-07 |
|
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: 57.29 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 908 AEQLRAEAELCSE-AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQhiqeleshleaeegaRQKLQL 986
Cdd:TIGR00618 196 AELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE---------------QLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 987 EKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLeerlaefssQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1066
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1067 ELEKlkrrlDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG---ARAQLLKSLREAQAGLAEAQEDLE 1143
Cdd:TIGR00618 332 AHVK-----QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihTLQQQKTTLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1144 AERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEM 1223
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1224 AEQLEQARRGKGVWEKTRL----SLEAEVSELKAELSSLQTSR-QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ 1298
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1299 RAQAELESVSTALSEAESKAIRLGKELssaESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAG 1378
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNIT---VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1379 RELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLL 1458
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHAL-----------------SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1459 STLEKKQRKFDQLLAEEKAAVLRAVEDRErieaegREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDV 1538
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLA------AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1539 GKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLakqlrdaev 1618
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL--------- 851
|
....*....
gi 148690794 1619 ERDEERKQR 1627
Cdd:TIGR00618 852 LKYEECSKQ 860
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
921-1279 |
1.23e-07 |
|
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: 56.44 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 921 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLeaeegarQKLQLEKVTTEAKMKKFEE 1000
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-------AELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1001 DLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE-- 1078
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1079 ---------SSELQEQMVEQKQRAEELLaQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1149
Cdd:pfam07888 182 qteeelrslSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1150 AKAEKQRRDLGEELEALRGELEDT----LDSTNAQQELRSKREQEVTELKKALE----------EESRAHEVSMQELRQR 1215
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEadkdrieklsAELQRLEERLQEERME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1216 HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEV 1279
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
876-1215 |
1.45e-07 |
|
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: 56.90 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 876 LQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQ 955
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 956 --LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSKERRLLEERLAEFSSQAA 1031
Cdd:pfam02463 725 drVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEreKTEKLKVEEEKEEKLKAQEEELR 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1032 EEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1111
Cdd:pfam02463 805 ALEEELKEEAELLEEEQLLIEQEEKIKEEELE-ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1112 LRAEEEG----GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSK 1186
Cdd:pfam02463 884 LKDELESkeekEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
330 340
....*....|....*....|....*....
gi 148690794 1187 REQEVTELKKALEEESRAHEVSMQELRQR 1215
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
861-1046 |
1.99e-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: 55.54 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEE----RTRLAEQLRAEAELCSEAE-------ETRARLA 929
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPlalllspEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 930 ARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQN 1009
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 148690794 1010 SKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1046
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1179-1593 |
2.22e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1179 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELK------ 1252
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEeleerl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1253 AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR-SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQ 1331
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1332 LHDTQELLQ-EETRAKLALGSRVRALEAEAAGLREQMEE--------------EVVARERAGRELQSTQAQLSEWRRRQE 1396
Cdd:COG4717 236 LEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1397 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELddatvdlgQQKQLLSTLEKKQRKFDQLLAEEK 1476
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--------QLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1477 AAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA--LRAELEALLSSKDDVGKNVHELERARKAAE- 1553
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEe 467
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 148690794 1554 -QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHER 1593
Cdd:COG4717 468 dGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1054-1784 |
3.04e-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: 56.00 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1054 MEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAllraeeeggaRAQLLKSLREAQA 1133
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK----------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1134 GLAEAQEDLEA----------ERVARAKAEKQRRDL-GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEES 1202
Cdd:pfam12128 316 AVAKDRSELEAledqhgafldADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1203 RAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-----VSELKAELSSLQTSRQEGEQKRrrlesQLQ 1277
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrLGELKLRLNQATATPELLLQLE-----NFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1278 EVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeeTRAKLALGSRVRALE 1357
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE---------LQLFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1358 AEAAGLREQMEEeVVARERAGRelqsTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERAR 1437
Cdd:pfam12128 542 KEAPDWEQSIGK-VISPELLHR----TDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1438 RRLQQELDDAtvdlgqqkqlLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGR-EREARALSLTRALEEEQEAREE 1516
Cdd:pfam12128 617 REKQAAAEEQ----------LVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1517 LERQNRALRAELEALLSS-KDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRlevtvqALKAQHERDL 1595
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK------ALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1596 QGRDdAGEERRRQLAKQLRD--AEVERDEERKQRALAMAA--RKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1671
Cdd:pfam12128 761 ASLG-VDPDVIAKLKREIRTleRKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1672 LWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQE----ELAASDRARRQAQQDRDEMAEEVASGNLSK------AA 1741
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEdansEQAQGSIGERLAQLEDLKLKRDYLSESVKKyvehfkNV 919
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 148690794 1742 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESL 1784
Cdd:pfam12128 920 IADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQW 962
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
861-1257 |
3.05e-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: 55.52 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSE---AEETRARLAARKQELeL 937
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiqsQEQDSEIVKNSKSEL-A 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 938 VVTELEA---RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK---LQLEKVTTEAKMK---KFEEDLLLLEDQ 1008
Cdd:pfam05557 198 RIPELEKeleRLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLEQELQswvKLAQDTGLNLRS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1009 NSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL------------- 1075
Cdd:pfam05557 278 PEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerdg 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1076 ----------DGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLrEAQAGLAEAQEDLEAE 1145
Cdd:pfam05557 358 yrailesydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-ERELQALRQQESLADP 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1146 RVARAKAEKQRRDLgEELEALRGELE---DTLDSTNAQQELRSKREQ---EVTELKKALEEESRAHEVSMQELRQRHSQA 1219
Cdd:pfam05557 437 SYSKEEVDSLRRKL-ETLELERQRLReqkNELEMELERRCLQGDYDPkktKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
|
410 420 430
....*....|....*....|....*....|....*....
gi 148690794 1220 LVEMAEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS 1257
Cdd:pfam05557 516 LKRLLKKLEDDLEQVLRLPETTSTMnFKEVLDLRKELES 554
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1246-1481 |
5.38e-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: 54.00 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1246 AEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAIRLGKEL 1325
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1326 SSAESQLHDTQELLQEETRAKLALGSR------VRALEAEAAGLREQMEEEVV-ARERAGRELQSTQAQLSEWRRRQEEE 1398
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1399 AAVLEAGEEARRRAAReaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAA 1478
Cdd:COG4942 173 RAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 148690794 1479 VLR 1481
Cdd:COG4942 250 ALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
957-1397 |
6.13e-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: 54.75 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 957 QSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEk 1036
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIE---LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1037 vksLNKLRLKYEATISdmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEEL---LAQLGRKEDELQAALLR 1113
Cdd:pfam05557 77 ---LNRLKKKYLEALN---KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTnseLEELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1114 AEEEGGARAQLLKSLREAQAGLAEAQEDLE-----AERVARAKAEKQR-RDLGEELEALRGELEdTLDSTNAQQELrskR 1187
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqeqdSEIVKNSKSELARiPELEKELERLREHNK-HLNENIENKLL---L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1188 EQEVTELKKALE--EESRAHEVSMqELRQRHSQALVEMAEQLEQ-----------ARRGKGVWEKTRLSLEAEVSELKAE 1254
Cdd:pfam05557 227 KEEVEDLKRKLEreEKYREEAATL-ELEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1255 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSErarsEAAEKLQRA-----------QAELESVSTALSEAESkAIRLGK 1323
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHK----ALVRRLQRRvllltkerdgyRAILESYDKELTMSNY-SPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1324 ELSSAESQLHDTQeLLQEETRAKL--------ALGSRVRALEAEAAGLREQMEEEVVARERAG-----RELQSTQAQLSE 1390
Cdd:pfam05557 381 RIEEAEDMTQKMQ-AHNEEMEAQLsvaeeelgGYKQQAQTLERELQALRQQESLADPSYSKEEvdslrRKLETLELERQR 459
|
....*..
gi 148690794 1391 WRRRQEE 1397
Cdd:pfam05557 460 LREQKNE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
863-1121 |
6.99e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 863 TRQDEVLQARAQELQkvqelqqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCS---------EAEETRARLAARKQ 933
Cdd:COG4913 609 RAKLAALEAELAELE----------EELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 934 ELEL---VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQklQLEKVTTEAKMKKFEEDLLLLEDQNS 1010
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD--ELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1011 KLSKE------RRLLEERLAEFSSQAAEEEEK-VKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRrldgesselq 1083
Cdd:COG4913 757 AALGDaverelRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE---------- 826
|
250 260 270
....*....|....*....|....*....|....*....
gi 148690794 1084 EQMVEQKQRAEELLAQL-GRKEDELQAALLRAEEEGGAR 1121
Cdd:COG4913 827 DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1175-1396 |
7.89e-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: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1175 DSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSqaLVEMAEQLEQarrgkgvwektrlsLEAEVSELKAE 1254
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1255 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSD--SERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQl 1332
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1333 hdtqeLLQEETRAKLALGSRVRALEAEAAGLREQMEEevvARERAgRELQSTQAQLSEWRRRQE 1396
Cdd:COG3206 307 -----LQQEAQRILASLEAELEALQAREASLQAQLAQ---LEARL-AELPELEAELRRLEREVE 361
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
866-1117 |
7.90e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.16 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 866 DEVLQArAQELQKVQ--ELQQQSAREVGelqGRVAQLEEERTRLAEQLRAEAELCSEAEETR-----ARLAARKQELELV 938
Cdd:PRK05771 19 DEVLEA-LHELGVVHieDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 939 VTELEARVGEEEECSRQLQSEKKRLQQHIQELE---------------SHLEAEEGARQKLQLEKVTTEAKMKKFEE--- 1000
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYist 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1001 ----DLLLLEDQNSKLSKERRLLEErlAEFSSQAAEEEEKVKSLnklrlkyeatISDMEDRLKKEEKGRQ----ELEKLK 1072
Cdd:PRK05771 175 dkgyVYVVVVVLKELSDEVEEELKK--LGFERLELEEEGTPSEL----------IREIKEELEEIEKEREslleELKELA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1073 RRLDGESSELQEQMVEQKQRAEELLAQLG-------------RKEDELQAALLRAEEE 1117
Cdd:PRK05771 243 KKYLEELLALYEYLEIELERAEALSKFLKtdktfaiegwvpeDRVKKLKELIDKATGG 300
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
994-1701 |
8.26e-07 |
|
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: 54.59 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 994 KMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAaeeEEKVKSLNKLRLKYEATISDMEDRLKK----EEKGRQELE 1069
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1070 KLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1149
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1150 AKAEKQRRDLGEE---LEALRGELEDTLDSTNAQQELRSKREQEVTELK--KALEEESRAHEVSMQELRQ-----RHSQA 1219
Cdd:TIGR00618 331 AAHVKQQSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKeldilQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1220 LVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTS--------RQEGEQKRRRLESQLQEVQGRSSDSERARS 1291
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1292 EAAEKLQRAQAELESVSTALSEAESKAIRLGkelssaesQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEv 1371
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDID--------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL- 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1372 vaRERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDL 1451
Cdd:TIGR00618 562 --KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1452 GQQkQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDR--ERIEAEGREREARALSLTraleeeqEAREELERQNRALRAELE 1529
Cdd:TIGR00618 640 ELA-LKLTALHALQLTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLT-------YWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1530 ALLSSKddvgKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQL 1609
Cdd:TIGR00618 712 HIEEYD----REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1610 AKQLRdaevERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL----KKMQVQMKELWREVEETRSSRDE 1685
Cdd:TIGR00618 788 QFFNR----LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRleekSATLGEITHQLLKYEECSKQLAQ 863
|
730
....*....|....*.
gi 148690794 1686 MFTLSRENEKKLKGLE 1701
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLN 879
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1029-1305 |
8.30e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 8.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1029 QAAEEEEKVKSlNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSelQEQMVEQKQRAEELLAQLGRKEDELQ 1108
Cdd:pfam17380 288 QQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1109 AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGE---ELEALRGELEDTldstnAQQELRS 1185
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1186 KREQEVTELKKA-LEEESRAHEvsMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSslqtsrqE 1264
Cdd:pfam17380 440 LEEERAREMERVrLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI-------E 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148690794 1265 GEQKRRRLESQLQEVQGRSSDSERARSeaAEKLQRAQAELE 1305
Cdd:pfam17380 511 EERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEME 549
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1161-1872 |
1.04e-06 |
|
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: 54.07 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1161 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWE-K 1239
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1240 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAeskAI 1319
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA---RD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1320 RLGKELSSA----ESQLHDTQ-----ELLQEETRAKLALGS-RVRALEAEAAG-LREQMEEEVVARERAGRELQSTQAQL 1388
Cdd:pfam12128 408 RQLAVAEDDlqalESELREQLeagklEFNEEEYRLKSRLGElKLRLNQATATPeLLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1389 SewrRRQEEEAAvleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRK 1467
Cdd:pfam12128 488 E---RLQSELRQ------------------ARKRRDQASEALRQASRRLEERQSALDELeLQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1468 FDQLLAE--EKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVgknvheL 1545
Cdd:pfam12128 547 WEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREK------Q 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1546 ERARKAAEQAASDLRTQVTELEDELTAAEDAKL---RLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEverde 1622
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD----- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1623 eRKQRALamaarkkleleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEETRSSrdemftlsrenekKLKGLEA 1702
Cdd:pfam12128 696 -KKHQAW-------------------------LEEQKEQKREARTEKQAYWQVVEGALDA-------------QLALLKA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1703 EVLRLQEELAASDRARRQaQQDRDEMAEEVASGNLSKAATleEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----KLV 1778
Cdd:pfam12128 737 AIAARRSGAKAELKALET-WYKRDLASLGVDPDVIAKLKR--EIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1779 LQVESLTTELSAER----SFSAKAESGRQQLERQIQELRA---RLGEEDAGARARQKMLIaalESKLAQAEEQLEQESRE 1851
Cdd:pfam12128 814 TQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASEKqqvRLSENLRGLRCEMSKLA---TLKEDANSEQAQGSIGE 890
|
730 740
....*....|....*....|.
gi 148690794 1852 RILSGKLVRRAEKRLKEVVLQ 1872
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1655-1945 |
1.54e-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: 53.53 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1655 KEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAasdrarRQAQQDRDEMAEEVAS 1734
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ------LRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1735 GNLSKAATLEEKRQLEGRLSQleeeleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRA 1814
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAK--------------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1815 RLGEEDAGARArqkmliaaLESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL 1894
Cdd:TIGR02169 372 ELEEVDKEFAE--------TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1895 KQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1945
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
864-1394 |
1.62e-06 |
|
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: 53.42 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 864 RQDEVLQARAQELQKvqELQQQSAREVG---ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL--- 937
Cdd:COG3096 525 EQRLRQQQNAERLLE--EFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 938 -------VVTELEARVGEEEECSRQLQSEKKRLQQHIQELEshLEAEEGARQKLQLEKVTTEAKMKKFEED--LLLLEDq 1008
Cdd:COG3096 603 awlaaqdALERLREQSGEALADSQEVTAAMQQLLEREREAT--VERDELAARKQALESQIERLSQPGGAEDprLLALAE- 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1009 nsklskerRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdRLKKEEKGRQE-------LEKLKRRLDGESSE 1081
Cdd:COG3096 680 --------RLGGVLLSEIYDDVTLEDAPYFSALYGPARHAIVVPDLS-AVKEQLAGLEDcpedlylIEGDPDSFDDSVFD 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1082 LQEQ----MVEQKQRAEEL-----LAQLGRKEDELQAALLRAEEEGGAR--AQLLKSLREAQAgLAEAQEDLEAERVARA 1150
Cdd:COG3096 751 AEELedavVVKLSDRQWRYsrfpeVPLFGRAAREKRLEELRAERDELAEqyAKASFDVQKLQR-LHQAFSQFVGGHLAVA 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1151 KAEkqrrDLGEELEAL---RGELEDTLDSTNAQ-QELRSKREQ---EVTELKKALeeeSRAHEVSMQELRQRhSQALVEM 1223
Cdd:COG3096 830 FAP----DPEAELAALrqrRSELERELAQHRAQeQQLRQQLDQlkeQLQLLNKLL---PQANLLADETLADR-LEELREE 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1224 AEQLEQARRGKGVWEKTRLSLEAEVSELK---AELSSLQTSRQEGEQKRRRLESQ---LQEVQGRS-----SDSERARSE 1292
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRphfsyEDAVGLLGE 981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1293 AA-------EKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLR 1364
Cdd:COG3096 982 NSdlneklrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeAEERARIRR 1061
|
570 580 590
....*....|....*....|....*....|....
gi 148690794 1365 EQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1394
Cdd:COG3096 1062 DELHEELSQnrsrRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
859-1237 |
1.98e-06 |
|
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: 52.84 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQQQSARE------VGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 932
Cdd:pfam09731 72 VSAVTGESKEPKEEKKQVKIPRQSGVSSEVAeeekeaTKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NS 1010
Cdd:pfam09731 152 KDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHldNV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1011 KLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK 1090
Cdd:pfam09731 232 EEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1091 QRAEELLAQlgrkedelqaallRAEEEGGARAQLLKSLREAQAgLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1170
Cdd:pfam09731 312 KHIERALEK-------------QKEELDKLAEELSARLEEVRA-ADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1171 EDTLDSTNAQQELRSKREQEvTELKKALEEESRAHEVSMQELRQR---HSQALVEMAEQLEQARRGKGVW 1237
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQLW 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1284-1502 |
2.50e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1284 SDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGL 1363
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1364 REQMEEEVVARERAGR----ELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRR 1439
Cdd:COG4942 103 KEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1440 LQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1502
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1018-1307 |
2.57e-06 |
|
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: 52.34 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1018 LLEERLAEFSSQAAEEEEkvksLNKLRLKyeATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1097
Cdd:pfam05667 208 LLERNAAELAAAQEWEEE----WNSQGLA--SRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1098 AQLGRKEDELQA-----------ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRrdLGEELE 1164
Cdd:pfam05667 282 SSFSGSSTTDTGltkgsrfthteKLQFTNEAPAATSSPPTKVETEEELQQQREEELEElqEQLEDLESSIQE--LEKEIK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1165 ALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAhEVSMQELR---QRHSQALVEMAEQleqarrgkgvWEKTR 1241
Cdd:pfam05667 360 KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDA-EENIAKLQalvDASAQRLVELAGQ----------WEKHR 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1242 LSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVqgrssdSERARSeAAEKLQRAQAELESV 1307
Cdd:pfam05667 429 VPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEV------AEEAKQ-KEELYKQLVAEYERL 487
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
857-1169 |
2.98e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 857 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERT-RLAEQLRAEAELCSEAEETRARLAARK 932
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELV----------VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMKKF 998
Cdd:pfam02029 105 ENNEEEensswekeekRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 999 EEDLLLLEDQNSKLSKERRLLEERlaefSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE 1078
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVK----SQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1079 SSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggaraqllkslreaqaglaeaQEDLEAERVARAKAEKQRRD 1158
Cdd:pfam02029 261 ESEEFEKLRQKQQEAELELEELKKKREERRK--LLEEEE---------------------QRRKQEEAERKLREEEEKRR 317
|
330
....*....|.
gi 148690794 1159 LGEELEALRGE 1169
Cdd:pfam02029 318 MKEEIERRRAE 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
860-1395 |
3.00e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.74 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 860 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQ------GRVAQLEEER-TRLAEQLRAEAELCSEAEETRARLAARK 932
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekkglGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELELVVTELEarVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVT-------TEAKMKKFEE----- 1000
Cdd:TIGR00606 478 QELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmemlTKDKMDKDEQirkik 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1001 ----DLLL-----------LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKK---EE 1062
Cdd:TIGR00606 556 srhsDELTsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgSQ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1063 KGRQELEKLKRRLDGES---------SELQEQMVEQK-----------QRAEELLAQLGRKEDELQAALLRAEEEGGARA 1122
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSkqramlagaTAVYSQFITQLtdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1123 QLLKSL---REAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDT---LDSTNAQQELRSKREQEVT--- 1192
Cdd:TIGR00606 716 SELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQetlLGTIMPEEESAKVCLTDVTime 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1193 ELKKALEEESRAHE------------VSMQELRQR---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1257
Cdd:TIGR00606 796 RFQMELKDVERKIAqqaaklqgsdldRTVQQVNQEkqeKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1258 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE------AAEKLQRAQAEL-ESVSTALSEAESKAIRLGKELSSAES 1330
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1331 QLHDTQELLQEETRAKLalgsrvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1395
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYL------KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
854-1095 |
3.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 854 IKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERtrlaeqlraeaelcSEAEETRARLAARKQ 933
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL--------------DELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 934 ELEL-VVTELEARVGEEEECSRQ---LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteakmKKFEEDLLLLEDQN 1009
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETE-------KRLEELRKELEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1010 SKLSKER-RLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgESSELQEQMVE 1088
Cdd:PRK03918 654 KKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKK 732
|
....*..
gi 148690794 1089 QKQRAEE 1095
Cdd:PRK03918 733 YKALLKE 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1016-1198 |
4.44e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1016 RRLLEerLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMveqkQRAEE 1095
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1096 LLAQlGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLD 1175
Cdd:COG1579 81 QLGN-VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 148690794 1176 stnaqqELRSKREQEVTELKKAL 1198
Cdd:COG1579 160 ------ELEAEREELAAKIPPEL 176
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
929-1357 |
4.49e-06 |
|
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: 51.57 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 929 AARKQELE---LVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGArqKLQLEKVTTEAKMKKfeedllll 1005
Cdd:pfam05701 28 AHRIQTVErrkLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEEL--KLNLERAQTEEAQAK-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1006 edQNSKLSKER-RLLEERLAEFSSQAAEEEEKVkslnkLRLKYEATISDMedRLKKEEKG--RQELEKLKRRLDGESSEL 1082
Cdd:pfam05701 98 --QDSELAKLRvEEMEQGIADEASVAAKAQLEV-----AKARHAAAVAEL--KSVKEELEslRKEYASLVSERDIAIKRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1083 QEQMVEQKQ---RAEELLAQLGRKEDEL---QAALLRAEEE--GGARA------QLLKSLREAQAGLAEAQEDLEAERVA 1148
Cdd:pfam05701 169 EEAVSASKEiekTVEELTIELIATKESLesaHAAHLEAEEHriGAALAreqdklNWEKELKQAEEELQRLNQQLLSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1149 RAKAEKQRR---DLGEELEA---------LRGELEDTLDSTNAQQELRSKREqEVTELKKALEEES------RAHEVSMQ 1210
Cdd:pfam05701 249 KSKLETASAlllDLKAELAAymesklkeeADGEGNEKKTSTSIQAALASAKK-ELEEVKANIEKAKdevnclRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1211 ELRQRHSQALVEMaeqleqaRRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEvqgrssdserAR 1290
Cdd:pfam05701 328 SELEKEKAELASL-------RQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQ----------AA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1291 SEAAEKLQRAQAELESVSTALSEAE-SKAirlgkELSSAESQLHDTQ-ELLQEETRAKLALGSrVRALE 1357
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEqAKA-----AASTVESRLEAVLkEIEAAKASEKLALAA-IKALQ 453
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1066-1402 |
4.54e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.22 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1066 QELEKLKRRLDGESSELQEQMVE-QKQRAE--ELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAGLAEAQEDL 1142
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAyGKLRRElaGLTRRLSAAEGELEELVARL-------AKLEAALREAEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1143 EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKA---LEEESRAHEVSMQELRQRHSQA 1219
Cdd:pfam19220 114 RDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERlalLEQENRRLQALSEEQAAELAEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1220 LVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQR 1299
Cdd:pfam19220 194 TRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1300 AQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALeAEAAGLREqmeeevVARERAGR 1379
Cdd:pfam19220 274 RDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML-TKALAAKD------AALERAEE 346
|
330 340
....*....|....*....|...
gi 148690794 1380 ELQSTQAQLSEWRRRQEEEAAVL 1402
Cdd:pfam19220 347 RIASLSDRIAELTKRFEVERAAL 369
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
867-1390 |
4.76e-06 |
|
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: 51.88 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARA-------QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 939
Cdd:COG3096 406 DVQQTRAiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 940 TELEArvGEEEECSRQL---QSEKKRLQQHIQELESHL-EAEEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQNSKLs 1013
Cdd:COG3096 486 GEVER--SQAWQTARELlrrYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAEL- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1014 kerrllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLkRRLDGESSELQEQMVEQKQRA 1093
Cdd:COG3096 563 ------EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-REQSGEALADSQEVTAAMQQL 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1094 EELLAQLGRKEDELQAALLRAEEE-------GGARAQLLKSLREAQAG--LAEAQEDLEAE-------RVARAKAEKQRR 1157
Cdd:COG3096 636 LEREREATVERDELAARKQALESQierlsqpGGAEDPRLLALAERLGGvlLSEIYDDVTLEdapyfsaLYGPARHAIVVP 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1158 DLGEELEALRGeLEDTL--------------DSTNAQQEL-------------------------RSKREQEVTELKKAL 1198
Cdd:COG3096 716 DLSAVKEQLAG-LEDCPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAER 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1199 EEESRAHEVSMQELR--QRHSQALVE-MAEQLEQARRGKGvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ 1275
Cdd:COG3096 795 DELAEQYAKASFDVQklQRLHQAFSQfVGGHLAVAFAPDP--EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1276 LQEVQGRSS-------DSERARSEAAE----KLQRAQAELESVSTALSEAESKAIRL------GKELSSAESQLHDTQEL 1338
Cdd:COG3096 873 LQLLNKLLPqanlladETLADRLEELReeldAAQEAQAFIQQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRR 952
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1339 LQEETRAKLALGSRVRALE-AEAAG-----------LREQMEEEVVARERAGRELQSTQAQLSE 1390
Cdd:COG3096 953 LKQQIFALSEVVQRRPHFSyEDAVGllgensdlnekLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1035-1311 |
4.91e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.69 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1035 EKVKSLnklrlkyEATISDMEDRLK-KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1113
Cdd:pfam00038 18 DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1114 AEEEGGARaqllkslREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELED--------------------- 1172
Cdd:pfam00038 91 YEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevrelqaqvsdtqvnvemdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1173 -TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwekTRLSLEAEVSEL 1251
Cdd:pfam00038 164 rKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1252 KAELSSLQTSRQEGEQkrrRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE---LESVSTAL 1311
Cdd:pfam00038 237 KKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEMARQLREyqeLLNVKLAL 296
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
865-1592 |
5.93e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.59 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 944
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 945 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllledqnSKLSKERRLLEERLA 1024
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI------------ERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1025 EFSSQaaeEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesselqeqmveqkQRAEELLAQLGRKE 1104
Cdd:TIGR00606 416 DLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---------------QQLEGSSDRILELD 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1105 DELQAALlrAEEEGGARAQLLKSLREAQAGLAEAQEDLeaERVARAKAEKQrRDLGEELEALRGELEDTLDSTNAQQELR 1184
Cdd:TIGR00606 478 QELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADL--DRKLRKLDQEM-EQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1185 SKREQEVTEL---------KKALEEESRAHEVSMQELRQRhsqaLVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAEL 1255
Cdd:TIGR00606 553 KIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDR----LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1256 SSLQTSRQEgEQKRRRLESQLqevqgrssdsERARSEAAeKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDT 1335
Cdd:TIGR00606 629 FDVCGSQDE-ESDLERLKEEI----------EKSSKQRA-MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1336 QELLQEETRaklALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraare 1415
Cdd:TIGR00606 697 ISDLQSKLR---LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK------------------ 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1416 AETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGRE 1495
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1496 REARalSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNvheLERARKAAEQAAsDLRTQVTELEDELTAAED 1575
Cdd:TIGR00606 836 HELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN---LQRRQQFEEQLV-ELSTEVQSLIREIKDAKE 909
|
730
....*....|....*..
gi 148690794 1576 AKLRLEVTVQALKAQHE 1592
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKE 926
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
899-1342 |
7.76e-06 |
|
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: 51.17 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 899 QLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 978
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 979 gaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRL 1058
Cdd:TIGR04523 180 --KEKLNIQKNIDKIKNKLLKLELLLSNLK--KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1059 KKEekgRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggarAQLLKSLREAqagLAEA 1138
Cdd:TIGR04523 256 NQL---KDEQNKIKKQL----SEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKE----QDWNKELKSE---LKNQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1139 QEDLEAERVARAKAEKQRRDLGEELEALRGELEDtLDSTNA--QQELRSKrEQEVTELKKALE---EESRAHEVSMQELR 1213
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTN-SESENSekQRELEEK-QNEIEKLKKENQsykQEIKNLESQINDLE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1214 QRHSQALV---EMAEQLEQARRGKGVWEK-------TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgRS 1283
Cdd:TIGR04523 398 SKIQNQEKlnqQKDEQIKKLQQEKELLEKeierlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS-RS 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1284 SDSERARSEAAEK-LQRAQAELESVSTALSEAESKAirlgKELSSAESQLHDTQELLQEE 1342
Cdd:TIGR04523 477 INKIKQNLEQKQKeLKSKEKELKKLNEEKKELEEKV----KDLTKKISSLKEKIEKLESE 532
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
896-1167 |
1.12e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.46 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 896 RVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV---VTELEA---RVGEEEEcsrqLQSEKKRLQqHIQE 969
Cdd:COG0497 149 AFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLrfqLEELEAaalQPGEEEE----LEEERRRLS-NAEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 970 LeshLEAEEGARQklqlekvtteakmkkfeedlLLLEDQNS---KLSKERRLLEeRLAEFSSQAAEEEEKVKSLnklrlk 1046
Cdd:COG0497 224 L---REALQEALE--------------------ALSGGEGGaldLLGQALRALE-RLAEYDPSLAELAERLESA------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1047 yEATISDMedrlkkeekgRQELEKLKRRLDGESSELQEqmVEQKQraeELLAQLGRK----EDELqaallraeeeggarA 1122
Cdd:COG0497 274 -LIELEEA----------ASELRRYLDSLEFDPERLEE--VEERL---ALLRRLARKygvtVEEL--------------L 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148690794 1123 QLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1167
Cdd:COG0497 324 AYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
943-1169 |
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 148690794 943 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllEDQNSKLSKERRLLEER 1022
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAefssQAAEEEEKVKSLNKL-----------RLKYEATISDMEDRLKKE-EKGRQELEKLKRRLDGESSELQEQMVEQK 1090
Cdd:COG3883 92 AR----ALYRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1091 QRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGE 1169
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
895-1208 |
1.65e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 895 GRVAQleEERtrlAEQLRAEAElcsEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEK--KRLQQHIQELES 972
Cdd:COG3096 779 GRAAR--EKR---LEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAelAALRQRRSELER 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 973 HLEAEEGA--RQKLQLEKVTTEAKM-KKFEEDLLLLEDQNskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1049
Cdd:COG3096 851 ELAQHRAQeqQLRQQLDQLKEQLQLlNKLLPQANLLADET--LADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAV 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1050 TISDME--DRLKKE-EKGRQELEKLKRRLD---------------------GESSELQEQMVEQKQRAEELLAQLGrkeD 1105
Cdd:COG3096 929 LQSDPEqfEQLQADyLQAKEQQRRLKQQIFalsevvqrrphfsyedavgllGENSDLNEKLRARLEQAEEARREAR---E 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1106 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV-----ARAKAEKQRRDLGEELEALRG---ELEDTLDST 1177
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSrrsQLEKQLTRC 1085
|
330 340 350
....*....|....*....|....*....|.
gi 148690794 1178 NAQQELRSKREQEVTELKKALEEESRAHEVS 1208
Cdd:COG3096 1086 EAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
956-1585 |
1.86e-05 |
|
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: 49.72 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 956 LQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERRLLEERLAEFSSQAAEEEE 1035
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1036 KVKSLNKLRLKYEATISDMEDRLKKEEKGRQELeklkrRLDGESS------ELQEQMVEQKQRAEELLAQLGRKEDELQA 1109
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1110 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE---LRSK 1186
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1187 REQEVTELKKALEEESrahevsmQELRQRHSQALVEMaeqleqarrgkgvwEKTRLSLEaevsELkaelssLQTSRQEGE 1266
Cdd:pfam05483 325 TICQLTEEKEAQMEEL-------NKAKAAHSFVVTEF--------------EATTCSLE----EL------LRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1267 QKRRRLESQLQEVQGRSSDSErarsEAAEKLQRAQAELESVSTALSEAESkairlgkeLSSAESQLHDTQELLQEETRAK 1346
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEK--------LLDEKKQFEKIAEELKGKEQEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1347 LALgsrVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEK 1426
Cdd:pfam05483 442 IFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-----------------HCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1427 TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRA 1506
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1507 LEEEQEAREELERQNRALRAELEallsskdDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEdakLRLEVTVQ 1585
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIE-------NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE---LELASAKQ 650
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
855-1105 |
1.92e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.93 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 855 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREvgelqgrvaQLEEERTRLAEqlrAEAELCSEAEETRA-----RLA 929
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEK---------KLEQERLRWTE---AESKWISLAEELRTeldasRAL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 930 ARKQELELvvtELEARVGEEEECSRQL--QSEKKRLQQ-------HIQELESHLEAEEGARQklqLEKVTTEAKMKKFEE 1000
Cdd:PLN03188 1081 AEKQKHEL---DTEKRCAEELKEAMQMamEGHARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAES 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1001 DLL-LLEDQNSKL----SKERRLLEERLAEFSSQAAEEEEKVKSLNKL--RLK-YEATISDMEDRLKKEE----KGRQEL 1068
Cdd:PLN03188 1155 KFInALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQI 1234
|
250 260 270
....*....|....*....|....*....|....*..
gi 148690794 1069 EKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKED 1105
Cdd:PLN03188 1235 DKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCM 1271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1051-1235 |
1.97e-05 |
|
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: 48.00 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1051 ISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggARAQL--LKSL 1128
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1129 REAQAglaeAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEEESRAHEVS 1208
Cdd:COG1579 89 KEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 148690794 1209 MQELRQRHSQALVEMAEQL----EQARRGKG 1235
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1289-1505 |
2.08e-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: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1289 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1368
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1369 EEvvaRERAGRELQSTQAQlsewRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1448
Cdd:COG4942 101 AQ---KEELAELLRALYRL----GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1449 VDLgqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1505
Cdd:COG4942 174 AEL---EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1005-1232 |
2.40e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.24 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1005 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKvksLNKLRLKYEatISDMEDRLKKEEkgrQELEKLKRRLdgesSELQE 1084
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNG--LVDLSEEAKLLL---QQLSELESQL----AEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1085 QMVEQKQRAEELLAQLGRKEDELQAALlraeeEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELE 1164
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1165 AlrgELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELR--QRHSQALVEMAEQLEQARR 1232
Cdd:COG3206 309 Q---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLE 375
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1214-1901 |
2.45e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1214 QRHSQALVEMAEQLEQARRgkgvweKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-E 1292
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKK------KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1293 AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLREQMEEEV 1371
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1372 VARERAGRELQSTQAQLsewrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDL 1451
Cdd:pfam02463 307 RRKVDDEEKLKESEKEK------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1452 GQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEAL 1531
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1532 LSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAK 1611
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1612 QLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE-LWREVEETRSSRDEMFTLS 1690
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1691 RENEKKLKGLEAEVLRLQE-ELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSEL 1769
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1770 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKlaqaEEQLEQES 1849
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKEL 776
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1850 RERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQL 1901
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
867-1278 |
2.66e-05 |
|
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: 49.36 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARAQELQKVQELQQQS-AREVGELQgrvaQLEEERTRLAEQLraeaeLCSEAEETRA---RLAARKQELELVVTEL 942
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEEElTRKIQPSD----SLEPEFPKKCRSL-----LNRWREKVFAlmvQLKAQDLEHRDSVKQL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1022
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIW 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1023 LAEFSSQAAEEEEKVKSLNKlRLKYEA----TISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLA 1098
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSN-RLSYAVrkvhTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1099 QLGRKEDELQAALLRAEEEGGA-RAQLLKSLREAQAGLAEAQEDLEAervarakaekqrrdLGEELE-ALRGELEDTLDS 1176
Cdd:pfam07111 496 ELQLSAHLIQQEVGRAREQGEAeRQQLSEVAQQLEQELQRAQESLAS--------------VGQQLEvARQGQQESTEEA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1177 TNAQQELRSKRE-------QEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE-QLEQARRGKGVWEKTRLSLEAEv 1248
Cdd:pfam07111 562 ASLRQELTQQQEiygqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEAR- 640
|
410 420 430
....*....|....*....|....*....|
gi 148690794 1249 selKAELSSLQTSRQEGEQKRRRLESQLQE 1278
Cdd:pfam07111 641 ---KEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1349-1865 |
2.67e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1349 LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareAETLTQRLAEKTE 1428
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE------------------LETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1429 AVERLerarrrlQQELDDATVDLGQQKQLLSTLEKKQrkfDQLLAEekAAVLRAveDRERIEAEGREREARALSLTRALE 1508
Cdd:PRK02224 266 TIAET-------EREREELAEEVRDLRERLEELEEER---DDLLAE--AGLDDA--DAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1509 EEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALK 1588
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1589 AQHERDLQGRDDAGE------------ERRRQLAKQLRDA----EVERDEERKQRALAMAARKKLELELEELKAQTSAAG 1652
Cdd:PRK02224 412 DFLEELREERDELREreaeleatlrtaRERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1653 QGKEEAVKQLKkmqvQMKELWREVEETRSSRDEMFTLSRENEKKL--KGLEAEVLRLQ-EELAASDRARRQAQQDRDEMA 1729
Cdd:PRK02224 492 EEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIeeKRERAEELRERaAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1730 EEVAsgnlSKAATLEEKRQ-LEGRLSQLeeeleeeqnnsellkDHYRKLVLQVESLTTELSAERS-FSAKAESGRQQLER 1807
Cdd:PRK02224 568 EEAR----EEVAELNSKLAeLKERIESL---------------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER 628
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1808 qIQELRAR---LGEEDAGARarqkmlIAALESKLAQAEEQLEQesreriLSGKLVRRAEKR 1865
Cdd:PRK02224 629 -LAEKRERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREER 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1179-1400 |
3.02e-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: 48.61 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1179 AQQELRSKREQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSL 1258
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1259 QTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQEL 1338
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1339 LQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAA 1400
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1071-1901 |
3.07e-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: 49.20 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1071 LKRRLDGESSELQEQM-VEQKQRAEELLAQLGRKEDELQAALLRAEEE---------GGARAQLLKSLREAQAGLAEAQE 1140
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLyLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtftrvvllpQGEFAQFLKAKSKEKKELLMNLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1141 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrahevsMQELRQRHSQaL 1220
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-------LQQTQQSHAY-L 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1221 VEMAEQLEQARRgkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLesqlqevqgRSSDSERARSEAAEKLQRA 1300
Cdd:TIGR00618 246 TQKREAQEEQLK----KQQLLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1301 QAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEEtraklalgSRVRALEAEAAGLREQMEEEVVARERAgRE 1380
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE--------IHIRDAHEVATSIREISCQQHTLTQHI-HT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1381 LQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLST 1460
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1461 LEKKQRKFDQLLAEEKAAVLRavedreriEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGK 1540
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1541 NVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA------QHERDLQGRDDAGEERRRQLAKQLR 1614
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipnlqNITVRLQDLTEKLSEAEDMLACEQH 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1615 DAEVERDEERKQRALAMAARKKLeleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEET-RSSRDEMFTLSREN 1693
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCS-----------------QELALKLTALHALQLTLTQERVREHaLSIRVLPKELLASR 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1694 EKKLKGLEAEVLRL---QEELAASDRARRQAQQDRDEMAEEVasgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSell 1770
Cdd:TIGR00618 679 QLALQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQA--- 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1771 KDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEedagararqkmliaaleskLAQAEEQLEQESR 1850
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------------------LKTLEAEIGQEIP 813
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1851 ERILsgklvrraEKRLKEVVLQVDEErrvadQVRDQLEKSNLRLKQLKRQL 1901
Cdd:TIGR00618 814 SDED--------ILNLQCETLVQEEE-----QFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1521-1945 |
3.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1521 NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHE-RDLQGRD 1599
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1600 DAGEERRRQLAKQLRD-AEVERDEERKQRALAMAARKKLELELeelkAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1678
Cdd:COG4717 149 EELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATE----EELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1679 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1758
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1759 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKaesgrqQLERQIQELRARLgeEDAGARARQKMLIAALESKL 1838
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELL------DRIEELQELLREA--EELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1839 AQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNL--RLKQLKRQLEEAEEEASRAQAGRR 1916
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|.
gi 148690794 1917 RLQRELEDVTESAE--SMNREVTTLRNRLRR 1945
Cdd:COG4717 457 ELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
906-1231 |
3.46e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 906 RLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVgEEEECSrqLQSEKKRLQQhiqELESHLEAeegARQKLQ 985
Cdd:PLN03188 898 RLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFL-EEELAS--LMHEHKLLKE---KYENHPEV---LRTKIE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 986 LEKVTTEAK-MKKF----EEDLLLLEDQNSKLS-------------KERRLLEERLAEFSSQA--------AEEEEKVKS 1039
Cdd:PLN03188 969 LKRVQDELEhYRNFydmgEREVLLEEIQDLRSQlqyyidsslpsarKRNSLLKLTYSCEPSQApplntipeSTDESPEKK 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1040 LNKLRLKYEATISD---MEDRLKKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQKQRAEELLAQLGRKEDELQA 1109
Cdd:PLN03188 1049 LEQERLRWTEAESKwisLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYADLEEKHIQLLA 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1110 ALLRAEE------EGGARAqllkSLREAQAGLAEAqedLEAERVA-RAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:PLN03188 1129 RHRRIQEgiddvkKAAARA----GVRGAESKFINA---LAAEISAlKVEREKERRYLRDENKSLQAQLRDTAEAVQAAGE 1201
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1183 L--RSKREQE--VTELKKALEEESRAHEV--SMQELRQRHSQALVEMAEQLEQAR 1231
Cdd:PLN03188 1202 LlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESR 1256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1005-1165 |
3.57e-05 |
|
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: 47.23 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1005 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQE 1084
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1085 QMVEQKQRAEELLAQLGRKEdELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAErvaRAKAEKQRRDLGEELE 1164
Cdd:COG1579 101 LKRRISDLEDEILELMERIE-ELEEELAELEAE---LAELEAELEEKKAELDEELAELEAE---LEELEAEREELAAKIP 173
|
.
gi 148690794 1165 A 1165
Cdd:COG1579 174 P 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
954-1100 |
3.64e-05 |
|
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: 47.23 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 954 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL---------SKERRLLEERLA 1024
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1025 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1100
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
858-978 |
3.75e-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: 48.22 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 858 PLLQVTRQDEVLQArAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 937
Cdd:COG4942 121 PLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148690794 938 VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 978
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1045-1166 |
3.92e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1045 LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLgrkEDELQAALLRAEEEGgarAQL 1124
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 148690794 1125 LKSLREAQAGLAEAQedleaervARAKAEKQRRDLGEELEAL 1166
Cdd:PRK00409 590 IKELRQLQKGGYASV--------KAHELIEARKRLNKANEKK 623
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1074-1231 |
4.11e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1074 RLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAE 1153
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1154 KQRRDLGEELEALR---GELEDTLDstnaqqelrskreqevtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQA 1230
Cdd:PRK09039 137 AQVELLNQQIAALRrqlAALEAALD---------------------ASEKRDRESQAKIADLGRRLNVALAQRVQELNRY 195
|
.
gi 148690794 1231 R 1231
Cdd:PRK09039 196 R 196
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
949-1099 |
4.26e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 949 EEECSRQLQSEKKRLQQHIQELEshLEA-EEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQnskLSKERRLLEERLAE 1025
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEAL--LEAkEEIHKLRNEFEKELRErrNELQKLEKRLLQKEEN---LDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1026 FSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLK------KEEKGRQELEKLKRRLDGESSELQEQMVEQ-----KQRAE 1094
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEEakeeaDKKAK 191
|
....*
gi 148690794 1095 ELLAQ 1099
Cdd:PRK12704 192 EILAQ 196
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
865-1156 |
4.78e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.81 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAAR-----KQELELVV 939
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekteKLKVEEEK 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 940 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEA--EEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1017
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1018 LLEERLAEFSSQAAEEEEKVKSLNKLRlkyeatisdmEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1097
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEK----------KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1098 AQlgRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR 1156
Cdd:pfam02463 943 EE--ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
862-1315 |
4.92e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.67 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 862 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAArkqELELVVTE 941
Cdd:NF041483 436 VELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAK--ADADELRSTATA---ESERVRTE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 942 LEARVG----EEEECSRQLQSEKKRLQQHIQEL--ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsklske 1015
Cdd:NF041483 511 AIERATtlrrQAEETLERTRAEAERLRAEAEEQaeEVRAAAERAARELREETERAIAARQAEAAEELTRLHTE------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1016 rrlLEERLAefssqAAEEEEKVKSLNKLRLKYEATisdmedrlkkEEKGRQELEKLKRRldgesSELQEQMVEQKQR-AE 1094
Cdd:NF041483 584 ---AEERLT-----AAEEALADARAEAERIRREAA----------EETERLRTEAAERI-----RTLQAQAEQEAERlRT 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1095 ELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArAKAEKQRRDLGEELEALRGELEDTL 1174
Cdd:NF041483 641 EAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG-TEAAEALAAAQEEAARRRREAEETL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1175 DS--TNAQQELRSKREQEVTELKKALE--EESRAHEVSMQELRQRHSQALVEMAEQLEQARRGK--GVWEKTrlslEAEV 1248
Cdd:NF041483 720 GSarAEADQERERAREQSEELLASARKrvEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSvaGLQEQA----EEEI 795
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1249 SELK--AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELE-SVSTALSEAE 1315
Cdd:NF041483 796 AGLRsaAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAErTVSEAIAEAE 865
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
864-1203 |
4.95e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 864 RQDEVLQARAQELQKVQELQQQSAREVGELQGRVaQLEEERTRLAEQLRAEAElcseaeETRARLAARKQELELVVTELE 943
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMI-QNAEKNILLLNQARLQAL------EDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 944 ARVGEEEECSRQLQSEKKrlqqHIQELESHLEAeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1023
Cdd:PLN02939 177 MRLSETDARIKLAAQEKI----HVEILEEQLEK---LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1024 AEFssqaAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrqeleklkrrldgesSELQEQMVEQKQRAEELLAQlgrK 1103
Cdd:PLN02939 250 IEV----AETEERVFKLEKERSLLDASLRELESKF---------------------IVAQEDVSKLSPLQYDCWWE---K 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1104 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRdLGEELEALRGELEDTLDSTNAQQEL 1183
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQL 380
|
330 340
....*....|....*....|
gi 148690794 1184 RSKREQEVTELKKALEEESR 1203
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESK 400
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1032-1145 |
5.18e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1032 EEEEKV----KSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgesSELQEQMVEQKQRAEELLAQLgRKEDEL 1107
Cdd:PRK00409 513 EDKEKLneliASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEA-KKEADE 588
|
90 100 110
....*....|....*....|....*....|....*...
gi 148690794 1108 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE 1145
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
899-1297 |
5.40e-05 |
|
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: 48.40 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 899 QLEEERTRLAEQL-----RAEAElcSEAEETRARLAARKQELELvvtELEARVGEEEECSRQLQSEKKRLQQHIQELESH 973
Cdd:pfam15818 1 QLLDFKTSLLEALeelrmRREAE--TQYEEQIGKIIVETQELKW---QKETLQNQKETLAKQHKEAMAVFKKQLQMKMCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 974 LEAEEGarqKLQLEKVTTEAKMKKFEEDLLLLedQNSKLSKERRLLE-ERLAEFSSQAAEEEEKvkSLNKLRlKYEATIS 1052
Cdd:pfam15818 76 LEEEKG---KYQLATEIKEKEIEGLKETLKAL--QVSKYSLQKKVSEmEQKLQLHLLAKEDHHK--QLNEIE-KYYATIT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1053 DMEDRLK----KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQaalLRAEEEggaraQLLKSL 1128
Cdd:pfam15818 148 GQFGLVKenhgKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQ---YKMGEE-----NINLTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1129 REAQagLAEAQEDLEAERVARAKaekqrrdLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELK---KALEEESRAH 1205
Cdd:pfam15818 220 KEQK--FQELQERLNMELELNKK-------INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEaelKALKENNQTL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1206 EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR--------QEGEQKRRRLESQLQ 1277
Cdd:pfam15818 291 ERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHiklqehynKLCNQKKFEEDKKFQ 370
|
410 420
....*....|....*....|
gi 148690794 1278 EVQGRSSDSERARSEAAEKL 1297
Cdd:pfam15818 371 NVPEVNNENSEMSTEKSENL 390
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
851-1045 |
5.56e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 851 RLFIKVKPLLQVTRQD----EVLQARAQELQKVQELQQQSAREVGE--------------------------LQGRVAQL 900
Cdd:PRK04863 918 NALAQLEPIVSVLQSDpeqfEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyedaaemlaknsdlnekLRQRLEQA 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 901 EEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE-----EEECSRQLQSEKKRLQQHIQELESHLE 975
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANRSRRN 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 976 AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSK------------ERRLLEERLAEFSSQAAEEEEKvKSLN 1041
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQvvNAKAGWcavlrlvkdngvERRLHRRELAYLSADELRSMSD-KALG 1156
|
....
gi 148690794 1042 KLRL 1045
Cdd:PRK04863 1157 ALRL 1160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1113-1454 |
6.38e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1113 RAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVT 1192
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1193 ELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRL 1272
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1273 ESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSR 1352
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1353 VRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVER 1432
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340
....*....|....*....|..
gi 148690794 1433 LERARRRLQQELDDATVDLGQQ 1454
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQ 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1015-1208 |
7.75e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1015 ERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRLKKEEKGRQELEKLKRRLDgessELQEQMVEQKQRAE 1094
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1095 ELLAQLGRKEDELQ--AALLRAEEEG-------------GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL 1159
Cdd:COG3883 90 ERARALYRSGGSVSylDVLLGSESFSdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148690794 1160 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVS 1208
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1256-1466 |
8.24e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 8.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1256 SSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE---------AAEKLQRAQAELESVSTALSEAESKAIRLGKELS 1326
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1327 SAESQLHDTQELLQE--ETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrrrQEEEAAVLEA 1404
Cdd:COG3206 244 ALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1405 GEEARRRAAREAETLTQRLAEKTEAVerleRARRRLQQELDDATVDLGQQKQLLSTLEKKQR 1466
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1049-1366 |
9.27e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1049 ATISDME---DRLKKEEKGRQELEKLKRRLDGESSELQEqmveqkqrAEELLAQLGRKEDELQAALLRAEEeggaRAQLL 1125
Cdd:PRK11281 60 LVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQ--------AQAELEALKDDNDEETRETLSTLS----LRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1126 KSLREAQAGLAEAQEDLEaervarakaekqrrDLGEELEALRGELEdtldstNAQQEL--RSKREQEVTELKKALEEESR 1203
Cdd:PRK11281 128 SRLAQTLDQLQNAQNDLA--------------EYNSQLVSLQTQPE------RAQAALyaNSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1204 AHEVSMQELRQRHsQALVEMaeQLEQARRgkgvwektrlslEAEVSELKAELssLQTSRQEGEQKRRRLESQLQEVQGRS 1283
Cdd:PRK11281 188 ALRPSQRVLLQAE-QALLNA--QNDLQRK------------SLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1284 SDSERARSEA-AEKLQRAQAELESVSTALSEAESKA-IRLGKELSSAESQLHdtqELLQEETRAKLALGsrvRALEAEAA 1361
Cdd:PRK11281 251 NSKRLTLSEKtVQEAQSQDEAARIQANPLVAQELEInLQLSQRLLKATEKLN---TLTQQNLRVKNWLD---RLTQSERN 324
|
....*
gi 148690794 1362 gLREQ 1366
Cdd:PRK11281 325 -IKEQ 328
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
859-1138 |
9.45e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 9.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQ------QQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaeetrarlaark 932
Cdd:COG0497 137 LLDPDAQRELLDAFAGLEELLEEYReayrawRALKKELEELRADEAERARELDLLRFQL--------------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 933 QELElvvtELEARVGEEEEcsrqLQSEKKRLQ------QHIQELESHLEAEEG--------ARQKLQlEKVTTEAKMKKF 998
Cdd:COG0497 196 EELE----AAALQPGEEEE----LEEERRRLSnaeklrEALQEALEALSGGEGgaldllgqALRALE-RLAEYDPSLAEL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 999 EEDL----LLLEDQNSKLSKERRLLE---ERLAEFssqaaeeEEKVKSLNKLRLKYEATISDMedrLKKEEKGRQELEKL 1071
Cdd:COG0497 267 AERLesalIELEEAASELRRYLDSLEfdpERLEEV-------EERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1072 krrldgesselqeqmveqkQRAEELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAG-LAEA 1138
Cdd:COG0497 337 -------------------ENSDERLEELEAELAEAEAELLEA-------AEKLSAARKKAAKkLEKA 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1500-1740 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1500 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLR 1579
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1580 LEVTVQALKAQHerdlqgrddagEERRRQLAKQLR---------------DAEVERDEERKQRALAMAARKKLELELEEL 1644
Cdd:COG4942 88 LEKEIAELRAEL-----------EAQKEELAELLRalyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1645 KAQTSAAGQgKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQD 1724
Cdd:COG4942 157 ADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*.
gi 148690794 1725 RDEMAEEVASGNLSKA 1740
Cdd:COG4942 236 AAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1708-1950 |
1.64e-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: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1708 QEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1787
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1788 LSAERSFSAKAESGRQQLERQiQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLK 1867
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1868 EVVLQVDEERRVADQVRDQLEKsnlRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1947
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 148690794 1948 LTF 1950
Cdd:COG4942 255 LPW 257
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
859-1084 |
2.04e-04 |
|
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: 45.57 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEER---TRLAEQLRAEAE----------LCSEAEETR 925
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLlelTRVNELLKAKFSedgtqkkmssLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 926 ARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE 1000
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLleyitELSCVSEQVEKYKLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1001 DLL--LLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKeekgrqELEKLKRRLDGE 1078
Cdd:pfam15905 246 AQLeeLLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNA------ELEELKEKLTLE 319
|
....*.
gi 148690794 1079 SSELQE 1084
Cdd:pfam15905 320 EQEHQK 325
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1662-1968 |
2.11e-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: 46.04 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1662 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAA 1741
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1742 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDA 1821
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1822 GARARQKMlIAALESKLAQAE------EQLEQE---SRERI-LSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSN 1891
Cdd:pfam07888 207 QVLQLQDT-ITTLTQKLTTAHrkeaenEALLEElrsLQERLnASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1892 LRLKQLKRQLeeaEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRgpltftTRTVRQVFRLEEGVASD 1968
Cdd:pfam07888 286 LQLADASLAL---REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE------ERMEREKLEVELGREKD 353
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
942-1196 |
2.13e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 942 LEARVGEEEECSRQLQSEKKRLQQHI---QELESHLEAEEGAR-QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1017
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIktyNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1018 LLEERLAEFSSQAAEEEEKVKSLNKLRLKYE---------ATISDMEDRLkkeEKGRQELEKLKRRLDgessELQEQMVE 1088
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI---TKIKDKLKELQHSLE----KLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1089 QKQRAEElLAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglaeAQEDLEAERVARAkaekqrrdlgEELEALRG 1168
Cdd:PHA02562 325 LEEIMDE-FNEQSKKLLELKNKI---STNKQSLITLVDKAKKVKA----AIEELQAEFVDNA----------EELAKLQD 386
|
250 260
....*....|....*....|....*...
gi 148690794 1169 ELEDtLDSTNAQQELRSKREQEVTELKK 1196
Cdd:PHA02562 387 ELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
925-1196 |
2.28e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 925 RARLAARKQELELVVTEL-EARVGEEEECSRQLQSEKKR--------LQQHIQELESHLEAEEGarqklqLEKVTTEAKM 995
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALhELGVVHIEDLKEELSNERLRklrslltkLSEALDKLRSYLPKLNP------LREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 996 KKFEEdllLLEDQNSKLSK-ERRL--LEERLAEFssqaaEEEEKVKSLNKLRLKYEATIsDMEDRLKKEEK------GRQ 1066
Cdd:PRK05771 82 KSLEE---LIKDVEEELEKiEKEIkeLEEEISEL-----ENEIKELEQEIERLEPWGNF-DLDLSLLLGFKyvsvfvGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1067 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLKSLREAQAGLaeaqe 1140
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlelEEEGTPSELIREIKEELEEI----- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1141 dleaervarakaEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKK 1196
Cdd:PRK05771 228 ------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
672-696 |
2.31e-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: 2.31e-04
10 20
....*....|....*....|....*
gi 148690794 672 YKESLSRLMATLSNTNPSFVRCIVP 696
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1709-1945 |
2.43e-04 |
|
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: 46.21 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1709 EELAASDRARRQAQQDRDEMaeEVASGNLSKA-ATLEEKRQLEGRLSQLEEELEEEQNNSELLKD-HYRKLVLQVESLTT 1786
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEEL--EEVEENIERLdLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1787 ELSAERSFSAKAESGRQQLERQIQELRARLGE----------------EDAGARARQKML-----IAALESKLAQAEEQL 1845
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEieqlleelnkkikdlgEEEQLRVKEKIGeleaeIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1846 EQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDV 1925
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260
....*....|....*....|
gi 148690794 1926 TESAESMNREVTTLRNRLRR 1945
Cdd:TIGR02169 398 KREINELKRELDRLQEELQR 417
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
870-1398 |
2.54e-04 |
|
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: 46.28 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 870 QARAQELQKVQELQQQS------------AREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 937
Cdd:pfam07111 136 EGSQRELEEIQRLHQEQlssltqaheealSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 938 VVTELEA---RVGEE---EECSRQLQSEKKRLQQHIQELESHleaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsk 1011
Cdd:pfam07111 216 QVTLVESlrkYVGEQvppEVHSQTWELERQELLDTMQHLQED-------RADLQATVELLQVRVQSLTHMLALQEEE--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1012 lskerrlLEERLAEFSSQAAEEEEKVKSLnkLRLKYEATISDMEDRLKKEEKGRQELEKLKrrldGESSELQEQMVEQKQ 1091
Cdd:pfam07111 286 -------LTRKIQPSDSLEPEFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLR----GQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1092 RaeellaqlgrkedelQAALLRAEEEGGARAQLLK-SLREAQAGLAEAQEdleaervARAKAEKQRRDLGEELEALRGEL 1170
Cdd:pfam07111 353 E---------------QAILQRALQDKAAEVEVERmSAKGLQMELSRAQE-------ARRRQQQQTASAEEQLKFVVNAM 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1171 EDTLDSTNAQQELRSKREQEVTELKKALEEESR---------AHEVSMQELRQRHS-------QALVEMAEQLEQARRgk 1234
Cdd:pfam07111 411 SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRkvhtikglmARKVALAQLRQESCpppppapPVDADLSLELEQLRE-- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1235 gvwEKTRLSLEAEVSELKAElSSLQTSRQEGEQKRRRLESQLQEVQgrssdserarseaaEKLQRAQAELESVSTALSEA 1314
Cdd:pfam07111 489 ---ERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLE--------------QELQRAQESLASVGQQLEVA 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1315 eskaiRLGKELSSAESQlHDTQELLQEETRAKLALGSRVRALEAEaagLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1394
Cdd:pfam07111 551 -----RQGQQESTEEAA-SLRQELTQQQEIYGQALQEKVAEVETR---LREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
....
gi 148690794 1395 QEEE 1398
Cdd:pfam07111 622 ATQE 625
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
982-1581 |
2.60e-04 |
|
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: 46.17 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 982 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlkyEATISDMEDRLKKE 1061
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS-----DLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1062 EKGR--QELEKLKRRLDgESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQ 1139
Cdd:TIGR04523 118 QKNKleVELNKLEKQKK-ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE---LNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1140 EDLEAER----VARAKAEKQRRDLGE--ELEALRGELEDTLdstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELR 1213
Cdd:TIGR04523 194 NKLLKLElllsNLKKKIQKNKSLESQisELKKQNNQLKDNI------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1214 QrhsqaLVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKrrRLESQLQEVQGRSSDSERARSEA 1293
Cdd:TIGR04523 268 Q-----LSEKQKELEQN-------NKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1294 AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAE---AAGLREQMEEE 1370
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnQEKLNQQKDEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1371 VVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL----ERARRRLQQELDD 1446
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1447 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--AL 1524
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieEL 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1525 RAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE 1581
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1740-1945 |
2.71e-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: 45.53 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1740 AATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEe 1819
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1820 dagARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKR 1899
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148690794 1900 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1945
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
892-1196 |
2.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 892 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE 971
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 972 SHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1051
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1052 SDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgRKEdelqaallraeeeggaraqllksLREA 1131
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL-----RKE-----------------------ADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1132 QAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLdSTNAQQELRSKREQEVTELKK 1196
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEEIFEKLKK 278
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
958-1732 |
2.96e-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: 46.19 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 958 SEKKRLQQHIQELES---HLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1034
Cdd:TIGR00606 166 SEGKALKQKFDEIFSatrYIKALETLRQVRQ----TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1035 EKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1108
Cdd:TIGR00606 242 SYENELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1109 AALLRAEEEGGARAQLLkSLREAQAGLAEAQEDLEAERVaraKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKre 1188
Cdd:TIGR00606 322 VDCQRELEKLNKERRLL-NQEKTELLVEQGRLQLQADRH---QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1189 qeVTELKKALEEESRAHEVSMQELRQRHSQALvEMAEQLEQARRGKG-VWEKTRLSLEAEVSELKAELSSLQTSRQ---- 1263
Cdd:TIGR00606 396 --HTLVIERQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKGLGrTIELKKEILEKKQEELKFVIKELQQLEGssdr 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1264 --EGEQKRRRLESQLQEVQGRSSDSERARSEAAekLQRAQAELESVSTALSE----------AESKAIRLGKELSSAESQ 1331
Cdd:TIGR00606 473 ilELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKDEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1332 LHDTQELLQEETRAKLALGSRVRALEAEAAGLRE---QMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEA 1408
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1409 RRRAAREAETLtQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQ----LLSTLEKKQRKFDQLLAEEKAAVLRAVE 1484
Cdd:TIGR00606 631 VCGSQDEESDL-ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1485 DRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS----KDDVGKNVHELERArKAAEQAASDLR 1560
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDiqrlKNDIEEQETLLGTI-MPEEESAKVCL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1561 TQVTELEDELTAAEDAKLRLEVTVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERD--EERKQRALAMAARKKL 1637
Cdd:TIGR00606 789 TDVTIMERFQMELKDVERKIAQQAAKLQGSDlDRTVQQVNQEKQEKQHELDTVVSKIELNRKliQDQQEQIQHLKSKTNE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1638 ELELEELKAQTSAAGQGKEEavkQLKKMQVQMKELWREVEEtrsSRDEMFTLSRENEKKLKGLEAEVLRLQEElaasdra 1717
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEE---QLVELSTEVQSLIREIKD---AKEQDSPLETFLEKDQQEKEELISSKETS------- 935
|
810
....*....|....*
gi 148690794 1718 RRQAQQDRDEMAEEV 1732
Cdd:TIGR00606 936 NKKAQDKVNDIKEKV 950
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
894-1061 |
3.43e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 894 QGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarKQELELVVTELEARVGEEEecsRQLQSEKKRLQQHIQELESH 973
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA-----KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 974 LEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLeERLAEFSSQAAEEE--EKVKSlnklRLKYEA-- 1049
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEK---KEEELEELIEEQLQEL-ERISGLTAEEAKEIllEKVEE----EARHEAav 173
|
170
....*....|..
gi 148690794 1050 TISDMEDRLKKE 1061
Cdd:PRK12704 174 LIKEIEEEAKEE 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
867-1394 |
3.99e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARAQEL-QKVQELQQQ--SAREVGELQGRVAQL------EEERTRLAEQLRaeaELCSEAEETRArLAARKQELEL 937
Cdd:PRK04863 445 EEFQAKEQEAtEELLSLEQKlsVAQAAHSQFEQAYQLvrkiagEVSRSEAWDVAR---ELLRRLREQRH-LAEQLQQLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 938 VVTELEARVGEEEECSRQLQSEKKRLQQHIQ---ELESHLEAEEGARQKLQLEKVTTEAK---MKKFEEDLLLLEDQNSK 1011
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrmaLRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1012 LSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQeqmveqkQ 1091
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDV-------TEYMQQLLERERELTVERDELAARKQALDEEIERLS-------Q 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1092 RAEELLAQLGRKEDELQAALLrAE-------EE--------GGARAQL----LKSLREAQAGLAEAQEDL---------- 1142
Cdd:PRK04863 667 PGGSEDPRLNALAERFGGVLL-SEiyddvslEDapyfsalyGPARHAIvvpdLSDAAEQLAGLEDCPEDLyliegdpdsf 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1143 -----EAERVARAKAEKQ-----------------RRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEE 1200
Cdd:PRK04863 746 ddsvfSVEELEKAVVVKIadrqwrysrfpevplfgRAAREKRIEQLRAEREEL-------AERYATLSFDVQKLQRLHQA 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1201 ESR---AH---------EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSL------------------------ 1244
Cdd:PRK04863 819 FSRfigSHlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladrvee 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1245 ------EAEV------------SELKAELSSLQTSRQEGEQKRRR---LESQLQEVQGRS---------------SDSER 1288
Cdd:PRK04863 899 ireqldEAEEakrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDyqqAQQTQRDAKQQAfaltevvqrrahfsyEDAAE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1289 ARSEAAE-------KLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEA 1360
Cdd:PRK04863 979 MLAKNSDlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgAEERA 1058
|
650 660 670
....*....|....*....|....*....|....*...
gi 148690794 1361 AGLREQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1394
Cdd:PRK04863 1059 RARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
919-1150 |
4.31e-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: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 919 SEAEETRARLAARKQELELVVTELEArvgeeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF 998
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA-----------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 999 EEDL----LLLEDQNSKLSKERRLLE--------ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1066
Cdd:COG3883 85 REELgeraRALYRSGGSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1067 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAER 1146
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
....
gi 148690794 1147 VARA 1150
Cdd:COG3883 245 SAAG 248
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1138-1349 |
4.97e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1138 AQEDLEAERVARAKAEKQRRDLGEELealRGELEdtldstnAQQELRSKREQEVTELKKALEEESRAHEVSMQ------- 1210
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEEL---RTELD-------ASRALAEKQKHELDTEKRCAEELKEAMQMAMEgharmle 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1211 ---ELRQRHSQALVEMAEQLE--------QARRG-KGVWEKTRLSLEAEVSELKAElsslqtsrqeGEQKRRRLESQLQE 1278
Cdd:PLN03188 1115 qyaDLEEKHIQLLARHRRIQEgiddvkkaAARAGvRGAESKFINALAAEISALKVE----------REKERRYLRDENKS 1184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1279 VQGRSSDSERARSEAAEKLQRAQAELESVSTALS---EAESKAIRLGKELSSA----ESQLHDTQELLQEETRAKLAL 1349
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKramDAEQEAAEAYKQIDKLkrkhENEISTLNQLVAESRLPKEAI 1262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
867-1168 |
5.16e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARV 946
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 947 GEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEF 1026
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1027 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1106
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1107 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1168
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
869-1368 |
6.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 869 LQARAQELQKVQELQQQSAREVGELQGRVAQLEE-ERTRLAEQLRAEAELCSEAEEtrarlaarKQELELVVTELEArvg 947
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKsHSITLKEIERLSIEYNNAMDD--------YNNLKSALNELSS--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 948 eeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE---------DLL----LLEDQN 1009
Cdd:PRK01156 247 --------LEDMKNRYESEIKTAESDLSMELEKNNYYkeleeRHMKIINDPVYKNRNYindyfkyknDIEnkkqILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1010 SKLSKERRLLE--ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1087
Cdd:PRK01156 319 AEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1088 EQKQRAEELLAQLgrkeDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV--------ARAKAEKQRRDL 1159
Cdd:PRK01156 399 IQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1160 GEELEALRGEL--------------------------EDTLDSTNAQQELRSKREQ------EVTELK----KALEEESR 1203
Cdd:PRK01156 475 NEKKSRLEEKIreieievkdidekivdlkkrkeylesEEINKSINEYNKIESARADledikiKINELKdkhdKYEEIKNR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1204 AHEVSMQELRQRHSQALVEMAE----QLEQARRGKGVWEKTRLSLEAEVSELKAEL----SSLQTSRQEGEQKRRRLESQ 1275
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddkSYIDKSIREIENEANNLNNK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1276 LQEVQGRSSDSERARsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA 1355
Cdd:PRK01156 635 YNEIQENKILIEKLR-GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570
....*....|...
gi 148690794 1356 LEAEAAGLREQME 1368
Cdd:PRK01156 714 LSDRINDINETLE 726
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1604-1927 |
6.35e-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: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1604 ERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMkelwREVEETRSSR 1683
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1684 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAsgNLSKAATLEEKR-----QLEGRLSQLEE 1758
Cdd:COG3096 354 EDL----EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQTRaiqyqQAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1759 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQKMLIAALE 1835
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1836 SKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEksnlrlkQLKRQLEEAEEEASRAQAGR 1915
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQR 580
|
330
....*....|..
gi 148690794 1916 RRLQRELEDVTE 1927
Cdd:COG3096 581 SELRQQLEQLRA 592
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1131-1387 |
6.36e-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: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1131 AQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEesrahevsmq 1210
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1211 eLRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-VSELkaeLSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERA 1289
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDF---LDRLSALSKIADADADLLEELKADKA----ELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1290 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEE 1369
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*...
gi 148690794 1370 EVVARERAGRELQSTQAQ 1387
Cdd:COG3883 229 AAAAAAAAAAAAAAAASA 246
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
898-1257 |
6.75e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 898 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAE 977
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 978 EGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDR 1057
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1058 LKKEEKGRQELEKLKRRldgesSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE 1137
Cdd:COG4372 166 LAALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1138 AQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHS 1217
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 148690794 1218 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1257
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1106-1278 |
8.92e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1106 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtlDSTNAQQELRS 1185
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1186 KREQEvtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEG 1265
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 148690794 1266 EQKRRRLESQLQE 1278
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1240-1624 |
8.93e-04 |
|
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: 44.18 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1240 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERARSEAAEKLQRAQAELESVStALSEAESKAI 1319
Cdd:COG5185 185 TLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKA----KEIINIEEALKGFQDPESELEDLA-QTSDKLEKLV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1320 RLGKELSsaESQLHDTQELLQeetraklalgsRVRALEAEAAGLREQMEEEVVARERAG---RELQSTQAQLSEWRRRQE 1396
Cdd:COG5185 260 EQNTDLR--LEKLGENAESSK-----------RLNENANNLIKQFENTKEKIAEYTKSIdikKATESLEEQLAAAEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1397 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDlgqqkQLLSTLEKKQRKFDQLLAEEK 1476
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELD-----SFKDTIESTKESLDEIPQNQR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1477 AA---VLRAVEDRERIEAEGREREARALsltraleeeqearEELERQNRALRAELEALLSSKDDVGKNVHELERAR--KA 1551
Cdd:COG5185 402 GYaqeILATLEDTLKAADRQIEELQRQI-------------EQATSSNEEVSKLLNELISELNKVMREADEESQSRleEA 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1552 AEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEER 1624
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1014-1229 |
8.99e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1014 KERRLLEERLAEFSSQAAEEEEK-------VKSLNKLRLKyeatiSDMEDRLKKE-------EKGRQELEKLKRRLDGES 1079
Cdd:COG0497 165 RAWRALKKELEELRADEAERAREldllrfqLEELEAAALQ-----PGEEEELEEErrrlsnaEKLREALQEALEALSGGE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1080 SELQEQMveqkQRAEELLAQLGRKEDELQAALLRAEEeggARAQLlkslREAQAGLAEAQEDLEA---------ERVARA 1150
Cdd:COG0497 240 GGALDLL----GQALRALERLAEYDPSLAELAERLES---ALIEL----EEAASELRRYLDSLEFdperleeveERLALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1151 KAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrAHEVSmqELRQRHSQALVE-MAEQLE 1228
Cdd:COG0497 309 RRLARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEA--AEKLS--AARKKAAKKLEKaVTAELA 384
|
.
gi 148690794 1229 Q 1229
Cdd:COG0497 385 D 385
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
877-1157 |
9.15e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 877 QKVQELQQqsarEVGELQGRVAQLEEERTRLAEQLRAEAELCSEA----EETRARLAARKQELELV---VTELEARVGEE 949
Cdd:PRK11637 47 DQLKSIQQ----DIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrklRETQNTLNQLNKQIDELnasIAKLEQQQAAQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 950 EE-CSRQLQSeKKRLQQHiQELESHLEAEEGARQK--LQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERLAEF 1026
Cdd:PRK11637 123 ERlLAAQLDA-AFRQGEH-TGLQLILSGEESQRGEriLAYFGYLNQARQETIAE----LKQTREELAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1027 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrqeleklkrrldgesselQEQMVEQKQraeellaqlgrKEDE 1106
Cdd:PRK11637 197 KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD---------------------QQQLSELRA-----------NESR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 148690794 1107 LQAALLRAEEEGGARAQllkslREAQaglaeaqedlEAERVARAKAEKQRR 1157
Cdd:PRK11637 245 LRDSIARAEREAKARAE-----REAR----------EAARVRDKQKQAKRK 280
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
874-1157 |
9.39e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 874 QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARlaaRKQELELVvtelearvgeeeecs 953
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK---ELREEAQELREK---RDELNEKV--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 954 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEE 1033
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1034 EEKVKSLNKLRLKyeatISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1113
Cdd:COG1340 149 LEKAKKALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 148690794 1114 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1157
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1218-1352 |
1.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1218 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLqtsrqegEQKRRRLESQLQEVQGrssdserARSEAAEKL 1297
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-------EAERSRLQALLAELAG-------AGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1298 QRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ------EETRAKLA-LGSR 1352
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDasekrdRESQAKIAdLGRR 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1419-1628 |
1.12e-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: 43.60 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1419 LTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREA 1498
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1499 RALSLTRALEEEQEAREELERQ----NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAE 1574
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1575 DAKLRLEVTVQALKAQhERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA 1628
Cdd:COG4942 192 ALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
884-1172 |
1.21e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 884 QQSAREVGELQGRVAQLEEERTRLAEQLRAeaelcseaeeTRARLAARKQELELVV----TELEARVGEEEECSRQLQSE 959
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQ----------LKEQLQLLNKLLPQANlladETLADRLEELREELDAAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 960 KKRLQQH---IQELESHLEA--------EEGARQKLQLEKVTTEAKMKKFE-------------EDLLLLEDQNSKLSKE 1015
Cdd:COG3096 909 QAFIQQHgkaLAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1016 rrlLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeEKGRQELEKLKRRLD---------------GESS 1080
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEelgvqadaeaeerarIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1081 ELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE-----AQEDLEAERVARA----K 1151
Cdd:COG3096 1063 ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAvlrlaRDNDVERRLHRRElaylS 1142
|
330 340
....*....|....*....|.
gi 148690794 1152 AEKQRRDLGEELEALRGELED 1172
Cdd:COG3096 1143 ADELRSMSDKALGALRLAVAD 1163
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
902-1299 |
1.22e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 902 EERTRLAEQLRAEAELCSEAEETRARLAARKQELelvvTELEARVGEEEEC-SRQLQSEKKRLQQHIQEleshleAEEGA 980
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSEL----KPSGQGGLDEEEAfLDRTAKREERRQKRLQE------ALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 981 RQklqLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLlEERLAEfssqAAEEEEKVKSLNKLRLKYEATISDMEDRLKK 1060
Cdd:pfam02029 87 KE---FDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1061 EEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1140
Cdd:pfam02029 159 EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1141 DLEAERVARAKAEKQRRDLGEelealrgeledtldstnaqqelrsKREQEvtelkkaleeesrahevsMQELRQRHSQAL 1220
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQE------------------------KESEE------------------FEKLRQKQQEAE 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1221 VEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAelsslqtsrQEGEQKRRRLEsqlqevqgrssDSERARSEAAEKLQR 1299
Cdd:pfam02029 277 LELEELKKKREERRKLLEEEEQRRKQEEAERKL---------REEEEKRRMKE-----------EIERRRAEAAEKRQK 335
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
875-1053 |
1.25e-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: 42.60 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 875 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcSEAEETRARLAARKQELELVVTELEARVGEEEECSR 954
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARL-------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 955 QLQSEKKrLQQHIQELESHleaeegARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1034
Cdd:COG1579 84 NVRNNKE-YEALQKEIESL------KRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*....
gi 148690794 1035 EKVKSLNKLRLKYEATISD 1053
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1078-1532 |
1.26e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.08 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1078 ESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV--ARAKAEKQ 1155
Cdd:COG3899 763 EAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARAlfNLGFILHW 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1156 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKG 1235
Cdd:COG3899 843 LGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLA 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1236 VWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvsTALSEAE 1315
Cdd:COG3899 923 AAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALE---AAAAALL 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1316 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1395
Cdd:COG3899 1000 ALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAA 1079
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1396 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1475
Cdd:COG3899 1080 AAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLAL 1159
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1476 KAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1532
Cdd:COG3899 1160 ALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1104-1379 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1104 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQEL 1183
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1184 RSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwektrlSLEAEVSELKAELSSLQTSRQ 1263
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----------ELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1264 EGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEET 1343
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 148690794 1344 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGR 1379
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
861-1141 |
1.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 861 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 940
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 941 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1020
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1021 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1100
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148690794 1101 GRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQED 1141
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1059-1315 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1059 KKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAEA 1138
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE----LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1139 QEDLEAeRVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEV-TELKKALEEESRAHE--VSMQELRQR 1215
Cdd:pfam15905 138 NELLKA-KFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqKNLEHSKGKVAQLEEklVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1216 ---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQK-RRRLESQLQEVQGRSSDSERARS 1291
Cdd:pfam15905 217 eksETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQElSKQIKDLNEKCKLLESEKEELLR 296
|
250 260
....*....|....*....|....
gi 148690794 1292 EAAEKLQRAQAELESVSTALSEAE 1315
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEE 320
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
859-1127 |
1.43e-03 |
|
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: 43.81 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 938
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 939 VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL-LEDQNSKLSKERR 1017
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLkYEEEPEELLLEEA 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1018 LLEERLAEFSSQaaEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1097
Cdd:pfam02463 946 DEKEKEENNKEE--EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
250 260 270
....*....|....*....|....*....|
gi 148690794 1098 AQLGRKEDELQAalLRAEEEGGARAQLLKS 1127
Cdd:pfam02463 1024 ELFVSINKGWNK--VFFYLELGGSAELRLE 1051
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1210-1382 |
1.48e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1210 QELRQRHSqalvemAEQLEQARRGkgvwektRLSLEAEVSELKAElsslqtsrqegEQKRRRLESQLQEVQGRSSDSERA 1289
Cdd:PTZ00491 664 QEAAARHQ------AELLEQEARG-------RLERQKMHDKAKAE-----------EQRTKLLELQAESAAVESSGQSRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1290 RSEAaeklqRAQAELESVSTALSEAE--SKAIRLGKELSSAESQLHDTQELLQEETRAKLALgSRVRAL-EAEAAGLREQ 1366
Cdd:PTZ00491 720 EALA-----EAEARLIEAEAEVEQAElrAKALRIEAEAELEKLRKRQELELEYEQAQNELEI-AKAKELaDIEATKFERI 793
|
170 180
....*....|....*....|
gi 148690794 1367 ME----EEVVARERAGRELQ 1382
Cdd:PTZ00491 794 VEalgrETLIAIARAGPELQ 813
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1655-1943 |
1.61e-03 |
|
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: 43.57 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1655 KEEAVKQLKKMQVQMKELWREVEETRSSR----DEMFTLSRENEKKLKGLEAEVLRLQEElaasDRARRQAQQDRDEMAE 1730
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1731 EVasgnlSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQ 1810
Cdd:pfam17380 373 EI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1811 ELRARLGEEDagaRARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRA-EKRLKEVVLQVDEERRVADQVRDQLEK 1889
Cdd:pfam17380 448 MERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1890 snlrlkqlkRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1943
Cdd:pfam17380 525 ---------RQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1258-1889 |
1.62e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1258 LQTSRQEGEQKRRRLESQLQevqgrssdserARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQE 1337
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIK-----------RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1338 LLQEETRAKLALGSR---VRALEAEAAGLREQMEEevvaRERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAR 1414
Cdd:PRK03918 236 LKEEIEELEKELESLegsKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1415 EAETLTqRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFdqllaeEKAAVLRAVEDRERIEAEGR 1494
Cdd:PRK03918 312 IEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY------EEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1495 EREAralsltraleeeqeareelerqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDeltaae 1574
Cdd:PRK03918 385 TPEK-------------------------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK------ 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1575 dAKLRLEVTVQALKAQHERDLQGRDDAG-----------EERRRQLAKQLRDAEVERDEERKQRALAMAARKKlelelee 1643
Cdd:PRK03918 434 -AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiEEKERKLRKELRELEKVLKKESELIKLKELAEQL------- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1644 lkaqtsaagqgkEEAVKQLKKMQVQ-MKELWREVEETRSsrdemftLSRENEKKLKGLEAEVLRLQE---ELAASDRARR 1719
Cdd:PRK03918 506 ------------KELEEKLKKYNLEeLEKKAEEYEKLKE-------KLIKLKGEIKSLKKELEKLEElkkKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1720 QAQQDRDEMAEEVASGNLSKAATLEEK-RQLEGRLSQLEEELEEEQNNSELLKdhyrklvlQVESLTTELSAERSFSAKA 1798
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEK--------ELKKLEEELDKAFEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1799 ESGRQQLERQIQELRARLGEEDAgARARQKMLiaALESKLAqaeeqleqesrerilsgklvrRAEKRLKEVVLQVDEERR 1878
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEY-EELREEYL--ELSRELA---------------------GLRAELEELEKRREEIKK 694
|
650
....*....|.
gi 148690794 1879 VADQVRDQLEK 1889
Cdd:PRK03918 695 TLEKLKEELEE 705
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1780-1923 |
1.66e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1780 QVESLTTELSAERSFSAKAESGRQQLERQIQelrarlGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLV 1859
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLG------SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148690794 1860 RRAEKRLKEVVLQVDEE-RRVADQVRDQLEKSNLRLKQLKRQLEE---AEEEASRAQAGRRRLQRELE 1923
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVE 361
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
865-1109 |
1.77e-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: 43.51 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 865 QDEVLQARAQELQKV--QELQQQSARevgeLQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVvtel 942
Cdd:pfam13166 262 GQPLPAERKAALEAHfdDEFTEFQNR----LQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVL---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 943 earvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAK--MKKFEEDLLLLEDQNSKLSKERRLLE 1020
Cdd:pfam13166 334 ----------NSQLDGLRRALEAKRKDPFKSIELDSVDAKIESINDLVASINelIAKHNEITDNFEEEKNKAKKKLRLHL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1021 erLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKgrqELEKLkrrlDGESSELQEQMVEQKQRAEE---LL 1097
Cdd:pfam13166 404 --VEEFKSEIDEYKDKYAGL-------EKAINSLEKEIKNLEA---EIKKL----REEIKELEAQLRDHKPGADEinkLL 467
|
250
....*....|..
gi 148690794 1098 AQLGRKEDELQA 1109
Cdd:pfam13166 468 KAFGFGELELSF 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1441-1702 |
1.99e-03 |
|
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: 43.19 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1441 QQELDDATVDLGQQKQLLSTLEKKQRKFDQ---LLAEEKAAVLRAVEDRERIEAEGREREAR-------ALSLTRALEEE 1510
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKRELErirqeeiAMEISRMRELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1511 QEAREELErQNRALRAELEALLSSK-------DDVGKNVHELERARKAAEQAAS-DLRTQVTELEDELTAAEDAKLRLEV 1582
Cdd:pfam17380 382 RLQMERQQ-KNERVRQELEAARKVKileeerqRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1583 TVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQ 1661
Cdd:pfam17380 461 QVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148690794 1662 LKKMQVQMKE------LWREVEETRSSRD------EMFTLSRENEKKLKGLEA 1702
Cdd:pfam17380 541 ERRKQQEMEErrriqeQMRKATEERSRLEamererEMMRQIVESEKARAEYEA 593
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1131-1402 |
2.00e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1131 AQAGLAEAQEDL--EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQevtelkkaleeesrahevs 1208
Cdd:PRK11281 24 SAFARAASNGDLptEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1209 mqeLRQRHSQAlvemAEQLEQARRgkgvwEKTRLSlEAEVSELKAELSSLQTsrqegeqkrRRLESQLQEVQgrssdser 1288
Cdd:PRK11281 85 ---LKQQLAQA----PAKLRQAQA-----ELEALK-DDNDEETRETLSTLSL---------RQLESRLAQTL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1289 arseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQM 1367
Cdd:PRK11281 135 ------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQN 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148690794 1368 EEEvvARERAGRE-LQST-QAQ---LSEWRRRQEEEAAVL 1402
Cdd:PRK11281 209 DLQ--RKSLEGNTqLQDLlQKQrdyLTARIQRLEHQLQLL 246
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1073-1697 |
2.03e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1073 RRLDGESSELQEQMVEQKQRAEELLAQLgrkedelqAALLRAEEEGGARAQllkSLREAQAGlaeaqedleAERVARAKA 1152
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMEL--------DALAVAEKAGQAEAE---GLRAALAG---------AEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1153 EKQRRDLgEELEALrgeledtldstnaQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1232
Cdd:pfam07111 136 EGSQREL-EEIQRL-------------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1233 GKGVWEKTRLSLEAEVSELKA------ELSSLQTSRQEGEQKRRRLESQLQEVQgrssdSERARSEAAEKLqrAQAELES 1306
Cdd:pfam07111 202 LRKQLSKTQEELEAQVTLVESlrkyvgEQVPPEVHSQTWELERQELLDTMQHLQ-----EDRADLQATVEL--LQVRVQS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1307 VSTALSEAESKAIRLGKELSSAESQL-HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVvareragrelqstq 1385
Cdd:pfam07111 275 LTHMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQV-------------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1386 AQLSEWRRRQEEEAAVLEageearrraareaetltQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKK- 1464
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQ-----------------RALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQl 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1465 ----------QRKFDQLLAEEKAAVLRAVEDRERIEAEGRERE------ARALSLTRALEEEQEAREELERQNRALRAEL 1528
Cdd:pfam07111 404 kfvvnamsstQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglmARKVALAQLRQESCPPPPPAPPVDADLSLEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1529 EALLSSKDDVGKNV--------HELERARKAAEQAASDLRTQVTELEDELTAAEDA----KLRLEVTVQA---------- 1586
Cdd:pfam07111 484 EQLREERNRLDAELqlsahliqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvGQQLEVARQGqqesteeaas 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1587 ----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVK-Q 1661
Cdd:pfam07111 564 lrqeLTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKeE 643
|
650 660 670
....*....|....*....|....*....|....*.
gi 148690794 1662 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKL 1697
Cdd:pfam07111 644 GQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
883-1070 |
2.30e-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: 41.83 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 883 QQQSAREVGELQGRVAQLEEERTRLAEQLraeAELCSEAEETRARLAARKQELElvvtelearvgeeeecsrQLQSEKKR 962
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELE------------------DLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 963 LQQHIQELESHLEaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKS--- 1039
Cdd:COG1579 64 LELEIEEVEARIK-----KYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAElea 138
|
170 180 190
....*....|....*....|....*....|..
gi 148690794 1040 -LNKLRLKYEATISDMEDRLKKEEKGRQELEK 1070
Cdd:COG1579 139 eLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1111-1587 |
2.42e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1111 LLRAEEEGGARAQLLKSLRE-AQAGLAEAQEDLEAER---------VARAKAEKQRRDLGEELEALRGELEDTLDstnAQ 1180
Cdd:COG3903 456 LEVEGGGGGPRYRLLETVREyAAERLAEAGERAAARRrhadyylalAERAAAELRGPDQLAWLARLDAEHDNLRA---AL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1181 QELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1260
Cdd:COG3903 533 RWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1261 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1340
Cdd:COG3903 613 AAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAA 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1341 EETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLT 1420
Cdd:COG3903 693 ALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAAL 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1421 QRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEkkqrkfDQLLAEEKAAVLRAVEDRERIEAEGREREARA 1500
Cdd:COG3903 773 AALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAA------ALAAAAAAAAAAAAALAAALAAAAAAAAAAAA 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1501 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRL 1580
Cdd:COG3903 847 AAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAA 926
|
....*..
gi 148690794 1581 EVTVQAL 1587
Cdd:COG3903 927 AAAAAAA 933
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
867-986 |
3.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 867 EVLQARAQELQKVQElqqQSAREVGELQGRVAQLEEERTRLAEQLRA-EAELCSEAEET-RARLAARKQELELVVTELEA 944
Cdd:PRK00409 519 NELIASLEELERELE---QKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 148690794 945 RVGEEEEC--SRQLQSEKKRLQQHIQELESHLEAEEGARQKLQL 986
Cdd:PRK00409 596 LQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
922-1088 |
3.32e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 922 EETRARLAARKQELELVVTELEARvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF--- 998
Cdd:PHA02562 205 EEQRKKNGENIARKQNKYDELVEE-------AKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 999 -------------------EEDLLL-LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA---TISDME 1055
Cdd:PHA02562 278 ikmyekggvcptctqqiseGPDRITkIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTnkqSLITLV 357
|
170 180 190
....*....|....*....|....*....|...
gi 148690794 1056 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVE 1088
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
917-1257 |
3.61e-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: 42.36 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 917 LCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE--SHLEAEEGARQKLQLEKVTTEAK 994
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIkrKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 995 MKKFEEDLlllEDQNSKLSKERRllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrQELEKLKRR 1074
Cdd:pfam13166 167 LREIEKDN---FNAGVLLSDEDR--KAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGKS----SAIEELIKN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1075 LD-----GESSELQEQMVEQ---------KQRAEELLAQLGRKEDELQAALLR-AEEEGGARAQLLKSLreaQAGLAEAQ 1139
Cdd:pfam13166 238 PDladwvEQGLELHKAHLDTcpfcgqplpAERKAALEAHFDDEFTEFQNRLQKlIEKVESAISSLLAQL---PAVSDLAS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1140 EDLEAERvARAKAEKQRRDLGEELEALRGELE-----------------------DTLDSTNAQQELRSKREQEVTELKK 1196
Cdd:pfam13166 315 LLSAFEL-DVEDIESEAEVLNSQLDGLRRALEakrkdpfksieldsvdakiesinDLVASINELIAKHNEITDNFEEEKN 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1197 ALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1257
Cdd:pfam13166 394 KAKKKLRLHLVEeFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1027-1152 |
3.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1027 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1106
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 148690794 1107 LQAAlLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaERVARAKA 1152
Cdd:COG2433 457 ERRE-IRKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
888-1073 |
3.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 888 REVGELQGRVAQLEEERTRLAEQ---LRAE-AELCSEAEETRARLAARKQELELVVTELEARVGEEEECSR------QLQ 957
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQverLEAEvEELEAELEEKDERIERLERELSEARSEERREIRKDREISRldreieRLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 958 SEKKRLQQHIQELESHLEAEEGARQKLQ---------LEKVTTEA------KMKKFEEDLLLLEDQNSKLSKERRLLEE- 1021
Cdd:COG2433 479 RELEEERERIEELKRKLERLKELWKLEHsgelvpvkvVEKFTKEAirrleeEYGLKEGDVVYLRDASGAGRSTAELLAEa 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1022 ------RLAEFSSQAAE------------EEEKVKSLNKL----RLKYEATISDMEDRLKKEEKgRQELEKLKR 1073
Cdd:COG2433 559 gpraviVPGELSEAADEvlfeegipvlpaEDVTIQEVDDLavvdEEELEAAIEDWEERAEERRR-EKKAEMLER 631
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
875-1318 |
4.59e-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: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 875 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLA---EQLRAEAELCSEAEETRARLAARKQELELVVTELearvgeeEE 951
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQL-------QE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 952 CSRQLQSEKKRLQQHIQELESHLeAEEGARQKlQLEKVTTEAKMKKFEEDllLLEDQNSKLSKERRLLE------ERLAE 1025
Cdd:pfam05622 74 ENFRLETARDDYRIKCEELEKEV-LELQHRNE-ELTSLAEEAQALKDEMD--ILRESSDKVKKLEATVEtykkklEDLGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1026 FSSQaaeeeekVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKED 1105
Cdd:pfam05622 150 LRRQ-------VKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1106 ELqAALLRAEEeggaraqllkSLREAQAGLAEAQEDLEAervarakAEKQRRDLGEElEALRGELEDTLDSTNAqqelrs 1185
Cdd:pfam05622 219 KL-EALQKEKE----------RLIIERDTLRETNEELRC-------AQLQQAELSQA-DALLSPSSDPGDNLAA------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1186 krEQEVTELKKALEEesRAHEVSMQELRQRHS--QALVEMAEQLEQARRGK-GVWEKTRLSLEaEVSELKAELSSLQTSR 1262
Cdd:pfam05622 274 --EIMPAEIREKLIR--LQHENKMLRLGQEGSyrERLTELQQLLEDANRRKnELETQNRLANQ-RILELQQQVEELQKAL 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1263 QEGEQKRRrlesqlqevqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKA 1318
Cdd:pfam05622 349 QEQGSKAE-----------DSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ 393
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1106-1397 |
4.82e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1106 ELQAALLRAEEE---GGARAQLLKSLREAQAGLAEAQEDLEAERVARakaekqRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:NF041483 82 QIQADQLRADAErelRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVESHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1183 -LRSKREQEVtelkKALEEESRAhevsmqELRQRHSQALVEMAEQLEQARRgkgvwektRLSLEAEVSELKAElSSLQTS 1261
Cdd:NF041483 156 qLRARTESQA----RRLLDESRA------EAEQALAAARAEAERLAEEARQ--------RLGSEAESARAEAE-AILRRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1262 RQEGEQKRRRLESQLQEV-----QGRSS---DSERAR--------------SEAAEKLQRAQAELESVstaLSEAESKAi 1319
Cdd:NF041483 217 RKDAERLLNAASTQAQEAtdhaeQLRSStaaESDQARrqaaelsraaeqrmQEAEEALREARAEAEKV---VAEAKEAA- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1320 rlGKELSSAESQ--------LHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQLSEW 1391
Cdd:NF041483 293 --AKQLASAESAneqrtrtaKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKART-VAAEDTAAQLAKA 369
|
....*.
gi 148690794 1392 RRRQEE 1397
Cdd:NF041483 370 ARTAEE 375
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
871-1156 |
5.20e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.56 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 871 ARAQELQKVQELQQQsarevgelqgrvAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEE 950
Cdd:pfam15558 15 ARHKEEQRMRELQQQ------------AALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE----QRKARLGREE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 951 EcsRQLQSEKKRLQQHIQELESHLEAEEGARQKlQLEKVTTEAKMKKFEEDLLLLED---QNSKLSKERRLLEERLAEFS 1027
Cdd:pfam15558 79 R--RRADRREKQVIEKESRWREQAEDQENQRQE-KLERARQEAEQRKQCQEQRLKEKeeeLQALREQNSLQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1028 S----QAAEEEEKVKSLN-KLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRldgeSSELQEQMVEQkqRAEELLAQLG 1101
Cdd:pfam15558 156 HkrqlKEREEQKKVQENNlSELLNHQARKVLVDCQAKAEELLRRlSLEQSLQR----SQENYEQLVEE--RHRELREKAQ 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 148690794 1102 RKEDELQAALLRAEEEGGARAQLLKSLREAqAGLAEAQEDLEAERVARAKAEKQR 1156
Cdd:pfam15558 230 KEEEQFQRAKWRAEEKEEERQEHKEALAEL-ADRKIQQARQVAHKTVQDKAQRAR 283
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
904-1062 |
5.27e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 904 RTRLAEQLRAEAELCSEAEETRARLAARKQELElvvteleARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK 983
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERA-------EKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 984 LQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----------RRLLEERLAEFSSQAAE--EEEKVKSLNKLRLKYEATI 1051
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEaeraeaekqrQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKAR 491
|
170
....*....|.
gi 148690794 1052 SDMEDRLKKEE 1062
Cdd:pfam15709 492 LEAEERRQKEE 502
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
868-1329 |
5.68e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.43 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 868 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 947
Cdd:COG5278 70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 948 EEEECsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1027
Cdd:COG5278 150 LMDEI-RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1028 SQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1107
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1108 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKR 1187
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1188 EQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQ 1267
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148690794 1268 KRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAE 1329
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1239-1390 |
5.69e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 41.13 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1239 KTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQevqgrssdSERARSEAA----EKLQRAQAELESvstALSEA 1314
Cdd:pfam14915 56 KTVFQYNGQLNVLKAENTMLNSKLENEKQNKERLETEVE--------SYRSRLAAAiqdhEQSQTSKRDLEL---AFQRE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148690794 1315 ESKAIRLGKELSSAESQLHDTQELL-QEETRAKlalgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSE 1390
Cdd:pfam14915 125 RDEWLRLQDKMNFDVSNLRDENEILsQQLSKAE----SKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKE 197
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1130-1340 |
5.90e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1130 EAQAGLAEAQEDLEAERVARAKAEKQRRDLgeELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAHE-VS 1208
Cdd:pfam17045 27 EGQTRALETRLDIREEELLSARNTLERKHK--EIGLLRQQLEELE---KGKQELVAKYEQQLQKLQEELSKLKRSYEkLQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1209 MQELRQRHSQA---------LVEMAEQLEQARRGKGVWEKTRL-------SLEAEVSELKAELSSLQTS--RQEGEQKRR 1270
Cdd:pfam17045 102 RKQLKEAREEAksreedrseLSRLNGKLEEFRQKSLEWEQQRLqyqqqvaSLEAQRKALAEQSSLIQSAayQVQLEGRKQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1271 RLESQLQEVQGRSSDSERARseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1340
Cdd:pfam17045 182 CLEASQSEIQRLRSKLERAQ----DSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1790-1882 |
6.19e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1790 AERSFSAKAESGRQQLERQIQELRAR--LGEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ESRERILSGKLVRRA 1862
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|
gi 148690794 1863 EKRLKEVVLQVDEERRVADQ 1882
Cdd:PRK11448 223 DQAAKRLELSEEETRILIDQ 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
882-1150 |
6.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 882 LQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEARVGEEEecSRQLQSEKK 961
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 962 RLQQHIQELESHLEAeegARQKLQLEKVTTEAkmkkfeedlLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLn 1041
Cdd:COG3206 230 EARAELAEAEARLAA---LRAQLGSGPDALPE---------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1042 klrlkyeatisdmedrlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGAR 1121
Cdd:COG3206 297 -----------------------RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
250 260
....*....|....*....|....*....
gi 148690794 1122 AQLLKSLREAQAGLAEAQEDLEAERVARA 1150
Cdd:COG3206 354 RRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
921-1043 |
6.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 921 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMK 996
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERElseaRSEERREIR 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 148690794 997 KfEEDLLLLEDQNSKLSKERRLLEERLAEFSsqaaEEEEKVKSLNKL 1043
Cdd:COG2433 463 K-DREISRLDREIERLERELEEERERIEELK----RKLERLKELWKL 504
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
851-959 |
6.92e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 851 RLFIKVKP--LLQVTRQDEVLQARAQELQKvqELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARL 928
Cdd:COG0542 403 RMEIDSKPeeLDELERRLEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 148690794 929 AARKQELELVVTELEARVGEEEECSRQLQSE 959
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
859-1170 |
7.22e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 859 LLQVTRQDEV--LQARAQELQKVQELQQQSAREVGELQGRV------AQLEEERTRLAEQLRAEAELCSEAEETRARLAA 930
Cdd:PRK04863 790 QLRAEREELAerYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 931 RKQELELV-----------VTELEARVGEEEECSRQLQSEKKRLQQH-------------IQELESHLEAEEgaRQKLQL 986
Cdd:PRK04863 870 AKEGLSALnrllprlnllaDETLADRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQLK--QDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 987 EKVTTEAKMKKF--------------EEDLLLLE---DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1049
Cdd:PRK04863 948 QQTQRDAKQQAFaltevvqrrahfsyEDAAEMLAknsDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1050 TISDMEDRLKKEEkgrQELEKLKRRLDGE--------SSELQEQMVEQKQRAEELLAQLGRKEDELQAallraeeeggar 1121
Cdd:PRK04863 1028 SYDAKRQMLQELK---QELQDLGVPADSGaeerararRDELHARLSANRSRRNQLEKQLTFCEAEMDN------------ 1092
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 148690794 1122 aqLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1170
Cdd:PRK04863 1093 --LTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRREL 1139
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1031-1377 |
7.24e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1031 AEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAA 1110
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1111 LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1190
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1191 VTELKKALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKR 1269
Cdd:COG4372 166 LAALEQELQALSEAEAEQaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1270 RRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL 1349
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*...
gi 148690794 1350 GSRVRALEAEAAGLREQMEEEVVARERA 1377
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1243-1354 |
7.75e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1243 SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGR-SSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1321
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148690794 1322 GK--ELSSAESQLHDTQELLQE------ETRAKLALGSRVR 1354
Cdd:PRK00409 604 VKahELIEARKRLNKANEKKEKkkkkqkEKQEELKVGDEVK 644
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1122-1944 |
8.49e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.48 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1122 AQLLKSLREAQAGLAEAQEDLEaeRVARAKAEKQRR--DLGEELEALRGELEDTLDSTnAQQELRSKREQEVTELKKALE 1199
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLV--EMARELEELSAResDLEQDYQAASDHLNLVQTAL-RQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1200 EESrahevsmqelrqrhsQALVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQtsRQEGEQKRRRLESQ---- 1275
Cdd:COG3096 365 EQE---------------EVVEEAAEQLAEA-------EARLEAAEEEVDSLKSQLADYQ--QALDVQQTRAIQYQqavq 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1276 -LQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKairlgkelssaesqLHDTQELLQEETRAKLALGSRVR 1354
Cdd:COG3096 421 aLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQK--------------LSVADAARRQFEKAYELVCKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1355 ALEAEAAGlreqmeeeVVARE--RAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVER 1432
Cdd:COG3096 487 EVERSQAW--------QTAREllRRYRSQQALAQRLQQLRAQLAE---------------------LEQRLRQQQNAERL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1433 LERARRRLQQELDDATvdlgQQKQLLSTLEKKQRKFDQLLAEekaavlrAVEDRERIEAEGREREARALSLTRALEEEqe 1512
Cdd:COG3096 538 LEEFCQRIGQQLDAAE----ELEELLAELEAQLEELEEQAAE-------AVEQRSELRQQLEQLRARIKELAARAPAW-- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1513 areelerqnRALRAELEALlsskddvgknvHELERARKAAEQAASDLRTQVTELEDELTAAEDaklRLEVTVQALKAQHE 1592
Cdd:COG3096 605 ---------LAAQDALERL-----------REQSGEALADSQEVTAAMQQLLEREREATVERD---ELAARKQALESQIE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1593 RDLQGrDDAGEERRRQLAKQL---------------------------RDAEVERDEERKQRALAmaARKKLELELEELK 1645
Cdd:COG3096 662 RLSQP-GGAEDPRLLALAERLggvllseiyddvtledapyfsalygpaRHAIVVPDLSAVKEQLA--GLEDCPEDLYLIE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1646 AQTSAAGQGKEEAVKQLKKMQVQMKElwREVEETRSSRDEMFTlSRENEKKLKGLEAEVLRLQEELAASdRARRQAQQDR 1725
Cdd:COG3096 739 GDPDSFDDSVFDAEELEDAVVVKLSD--RQWRYSRFPEVPLFG-RAAREKRLEELRAERDELAEQYAKA-SFDVQKLQRL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1726 DEMAEEVASGNLSKA---------ATLEEKR-QLEGRLSQLEEELEEEQNNSELLKDHY---RKLVLQVESLTTELSAER 1792
Cdd:COG3096 815 HQAFSQFVGGHLAVAfapdpeaelAALRQRRsELERELAQHRAQEQQLRQQLDQLKEQLqllNKLLPQANLLADETLADR 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1793 SFSAKAESGR-QQLERQIQELRARLGEEDAgararqkmLIAALESKLAQaEEQLEQESRERILSGKLVRRAEKRLKEVVl 1871
Cdd:COG3096 895 LEELREELDAaQEAQAFIQQHGKALAQLEP--------LVAVLQSDPEQ-FEQLQADYLQAKEQQRRLKQQIFALSEVV- 964
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148690794 1872 qvdeERRVA---DQVRDQLEKSNLRLKQLKRQLEeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLR 1944
Cdd:COG3096 965 ----QRRPHfsyEDAVGLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRD 1029
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
954-1211 |
8.50e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 954 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllLEDQNSKLSKERRLLEERLAEFSSQaaee 1033
Cdd:pfam15905 83 RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------LEKQLLELTRVNELLKAKFSEDGTQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1034 eEKVKSLN----KLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV-------EQKQRAEELLAQLgr 1102
Cdd:pfam15905 152 -KKMSSLSmelmKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVstekekiEEKSETEKLLEYI-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1103 keDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArakAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1182
Cdd:pfam15905 229 --TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
|
250 260
....*....|....*....|....*....
gi 148690794 1183 LRSKreqEVTELKKALEEESRAHEVSMQE 1211
Cdd:pfam15905 304 TLNA---ELEELKEKLTLEEQEHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
866-1123 |
9.03e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 866 DEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEAR 945
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 946 VGEEEECSRQLQsekkRLQQHIQELESHLEAE--EGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1023
Cdd:COG3883 85 REELGERARALY----RSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1024 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1103
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260
....*....|....*....|
gi 148690794 1104 EDELQAALLRAEEEGGARAQ 1123
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAG 256
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1073-1222 |
9.54e-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: 40.48 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1073 RRLDGESSELQEQM---VEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1149
Cdd:pfam00529 54 TDYQAALDSAEAQLakaQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148690794 1150 AKAEKQRRDLgEELEALRGELEDTLDSTNAQQE-LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVE 1222
Cdd:pfam00529 134 PIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1244-1402 |
1.00e-02 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.91 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148690794 1244 LEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESkairlGK 1323
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN-----NK 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148690794 1324 ELSSAESQLhDTQELLQEEtraklalgsrvraLEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVL 1402
Cdd:COG1579 90 EYEALQKEI-ESLKRRISD-------------LEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| |
