|
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 ... |
115-784 |
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: 1345.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGLL 354
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 355 PEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 434
Cdd:cd14930 241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 435 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 514
Cdd:cd14930 321 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 515 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLH 594
Cdd:cd14930 401 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 595 YAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 674
Cdd:cd14930 481 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 675 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 754
Cdd:cd14930 561 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 28801584 755 DGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14930 641 DGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETLESLRVLGL 353
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 594 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 671
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 28801584 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
861-1941 |
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: 1281.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 861 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1100
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1181 LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR 1260
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1261 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEE 1340
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1341 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1420
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1421 LAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1500
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1501 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1581 TVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL 1660
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1661 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1740
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1741 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAG 1820
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1821 ARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLE 1900
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 28801584 1901 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1941
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQETLESLRVL 351
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 431
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 432 ADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 512 EEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK-FQRPRNLRDQADF 590
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 591 SVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMFRTVGQLY 670
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 671 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 750
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 28801584 751 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLR 349
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 589
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQ 668
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 749 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
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: 1131.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 265
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 266 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 344
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 345 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 424
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 425 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 505 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPrNL 584
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 664
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 28801584 745 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-784 |
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: 1115.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGL 353
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 594 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYK 671
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 28801584 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
115-784 |
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: 1100.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVLGL 353
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 594 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 671
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 28801584 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG----VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLR 349
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 589
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQL 669
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd15896 561 YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 640
|
650 660 670
....*....|....*....|....*....|....*
gi 28801584 750 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd15896 641 PKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
104-784 |
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 28801584 104 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 183
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 184 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGS----GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELF 341
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiDGiDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 342 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 421
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 422 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 581
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 582 RnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGPPGGRPRRG 661
Cdd:pfam00063 475 R-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 662 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 28801584 742 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
96-796 |
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 28801584 96 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 175
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 176 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpGELERQLLQANPILEAFGNAKTVKNDNS 255
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 256 SRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 334
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTvD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 335 GQE-RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNT-AAQKLCRLLGLGVTDFSRALL 412
Cdd:smart00242 235 GIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 413 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCIN 492
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 493 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQ 572
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 573 GSHPKFQRPRNlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGdg 652
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS-----NAGSKK-- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 653 ppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:smart00242 543 ---------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 733 LFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 796
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
94-1171 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 94 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 173
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 174 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkEPGVPGELERQLLQANPILEAFGNAKTVKND 253
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-----STVEISSIEKQILATNPILEAFGNAKTVRND 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 254 NSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS 333
Cdd:COG5022 214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 334 PGQ--ERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 411
Cdd:COG5022 294 IDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 412 LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCI 491
Cdd:COG5022 373 VKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 492 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKSFVEKVAQ- 570
Cdd:COG5022 452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQr 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 571 -EQGSHPKFQRPRnLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVgleqvssl 649
Cdd:COG5022 530 lNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 650 gdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP 729
Cdd:COG5022 600 ---------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 730 NRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVS 805
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 806 FQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKVQ--ELQQQ 883
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQktIKREK 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 884 SAREvgelqgrvaQLEEERTRLAEQLRAEAelcSEAEEtrarlaARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ 963
Cdd:COG5022 831 KLRE---------TEEVEFSLKAEVLIQKF---GRSLK------AKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 964 HIQELEShleaeegarQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERRLLEERlaEFSSQAAEEEEKVKSLNKLR 1042
Cdd:COG5022 893 SISSLKL---------VNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLH 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1043 L---KYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK--QRAEELLAQLGRKEDELQAALLRAEEEGG 1117
Cdd:COG5022 961 EvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSASKIISSEST 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1118 ARAQlLKSLREAQAGLAEAQEDLEaervARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:COG5022 1041 ELSI-LKPLQKLKGLLLLENNQLQ----ARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RELFQETLES 347
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 348 LRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNT--DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppggrprrgmfr 664
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 tvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd00124 519 -----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 28801584 745 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 268
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 346
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 347 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 426
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 427 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 505
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 506 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR-- 582
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 583 -NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRG 661
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 662 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:cd14927 553 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 28801584 742 EILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14927 633 RILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQA 588
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 589 D--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 666
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14913 550 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 28801584 747 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 352
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 433 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLR---DQA 588
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 589 DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRRGMFRTVGQ 668
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKGGGFATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 749 IpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
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: 707.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQETLESLRVLG 352
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 433 DFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD---QA 588
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGkgpEA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 589 DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRRGMFRTVGQ 668
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRGSSFMTVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14934 544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 749 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14934 624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
116-784 |
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 28801584 116 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGrkEPGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQETLESLRVLG 352
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 433 DFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 512 EEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK--FQRPRnlRDQAD 589
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR--FSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrgmfRTVGQL 669
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------------KTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....*
gi 28801584 750 PKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA---LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGL 353
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 434 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD--QAD 589
Cdd:cd14929 396 EYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKkfEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrgmFRTVGQL 669
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS---FQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 750 PKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
116-784 |
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: 692.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD-- 586
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGkp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 666
Cdd:cd14917 476 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14917 550 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 28801584 747 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14917 630 AAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 508
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 509 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNL--R 585
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVkgK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 586 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRprrgmFRT 665
Cdd:cd14916 476 QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-----FQT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14916 551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 28801584 746 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14916 631 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
117-784 |
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 28801584 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 196
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 197 GAGKTENTKKVIQYLAHVA-SSPKGRKEPG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAvTGEKKKEESGkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 352
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 431
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 432 ADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 511 QEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQAD 589
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 --FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRGMFRTVG 667
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 747
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 28801584 748 AIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 349
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 429 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRD 586
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 QAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRGMFR 664
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKGSSFQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14912 553 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 28801584 745 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
116-784 |
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: 661.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 349
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 429 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD 586
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 --QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRRGMFR 664
Cdd:cd14910 476 kvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 28801584 745 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14910 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGRKE--PG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQETL 345
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 424
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 425 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 503
Cdd:cd14923 316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 504 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPR 582
Cdd:cd14923 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 583 NLRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPGGRPRR 660
Cdd:cd14923 471 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 661 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 740
Cdd:cd14923 547 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 28801584 741 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14923 627 YRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 349
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 429 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD 586
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 QAD--FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRRGMFR 664
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14915 551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 28801584 745 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14915 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDYVQKAQ 427
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFnhTMF 507
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RD--QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggrprrGM 662
Cdd:cd01378 468 FElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK------------KR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 663 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd01378 531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 28801584 743 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKK-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 511 QEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADF 590
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 591 SVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLY 670
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGKPTVGDTF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 671 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 750
Cdd:cd14883 548 KHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARS 627
|
650 660 670
....*....|....*....|....*....|....
gi 28801584 751 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14883 628 ADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLESLRVLGL 353
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 514 YQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRdqadFSVL 593
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA----FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 594 HYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKES 673
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 674 LSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGF 753
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SAS 616
|
650 660 670
....*....|....*....|....*....|.
gi 28801584 754 MDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01383 617 QDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
115-784 |
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: 594.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVAsspkGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQHS-----WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQETLESLRVLG 352
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKK--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 508
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 509 LEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlRDQ 587
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS-DLN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 588 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPrrgmfrTVG 667
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP------TLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 747
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 28801584 748 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01381 612 IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQETLESLRVL 351
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGRD-YVQKAQ 427
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTPDgIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQ 587
Cdd:cd01384 394 KMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 588 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPRRGM-FRTV 666
Cdd:cd01384 469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTSSSSkFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 28801584 747 NAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
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 ... |
115-784 |
1.53e-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: 1.53e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETLESLRVLGL 353
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRIKVGRDYVQ 424
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGGAKGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 425 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 502
Cdd:cd01382 299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 503 NHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPR 582
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 583 --------NLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQVSSLGDGPP 654
Cdd:cd01382 452 ksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFESSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 655 GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 734
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 28801584 735 QEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
115-784 |
9.06e-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: 9.06e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 189
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 190 ILCTGESGAGKTENTKKVIQYLAHVAS-----SPKGRKEPGVPGE-----LERQLLQANPILEAFGNAKTVKNDNSSRFG 259
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgASGEGEAASEAIEqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 260 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 338
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 339 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 415
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 416 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 495
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 496 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 565
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 566 ------EKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 639
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 640 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 719
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 720 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
1.42e-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: 1.42e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL----------FQET 344
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvddvadFEEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 345 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCR---LLGLGVTDFSRALLTPRIKV-GR 420
Cdd:cd14872 222 VLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 421 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 500
Cdd:cd14872 302 DPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 501 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQR 580
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 581 PRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdgppggrPRR 660
Cdd:cd14872 459 AEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------------DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 661 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 740
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 28801584 741 YEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
116-784 |
1.30e-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: 1.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR--------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELFQETLESLR 349
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVL----KKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 503
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 504 HTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPkFQRPR 582
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 583 nlRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgppggrprrgm 662
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 663 frTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 28801584 743 ILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
115-784 |
1.91e-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: 1.91e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE--------RELFQETL 345
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 581
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 582 rnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgppggrprrg 661
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 662 mfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:cd14897 522 ------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRY 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 28801584 742 EILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
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, ... |
115-784 |
9.20e-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: 9.20e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 274
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQETLESLRVLG 352
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD 589
Cdd:cd01387 391 EQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--MPLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 590 FSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRGmfRTVGQL 669
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT--PTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 750 PKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 784
Cdd:cd01387 623 PRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
115-784 |
3.75e-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: 3.75e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 510 EQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGSHPKFQR----PRNLR 585
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 586 DQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMfRT 665
Cdd:cd14903 463 TQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT-TT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 28801584 746 PNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 784
Cdd:cd14903 620 PEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
115-782 |
1.66e-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: 1.66e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 186
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 187 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 264
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 265 NFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQER------ 338
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCYDRrdgvdd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 339 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI-VLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI 416
Cdd:cd14901 237 sVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLcFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 417 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFEQLCINYTN 495
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 496 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSH 575
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 576 PKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSlgdgppg 655
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 656 grprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 735
Cdd:cd14901 531 ---------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHD 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 28801584 736 EFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 782
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 ... |
115-784 |
2.45e-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: 2.45e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLahVASSPKGRKEpGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGS-GV----EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQETLESLRVLG 352
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 507 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnLRD 586
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ-VME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 QAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL----------------- 649
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 650 -GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 710
Cdd:cd01385 541 aGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 711 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
115-746 |
1.07e-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: 1.07e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI----- 268
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 269 ----AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKADLLL-EPCS 321
Cdd:cd14888 155 msgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISIDMSSfEPHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 322 HYRFLT-NGPSSSPG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL--- 396
Cdd:cd14888 235 KFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 397 CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIA 476
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 477 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWF 556
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 557 PKATDKSFVEKVAQEQGSHPKFQRPRNlrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKd 636
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 637 vegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14888 549 -----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 28801584 717 VLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
115-784 |
1.26e-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: 1.26e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIvlkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 431
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNI---EFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 432 ADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 512 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQadFS 591
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNN--FG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 592 VLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMFRTVGQLYK 671
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRRPTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|...
gi 28801584 752 GFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
2.69e-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: 2.69e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 187
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 188 QSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQEREL-F 341
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDDATeF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 342 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNivLKKERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLTPRIK 417
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 418 VGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQLNSFE 487
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 488 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDKSFVE 566
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 567 KVAQEQ-GSHPKFQRPRNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleq 645
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 646 vsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 725
Cdd:cd14892 536 -----------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 726 QGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 784
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
115-784 |
7.75e-148 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 474.13 E-value: 7.75e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 185
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 186 EDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE-----------LERQLLQANPILEAFGNAKTVKNDN 254
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 255 SSRFGKFIRINFDI-AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNGPSS 332
Cdd:cd14907 161 SSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 333 SPGQER----ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAA-QKLCRLLGLGVTD 406
Cdd:cd14907 241 CYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 407 FSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIAGFE 479
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 480 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEECWFP 557
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 558 KATDKSFVEKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDV 637
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 638 EGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGV 717
Cdd:cd14907 557 DG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 718 LEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 784
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
117-784 |
3.88e-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: 3.88e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 192
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 193 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYI 272
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELFQETLESLR 349
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 350 VLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEmDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 429 KEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd14889 312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNl 584
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRS- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 rDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFR 664
Cdd:cd14889 466 -KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRKQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14889 545 SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL 624
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 28801584 745 --TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 784
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 ... |
116-744 |
3.94e-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: 3.94e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 181
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 182 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSP-KGRKEPGVPGE-LERQLLQANPILEAFGNAKTVKNDNSSR 257
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNlAASVSMGKSTSgIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 258 FGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngpssspgqe 337
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 338 RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAAQKL------CRLLGLGVTDFSRA 410
Cdd:cd14900 218 RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEKA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 411 LLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFEIFQLNSF 486
Cdd:cd14900 298 LSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVE 566
Cdd:cd14900 378 EQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 567 KVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDplndnvaaLLHQstdrltaeiwkdvegivglEQV 646
Cdd:cd14900 455 KLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ-------------------EAV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 647 SslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 726
Cdd:cd14900 508 D--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARA 572
|
650
....*....|....*...
gi 28801584 727 GFPNRILFQEFRQRYEIL 744
Cdd:cd14900 573 GFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
115-784 |
6.70e-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: 6.70e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAHVASspkGRKEPGVPgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQETLESLRV 350
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEEITAMLRTVSAVLQFGNIVLkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 431 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 511 QEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGSHPKFQRPRNLRDQ 587
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 588 adFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPRrgmfRTVG 667
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP----KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 747
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 28801584 748 AIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 784
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
115-784 |
6.89e-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: 6.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 187
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 188 QSILCTGESGAGKTENTKKVIQYLAH------------VASSPKGRKEPGVpgELERQLLQANPILEAFGNAKTVKNDNS 255
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 256 SRFGKFIRINFDIAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSS 333
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 334 PG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK----ERNTDQATMPDNTAAQKLCRLLGLGVTDFS 408
Cdd:cd14891 234 DNiDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 409 RALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSF 486
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDK 562
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 563 SFVEKVAQEQGSHPKFQRP--RNLRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegi 640
Cdd:cd14891 465 KLNETLHKTHKRHPCFPRPhpKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 641 vgleqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 720
Cdd:cd14891 528 ---------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 721 IRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14891 581 CEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
115-746 |
4.06e-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: 4.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 184
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 185 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPG-ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPGQER---- 338
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARKRAVadky 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 339 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTP 414
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 415 RIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFEIFQLNSF 486
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE 566
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 567 KVAQEQGShpkfqrprnlRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQV 646
Cdd:cd14902 478 KFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 647 SSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 723
Cdd:cd14902 539 DSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650 660
....*....|....*....|...
gi 28801584 724 CRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
115-784 |
4.17e-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: 4.17e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 274
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR--------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 352
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRDYVQKAQTK 429
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 430 EQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 508 VLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrDQ 587
Cdd:cd14896 390 AQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 588 ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrprrgmfrTVG 667
Cdd:cd14896 465 PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------------TLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpN 747
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-S 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 28801584 748 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
113-795 |
8.00e-126 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 417.51 E-value: 8.00e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 113 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 191
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 192 CTGESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMD----LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEEITAMLRTVSAVLQFGNI-VLKKERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVeIEGKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:PTZ00014 499 IVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RDQaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdgppggrprrg 661
Cdd:PTZ00014 576 SNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL--------------- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 662 mfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:PTZ00014 640 ----IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQF 715
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 742 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEER 795
Cdd:PTZ00014 716 KYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 184
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 185 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 261
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 262 IRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTNG--PS 331
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGgaPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 332 SSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQK----LCRLLGLGVTDF 407
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 408 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSF 486
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFV 565
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 566 EKV--------AQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLM-KNMDPLNdnvaallhqstdrLTAEIwkd 636
Cdd:cd14908 477 SRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTADS--- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 637 vegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14908 541 -------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 717 VLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL----YR 775
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQ 673
|
....*....
gi 28801584 776 VGQSKIFFR 784
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
115-780 |
6.80e-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: 6.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 192
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 193 TGESGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 271 YIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TNGPSSSP 334
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 335 GQEREL---FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQAT--MPDNTAA-QKLCRLLGLGVTDFS 408
Cdd:cd14906 241 NNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 409 RALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFLGILDIA 476
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 477 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWF 556
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 557 PKATDKSFVEKVAQEQGSHPKFQRpRNLrDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkd 636
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 637 vegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14906 549 ---KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 717 VLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 780
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
115-782 |
2.76e-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: 2.76e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMD----LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 352
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGN--IVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNvkITGKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 507 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRD 586
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 587 QaDFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrprrgmfrtV 666
Cdd:cd14876 469 I-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL----------------I 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14876 532 GSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL 611
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 747 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 782
Cdd:cd14876 612 GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
116-745 |
3.10e-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: 392.01 E-value: 3.10e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 183
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 184 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGElerQLLQANPILEAFGNAKTVKNDNSSR 257
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 258 FGKFIRINF-----DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNG- 329
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 330 --PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---------------QATMPDNTA 392
Cdd:cd14895 232 cyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 393 AQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR-----SPR 464
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalNPN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 465 QGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIEr 539
Cdd:cd14895 392 KAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 540 pANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD--FSVLHYAGKVDYKASEWLMKNMDPLNDN 617
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 618 VAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHE 697
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 28801584 698 KRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
115-784 |
7.91e-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: 7.91e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgelerqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEK--------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---FQETLESL 348
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaFSKLQAAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL------------LTPRI 416
Cdd:cd01386 231 KTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 417 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN---------SFE 487
Cdd:cd01386 311 QESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 488 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLALLDEECW 555
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 556 FPKATDKSFVEKV--AQEQGSHPKFQRPRNLRDQA-DFSVLHYAGK--VDYKASEWLMK-NMDPLNDNVAALLHQSTDRL 629
Cdd:cd01386 467 YPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 630 TAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--- 706
Cdd:cd01386 547 AAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStss 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 707 -----------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELD 770
Cdd:cd01386 596 paagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 28801584 771 PNLYRVGQSKIFFR 784
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
115-746 |
9.68e-112 |
|
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: 9.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 190
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 191 LCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELFQETLESLRV 350
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCFEVTREAMLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV--QK 425
Cdd:cd14880 238 LGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 505
Cdd:cd14880 318 PCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 506 MFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGSHPKFQRPRnL 584
Cdd:cd14880 398 YLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK-L 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrPRRGMFR 664
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG---------QSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
..
gi 28801584 745 TP 746
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 ... |
115-784 |
8.45e-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: 365.75 E-value: 8.45e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 188
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 189 SILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 268
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLE 346
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 347 SLRVLgLLPEEITAMLRTVSAVLQFGNIVLKKERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYV 423
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 424 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE----KVAQE-----Q 572
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSscksKIKNNsfipgK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 573 GShpkfqrprnlrdQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdg 652
Cdd:cd14886 466 GS------------QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMK------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 653 ppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd14886 527 ----------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYND 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 733 LFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14886 597 TFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
115-784 |
3.05e-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: 3.05e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 191
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 192 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKEpgVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 267
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQRS--IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 268 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPSSSPGQERE 339
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 340 LFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLtprIKVG 419
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 420 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQLCINYTNE 496
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 497 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQE-QGSH 575
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 576 PKFQRPRN-LRDQadFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgpp 654
Cdd:cd14875 470 PYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 655 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 734
Cdd:cd14875 539 ----------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 735 QEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 784
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
115-741 |
3.88e-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: 3.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 181
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---------LERQLLQANPILEAFGNAKTVKN 252
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 253 DNSSRFGKFIRINF-DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 326
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 327 TNGPSSSPG---QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL-----KKERNT--DQATMPDNTAA--- 393
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 394 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 463
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 464 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 537
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 538 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPL 614
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 615 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 692
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 28801584 693 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
116-748 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 195
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLA-HVASSPKgrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiaGYIVG 274
Cdd:cd14898 78 SGSGKTENAKLVIKYLVeRTASTTS----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLESLRVLGLL 354
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 355 peEITAMLRTVSAVLQFGNIVLKKERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 434
Cdd:cd14898 220 --NFKSIEDCLLGILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 435 ALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 514
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 515 QREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAqeqgshpKFQRpRNLRDQAD--FSV 592
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIK-------KYLN-GFINTKARdkIKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 593 LHYAGKVDYKASEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKE 672
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL-----------------VKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 673 SLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
115-784 |
5.76e-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: 327.76 E-value: 5.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 186
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 266
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 267 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqerelFQETLE 346
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD------------LRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 347 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA--------AQKLCRLL-------GLGVTDFSRAL 411
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 412 LT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR------- 464
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 465 ------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI---------PWTF-LD 525
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsafPFSFpLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 526 FGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQ--EQGSHPKFQRPRNL 584
Cdd:cd14887 463 STLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKniINSAKYKNITPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 585 RDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGGRPRRGMFR 664
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 28801584 745 TPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14887 687 LPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
112-783 |
1.03e-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: 1.03e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 112 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 181
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGK 260
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 261 FIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-----PSSSPG 335
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgchplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 336 QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI--VLKKERNTDqATMPDNTAA-QKLCRLLGLGVTDFsRALL 412
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 413 TPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEifQL---- 483
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--NRsstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 484 -NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC-WFPKATD 561
Cdd:cd14879 384 gNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 562 KSFVEKVAQEQGSHPKFQRPRNLRDQAD---FSVLHYAGKVDYKASEWLMKNMDPLndnvaallhqSTDRLTaeiwkdve 638
Cdd:cd14879 461 EQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 639 givgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVL 718
Cdd:cd14879 523 -----------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 719 EGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 783
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 191
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 192 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DIAG 270
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELFQETL---- 345
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLNREKLavlk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 502
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 503 NHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----FPKATdKSF 564
Cdd:cd14878 393 NEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnLPKKL-QSL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 565 VEKVAQEQGSHPKFQRPRN--LRDQ-ADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegiv 641
Cdd:cd14878 460 LESSNTNAVYSPMKDGNGNvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 642 gleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 721
Cdd:cd14878 534 -----SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 722 RICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
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 ... |
115-784 |
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 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG----PSSSPGQERELFQETLESLRV 350
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKnvviPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 351 LGLLPEeitaMLRTVSAVLQFGNIV---LKKERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14937 228 HDMKDD----LFLTLSGLLLLGNVEyqeIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 505
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 506 MFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlR 585
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--K 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 586 D-QADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppggRPRRGMF 663
Cdd:cd14937 457 DiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG------RKNLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 664 RtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEI 743
Cdd:cd14937 524 K-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEY 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 28801584 744 LTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 784
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 ... |
115-736 |
1.41e-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: 1.41e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 186
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 266
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-------ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 267 D---------IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL---------- 326
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 327 ----------TNGPSSSPGQEREL-FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKkerntdqatmpdntAAqk 395
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK--------------AA-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 396 lCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-----------DRSPR 464
Cdd:cd14884 298 -AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdnEDIYS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 465 QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDLIERpanpp 544
Cdd:cd14884 377 INEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 545 gLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGSH------PKFQRPRNLRDQAD---FSVLHYAGKVDYKASE 605
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADGTAKKQNIKkniFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 606 WLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRLMATLSNTN 685
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 686 PSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
116-783 |
2.88e-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: 255.81 E-value: 2.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 188
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 189 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDi 268
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQEREL-FQETL 345
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAArFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 346 ESLRVLGLlpeEITAMLRTVSAVLQFGNIVLKkERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14881 222 ACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQLCINYTNEK 497
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 498 LQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKVAQEQGSHP 576
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 577 KFQRPRNLRDQAdFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSSLGdgppgg 656
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCNFG------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 657 rprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14881 503 ------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 737 FRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 783
Cdd:cd14881 577 FNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
116-744 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 196 SGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--------GNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER----------ELFQE 343
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 344 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 423
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 424 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 502 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQGSHPKfqr 580
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 581 prnLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdgppggrprr 660
Cdd:cd14882 462 ---KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 661 gmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14882 521 ---RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
....*...
gi 28801584 737 FRQRYEIL 744
Cdd:cd14882 598 FLRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
116-784 |
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 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSK-----YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQETLESLRVLG 352
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAqtkeqa 432
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 433 dfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 513 EYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrdqaDFS 591
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPN-----KFG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 592 VLHYAGKVDYKASEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGMFRTVGQLYK 671
Cdd:cd14905 446 IEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 672 ESLS--RLMATLSNTNPS-----------------------------------------------FVRCIVPNHEKRAGK 702
Cdd:cd14905 513 SPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIKPNSKKTHLT 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 703 LEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALELDPNLYRVG 777
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVG 666
|
....*..
gi 28801584 778 QSKIFFR 784
Cdd:cd14905 667 NTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
115-749 |
7.01e-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: 7.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 193
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 194 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIV 273
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVT-------TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 274 GANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVL 351
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKVGrdyvqKA 426
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSEDG-----TT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 427 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14874 293 IDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 507 FVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlR 585
Cdd:cd14874 371 FHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-K 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 586 DQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggrprrgmfrt 665
Cdd:cd14874 448 ERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS------------------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 28801584 746 PNAI 749
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
118-742 |
2.35e-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: 229.09 E-value: 2.35e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 118 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 187
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 188 QSILCTGESGAGKTENTKKVIQYLAHVASS----PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSPGQER 338
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 339 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL------KKERNTDQATMPDNTAAqklCRLLGLGVTDFSRALL 412
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGGANSTTVSDAQS---CALKDPAQILLAAKLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 413 TPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQG----AS 468
Cdd:cd14893 321 EVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinSQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 469 FLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQPCIDLIER 539
Cdd:cd14893 401 GVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFED 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 540 PanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD------------FSVLHYAGKVDYKASEWL 607
Cdd:cd14893 481 K--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGLS 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 608 MKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYKESLS------- 675
Cdd:cd14893 559 SKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSARESKNitdsaat 630
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 676 -------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd14893 631 dvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
137-271 |
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 28801584 137 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 215
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28801584 216 SS--PKGRKEPGVP-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
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 ... |
116-782 |
1.02e-52 |
|
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: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 195 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPG-----------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFG 259
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEednihneentdYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 260 KFIRINFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNgpSSSPGQERE 339
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNN--EKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 340 LFQETLESLRVLGLL---PEEITAMLRTVSAVLQFGNI----------VLKKER----------------NTDQATMPDN 390
Cdd:cd14938 239 YSGKILELLKSLNYIfddDKEIDFIFSVLSALLLLGNTeivkafrkksLLMGKNqcgqninyetilseleNSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 391 TAAQKL-CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 467
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 468 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 547
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 548 ALLDEECwFPKATDKS-FVEKVAQEQGSHPKFQRPRN-LRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQS 625
Cdd:cd14938 477 SLLENVS-TKTIFDKSnLHSSIIRKFSRNSKYIKKDDiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 626 TDRLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNH 696
Cdd:cd14938 556 ENEYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 697 EKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYR 775
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 28801584 776 VGQSKIF 782
Cdd:cd14938 705 IGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1032-1684 |
8.65e-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: 8.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1032 EEKVKSLNKLRlkyeatisDMEDRLKKEEKGRQELEklkRRLDgessELQEQmVEQKQRAEELLAQLgrKEDELQAALLR 1111
Cdd:COG1196 172 ERKEEAERKLE--------ATEENLERLEDILGELE---RQLE----PLERQ-AEKAERYRELKEEL--KELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1112 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELedtldstnaqQELRSKREQevte 1191
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE----------YELLAELAR---- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1192 lkkalEEESRAHEvsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1271
Cdd:COG1196 300 -----LEQDIARL---EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1272 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1351
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1352 RALEAEAAGLREQMEEEvvARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1431
Cdd:COG1196 452 AELEEEEEALLELLAEL--LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1432 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdqlLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEA 1511
Cdd:COG1196 530 IGVEAAYEAALEAALAAALQNIVVEDDEVAAAA-----IEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1512 REELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQA--ASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH 1589
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLreVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1590 ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1669
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650
....*....|....*
gi 28801584 1670 LWREVEETRSSRDEM 1684
Cdd:COG1196 765 LERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
920-1529 |
1.18e-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: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 920 EETRARLAarkqELELVVTELEARVGEEEEcsrqlQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtteAKMKKFEED 999
Cdd:COG1196 182 EATEENLE----RLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRELE-----AELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1000 LLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQEL----EKLKRRLDg 1075
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELeerlEELEEELA- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1076 essELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1155
Cdd:COG1196 327 ---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1156 DLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEvsmqELRQRHSQALVEMAEQLEQARRGKGVW 1235
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA----ELEEEEEALLELLAELLEEAALLEAAL 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1236 EKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ--RAQAELESVSTALSEAE 1313
Cdd:COG1196 480 AELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1314 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1393
Cdd:COG1196 560 AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1394 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1473
Cdd:COG1196 640 VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1474 KAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA----LRAELEAL 1529
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERelerLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1147-1743 |
5.36e-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: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1147 RAKAEKQ----RRDLgEELEALRGELEDTLDSTnaqqelrsKREQEVTELKKALEEESRAHEVSMQELRQRHSQA-LVEM 1221
Cdd:COG1196 174 KEEAERKleatEENL-ERLEDILGELERQLEPL--------ERQAEKAERYRELKEELKELEAELLLLKLRELEAeLEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1222 AEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE 1301
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1302 LESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQS 1381
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1382 TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEK 1461
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1462 KQRKfdqllAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddVGKNVH 1541
Cdd:COG1196 485 ELAE-----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL-----QNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1542 ELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEE 1621
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1622 RKQRALAMAARKKLELELEELKAQT-SAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEmfTLSRENEKKLKGLEA 1700
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEA 712
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 28801584 1701 EVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEE 1743
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1395 |
5.50e-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: 5.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 867 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 946
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 947 EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLEERLAEFSS 1026
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE---ALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1027 QAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1106
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1107 AALLRAEEEGGARAQLLKSLREAQAGL-AEAQEDLEAERVARAKAEKQRRDLGEELEALR--GELEDTLDSTNAQQELRS 1183
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLeAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgvEAAYEAALEAALAAALQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 KREQEVTELKKALEE-----ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1258
Cdd:COG1196 551 IVVEDDEVAAAAIEYlkaakAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1259 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA----ESQLHDTQ 1334
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAllaeEEEERELA 710
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1335 ELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1395
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1613 |
2.74e-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: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 862 RQDEVLQARAQELQKVQELQQQ-SAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgr 1100
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 kedELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:TIGR02168 434 ---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1181 LRSKREQE------VTELKKALEEESRAHEVSMQELRQ----RHSQALVEMAEQLEQARRGKGVW----EKTRLSLEAEV 1246
Cdd:TIGR02168 511 LLKNQSGLsgilgvLSELISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTFlpldSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1247 SELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSA 1326
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTN 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1327 ESQLHDTQELlqEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEE 1405
Cdd:TIGR02168 670 SSILERRREI--EELEEKIEeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1406 ARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRE 1485
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1486 RIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELE 1565
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 28801584 1566 DELTAAEDAKLRLevtvQALKAQHERDLQGrddaGEERRRQLAKQLRD 1613
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 ... |
234-725 |
1.38e-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: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 234 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDIAGY---IVGANIETYLLEKSRAIRQA------KDECSFHIFYQ 302
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 303 LLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGLLPEEITAMLRTVS 366
Cdd:cd14894 329 MVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 367 AVLQFGNIVLKKERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALEALA 440
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 441 KATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQqlfnh 504
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 505 tmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQEQGS 574
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 575 HPKfQRPRNLRDQA----------DFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVG 642
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlGWSP 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 643 LEQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIR 722
Cdd:cd14894 717 NTNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 28801584 723 ICR 725
Cdd:cd14894 793 ICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1144-1943 |
1.87e-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: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1144 RVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKALEEeSRAHEVSMQ 1208
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1209 ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR 1288
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1289 SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEE 1368
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1369 VVARERAGRELQS-----TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELD 1443
Cdd:TIGR02168 413 EDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1444 DATVDLGQQKQL---LSTLEKKQRKFDQLL----------AEEKAAVLRAV-EDRERIEAEGREREARALS-LTRALEEE 1508
Cdd:TIGR02168 493 SLERLQENLEGFsegVKALLKNQSGLSGILgvlselisvdEGYEAAIEAALgGRLQAVVVENLNAAKKAIAfLKQNELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1509 QEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE----VTVQA 1584
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPgyriVTLDG 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1585 LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1664
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1665 VQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNlskaatlEEK 1744
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-------EAL 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1745 RQLEGRLsqleeeleeeqnnsELLKDHYRKLVLQVESLTTELSAersfsakAESGRQQLERQIQELRARLgEEDAGARAR 1824
Cdd:TIGR02168 806 DELRAEL--------------TLLNEEAANLRERLESLERRIAA-------TERRLEDLEEQIEELSEDI-ESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1825 QKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAee 1904
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL-- 941
|
810 820 830
....*....|....*....|....*....|....*....
gi 28801584 1905 easrAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02168 942 ----QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1285-1876 |
2.81e-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: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1285 ERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQ 1364
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1365 MEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDD 1444
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1445 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRA 1524
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1525 ELEALLSSKDDVGKnvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERR 1604
Cdd:COG1196 464 LLAELLEEAALLEA---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1605 RQLAKQLRDAEVERDEER--------KQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1676
Cdd:COG1196 541 EAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1677 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1756
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1757 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSfsakAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKL 1836
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAERE----ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 28801584 1837 AQ-------AEEQL-EQESRERILSGKL--VRRAEKRLKEVVLQVDEERR 1876
Cdd:COG1196 777 EAlgpvnllAIEEYeELEERYDFLSEQRedLEEARETLEEAIEEIDRETR 826
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1525 |
4.24e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.39 E-value: 4.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 870 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQElELVVTELEARVGEEE 948
Cdd:PTZ00121 1171 KAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 949 ECSRQLQSEKKRLQQHIQELESHLEAEEgARQKLQLEKvtteAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQA 1028
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1029 AEEEEKvkSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRldGESSELQEQmvEQKQRAEELL--AQLGRKEDELQ 1106
Cdd:PTZ00121 1324 AEEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKE--EAKKKADAAKkkAEEKKKADEAK 1397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1107 aallRAEEEGGARAQLLKSLREAQAGLAEAQEdlEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKRE 1186
Cdd:PTZ00121 1398 ----KKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1187 QEvtELKKALEEESRAHEVsmqelrQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE--LKAELSSLQTSRQEGE 1264
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADeaKKAEEAKKADEAKKAE 1543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1265 QKRRRLEsqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAK 1344
Cdd:PTZ00121 1544 EKKKADE--LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1345 LALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAE- 1423
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEa 1701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1424 -KTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRKFDQLLAEEkaavlravEDRERIEAEGREREARALSL 1501
Cdd:PTZ00121 1702 kKAEELKKKEAEEKKKAEELKKAeEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEEI 1773
|
650 660
....*....|....*....|....
gi 28801584 1502 TRALEEEQEAREELERQNRALRAE 1525
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
920-1732 |
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 28801584 920 EETRARLAARKQELELV---VTELEARVGeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteaKMKKF 996
Cdd:TIGR02168 175 KETERKLERTRENLDRLediLNELERQLK-----SLERQAEKAERYKELKAELRELELALLVLRLEELRE-----ELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 997 EEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrQELEKLKRRLDGE 1076
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1077 SSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1156
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1157 LGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALeEESRAHEVSMQelrqrhsqaLVEMAEQLEQarrgkgvwe 1236
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKL-EEAELKELQAE---------LEELEEELEE--------- 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1237 ktrlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserarseaAEKLQRAQAELESVSTALSEAESKA 1316
Cdd:TIGR02168 452 -----LQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-----------LDSLERLQENLEGFSEGVKALLKNQ 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1317 IRLGKELSSAESQLHDTQELlqeETRAKLALGSRVRAL----EAEAAGLREQMEEEVVAR-------ERAGRELQSTQAQ 1385
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGY---EAAIEAALGGRLQAVvvenLNAAKKAIAFLKQNELGRvtflpldSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1386 LSEWrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQEL-------------------DDAT 1446
Cdd:TIGR02168 593 ILKN---IEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsAKTN 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1447 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRaleeeqeareelerQNRALRAEL 1526
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR--------------QISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1527 EALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQH---ERDLQG-RDDAGEE 1602
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDElRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1603 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTS--AAGQGKEEAVKQLKKMQVQMKELWREVEETRSS 1680
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEieELEELIEELESELEALLNERASLEEALALLRSE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1681 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1732
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1388 |
1.58e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.85 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 841 KLRNWQWWRLFIKVKPLLQVTRQ-----------DEVLQA----------RAQELQKVQELQQQS--AREVGELQGRVaq 897
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaikaeearkaDELKKAeekkkadeakKAEEKKKADEAKKKAeeAKKADEAKKKA-- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 898 leEERTRLAEQLRAEAELCSEAEET-RARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 976
Cdd:PTZ00121 1325 --EEAKKKADAAKKKAEEAKKAAEAaKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEE 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 977 GARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRL 1056
Cdd:PTZ00121 1403 DKKKADELKK--AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK---KAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1057 KKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL-AQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAE 1135
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE----LKK 1553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1136 AQEDLEAERVARA----KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEvtELKKALEEESRAHEV-SMQEL 1210
Cdd:PTZ00121 1554 AEELKKAEEKKKAeeakKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELkKAEEE 1631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1211 RQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE 1290
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1291 A-----AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEaaGLREQM 1365
Cdd:PTZ00121 1712 AeekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEED 1789
|
570 580
....*....|....*....|...
gi 28801584 1366 EEEVVARERAGRELQSTQAQLSE 1388
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1495 |
7.73e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 107.53 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 862 RQDEVLQARAQELQKVQELQQ-QSAREVGELQGRVAQLEEERTRLAEQLRaEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKaEDARKAEEARKAEDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEEL 1193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 ----EARVGEE----EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--LLEDQNSKL 1010
Cdd:PTZ00121 1194 rkaeDARKAEAarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMahFARRQAAIK 1273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1011 SKERRLLEE-RLAEFSSQAAE--EEEKVKSLNKLRLKYEATisdmedrlKKEEKGRQELEKLKRRLDgessELQEQMVEQ 1087
Cdd:PTZ00121 1274 AEEARKADElKKAEEKKKADEakKAEEKKKADEAKKKAEEA--------KKADEAKKKAEEAKKKAD----AAKKKAEEA 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1088 KQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLK----SLREAQAGLAEAQED-LEAERVARAKAEKQRRD 1156
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEaaekkkEEAKKKADAAKkkaeEKKKADEAKKKAEEDkKKADELKKAAAAKKKAD 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1157 lgeelealrgELEDTLDSTNAQQELRSKREQ--EVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGV 1234
Cdd:PTZ00121 1422 ----------EAKKKAEEKKKADEAKKKAEEakKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1235 WEKTRlsLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-------EAAEKLQRAQaELESVST 1307
Cdd:PTZ00121 1492 AEEAK--KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEkkkadelKKAEELKKAE-EKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1308 ALSEAESK--AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ 1385
Cdd:PTZ00121 1569 AKKAEEDKnmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1386 LSEWRRRQEEEAAVLEAGEEARRRAAReaetltqrlaEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRK 1465
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDK----------KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK 1717
|
650 660 670
....*....|....*....|....*....|
gi 28801584 1466 FDQLLAEEKAAVLRAVEDRERIEAEGRERE 1495
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1496 |
1.64e-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: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 939 ELEARVgeeeecsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEedlllLEDQNSKLSKERRLLE 1018
Cdd:TIGR02168 383 TLRSKV-------AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1019 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdrlkkEEKGRQE-LEKLKRRLDGESSELQEQMVEQKQRAEEL--L 1095
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELA-----QLQARLDsLERLQENLEGFSEGVKALLKNQSGLSGILgvL 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1096 AQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAGLA-EAQEDLEAERVA-----RAKAEKQRRDLGEELEALRGELE 1169
Cdd:TIGR02168 526 SELISVDEGYEAAI---EAALGGRLQAVVVENLNAAKKAiAFLKQNELGRVTflpldSIKGTEIQGNDREILKNIEGFLG 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1170 --------------------------DTLDSTNAQQEL-------------------------------RSKREQEVTEL 1192
Cdd:TIGR02168 603 vakdlvkfdpklrkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEEL 682
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1193 KKALEE-ESRAHEVSMQelRQRHSQALVEMAEQLEQARRGKgvwektrLSLEAEVSELKAELSSLQTSRQEGEQKRRRLE 1271
Cdd:TIGR02168 683 EEKIEElEEKIAELEKA--LAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1272 SQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRV 1351
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1352 RALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL 1431
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1432 ERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVED-----RERIEAEGREREA 1496
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
863-1736 |
5.50e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.45 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQElelvvtelEA 942
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE--------DA 1139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 943 RVGEEeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERRLLEERLA 1022
Cdd:PTZ00121 1140 RKAEE---ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEE--LRKAEDARKAEAARKAEEERKA 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1023 EfSSQAAEEEEKVKSLNKLRlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM-VEQKQRAEELL-AQLGR 1100
Cdd:PTZ00121 1215 E-EARKAEDAKKAEAVKKAE---EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELKkAEEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 KEDEL-QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQ 1179
Cdd:PTZ00121 1291 KADEAkKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1180 ELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRlslEAEVSELKAELS-SLQ 1257
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKaEEDKKKADELKKAAAAKKKADEAKKKAEEKK---KADEAKKKAEEAkKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1258 TSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAirlgKELSSAESQLHDTQELL 1337
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE-------EAKKKA----DEAKKAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1338 QEEtRAKLALGSRvRALEAEAAGLREQMEEEVVARE-RAGREL-QSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAE 1415
Cdd:PTZ00121 1517 KAE-EAKKADEAK-KAEEAKKADEAKKAEEKKKADElKKAEELkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI 1594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1416 TLTQRLAEKTEAVERLERARRRLQ----QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEG 1491
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKKAEEAkikaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1492 REREAralslTRALEEEQEAREELERQNRALRAELEALlssKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAA 1571
Cdd:PTZ00121 1675 KKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEEL---KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1572 EDAKLRLEvtvQALKAQHERdlQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA--LAMAARKKLELELEELKAQTSAA 1649
Cdd:PTZ00121 1747 EEAKKDEE---EKKKIAHLK--KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNFANIIEGGKEGNLVI 1821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1650 GQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEE 1729
Cdd:PTZ00121 1822 NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
....*..
gi 28801584 1730 VASGNLS 1736
Cdd:PTZ00121 1902 IPNNNMA 1908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
877-1395 |
1.66e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.45 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 877 VQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEEECSRQLQS 956
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 957 EKKRLQQHIQELESHlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVK 1036
Cdd:PRK03918 267 RIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1037 SLNKLRLKYEAtisdMEDRLKKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQKQRAEEllaQLGRKEDELQAALLRAE 1113
Cdd:PRK03918 346 KLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1114 EEGGARAQLLKSLREAQAGL----AEAQEDLEAERVARAKAE-----KQRRDLGEELEALRGELEDTLDSTNAQQELRsk 1184
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEEKERKLRKELRELEKVLKKESELI-- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1185 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLE--------QARRGKGVwEKTRLSLEAEVSELKAELSSL 1256
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKgeikslkkELEKLEEL-KKKLAELEKKLDELEEELAEL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1257 QTS-RQEGEQKRRRLESQLQEVQGRSSDSERARSeAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQE 1335
Cdd:PRK03918 576 LKElEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1336 LLQEETRAKLAlgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEE 1395
Cdd:PRK03918 655 KYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
948-1743 |
2.13e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 102.53 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 948 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RRLLEERLAE 1023
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1024 FSSQA-----AEEEEKVKSLNKlrlkyeatisdMEDRLKKEEKGRQELEklkRRLDGESSELQEQMVEQKQRAEELlaql 1098
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRK-----------AEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEEA---- 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1099 grKEDELQAAllRAEEEggaraqllkSLREAQAGLAEAQEDLEAERVARAKAEKQRRdlgeelealRGELEDTLDSTNAQ 1178
Cdd:PTZ00121 1236 --KKDAEEAK--KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1179 QELRSKREQEVTELKKALEEESRAHEVSMQ-ELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSlEAEVSELKAELSSLQ 1257
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1258 TSrqEGEQKRRRLESQLQEVqgRSSDSERARSE----AAEKLQRAQAELESVSTALSEAESKaiRLGKELSSAESQLHDT 1333
Cdd:PTZ00121 1373 KE--EAKKKADAAKKKAEEK--KKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1334 QELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEaavleageearrraarE 1413
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK----------------K 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1414 AETLTQRLAEKTEAVERLERARRRLQQELDDAtvdlgqqkqllstleKKQRKFDQLlaeEKAAVLRAVEDRERIEAEGRE 1493
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKA---------------EEKKKADEL---KKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1494 REARALSLTRALeeeqeareelerqnralraELEALLSSKDDVGKNVHELERARKAaeqaasdlrtqvteleDELTAAED 1573
Cdd:PTZ00121 1573 EEDKNMALRKAE-------------------EAKKAEEARIEEVMKLYEEEKKMKA----------------EEAKKAEE 1617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1574 AKLRLEvtvQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVE---RDEERKQRALAMAARKKLELELEELKAQTSAAG 1650
Cdd:PTZ00121 1618 AKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1651 QGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1730
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
810
....*....|...
gi 28801584 1731 ASGNLSKAATLEE 1743
Cdd:PTZ00121 1771 EEIRKEKEAVIEE 1783
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1577 |
2.25e-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: 2.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 858 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 937
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 938 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLL 1017
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1018 EERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAE---EL 1094
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1095 LAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglAEAQEDLEAERVARA------KAEKQRRDLGEELEAlrGEL 1168
Cdd:TIGR02169 527 VAQLGSVGERYATAI---EVAAGNRLNNVVVEDDAVA--KEAIELLKRRKAGRAtflplnKMRDERRDLSILSED--GVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1169 EDTLDSTNAQQELRSKREQEV--TELKKALEEESRAhevsMQELRqrhsqaLVEMAEQLEQ--------ARRGKGVWEKT 1238
Cdd:TIGR02169 600 GFAVDLVEFDPKYEPAFKYVFgdTLVVEDIEAARRL----MGKYR------MVTLEGELFEksgamtggSRAPRGGILFS 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1239 RlSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIR 1318
Cdd:TIGR02169 670 R-SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1319 LGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAglREQMEEevvarerAGRELQSTQAQLSEWRRRQEEeaa 1398
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPE-------IQAELSKLEEEVSRIEARLRE--- 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1399 vleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVL 1478
Cdd:TIGR02169 817 ------------------IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1479 RAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERArKAAEQAASDLR 1558
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI-PEEELSLEDVQ 957
|
730
....*....|....*....
gi 28801584 1559 TQVTELEDELTAAEDAKLR 1577
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNML 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
866-1212 |
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 28801584 866 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARLAARKQELElvvtELEARVG 945
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLA----RLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 946 EEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1025
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1026 SQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEklkrrldGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1105
Cdd:TIGR02168 824 ERLESLERRIAAT-------ERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1106 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEEL-EALRGELEDTLDSTNAQQELRSK 1184
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEE 969
|
330 340
....*....|....*....|....*...
gi 28801584 1185 REQEVTELKKALEEESRAHEVSMQELRQ 1212
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEE 997
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
942-1824 |
1.53e-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: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 942 ARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteAKMKKFEEDLLLLED-QNSKLSKERRLLEER 1020
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREyEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqeleKLKRRLDGESSELQEQMveqkqraEELLAQLGR 1100
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEKI-------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAK-------AEKQRRDLGEELEALRGELedtld 1173
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKlteeyaeLKEELEDLRAELEEVDKEF----- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1174 stnaqQELRSKREQEVTELKKALEE--ESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKA 1251
Cdd:TIGR02169 381 -----AETRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1252 ELSSLQTSRQEGEQKRRRLESQLQEVqgrssdsERARSEAAEKLQRAQAELESVSTalSEAESKAIRlgKELSSAESQLH 1331
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRV-------EKELSKLQRELAEAEAQARASEE--RVRGGRAVE--EVLKASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1332 DT-QELLQEETRAKLALGSrvraleaeAAGLREQ---MEEEVVA--------RERAGR-------ELQSTQAQLSEWRRR 1392
Cdd:TIGR02169 525 GTvAQLGSVGERYATAIEV--------AAGNRLNnvvVEDDAVAkeaiellkRRKAGRatflplnKMRDERRDLSILSED 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1393 -------------QEEEAAVL----------EAGEEARRRAAREAETLTQRLAEKTEAV-------ERLERARRRLQQEL 1442
Cdd:TIGR02169 597 gvigfavdlvefdPKYEPAFKyvfgdtlvveDIEAARRLMGKYRMVTLEGELFEKSGAMtggsrapRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1443 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARAlsltraleeeqeareeleRQNRAL 1522
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE------------------EKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1523 RAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvQALKAQHERDLQGRDDAGEE 1602
Cdd:TIGR02169 739 LEELEEDLS----------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEE 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1603 RRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVeetrssrd 1682
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAL-------- 877
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1683 emftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQ 1762
Cdd:TIGR02169 878 ------RDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1763 NnsellkdhYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL---RARLGEEDAGARAR 1824
Cdd:TIGR02169 952 S--------LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELkekRAKLEEERKAILER 1008
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1194 |
4.59e-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: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 862 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELE 941
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 942 ARVGEEEECSRQLqsEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1021
Cdd:TIGR02169 772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1022 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1101
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1102 EDELqAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRrdlgEELEALRGELEDTLDSTNAQQEL 1181
Cdd:TIGR02169 930 EEEL-SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEY----EEVLKRLDELKEKRAKLEEERKA 1004
|
330
....*....|...
gi 28801584 1182 RSKREQEVTELKK 1194
Cdd:TIGR02169 1005 ILERIEEYEKKKR 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1388 |
4.96e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.81 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 936
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 937 VtELEARVGEEEECSRQLQSEKKRLQQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1013
Cdd:PRK03918 296 I-KLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1014 RRlLEERLAEFSSQAAEE-----EEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL--------DGESSEL 1080
Cdd:PRK03918 375 ER-LKKRLTGLTPEKLEKeleelEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1081 QEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKsLREAQAGLAEAQEDLEAERVARAKAE-KQRRDLGE 1159
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1160 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQALVEMAEQLEQARRGKGVWEKTR 1239
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL----KELEELGFESVEELEERLKELEPFYNEYLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1240 lSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEaaEKLQRAQAELESVSTALSEAESKAIRL 1319
Cdd:PRK03918 609 -DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEEL 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1320 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEaEAAGLREQMEE-EVVARERAGRELQSTQAQLSE 1388
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKyKALLKERALSKVGEIASEIFE 754
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
919-1302 |
8.27e-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: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 919 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL---QLEKVTTEAKMKK 995
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 996 FEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDG 1075
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1076 ESSELQEqmveqkqRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1155
Cdd:TIGR02168 818 EAANLRE-------RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1156 DLGEELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAhEVSMQELRQR---HSQALVEMAEQLEQARrgk 1232
Cdd:TIGR02168 891 LLRSELEELSEELRELE---SKRSELRRELEELREKLAQLELRLEGL-EVRIDNLQERlseEYSLTLEEAEALENKI--- 963
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1233 gvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARseaaEKLQRAQAEL 1302
Cdd:TIGR02168 964 ---EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAK----ETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1719 |
6.87e-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: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 887 EVGELQGRVAQLEEERTRLAEQLRAEAElcsEAEETRArLAARKQELElvVTELEARVGEEEECSRQLQSEKKRLQQHIQ 966
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRRERE---KAERYQA-LLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 967 ELESHLE--AEEGARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1044
Cdd:TIGR02169 255 KLTEEISelEKRLEEIEQLLEELNKKI-KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1045 YEATISDMEDRLKKEEKGR-----------QELEKLKRRLDGESSELQEQMVEQKQRAEEL------LAQLGRKEDELQA 1107
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRdklteeyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLeklkreINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1108 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE-RVARAKAEKQRRDLG---EELEALRGELEDTldstnaqQELRS 1183
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSkyeQELYDLKEEYDRV-------EKELS 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 KREQEVTELKKaleeesrahEVSMQELRQRHSQALVEMAEQLEQARRGK-----GVWEKTRLSLE-AEVSELKAELSSLQ 1257
Cdd:TIGR02169 487 KLQRELAEAEA---------QARASEERVRGGRAVEEVLKASIQGVHGTvaqlgSVGERYATAIEvAAGNRLNNVVVEDD 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1258 TSRQEGEQ--KRRRLESQ----LQEVQGRSSDSERARSEA----AEKLQRAQAELESV------STALSEAESKAIRLGK 1321
Cdd:TIGR02169 558 AVAKEAIEllKRRKAGRAtflpLNKMRDERRDLSILSEDGvigfAVDLVEFDPKYEPAfkyvfgDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1322 E--LSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAV 1399
Cdd:TIGR02169 638 KyrMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1400 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLR 1479
Cdd:TIGR02169 718 IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1480 AveDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRT 1559
Cdd:TIGR02169 798 A--ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1560 QVTELEDELTAAEDAKLRLEVTVQALkaqherdlqgrddagEERRRQLAKQLRDAEvERDEERKQRALAMAARKKLELEL 1639
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLREL---------------ERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEIEDP 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1640 EELKAQTSAAGQGKEEAVKQLKKMQVQMKELW-------REVEETRSSRDEMftlsrenEKKLKGLEAEVLRLQEELAAS 1712
Cdd:TIGR02169 940 KGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDEL-------KEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 28801584 1713 DRARRQA 1719
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1180-1957 |
7.23e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.42 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1180 ELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQAL--VEMAEQLEQARRGkgvwEKTRLSLEAEvselKAELSSLQ 1257
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkAEDARKAEEARKA----EDARKAEEAR----KAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1258 TSRQEGEQKRRRLESQLQEVQGRSSDSERARS-EAAEKLQRAqaelESVSTALSEAESKAIRLGKELSSAESQLHDTQEL 1336
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKA----EDARKAEAARKAEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1337 LQEETRAKlalgsrvrALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAET 1416
Cdd:PTZ00121 1231 KAEEAKKD--------AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKK 1302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1417 LTQRLAEKTEaverlerarrrLQQELDDATVDLGQQKQLLSTLEKKQRKfdqllAEEKAAVLRAVEDRERIEAEGREREA 1496
Cdd:PTZ00121 1303 KADEAKKKAE-----------EAKKADEAKKKAEEAKKKADAAKKKAEE-----AKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1497 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDlrtqvtelEDELTAAEDAKL 1576
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--------AEEKKKADEAKK 1438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1577 RLEVTVQA----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRAlamaarkkleLELEELKAQTSAAGQG 1652
Cdd:PTZ00121 1439 KAEEAKKAdeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA----------EEAKKKADEAKKAAEA 1508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1653 KEEAVKQLKKMQVQMKELWREVEETRSSRDemftLSRENEKKlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAS 1732
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1733 GNLSKAATLEEKRQLEgrlSQLEEELEEEQNNSELLKDHYRKLvlQVESLTTElSAERSFSAKAESGRQQLERQIQELRA 1812
Cdd:PTZ00121 1581 RKAEEAKKAEEARIEE---VMKLYEEEKKMKAEEAKKAEEAKI--KAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1813 RlgEEDAGARARQKMLIAALESKlaQAEEQLEQESRERILSGKLVRRAE--KRLKEVVLQVDEERRVADQVRDQLEKSNL 1890
Cdd:PTZ00121 1655 A--EEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKI 1730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1891 RLKQLKR----------QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1957
Cdd:PTZ00121 1731 KAEEAKKeaeedkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1164 |
8.18e-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: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 939 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1018
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1019 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1098
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1099 grkedelqaallraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVA-RAKAEKQRRDLGEELEAL 1164
Cdd:TIGR02168 939 ---------------------DNLQERLSEEYSLTLEEAEALENKIEDdEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-1943 |
1.84e-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: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1288 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAEsqlhDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQME 1366
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1367 EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1446
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1447 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1526
Cdd:TIGR02168 330 SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1527 EALLSSKDDVGKNVHELERARKAA------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERdLQ 1594
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAelkelqaeleelEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ-LQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1595 GRDDAGEERRRQ------------------------------------------LAKQLRDAEVERDEERKQ-------- 1624
Cdd:TIGR02168 489 ARLDSLERLQENlegfsegvkallknqsglsgilgvlselisvdegyeaaieaaLGGRLQAVVVENLNAAKKaiaflkqn 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1625 ---RALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKK---------------------------MQVQMKELWREV 1674
Cdd:TIGR02168 569 elgRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKfdpklrkalsyllggvlvvddldnaleLAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1675 EET------------RSSRDEMFTLSRENEkkLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLE 1742
Cdd:TIGR02168 649 TLDgdlvrpggvitgGSAKTNSSILERRRE--IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1743 EKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGAR 1822
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1823 ARQKMLiAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEerrvadqVRDQLEKSNLRLKQLKRQLEEA 1902
Cdd:TIGR02168 807 ELRAEL-TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEAL 878
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 28801584 1903 EEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
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 ... |
941-1876 |
7.65e-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: 7.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGR 1100
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 KEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1181 LRSKREQEVTELKKALEEEsrahevsMQELRQRHSQALVEMAEQleqarrgkgvwEKTRLSLEAEVSELKAELSSLQTSR 1260
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQL-------EDLLKEEKKEELEILEEE-----------EESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1261 QEGEQKRRRLESQLQEVQGRSSdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEe 1340
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKL-------QEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1341 tRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR 1420
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1421 LAEKTEAVERLERARRRLQQELDDATVDLGqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1500
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESA--KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1501 LTRALEEEQEAREELErqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam02463 690 AKEEILRRQLEIKKKE-----QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1581 TVQALKAQHERDlqgrddagEERRRQLAKQLRDAEVERDEERKQRALAMAarkkleleleelkaqtsaagqgKEEAVKQL 1660
Cdd:pfam02463 765 EKSELSLKEKEL--------AEEREKTEKLKVEEEKEEKLKAQEEELRAL----------------------EEELKEEA 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1661 KKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1740
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1741 LEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAErsfsAKAESGRQQLERQIQELRARLGEEdag 1820
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE----EADEKEKEENNKEEEEERNKRLLL--- 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1821 ararQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERR 1876
Cdd:pfam02463 968 ----AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1071-1850 |
8.95e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1071 RRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARAKA 1150
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEA-----------RKAEEAKKKAEDARKAEEARKAED 1138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1151 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR 1230
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK-----AEAARKAEEERK 1213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1231 GkgvwEKTRLSLEAEVSElkaELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERArsEAAEKLQRAQAELESVSTALS 1310
Cdd:PTZ00121 1214 A----EEARKAEDAKKAE---AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA--HFARRQAAIKAEEARKADELK 1284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1311 EAESKaiRLGKELSSAEsQLHDTQELLQEETRAKLALGSRVRALEA--EAAGLREQMEEEVVARERAGRELQSTQAQLSe 1388
Cdd:PTZ00121 1285 KAEEK--KKADEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAkkKADAAKKKAEEAKKAAEAAKAEAEAAADEAE- 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1389 wRRRQEEEAAVLEAGEEARRRAAREAETLTQRlaeKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRkfdq 1468
Cdd:PTZ00121 1361 -AAEEKAEAAEKKKEEAKKKADAAKKKAEEKK---KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKK---- 1432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1469 llAEEkaAVLRAVEDRERIEAEGREREAR-ALSLTRALEEEQEAREELERQNRALRAelEALLSSKDDVGKNVHELERAR 1547
Cdd:PTZ00121 1433 --ADE--AKKKAEEAKKADEAKKKAEEAKkAEEAKKKAEEAKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADEAKKAA 1506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1548 KAAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvqALKAQHERDLQGRDDAGEERRRQLAKQLRDAevERDEERKQRAL 1627
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKKKADELKKAEELKKAEEKKKAEEA--KKAEEDKNMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1628 AMA--ARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETRSSRDEMFTLSRENEKKlkgleAEVLRL 1705
Cdd:PTZ00121 1581 RKAeeAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL-KKAEEEKKKVEQLKKKEAEEKKK-----AEELKK 1654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1706 QEElaasDRARRQAQQDRDEMAEEVASGNLSKAAtlEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKlvlqVESLTTE 1785
Cdd:PTZ00121 1655 AEE----ENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK----AEELKKA 1724
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1786 LSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALE---SKLAQAEEQLEQESRER 1850
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEirkEKEAVIEEELDEEDEKR 1792
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
890-1488 |
3.27e-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: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 890 ELQGRVAQLEEERTRLaEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELE 969
Cdd:COG4913 239 RAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEL--EELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 970 SHLEAEEGARQKLQlekvttEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAeeeekvkslnKLRLKYEATI 1049
Cdd:COG4913 316 ARLDALREELDELE------AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLA----------ALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1050 SDMEDRlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRA----EEEGGARAQLLKS 1125
Cdd:COG4913 380 EEFAAL-------RAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1126 LREAQAGL---AEAQEDLEAERVARAKAEK----QRRDL----GEELEALRgeledTLDSTNAQQELRSKR--EQEVTEL 1192
Cdd:COG4913 453 LGLDEAELpfvGELIEVRPEEERWRGAIERvlggFALTLlvppEHYAAALR-----WVNRLHLRGRLVYERvrTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1193 KKALEEESRAHEVS----------MQELRQRHSQALVEMAEQLEQARRG----------KGVWEK--------------- 1237
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphpfrawlEAELGRRFDYVCVDSPEELRRHPRAitragqvkgnGTRHEKddrrrirsryvlgfd 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1238 --TRL-SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRS--SDSERARSEAAEKLQRAQAELESVSTALSEa 1312
Cdd:COG4913 608 nrAKLaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAELEAELERLDASSDD- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1313 eskairlgkeLSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1392
Cdd:COG4913 687 ----------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1393 QEEEAAVLEAGEEARRRAAREAETLTQRLAEK-TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLE-----KKQRKF 1466
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEedglpEYEERF 836
|
650 660 670
....*....|....*....|....*....|.
gi 28801584 1467 DQLLAE----EKAAVLRAVED-----RERIE 1488
Cdd:COG4913 837 KELLNEnsieFVADLLSKLRRaireiKERID 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
924-1396 |
7.55e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 924 ARLAAR--KQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1001
Cdd:PRK02224 174 ARLGVErvLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1002 LLEDqnskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQ 1081
Cdd:PRK02224 252 ELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1082 EQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggaraqllksLREAQaglAEAQEDLEAERVARAKAEKQRRDLGEEL 1161
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEE-----------LREEA---AELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1162 EALRGELEDTLDSTNAQQELRskreQEVTELKKALEEESRAHEVSMQELRQRhsqalVEMAEQLEQARR----GKGVWEK 1237
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFL----EELREERDELREREAELEATLRTARER-----VEEAEALLEAGKcpecGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1238 TRLSL----EAEVSELKAELSSLQTSRQEGEQKRRRLESqLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAE 1313
Cdd:PRK02224 465 PHVETieedRERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1314 SKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLrEQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1393
Cdd:PRK02224 544 ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELN 622
|
...
gi 28801584 1394 EEE 1396
Cdd:PRK02224 623 DER 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1487-1930 |
1.27e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1487 IEAEGREREARALSLTRALEEEQEAREELERQnrALRAELEALLSskddvgknvhELERARKAAEQAASDLRTQVTELED 1566
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELE--ELEAELEELEA----------ELAELEAELEELRLELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1567 ELTAAEDAKLRLEVTVQALKAQHER--DLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKA 1644
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1645 QTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRD 1724
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1725 EMAEEVAsgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLE 1804
Cdd:COG1196 446 EAAEEEA--ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1805 RQIQELRARLGEEDAGAR----ARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQ 1880
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 28801584 1881 VRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESM 1930
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1220-1937 |
1.76e-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: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1220 EMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEqKRRRLESQLQEVQG-----RSSDSERARSEAAEK 1294
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1295 LQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARE 1373
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1374 RAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQK 1453
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1454 QLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSK 1533
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1534 DDVGKNVHELERARKAAEQAASDLRTQVTELEDEL-----TAAEDAKLRlEVTVQALKAQHERDLQG---RDDAGEERRR 1605
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgTVAQLGSVG-ERYATAIEVAAGNRLNNvvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1606 QLAKQLRDAEVE-------RDEERKQRALAM-----------------------------------AARKKLEL------ 1637
Cdd:TIGR02169 565 ELLKRRKAGRATflplnkmRDERRDLSILSEdgvigfavdlvefdpkyepafkyvfgdtlvvedieAARRLMGKyrmvtl 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1638 ---------------ELEELKAQTSAAGQGKEEAVK-QLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAE 1701
Cdd:TIGR02169 645 egelfeksgamtggsRAPRGGILFSRSEPAELQRLReRLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1702 VLRLQEELAAS--------------DRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSel 1767
Cdd:TIGR02169 725 IEQLEQEEEKLkerleeleedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSK-- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1768 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEdagaRARQKMLIAALESKLAQAEeqlEQES 1847
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI----EKEIENLNGKKEELEEELE---ELEA 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1848 RERILSGKLVRRAEKRlKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRE------LE 1921
Cdd:TIGR02169 876 ALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeelsLE 954
|
810
....*....|....*.
gi 28801584 1922 DVTESAESMNREVTTL 1937
Cdd:TIGR02169 955 DVQAELQRVEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1062-1872 |
2.01e-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: 76.31 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1062 GRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKslREAQAglaeaQEDLE 1141
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRR--RESQS-----QEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1142 aervarakaeKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKALeeesRAHEVSMQELRQrhsqALVEm 1221
Cdd:pfam15921 145 ----------NQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMM----LSHEGVLQEIRS----ILVD- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1222 aeqLEQARrGKGVWEKTRLSlEAEVSELKAELSSLQtsrqegeqkrRRLESQLQEVQGR----SSDSERARSEAAEK--- 1294
Cdd:pfam15921 196 ---FEEAS-GKKIYEHDSMS-TMHFRSLGSAISKIL----------RELDTEISYLKGRifpvEDQLEALKSESQNKiel 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1295 -LQRAQAELESVstaLSEAESKAIRLGKELSSAESQLHDTQ---ELLQEETRAKLALGSR-VRALEAEAAGLREQMEEEV 1369
Cdd:pfam15921 261 lLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1370 VARERAGRELqstqaqlsewrrrqeEEAAVLEAGEearrraareaetLTQRLAEKTEAVERLERARRRLQQELddatVDL 1449
Cdd:pfam15921 338 RMYEDKIEEL---------------EKQLVLANSE------------LTEARTERDQFSQESGNLDDQLQKLL----ADL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1450 GQQKQLLStLEKKQRK--FDQLLAEEKAA--VLRAVEDR----ERIEAEGREREARALSLTRALEEEQEAREELERQNRA 1521
Cdd:pfam15921 387 HKREKELS-LEKEQNKrlWDRDTGNSITIdhLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1522 LRAELEallSSKDDVGKNVHELERAR---KAAEQAASDLRTQVTELED--ELTAAEDAKLRLEVTVQALKAQHerdLQGR 1596
Cdd:pfam15921 466 LTAQLE---STKEMLRKVVEELTAKKmtlESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELQH---LKNE 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1597 DDageerrrqlakQLRDAEVERDEERKQRAlamAARKKLELELEELKAQTSAAGQGKEEAvkqlKKMQVQMKELWREVEE 1676
Cdd:pfam15921 540 GD-----------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQLVGQHGRTA----GAMQVEKAQLEKEIND 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1677 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEEL-----AASDRAR--RQAQQDRDEMAEEVASGNLSKAATLEEKRQLEG 1749
Cdd:pfam15921 602 RRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnAGSERLRavKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKR 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1750 RLSQLEEEleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRARLG------- 1815
Cdd:pfam15921 682 NFRNKSEE----------METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDalqskiq 751
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1816 --EEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVD 1872
Cdd:pfam15921 752 flEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
925-1557 |
2.63e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.49 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 925 RLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ---HIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdll 1001
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrEINEISSELPELREELEKLEKEVKELEELKEEIEE--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1002 lLEDQNSKLSKERRLLEERLAEFSSQAAEE-------EEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRRLD 1074
Cdd:PRK03918 243 -LEKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1075 GESSELQEQMVEQKQRAEELlAQLGRKEDELQAALLRAEEeggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKqr 1154
Cdd:PRK03918 321 EEINGIEERIKELEEKEERL-EELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKLEKEL-- 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1155 rdlgEELEALRGELEDTLDSTNAQqelRSKREQEVTELKKALEEESRAHE---VSMQELRQRHSQALveMAEQLEQARRg 1231
Cdd:PRK03918 394 ----EELEKAKEEIEEEISKITAR---IGELKKEIKELKKAIEELKKAKGkcpVCGRELTEEHRKEL--LEEYTAELKR- 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1232 kgvWEKTRLSLEAEVSELKAELSSLQTSRqEGEQKRRRLESQLQEVQgrsSDSERARSEAAEKLQRAQAELESVstalse 1311
Cdd:PRK03918 464 ---IEKELKEIEEKERKLRKELRELEKVL-KKESELIKLKELAEQLK---ELEEKLKKYNLEELEKKAEEYEKL------ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1312 aESKAIRLGKELSSAESQLHDTQELLQEetraKLALGSRVRALEAEAAGLREQMEEEVVARERagrELQSTQAQLSEWRR 1391
Cdd:PRK03918 531 -KEKLIKLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKELEELGFESVE---ELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1392 RQEEeaavleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLgqqKQLLSTLEKKQRKFDQlla 1471
Cdd:PRK03918 603 EYLE------------------LKDAEKELEREEKELKKLEEELDKAFEELAETEKRL---EELRKELEELEKKYSE--- 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1472 eekaavlravEDRERIEAEGREREaRALSltraleeeqeareelerqnrALRAELEALLSSKDDVGKNVHELERARKAAE 1551
Cdd:PRK03918 659 ----------EEYEELREEYLELS-RELA--------------------GLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
....*.
gi 28801584 1552 QAASDL 1557
Cdd:PRK03918 708 KAKKEL 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
859-1472 |
3.34e-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: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------TRLAEQLRAEAELCSEAEETRARLAAR 929
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 930 KQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIqelESHLEAEEGARQKLQLEKVTTEAK-MKKFEEDLLLLEDQ-- 1006
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQhIHTLQQQKTTLTQKlq 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1007 --NSKLSKERRLLEERLAEFSSQAAEEEEKV--KSLNKLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRLDGESSELQ 1081
Cdd:TIGR00618 397 slCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1082 --EQMVEQKQRAEELLAQLGRKEDELQ----------AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE------ 1143
Cdd:TIGR00618 477 tkEQIHLQETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQltserk 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1144 RVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMA 1222
Cdd:TIGR00618 557 QRASLKEQMQEiQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1223 EQLEQARrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAEL 1302
Cdd:TIGR00618 637 CSQELAL------KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1303 ESVSTA---LSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLalgsrvraleAEAAGLREQMEEEVVARERAGREL 1379
Cdd:TIGR00618 711 THIEEYdreFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVL----------KARTEAHFNNNEEVTAALQTGAEL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1380 QSTQAQLSEWRRRQEE---EAAVLEAGEEARRRAAREAETLTQ-RLAEKTEAVERLERARRRLQQELDDATVDLGQQKQL 1455
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthLLKTLEAEIGQEIPSDEDILNLQCeTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
650
....*....|....*..
gi 28801584 1456 LSTLEKKQRKFDQLLAE 1472
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDK 877
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1238-1933 |
3.72e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.56 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1238 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQ--GRSSDSERARSEAAEKLQRAQAELESVSTALSEAESK 1315
Cdd:PTZ00121 1058 GKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGkaEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1316 AIRLGKELSSAESQLHDTQELLQEETRaklalgsrvRALEAEAAGLREQMEEEVVARE--RAGRELQSTQAQLSEWRRRQ 1393
Cdd:PTZ00121 1138 DARKAEEARKAEDAKRVEIARKAEDAR---------KAEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKA 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1394 EEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEE 1473
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1474 --KAAVLRAVEDRERI-EAEGREREARalsltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAA 1550
Cdd:PTZ00121 1289 kkKADEAKKAEEKKKAdEAKKKAEEAK--------------------------------------------KADEAKKKA 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1551 EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMA 1630
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1631 ARKKLELELEELKAQTSAAGQGKEEAVK--QLKKMQVQMK---ELWREVEETRSSRDemftLSRENEKKLKGLEAEvlRL 1705
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKadEAKKKAEEAKkadEAKKKAEEAKKAEE----AKKKAEEAKKADEAK--KK 1478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1706 QEELAASDRARRQAQQDRDEmAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1785
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKK-ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1786 LSAERSfsAKAESGRQQLERQIQELRaRLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAE--KR 1863
Cdd:PTZ00121 1558 KKAEEK--KKAEEAKKAEEDKNMALR-KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEekKK 1634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1864 LKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAqagrrrlQRELEDVTESAESMNRE 1933
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA-------KKAEEDEKKAAEALKKE 1697
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1138-1628 |
3.77e-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: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1138 EDLEAERVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQQELRSK-----REQEVTELKKALEEESRAHEVSMQELRQ 1212
Cdd:COG4913 235 DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1213 RHSQ--ALVEMAEQLEQARRGKGVwektrlsleAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSE----R 1286
Cdd:COG4913 314 LEARldALREELDELEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAeefaA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1287 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeetraklALGSRVRALEAEAAGLREQME 1366
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA--------------SLERRKSNIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1367 EEVVARERAGR---ELQSTQAQLSEWRR---------------RQEEEAAVL-----------------EAGEEARRRAA 1411
Cdd:COG4913 451 EALGLDEAELPfvgELIEVRPEEERWRGaiervlggfaltllvPPEHYAAALrwvnrlhlrgrlvyervRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1412 REAETLTQRLAEKTEAVERLERARRRLQ---------QELDDA----TVDlGQQKQLLSTLEKKQRK------------- 1465
Cdd:COG4913 531 LDPDSLAGKLDFKPHPFRAWLEAELGRRfdyvcvdspEELRRHpraiTRA-GQVKGNGTRHEKDDRRrirsryvlgfdnr 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1466 -----FDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--ALRAELEALLSSKDDVGk 1538
Cdd:COG4913 610 aklaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLDASSDDLA- 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1539 nvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDlqgRDDAGEERRRQLAKQLRDAEVER 1618
Cdd:COG4913 689 ---ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALLEERFAAALGDA 762
|
570
....*....|
gi 28801584 1619 DEERKQRALA 1628
Cdd:COG4913 763 VERELRENLE 772
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
872-1388 |
8.77e-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: 73.60 E-value: 8.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 872 QELQKVQELQQQSAREVGELQGRVAQL------------------EEERTR---LAEQLRAEAELCSEAEETRARLAark 930
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLliqitekenkmkdltfllEESRDKanqLEEKTKLQDENLKELIEKKDHLT--- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKL 1010
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1011 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDG-------ES 1077
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFllqarekEI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1078 SELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG-------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1150
Cdd:pfam05483 453 HDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAhcdklllENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1151 EKQRRDLGE-------ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR--HSQALVEM 1221
Cdd:pfam05483 533 LKQIENLEEkemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKNIEE 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1222 AEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS--------LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAA 1292
Cdd:pfam05483 613 LHQENKALKKKGSAENKQLNAyEIKVNKLELELASakqkfeeiIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1293 EKLQRAQAELESVSTALSEAESKAIRLGKELSSaESQLHDTQEllQEETRAKLALGSRVRALEAEAAGLREQMEEEVVAR 1372
Cdd:pfam05483 693 EIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEK 769
|
570
....*....|....*.
gi 28801584 1373 ERAGRELQSTQAQLSE 1388
Cdd:pfam05483 770 EKLKMEAKENTAILKD 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
865-1387 |
2.89e-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: 72.16 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 865 EVLQARAQELQKVQELQQQSAR------EVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarkqeLELVVT 938
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA--------LQTVIE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 939 ELEARVGEEEECSRQLQSEKKRL-----------QQHIQELE---SHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1004
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1005 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNkLRLKYEATIsdmedrLKKEEKGRQELEKLKRRLDGESSELQeQM 1084
Cdd:pfam10174 317 NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALR-LRLEEKESF------LNKKTKQLQDLTEEKSTLAGEIRDLK-DM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1085 VEQKQRA--------EELLAQLGRKE---DELQAALLRAEEEGGARAQLLKSLREAqagLAEAQEDLEAERVARAKAEKQ 1153
Cdd:pfam10174 389 LDVKERKinvlqkkiENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDTALTTLEEA---LSEKERIIERLKEQREREDRE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1154 RRdlgEELEALRGELEDTLDSTNAQQELRSKREQEVTELKkaleEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKG 1233
Cdd:pfam10174 466 RL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1234 VWEKTRLSleAEVSELKAELSSlqtsrqegeqKRRRLEsqlQEVQGRSSDSERARSEAA---EKLQRAQAELESVSTALS 1310
Cdd:pfam10174 539 QLKKAHNA--EEAVRTNPEIND----------RIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIA 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1311 EAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLS 1387
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1278 |
3.60e-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: 3.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 853 KVKPLLQVTRQDEVLQARAQELQ-KVQELQQQSAREV-GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1010
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1011 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEkgrQELEKLKRRLDGESSELqEQMVEQKQR 1090
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKEL-KKLNEEKKE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1091 AEELLAQLGRKEDELQaallraeeeggaraqllkslreaqaglaEAQEDLEAERvarAKAEKQRRDLGEELEalrgELED 1170
Cdd:TIGR04523 508 LEEKVKDLTKKISSLK----------------------------EKIEKLESEK---KEKESKISDLEDELN----KDDF 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1171 TLDSTNAQQELRSKrEQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQarrgkgvWEKTRLSLEAEVSELK 1250
Cdd:TIGR04523 553 ELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQE-EKQELIDQKEKEKKDLIKEIEE-------KEKKISSLEKELEKAK 623
|
410 420
....*....|....*....|....*...
gi 28801584 1251 AELSSLQTSRQEGEQKRRRLESQLQEVQ 1278
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
867-1228 |
8.33e-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: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 867 LQARAQELQKVQELQQQsarevgelQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 946
Cdd:COG3096 329 YQAASDHLNLVQTALRQ--------QEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 947 EEECSRQLQSEKKRLQQHIQELEShleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERRLLEERLAEFSS 1026
Cdd:COG3096 401 YQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVADA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1027 QAAEEEEKVKSLNKlrlkyeatISDMEDRLKKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQKQRAEELLAQL 1098
Cdd:COG3096 470 ARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEEF 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1099 GRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:COG3096 542 CQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEA 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1172 LDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQA 1228
Cdd:COG3096 622 LADS-----------QEVTAAMQQLLEREREATVERDELAAR-KQALESQIERLSQP 666
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-1276 |
9.23e-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: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 788 LAQLEEERdlkvtdiivsfqaaargylarrafqrrqqqqsalrvmqrncaaylklrnwqwwrlfikvkpLLQVTRQDEVL 867
Cdd:COG1196 360 LAEAEEAL-------------------------------------------------------------LEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 868 QARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEE 947
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 948 EECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQ 1027
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1028 AAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQE---LEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1104
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1105 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDtldstnAQQELRSK 1184
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE------LAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1185 REQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELsslqtSRQEGE 1264
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP-----DLEELE 766
|
490
....*....|..
gi 28801584 1265 QKRRRLESQLQE 1276
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
895-1929 |
1.10e-11 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 70.63 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 895 VAQLEEERTRLAEQLRAEAELCSEAEEtraRLAARKQELELVVTELEARVGEE--------EECSRQLQSEKKRLQQHIQ 966
Cdd:NF041483 246 AAESDQARRQAAELSRAAEQRMQEAEE---ALREARAEAEKVVAEAKEAAAKQlasaesanEQRTRTAKEEIARLVGEAT 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 967 ELESHLEAEEG---ARQKLQLEKVTTEAKMKKfeeDLLLLEDQNSKLSKERRLLEERLAEFSSQA-------AEEEEKVK 1036
Cdd:NF041483 323 KEAEALKAEAEqalADARAEAEKLVAEAAEKA---RTVAAEDTAAQLAKAARTAEEVLTKASEDAkattraaAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1037 SLNKL---RLKYEAtiSDMEDRLK-------KEEKGRQ-ELEKLKRRLDGESSELQEQMVEQKQRaeellaqlgrkedel 1105
Cdd:NF041483 400 REAEAeadRLRGEA--ADQAEQLKgaakddtKEYRAKTvELQEEARRLRGEAEQLRAEAVAEGER--------------- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1106 qaalLRAEEEGGARAQLLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRS 1183
Cdd:NF041483 463 ----IRGEARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 KREQEVTELKKALEEESRahevsmqELRqrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEvSELKAELSSLQTSRQEG 1263
Cdd:NF041483 539 EAEEQAEEVRAAAERAAR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1264 EQKRRRlesqlqevqgRSSDSERARSEAAEKLQ--RAQAELES----------VSTALSEAESKAIRLGKELSSAESQLH 1331
Cdd:NF041483 603 ERIRRE----------AAEETERLRTEAAERIRtlQAQAEQEAerlrteaaadASAARAEGENVAVRLRSEAAAEAERLK 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1332 DTQELLQEETRAKLALGSRVRALEAeAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAA 1411
Cdd:NF041483 673 SEAQESADRVRAEAAAAAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLASARKRVEEA 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1412 ReaeTLTQRLAEKTEA-VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAV 1477
Cdd:NF041483 752 Q---AEAQRLVEEADRrATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAER 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1478 LRAVEDRERIEAEGREREARALSLtraleeeqeareelerqnralraeleallsSKDDVGKNVHELERARKAAEQAASDL 1557
Cdd:NF041483 829 ERASEDANRLRREAQEETEAAKAL------------------------------AERTVSEAIAEAERLRSDASEYAQRV 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1558 RTqvtELEDELTAAEDAKLRLEVtvqalkaqherdlQGRDDAgeERRRQLAKQLRDAEVERDEERKQRALAMAARKKLEL 1637
Cdd:NF041483 879 RT---EASDTLASAEQDAARTRA-------------DAREDA--NRIRSDAAAQADRLIGEATSEAERLTAEARAEAERL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1638 ELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSR-ENEKKLKGLEAEVLRLQEELAAS---- 1712
Cdd:NF041483 941 RDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRtEAERVKAEAAAEAERLRTEAREEadrt 1020
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1713 -DRARRQAQQDRDEMAEEV---ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----------KLVLQ 1778
Cdd:NF041483 1021 lDEARKDANKRRSEAAEQAdtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERivaeatvegnSLVEK 1100
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1779 VESLTTEL--SAERSFSA---KAESGRQQLERQIQELRARLGEEDA----GARARQKMLIAALESKLAQAEEQLEQ---- 1845
Cdd:NF041483 1101 ARTDADELlvGARRDATAireRAEELRDRITGEIEELHERARRESAeqmkSAGERCDALVKAAEEQLAEAEAKAKElvsd 1180
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1846 ----ESRERILSgklVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL-KQLKRQLEEAEEEASRAQAGRRRLQrel 1920
Cdd:NF041483 1181 anseASKVRIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQ--- 1254
|
....*....
gi 28801584 1921 eDVTESAES 1929
Cdd:NF041483 1255 -DVLEALES 1262
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
859-1275 |
1.80e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.41 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAeAELCSEAEETRARLA----------A 928
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-LPLYQELEALEAELAelperleeleE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 929 RKQELELVVTELEARVGEEEECSRQLQSEKKRL----QQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1004
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1005 DQNSKLSKERRLLEER--------LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEE----KGRQELEKLKRR 1072
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKaslgKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1073 LDGESSELQEQMVEQ---KQRAEELLAQLGRKEDELQAALLRAEEEgGARAQLLKSLREAQAGLAEAQEDLEAERVARAK 1149
Cdd:COG4717 314 EELEEEELEELLAALglpPDLSPEELLELLDRIEELQELLREAEEL-EEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1150 AEKQRRDLGEELEALRGELEdtldstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE---QLE 1226
Cdd:COG4717 393 QAEEYQELKEELEELEEQLE---------ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAEleaELE 463
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1227 QARRGKGVWEKT--RLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQ 1275
Cdd:COG4717 464 QLEEDGELAELLqeLEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1118-1330 |
3.26e-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: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1118 ARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALE 1197
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1198 EESRA---HEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQL 1274
Cdd:COG4942 101 AQKEElaeLLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1275 QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQL 1330
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 ... |
1261-1943 |
5.50e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.28 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1261 QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQrAQAELesvstaLSEAESKAIRLGKELSSAESQLHDTQELLQEE 1340
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETEL------CAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1341 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrRRQEEEAAVLEageearrraareaetltqr 1420
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI----KKLEEDILLLE------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1421 laektEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEekaavlraVEDRERIEAEGRErearals 1500
Cdd:pfam01576 145 -----DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--------LEERLKKEEKGRQ------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1501 ltraleeeqeareelerqnralraeleallsskddvgknvhELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam01576 205 -----------------------------------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1581 TVQALKAQHErDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQ------TSAAGQ--- 1651
Cdd:pfam01576 244 ELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldTTAAQQelr 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1652 -GKEEAVKQLKKMQVqmkelwrevEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1730
Cdd:pfam01576 323 sKREQEVTELKKALE---------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1731 ASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQEL 1810
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1811 RARLGEEdagarARQKMLIA----ALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLE 1886
Cdd:pfam01576 474 QELLQEE-----TRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1887 KSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
907-1392 |
7.76e-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: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 907 EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEEcsrQLQSEKKRLQQHIQELESHLEAeegARQKLQLEK 986
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQE---ERQETSAELNQLLRTLDDQWKE---KRDELNGEL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 987 VTTEAKMKKFEEDLLLLEDQNSKLSKER----RLLEERLAEFSSQAAEEEEKVKSL----NKLRLKYEATISDMEDRLKK 1058
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKALtgkhQDVTAKYNRRRSKIKEQNNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1059 EEKG-RQELEKLK----RRLDGESSELQEQmvEQKQRaEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSlREAQAGL 1133
Cdd:pfam12128 391 DIAGiKDKLAKIReardRQLAVAEDDLQAL--ESELR-EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1134 AEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRA--HEVSMQELR 1211
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTllHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1212 QRHSQALVEMAEQLEQARRGKGVWEKT----------RLSLE--------AEVSELKAELSSLQTSRQEGEQKRRRLESQ 1273
Cdd:pfam12128 547 WEQSIGKVISPELLHRTDLDPEVWDGSvggelnlygvKLDLKridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1274 L-------QEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL-GKELSSAESQL----HDTQELLQEET 1341
Cdd:pfam12128 627 LvqangelEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEAQLkqldKKHQAWLEEQK 706
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1342 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRE-LQSTQAQLSEWRRR 1392
Cdd:pfam12128 707 EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgAKAELKALETWYKR 758
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
857-1623 |
8.84e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 8.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEVLQARAQELQKVQELQQQSARE-VGELQGRVAQLEEERTRLAEQLRAEaelcSEAEETRarlaarKQELEL 935
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQEMQMERDAMADIRRRE----SQSQEDL------RNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 936 VVTELEArvgeeEECSRQLQSEKKRLQqhIQELESHLEAEEGARQKLQLEKVT-TEAKMKKFEE----DLLLLEDQNSKL 1010
Cdd:pfam15921 150 TVHELEA-----AKCLKEDMLEDSNTQ--IEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEhdsmSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1011 SKERRLLEERLAEFSSQAAEEEEKVKSL-----NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1085
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALksesqNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1086 EQKQRAEELLAQLGRKEDELQAALlraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:pfam15921 303 IIQEQARNQNSMYMRQLSDLESTV----------SQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1166 GELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQrhsqalvEMAEQLEQARRgkgvwektrlsLEAE 1245
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR-------ELDDRNMEVQR-----------LEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1246 VSELKAELSSlqtsrqegeqkrrRLESQLQEVQGRSsdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1325
Cdd:pfam15921 435 LKAMKSECQG-------------QMERQMAAIQGKN--------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1326 AESQLHDTQELLQEETRAklalgsrVRALEAEAAGLREQME---EEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLea 1402
Cdd:pfam15921 494 SERTVSDLTASLQEKERA-------IEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVI-- 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1403 geearRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAE---EKAAV-- 1477
Cdd:pfam15921 565 -----EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDlelEKVKLvn 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1478 -----LRAVED---------------RERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS-KDDV 1536
Cdd:pfam15921 640 agserLRAVKDikqerdqllnevktsRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlKSME 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1537 GKNVHELERARKAAEQAASDlRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRqLAKQLrdaEV 1616
Cdd:pfam15921 720 GSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNK-MAGEL---EV 794
|
....*..
gi 28801584 1617 ERDEERK 1623
Cdd:pfam15921 795 LRSQERR 801
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1058-1922 |
9.26e-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: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1058 KEEKGRQELEKLKRRLD------GESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaraqLLKSLREAQA 1131
Cdd:TIGR02169 171 KKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------LERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1132 GLAEAQEDLEaervaraKAEKQRRDLGEELEALRGELEDtldstnAQQELRSKREQEVTELKKALeeesraHEVSMQELR 1211
Cdd:TIGR02169 245 QLASLEEELE-------KLTEEISELEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKI------GELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1212 QRHSQALVEMAEQLEQARRGKGVWEKTRL-----SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSER 1286
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLlaeieELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1287 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1366
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1367 EEvvarERAGRELQSTQAQLSEWRRRQEEEAAVleageearrraareaetltqrlAEKTEAVERLERARRRLQQELDDAT 1446
Cdd:TIGR02169 466 KY----EQELYDLKEEYDRVEKELSKLQRELAE----------------------AEAQARASEERVRGGRAVEEVLKAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1447 VD--LGQQKQLLSTLEKKQrkfdqlLAEEKAAVLRA----VED----RERIEAEGREREARALSLTRALEEEQEAREELE 1516
Cdd:TIGR02169 520 IQgvHGTVAQLGSVGERYA------TAIEVAAGNRLnnvvVEDdavaKEAIELLKRRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1517 RQNRALRAELEalLSSKDDVGKN-----------VHELERARKAAEQA-ASDLRTQVTELEDELTAAEDAKLRLEVTVQA 1584
Cdd:TIGR02169 594 SEDGVIGFAVD--LVEFDPKYEPafkyvfgdtlvVEDIEAARRLMGKYrMVTLEGELFEKSGAMTGGSRAPRGGILFSRS 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1585 LKAQHERdLQGRDDAGEERRRQLAKQLRDAEVERDEerkqralAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1664
Cdd:TIGR02169 672 EPAELQR-LRERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1665 VQMKELWREVEETRSSRDEmftlsreNEKKLKGLEAEVLRLQEELAA-----SDRARRQAQQDRDEMAEEVASGNLSKAA 1739
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKE-------LEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1740 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHyrklvlqveslttelsaersfsakaesgRQQLERQIQELRARLGEEDA 1819
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ----------------------------IKSIEKEIENLNGKKEELEE 868
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1820 gararqkmLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQL 1899
Cdd:TIGR02169 869 --------ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
890 900
....*....|....*....|....*....
gi 28801584 1900 EEAEEEAS------RAQAGRRRLQRELED 1922
Cdd:TIGR02169 941 GEDEEIPEeelsleDVQAELQRVEEEIRA 969
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
870-1181 |
1.35e-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: 66.69 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 870 RAQELQKVQELQQQSAREVGElQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAARKQELELVVTELEARVGEEEE 949
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAE-KARQAEMDRQAAIYAEQERMAME--RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 950 CSRQLQSEKKRLQQHIQEleshlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAA 1029
Cdd:pfam17380 379 ELERLQMERQQKNERVRQ-----ELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRL 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1030 EEEEKVKSLNKLRlKYEATISDMEDRLKKEEKGRQELEKLKRR-LDGESSELQEQMVEQKQRAEELLAQLgrkeDELQAA 1108
Cdd:pfam17380 454 EEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERKRKLLEKEM----EERQKA 528
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1109 LLRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARA--KAEKQRRDLgEELEALRGELEDTLDSTNAQQEL 1181
Cdd:pfam17380 529 IYEEERR-----------REAEEERRKQQEMEERRRIQEQmrKATEERSRL-EAMEREREMMRQIVESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1005-1213 |
1.36e-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: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1005 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM 1084
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1085 VEQKQRAEELLAQLGRKEDELQAALLRAEEEGG--------------ARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1150
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLdavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28801584 1151 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQR 1213
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1241-1899 |
1.54e-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: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1241 SLEAEVSELKAELSSLQTSRQEGEQKRRRLEsQLQEVQgrssdserarsEAAEKLQRAQAELESVSTALSEAESKAIRLG 1320
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIE-LLEPIR-----------ELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1321 KELssAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMeeevvaRERAGRELQSTQAQLSEWRRRQEEeaavl 1400
Cdd:COG4913 290 LEL--LEAELEELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDRLEQLEREIERLERELEE----- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1401 eageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDAtvdLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRA 1480
Cdd:COG4913 357 ----------------RERRRARLEALLAALGLPLPASAEEFAAL---RAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1481 VEDRERIEAEGREREARALSLTRALEeeqeareelerqnrALRAELEALLSSKDD----VGK--NVHELERA-RKAAEQA 1553
Cdd:COG4913 418 RRELRELEAEIASLERRKSNIPARLL--------------ALRDALAEALGLDEAelpfVGEliEVRPEEERwRGAIERV 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1554 asdLRTQVTEL--EDELTAA-----EDAKLRLEVTVQALKAQHERDLQGRDDAG--------------EERRRQLAKQLR 1612
Cdd:COG4913 484 ---LGGFALTLlvPPEHYAAalrwvNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrAWLEAELGRRFD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1613 DAEVERDEERKQRALAMaarkkleleleelkaqtSAAGQGKEEAVKQLKKMQVQMKELWReveetrssrdemftLSRENE 1692
Cdd:COG4913 561 YVCVDSPEELRRHPRAI-----------------TRAGQVKGNGTRHEKDDRRRIRSRYV--------------LGFDNR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1693 KKLKGLEAEVLRLQEELAASDRARRQAQQDRDemaeevasgnlskaaTLEEKRQLEGRLSQLEEELEEEQNnsellkdhy 1772
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELD---------------ALQERREALQRLAEYSWDEIDVAS--------- 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1773 rkLVLQVESLTTELSAERSFSAKAEsgrqQLERQIQELRARLgEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ES 1847
Cdd:COG4913 666 --AEREIAELEAELERLDASSDDLA----ALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdrlEA 738
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1848 RERILSGKLVRRAEKRLKEVVLQvDEERRVADQVRDQLEKSNLRLKQLKRQL 1899
Cdd:COG4913 739 AEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
960-1498 |
1.71e-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: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 960 RLQQHIQELES-HLEAEEGARQKLQLEKVTTEA-KMKKFEEDLLLLEDQNSKL-----SKERRLLEERLAEFSSQAAEEE 1032
Cdd:COG4913 229 ALVEHFDDLERaHEALEDAREQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1033 EKVkslnklrlkyeatisdmeDRLKKEEKG-RQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1111
Cdd:COG4913 309 AEL------------------ERLEARLDAlREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1112 AEEEG-GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQ 1187
Cdd:COG4913 371 LGLPLpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1188 EVTELKKALEEESRAHEVSMQ------ELRQR------------HSQA---LVEmAEQLEQARR--------GKGVWEKT 1238
Cdd:COG4913 441 RLLALRDALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFAltlLVP-PEHYAAALRwvnrlhlrGRLVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1239 RLSLEAEVSE---------------------LKAELSSLQ-----TSRQEGEQKRRRLESQLQEVQGRSS----DSERAR 1288
Cdd:COG4913 520 RTGLPDPERPrldpdslagkldfkphpfrawLEAELGRRFdyvcvDSPEELRRHPRAITRAGQVKGNGTRhekdDRRRIR 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1289 SE------AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKlalgsRVRALEAEAAGLR 1362
Cdd:COG4913 600 SRyvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1363 EQMEEEvvarERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVERLerarrrlQQEL 1442
Cdd:COG4913 675 AELERL----DASSDDLAALEEQLEELEAELEE---------------------LEEELDELKGEIGRL-------EKEL 722
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1443 DDATVDLGQQKQLLSTLEKKQRKFDQLLAEEK--AAVLRAVEDRERIEAEGREREARA 1498
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRA 780
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
889-1747 |
1.71e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.52 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 889 GELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTelearvgeeeecSRQLQSEKKRLQQHIQEL 968
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT------------ALRQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 969 ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFsSQAAEEEEKVKSLNKLRLKYEAT 1048
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLPDLTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1049 ISDMEDRLK-KEEKGRQELEKLKRRLDgesseLQEQMVEQKQRAEELLAQLGRKEDELQA-----ALLRAEEEGGARAQL 1122
Cdd:PRK04863 440 AEDWLEEFQaKEQEATEELLSLEQKLS-----VAQAAHSQFEQAYQLVRKIAGEVSRSEAwdvarELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1123 LKSLReaqAGLAEAQEDLEAERVA-RAKAEKQRR-----DLGEELEALRGELEDTLDSTNAQQElrskreqEVTELKKAL 1196
Cdd:PRK04863 515 LQQLR---MRLSELEQRLRQQQRAeRLLAEFCKRlgknlDDEDELEQLQEELEARLESLSESVS-------EARERRMAL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1197 EEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQE 1276
Cdd:PRK04863 585 RQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIER 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1277 VQGRSSDSerarseaAEKLQRAQAELESVSTA-------LSEAESKAIRLG--------KELSSAESQL----------- 1330
Cdd:PRK04863 664 LSQPGGSE-------DPRLNALAERFGGVLLSeiyddvsLEDAPYFSALYGparhaivvPDLSDAAEQLagledcpedly 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1331 -------------HDTQEL----LQEETRAKLALgSRV--------RALEAEAAGLREQMEEEVVARERAGRELQSTQ-- 1383
Cdd:PRK04863 737 liegdpdsfddsvFSVEELekavVVKIADRQWRY-SRFpevplfgrAAREKRIEQLRAEREELAERYATLSFDVQKLQrl 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1384 ---------------------AQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQR------------------LAEK 1424
Cdd:PRK04863 816 hqafsrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGlsalnrllprlnlladetLADR 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1425 TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLlaeeKAAVLRAVEDRERIEAegrerEARALSltra 1504
Cdd:PRK04863 896 VEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQL----KQDYQQAQQTQRDAKQ-----QAFALT---- 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1505 leeeqeareeLERQNRALRAELEA--LLSSKDDvgkNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTV 1582
Cdd:PRK04863 963 ----------EVVQRRAHFSYEDAaeMLAKNSD---LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1583 QALKAQH---ERDLQG---RDDAGEE-----RRRQLAKQLRDAEVERDEERKQRALAMAARkkleleleelkaqtsaagq 1651
Cdd:PRK04863 1030 DAKRQMLqelKQELQDlgvPADSGAEeraraRRDELHARLSANRSRRNQLEKQLTFCEAEM------------------- 1090
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1652 gkEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSREN--EKKLKGLEAEVLRLQEELAASDRAR---RQAQQDRDEM 1726
Cdd:PRK04863 1091 --DNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNgvERRLHRRELAYLSADELRSMSDKALgalRLAVADNEHL 1168
|
970 980
....*....|....*....|.
gi 28801584 1727 AEEVASgnLSKAATLEEKRQL 1747
Cdd:PRK04863 1169 RDVLRL--SEDPKRPERKVQF 1187
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
867-1338 |
3.45e-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: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 867 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLA-EQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 945
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 946 EEEECSRQLQSEKKRLQQH---IQELESHLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLskerrlleERLA 1022
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAeqlRQNLEKQQSSLAEAEQRIK----ELEFEIQSQEQDSEIVKNSKSEL--------ARIP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1023 EFSSQAAEEEEKVKSLNKLR---LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQE-----QMVEQKQRAEEL 1094
Cdd:pfam05557 201 ELEKELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwvklaQDTGLNLRSPED 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1095 LAqlGRKEDELQAALLRAEEEGGARAQLL---KSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL-------GEELEAL 1164
Cdd:pfam05557 281 LS--RRIEQLQQREIVLKEENSSLTSSARqleKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvlllTKERDGY 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1165 RGELED-----TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQaLVEMAEQLEQARRGKGVWEKTR 1239
Cdd:pfam05557 359 RAILESydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQ-QAQTLERELQALRQQESLADPS 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1240 LSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQL--QEVQGRS---------------SDSERARSEAAEKLQ------ 1296
Cdd:pfam05557 438 YSKE-EVDSLRRKLETLELERQRLREQKNELEMELerRCLQGDYdpkktkvlhlsmnpaAEAYQQRKNQLEKLQaeierl 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1297 -----RAQAELESV----STALSEAESKAIRLGKELSSAESQLHDTQELLQ 1338
Cdd:pfam05557 517 krllkKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1012-1871 |
5.22e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.98 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1012 KERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRA 1091
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDL-------EQDYQAASDHLNLVQTALRQQEKIER-YQADLEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1092 EELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:PRK04863 372 EEADEQQ----EENEARAEAAEEE----------VDELKSQLADYQQALDVQQ-TRAIQYQQAVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1172 LDSTNAQQELRSKREQEVTELKKALEEESRAHevsmQELRQRHSQAL---------VEMAEQLEQARRGKGVWEKTRLsL 1242
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVA----QAAHSQFEQAYqlvrkiageVSRSEAWDVARELLRRLREQRH-L 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1243 EAEVSELKAELSSLQTSRQEgeqkRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAirlgke 1322
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR------ 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1323 lssaeSQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQ---LSEWRRRQEEEAAV 1399
Cdd:PRK04863 582 -----MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERereLTVERDELAARKQA 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1400 LEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRlqqELDDA---------------TVDLGQQKQLLSTL----- 1459
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIYDDV---SLEDApyfsalygparhaivVPDLSDAAEQLAGLedcpe 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1460 -----EKKQRKFDQ--LLAEE-KAAVLRAVEDRE----RIEAE---GRE-REARALsltraleeeqeareelerqnrALR 1523
Cdd:PRK04863 734 dlyliEGDPDSFDDsvFSVEElEKAVVVKIADRQwrysRFPEVplfGRAaREKRIE---------------------QLR 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1524 AELEALLSSKDDVGKNVHELERARKAA----------------EQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA 1587
Cdd:PRK04863 793 AEREELAERYATLSFDVQKLQRLHQAFsrfigshlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKE 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1588 QHE--RDLQGR-----DDAGEERRRQLAKQLRDAEV-ERDEERKQRALAMAARKKleleleelkaqtsAAGQGKEEAVKQ 1659
Cdd:PRK04863 873 GLSalNRLLPRlnllaDETLADRVEEIREQLDEAEEaKRFVQQHGNALAQLEPIV-------------SVLQSDPEQFEQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1660 LKKMQVQMKELWREVeetrssRDEMFTLSRENEKKLK-GLEAEVLRLQEELAASDRAR---RQAQQDRDEMAEEVasgnl 1735
Cdd:PRK04863 940 LKQDYQQAQQTQRDA------KQQAFALTEVVQRRAHfSYEDAAEMLAKNSDLNEKLRqrlEQAEQERTRAREQL----- 1008
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1736 skaatleekRQLEGRLsqleeeleeeqnnsellkDHYRKLVLQVESlttelsaerSFSAKAESgRQQLERQIQEL--RAR 1813
Cdd:PRK04863 1009 ---------RQAQAQL------------------AQYNQVLASLKS---------SYDAKRQM-LQELKQELQDLgvPAD 1051
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1814 LGEEDAgARARQKMLIAAL---ESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQV 1871
Cdd:PRK04863 1052 SGAEER-ARARRDELHARLsanRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQV 1111
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
863-1255 |
7.31e-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: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 943 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLA 1022
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1023 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELqeqmveqkqraEELLAQLGRKE 1102
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-----------SSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1103 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDL------EAERVARAKAEKQRRD--LGEEL---EALRGELEDT 1171
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALREGRARWAQERETLqqsaeaDKDRIEKLSAELQRLEerLQEERmerEKLEVELGRE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1172 LDSTNAQqelRSKREQEVTELKKALEEESRAhevsmQELRQRHSQALVEMAEQLEQaRRGKGVWEKTRLSLEAEVSELKA 1251
Cdd:pfam07888 352 KDCNRVQ---LSESRRELQELKASLRVAQKE-----KEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDS 422
|
....
gi 28801584 1252 ELSS 1255
Cdd:pfam07888 423 PLSD 426
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
890-1492 |
7.40e-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: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 890 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTE----------LEARVGEEEECSRQLQSEKK 959
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 960 RLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSL 1038
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1039 NKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSE----LQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEE 1114
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1115 EGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQ---------------- 1178
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKeveleelkkilaedek 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1179 ------------QELRSKrEQEVTELKKALEEESRAHEVSMQELR---QRHSQALVEMAEQLEQ---------ARRGKGV 1234
Cdd:pfam05483 420 lldekkqfekiaEELKGK-EQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKTELEKeklknieltAHCDKLL 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1235 WEKTRLSLEAE--VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEA 1312
Cdd:pfam05483 499 LENKELTQEASdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSI 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1313 ESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1392
Cdd:pfam05483 579 EYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDN 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1393 QEEEAAVleageearrraareAETLTQRLAEKTEAVERLERARRRLQQELDDATvdlgQQK--QLLSTLEKKQRKFDQLL 1470
Cdd:pfam05483 659 YQKEIED--------------KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC----QHKiaEMVALMEKHKHQYDKII 720
|
650 660
....*....|....*....|..
gi 28801584 1471 aEEKAAVLRAVEDRERIEAEGR 1492
Cdd:pfam05483 721 -EERDSELGLYKNKEQEQSSAK 741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1522-1943 |
1.66e-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: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1522 LRAELEALLSSKDDVGKNVHELERAR-KAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAG 1600
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1601 EERRRQLAKQLRDAEVERDeERKQRALAMAarkkleleleelkAQTSAAGQGKEEAVKQLKKMQVQMKELwreVEETRSS 1680
Cdd:COG4913 337 GDRLEQLEREIERLERELE-ERERRRARLE-------------ALLAALGLPLPASAEEFAALRAEAAAL---LEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1681 RDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRAR----RQAQQDRDEMAEE--------------------------- 1729
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEAlgldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1730 -------------VASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDH--YRKLVLQVESLTTELSAE--RSF 1792
Cdd:COG4913 480 iervlggfaltllVPPEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1793 S-AKAESGrQQLER---------QIQELRARlGEEDA----------GARARQKmlIAALESKLAQAEEQLEQ-ESRERI 1851
Cdd:COG4913 560 DyVCVDSP-EELRRhpraitragQVKGNGTR-HEKDDrrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1852 LSGKL-----VRRAEKRLKEV------VLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQREL 1920
Cdd:COG4913 636 LEAELdalqeRREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500
....*....|....*....|...
gi 28801584 1921 EDVTESAESMNREVTTLRNRLRR 1943
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEA 738
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
998-1834 |
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 28801584 998 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDgES 1077
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1078 SELQEQMVEQKQRAEELLAQLgrkeDELQAALLRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDL 1157
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEE----------VDSLKSQLADYQQALDVQQ-TRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1158 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEeesraHEVSM-QELRQRHSQA---LVEMAEQLEQARrgkg 1233
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE-----QKLSVaDAARRQFEKAyelVCKIAGEVERSQ---- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1234 VWEKTRLSLEaEVSELKAELSSLQTSRQEGEQKRRRLESQ------LQEVQGRSSDSERARSEAAEKLQRAQAELESVST 1307
Cdd:COG3096 493 AWQTARELLR-RYRSQQALAQRLQQLRAQLAELEQRLRQQqnaerlLEEFCQRIGQQLDAAEELEELLAELEAQLEELEE 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1308 ALSEAESKAIRLGKELSSAESQ-------------LHDTQELLQEETRAKLAlgsrvraleaEAAGLREQMEEeVVARER 1374
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALA----------DSQEVTAAMQQ-LLERER 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1375 agrELQSTQAQLSEWRRRQEEEAAVLEAGEEARRraareaeTLTQRLAEKTEAVERLERARRRLqqeLDDATV------- 1447
Cdd:COG3096 641 ---EATVERDELAARKQALESQIERLSQPGGAED-------PRLLALAERLGGVLLSEIYDDVT---LEDAPYfsalygp 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1448 --------DLGQQKQLLSTL----------EKKQRKFDQLL---AEEKAAVLRAVEDRE----RIEAE---GRE-REARA 1498
Cdd:COG3096 708 arhaivvpDLSAVKEQLAGLedcpedlyliEGDPDSFDDSVfdaEELEDAVVVKLSDRQwrysRFPEVplfGRAaREKRL 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1499 lsltraleeeqeareelerqnRALRAELEALLSSKDDVGKNVHELERARKAAEQ----------------AASDLRTQVT 1562
Cdd:COG3096 788 ---------------------EELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghlavafapdpeaELAALRQRRS 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1563 ELEDELTAAEDAKLRLEVTVQALKAQHE--RDLQGR-----DDAGEERRRQLAKQLRDAEVERDEERKQRAlAMAARKKL 1635
Cdd:COG3096 847 ELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGK-ALAQLEPL 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1636 ELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELwREVEETR-----SSRDEMFTLSRE-NEKklkgLEAEVLRLQEEL 1709
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRphfsyEDAVGLLGENSDlNEK----LRARLEQAEEAR 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1710 AASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKdhyrklvlqVESLTTELSAE 1789
Cdd:COG3096 1001 REAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIR---------RDELHEELSQN 1071
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 28801584 1790 RSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALES 1834
Cdd:COG3096 1072 RSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1086-1326 |
4.02e-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: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1086 EQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1166 GELEDTLDSTnAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQarrgkgvwekTRLSLEAE 1245
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----------DLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1246 VSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSS 1325
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 28801584 1326 A 1326
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1125 |
5.97e-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: 5.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 896 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEae 975
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 976 egaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL--LEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDME 1053
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1054 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRaeelLAQLGRKEDELQAALLRAEEEGGARAQLLKS 1125
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAE----LAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1154-1956 |
6.11e-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: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1154 RRDLGEELEALRGELeDTLDStnAQQELRSKREQevtelKKALEEESRAHEvSMQELRQRHS--QALVEMAeQLEQARRG 1231
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLER--AHEALEDAREQ-----IELLEPIRELAE-RYAAARERLAelEYLRAAL-RLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1232 KGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserARSEAAEKLQRAQAELESVSTALSE 1311
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1312 AESKAIRLGKELSSAESQLHDTQELLQEetraklalgsRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRR 1391
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1392 RQ----EEEAAVLEAgeearrraareaetLTQRLAEKTEAVERLErarrrlqqELDDatVDLGQQK------QLLSTLek 1461
Cdd:COG4913 434 RKsnipARLLALRDA--------------LAEALGLDEAELPFVG--------ELIE--VRPEEERwrgaieRVLGGF-- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1462 kqrKFDqLLAEEK--AAVLRAVEDR--------ERIEAEGREREARAL---SLTRALEEEQEareelerqnrALRAELEA 1528
Cdd:COG4913 488 ---ALT-LLVPPEhyAAALRWVNRLhlrgrlvyERVRTGLPDPERPRLdpdSLAGKLDFKPH----------PFRAWLEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1529 LLSSKDDVGK--NVHELERARKAaeqaasdlrtqvteledeltaaedaklrleVTVQALkAQHERDLQGRDDAGEERRRQ 1606
Cdd:COG4913 554 ELGRRFDYVCvdSPEELRRHPRA------------------------------ITRAGQ-VKGNGTRHEKDDRRRIRSRY 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1607 L-----AKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAgqgkeEAVKQLKKMQVQMKELWREVEETRSSR 1681
Cdd:COG4913 603 VlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAL-----QRLAEYSWDEIDVASAEREIAELEAEL 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1682 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEE 1761
Cdd:COG4913 678 ERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1762 QNNSELLKDHYRKLvlqVESLTTELSAERsfsAKAESGRQQLERQIQELRAR-------LGEEDAGARARQKMLIAALES 1834
Cdd:COG4913 754 RFAAALGDAVEREL---RENLEERIDALR---ARLNRAEEELERAMRAFNREwpaetadLDADLESLPEYLALLDRLEED 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1835 KLAQAEEQLEQEsrerilsgkLVRRAEKRLKEVVLQVDEERRvadQVRDQLEKSNLRLKQLK----RQLEEAEEEASRAQ 1910
Cdd:COG4913 828 GLPEYEERFKEL---------LNENSIEFVADLLSKLRRAIR---EIKERIDPLNDSLKRIPfgpgRYLRLEARPRPDPE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1911 AgrRRLQRELEDVTESAESMNRE--------VTTLRNRLRRGPLTFTTRTVRQV 1956
Cdd:COG4913 896 V--REFRQELRAVTSGASLFDEElsearfaaLKRLIERLRSEEEESDRRWRARV 947
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1091 |
7.00e-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: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 943 RVGE-EEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1021
Cdd:COG4942 98 ELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1022 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRA 1091
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
965-1343 |
7.01e-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: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 965 IQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1044
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1045 YEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK--EDELQAALLRAEEEG------ 1116
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKiaEYTKSIDIKKATESLeeqlaa 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1117 -GARAQLLKSLREAQAGLAEAQEDLeaervarakaEKQRRDLGEELEALRGELE---DTLDSTNAQQELRSKrEQEVTEL 1192
Cdd:COG5185 321 aEAEQELEESKRETETGIQNLTAEI----------EQGQESLTENLEAIKEEIEnivGEVELSKSSEELDSF-KDTIEST 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1193 KKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQkrrrlES 1272
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQ---IEQATSSNEEVSKLLNELISELNKVMREADE-----ES 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1273 QLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRA 1343
Cdd:COG5185 462 QSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1103-1503 |
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 28801584 1103 DELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNA 1177
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1178 QQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQ 1257
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1258 TSRQEGEQKRR--------RLESQLQEVQGRSSDSERARSEAAE--------------KLQRAQAELESVSTALSEAESK 1315
Cdd:COG4717 234 NELEAAALEERlkearlllLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallflLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1316 AIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQlsewrrrQEE 1395
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVE-------DEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1396 EAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQ--QELDDATVDL----GQQKQLLSTLEKKQRKFDQL 1469
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEleEELEELEEELeeleEELEELREELAELEAELEQL 465
|
410 420 430
....*....|....*....|....*....|....
gi 28801584 1470 LAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1503
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
858-1339 |
1.52e-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: 60.13 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 858 LQVTRQDEVLQARAQELQKVQELQ-------QQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQmaaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELVVtelearvgeeEECSRQLQSEKKRLQQHIQELEsHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1010
Cdd:pfam15921 506 QEKERAI----------EATNAEITKLRSRVDLKLQELQ-HLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENM 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1011 SKerrLLEERLAEFSSQAAEEEEKVKSLNKLRLKYE--ATISDMEDRLKKEEKGR-QELEKLKRRLDGESSELQEQMVEQ 1087
Cdd:pfam15921 575 TQ---LVGQHGRTAGAMQVEKAQLEKEINDRRLELQefKILKDKKDAKIRELEARvSDLELEKVKLVNAGSERLRAVKDI 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1088 KQRAEELLAQLGRKEDELQA------ALLR-----AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRD 1156
Cdd:pfam15921 652 KQERDQLLNEVKTSRNELNSlsedyeVLKRnfrnkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1157 LGEELEALRGELEDTLDSTNAQQELRSKREQEvtelKKALEEESrahevsmQELRQRHSQALVE---MAEQLEQARRGKG 1233
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKE----KHFLKEEK-------NKLSQELSTVATEknkMAGELEVLRSQER 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1234 VWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ----LQEVQG---RSSDSERARSEAAEKLQRAQAEL---E 1303
Cdd:pfam15921 801 RLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhtldVKELQGpgyTSNSSMKPRLLQPASFTRTHSNVpssQ 880
|
490 500 510
....*....|....*....|....*....|....*.
gi 28801584 1304 SVSTALSEAESKAIRLgkelssAESQLHDTQELLQE 1339
Cdd:pfam15921 881 STASFLSHHSRKTNAL------KEDPTRDLKQLLQE 910
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1021-1230 |
1.79e-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: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQrAEELLAQLGR 1100
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 KEDELQAALLRAEEEGGARAQLL--KSLREAQAGLAEAQEDLEAERVAR--AKAEKQRRDLGEELEALRGELEDTLDSTN 1176
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1177 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1230
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
952-1396 |
1.88e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 952 RQLQSEKKRLQQhIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLED--QNSKLSKERRLLEERLAEFSSQAA 1029
Cdd:COG4717 71 KELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1030 EEEEKVKSLNKLRlkyeatiSDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1109
Cdd:COG4717 150 ELEERLEELRELE-------EELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1110 LRAEEE------GGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLG-------------EELEALRGELED 1170
Cdd:COG4717 223 EELEEEleqlenELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGvlflvlgllallfLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1171 TLDSTNAQQELRSKREQEVTELKKA--LEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSE 1248
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAAlgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1249 LKAELSSLQTSRQEGEQKRRRLESQLQEVqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAES 1328
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQL--EELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1329 QLHDtqellqeetrakLALGSRVRALEAEAAGLREQMEEEvvarERAGRELQSTQAQLSEWRRRQEEE 1396
Cdd:COG4717 461 ELEQ------------LEEDGELAELLQELEELKAELREL----AEEWAALKLALELLEEAREEYREE 512
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
869-1620 |
3.26e-08 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 59.07 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 869 ARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAE-LCSEAEEtrarlaarkqelelvvtelEARVGEE 947
Cdd:NF041483 299 AESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEkLVAEAAE-------------------KARTVAA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 948 EECSRQLQSEKKrlqqhiqeleshlEAEEGARQKLQLEKVTTEAKMKKFEedlllledqnsklsKERRLLEERLAEFSSQ 1027
Cdd:NF041483 360 EDTAAQLAKAAR-------------TAEEVLTKASEDAKATTRAAAEEAE--------------RIRREAEAEADRLRGE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1028 AAEEEEKVKSLNKlrlkyeatisdmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRaeellaqlgrkedelqa 1107
Cdd:NF041483 413 AADQAEQLKGAAK-------------DDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGER----------------- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1108 alLRAEEEGGARAQLLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRSKR 1185
Cdd:NF041483 463 --IRGEARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1186 EQEVTELKKALEEESRahevsmqELRqrhsqalvEMAEQLEQARRGKGVWEKTRLSLEAEvSELKAELSSLQTSRQEGEQ 1265
Cdd:NF041483 541 EEQAEEVRAAAERAAR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEAER 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1266 KRRRlesqlqevqgRSSDSERARSEAAEKLQ--RAQAELES----------VSTALSEAESKAIRLGKELSSAESQLHDT 1333
Cdd:NF041483 605 IRRE----------AAEETERLRTEAAERIRtlQAQAEQEAerlrteaaadASAARAEGENVAVRLRSEAAAEAERLKSE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1334 QELLQEETRAKLALGSRVRALEAeAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLeagEEARRRAARE 1413
Cdd:NF041483 675 AQESADRVRAEAAAAAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEL---LASARKRVEE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1414 AETLTQRLAEKTEA-VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAVLR 1479
Cdd:NF041483 751 AQAEAQRLVEEADRrATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAERER 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1480 AVEDRERIEAEGREREARALSL---TRALEEEQEAREELERQNRALRAELEAllssKDDVGKNVHELERARKAAEQAASD 1556
Cdd:NF041483 831 ASEDANRLRREAQEETEAAKALaerTVSEAIAEAERLRSDASEYAQRVRTEA----SDTLASAEQDAARTRADAREDANR 906
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1557 LRTQVTELEDEL---TAAEDAKLRLEVTVQALKAQHERDLQG---RDDAGEERRRQLAKQLRDAEVERDE 1620
Cdd:NF041483 907 IRSDAAAQADRLigeATSEAERLTAEARAEAERLRDEARAEAervRADAAAQAEQLIAEATGEAERLRAE 976
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
860-1398 |
3.77e-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: 58.98 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 860 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRvaQLEEERTRLAeQLRaeaelcSEAEETRARLAARKQELELVVTE 939
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR--QLSDLESTVS-QLR------SELREAKRMYEDKIEELEKQLVL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 940 LEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEgarQKLQLEKvttEAKMKKFEEDL----------LLLEDQNSK 1009
Cdd:pfam15921 354 ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE---KELSLEK---EQNKRLWDRDTgnsitidhlrRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1010 LSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgESSElqeqmveqkQ 1089
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL--ESSE---------R 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1090 RAEELLAQLGRKEDELQAA---LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1166
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATnaeITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQ 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1167 ELEDTLDSTNAQQELRSKREQEVTELKKALEE---ESRAHEVSMQELRQRHSQALVEMAEQL----EQARRGKGVwEKTR 1239
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQEfkiLKDKKDAKIRELEARVSDLELEKVKLVnagsERLRAVKDI-KQER 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1240 LSLEAEVSELKAELSSLQtsrQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1319
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLS---EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGM 732
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1320 GKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQlsewRRRQEEEAA 1398
Cdd:pfam15921 733 QKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQ----ERRLKEKVA 807
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1053-1305 |
5.41e-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: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1053 EDRLKKEEKGRQELEKLKRRLDGESSELQEQ-----MVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLR 1127
Cdd:COG4913 616 EAELAELEEELAEAEERLEALEAELDALQERrealqRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLE 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1128 EAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSM 1207
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERI 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1208 QELRQRHSQALVEMAEQLEQARRgkgVWEKTRLSLEAEVSEL---KAELSSLQTS---RQEGEQKRRRLESQLQEVQGRS 1281
Cdd:COG4913 776 DALRARLNRAEEELERAMRAFNR---EWPAETADLDADLESLpeyLALLDRLEEDglpEYEERFKELLNENSIEFVADLL 852
|
250 260
....*....|....*....|....
gi 28801584 1282 SDSERARSEAAEKLQRAQAELESV 1305
Cdd:COG4913 853 SKLRRAIREIKERIDPLNDSLKRI 876
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
864-1228 |
8.39e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 864 DEVLQARAQ------ELQKVQELQQQSAREVGELQGRVAQLEEER-------------TRLAEQL-RAEAELcseaEETR 923
Cdd:PRK04863 286 EEALELRRElytsrrQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtaLRQQEKIeRYQADL----EELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 924 ARLAARKQELELV---VTELEARVGEEEECSRQLQSEKKRLQQHIQELESH-------LEAEEGARQKLQLEKVTTEakm 993
Cdd:PRK04863 362 ERLEEQNEVVEEAdeqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaVQALERAKQLCGLPDLTAD--- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 994 kKFEEDLLLLEDQNSKLSKERRLLEERLAeFSSQAAEEEEKVKSLNKlrlkyeaTISDMEDRLKKEEKGRQELEKLK--R 1071
Cdd:PRK04863 439 -NAEDWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLVR-------KIAGEVSRSEAWDVARELLRRLReqR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1072 RLDGESSELQ------EQMVEQKQRAEELLAQLGRK-------EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1138
Cdd:PRK04863 510 HLAEQLQQLRmrlselEQRLRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLE 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1139 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTnaqqelrskreQEVTELKKALEEESRAHEVSMQELRQRhSQAL 1218
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-----------QDVTEYMQQLLERERELTVERDELAAR-KQAL 657
|
410
....*....|
gi 28801584 1219 VEMAEQLEQA 1228
Cdd:PRK04863 658 DEEIERLSQP 667
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
906-1625 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 906 AEQLRAEAELCSE-AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQhiqeleshleaeegaRQKLQL 984
Cdd:TIGR00618 196 AELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEE---------------QLKKQQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 985 EKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLeerlaefssQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1064
Cdd:TIGR00618 261 LLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1065 ELEKlkrrlDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGG---ARAQLLKSLREAQAGLAEAQEDLE 1141
Cdd:TIGR00618 332 AHVK-----QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhihTLQQQKTTLTQKLQSLCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1142 AERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEM 1221
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1222 AEQLEQARRGKGVWEKTRL----SLEAEVSELKAELSSLQTSR-QEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQ 1296
Cdd:TIGR00618 487 RKKAVVLARLLELQEEPCPlcgsCIHPNPARQDIDNPGPLTRRmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1297 RAQAELESVSTALSEAESKAIRLGKELssaESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAG 1376
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNIT---VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1377 RELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLL 1456
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHAL-----------------SIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1457 STLEKKQRKFDQLLAEEKAAVLRAVEDRErieaegREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDV 1536
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLA------AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1537 GKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLakqlrdaev 1616
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL--------- 851
|
....*....
gi 28801584 1617 ERDEERKQR 1625
Cdd:TIGR00618 852 LKYEECSKQ 860
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
919-1277 |
1.17e-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: 56.83 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 919 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLeaeegarQKLQLEKVTTEAKMKKFEE 998
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-------AELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 999 DLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE-- 1076
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1077 ---------SSELQEQMVEQKQRAEELLaQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:pfam07888 182 qteeelrslSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1148 AKAEKQRRDLGEELEALRGELEDT----LDSTNAQQELRSKREQEVTELKKALE----------EESRAHEVSMQELRQR 1213
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEadkdrieklsAELQRLEERLQEERME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1214 HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEV 1277
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 ... |
874-1213 |
1.46e-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: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 874 LQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQ 953
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 954 --LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSKERRLLEERLAEFSSQAA 1029
Cdd:pfam02463 725 drVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEreKTEKLKVEEEKEEKLKAQEEELR 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1030 EEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAL 1109
Cdd:pfam02463 805 ALEEELKEEAELLEEEQLLIEQEEKIKEEELE-ELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1110 LRAEEEG----GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSK 1184
Cdd:pfam02463 884 LKDELESkeekEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
330 340
....*....|....*....|....*....
gi 28801584 1185 REQEVTELKKALEEESRAHEVSMQELRQR 1213
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1044 |
1.97e-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: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEE----RTRLAEQLRAEAELCSEAE-------ETRARLA 927
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPlalllspEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 928 ARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQN 1007
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 28801584 1008 SKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLK 1044
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1177-1591 |
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 28801584 1177 AQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELK------ 1250
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEeleerl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1251 AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR-SEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQ 1329
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1330 LHDTQELLQ-EETRAKLALGSRVRALEAEAAGLREQMEE--------------EVVARERAGRELQSTQAQLSEWRRRQE 1394
Cdd:COG4717 236 LEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1395 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELddatvdlgQQKQLLSTLEKKQRKFDQLLAEEK 1474
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--------QLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1475 AAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRA--LRAELEALLSSKDDVGKNVHELERARKAAE- 1551
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELeeLEEELEELEEELEELREELAELEAELEQLEe 467
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 28801584 1552 -QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHER 1591
Cdd:COG4717 468 dGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
859-1255 |
2.89e-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: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSE---AEETRARLAARKQELeL 935
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiqsQEQDSEIVKNSKSEL-A 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 936 VVTELEA---RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK---LQLEKVTTEAKMK---KFEEDLLLLEDQ 1006
Cdd:pfam05557 198 RIPELEKeleRLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEaatLELEKEKLEQELQswvKLAQDTGLNLRS 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1007 NSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRL------------- 1073
Cdd:pfam05557 278 PEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerdg 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1074 ----------DGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLrEAQAGLAEAQEDLEAE 1143
Cdd:pfam05557 358 yrailesydkELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-ERELQALRQQESLADP 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1144 RVARAKAEKQRRDLgEELEALRGELE---DTLDSTNAQQELRSKREQ---EVTELKKALEEESRAHEVSMQELRQRHSQA 1217
Cdd:pfam05557 437 SYSKEEVDSLRRKL-ETLELERQRLReqkNELEMELERRCLQGDYDPkktKVLHLSMNPAAEAYQQRKNQLEKLQAEIER 515
|
410 420 430
....*....|....*....|....*....|....*....
gi 28801584 1218 LVEMAEQLEQARRGKGVWEKTRLSL-EAEVSELKAELSS 1255
Cdd:pfam05557 516 LKRLLKKLEDDLEQVLRLPETTSTMnFKEVLDLRKELES 554
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1052-1782 |
2.99e-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: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1052 MEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAAllraeeeggaRAQLLKSLREAQA 1131
Cdd:pfam12128 246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK----------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1132 GLAEAQEDLEA----------ERVARAKAEKQRRDL-GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEES 1200
Cdd:pfam12128 316 AVAKDRSELEAledqhgafldADIETAAADQEQLPSwQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1201 RAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-----VSELKAELSSLQTSRQEGEQKRrrlesQLQ 1275
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrlksrLGELKLRLNQATATPELLLQLE-----NFD 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1276 EVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHdtqellqeeTRAKLALGSRVRALE 1355
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE---------LQLFPQAGTLLHFLR 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1356 AEAAGLREQMEEeVVARERAGRelqsTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERAR 1435
Cdd:pfam12128 542 KEAPDWEQSIGK-VISPELLHR----TDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1436 RRLQQELDDAtvdlgqqkqlLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGR-EREARALSLTRALEEEQEAREE 1514
Cdd:pfam12128 617 REKQAAAEEQ----------LVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDKKNKALAERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1515 LERQNRALRAELEALLSS-KDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRlevtvqALKAQHERDL 1593
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEqKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELK------ALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1594 QGRDdAGEERRRQLAKQLRD--AEVERDEERKQRALAMAA--RKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE 1669
Cdd:pfam12128 761 ASLG-VDPDVIAKLKREIRTleRKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1670 LWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQE----ELAASDRARRQAQQDRDEMAEEVASGNLSK------AA 1739
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEdansEQAQGSIGERLAQLEDLKLKRDYLSESVKKyvehfkNV 919
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 28801584 1740 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESL 1782
Cdd:pfam12128 920 IADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQW 962
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1244-1479 |
5.24e-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: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1244 AEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvstalsEAESKAIRLGKEL 1323
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA-------ALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1324 SSAESQLHDTQELLQEETRAKLALGSR------VRALEAEAAGLREQMEEEVV-ARERAGRELQSTQAQLSEWRRRQEEE 1396
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1397 AAVLEAGEEARRRAAReaeTLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAA 1476
Cdd:COG4942 173 RAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
...
gi 28801584 1477 VLR 1479
Cdd:COG4942 250 ALK 252
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
955-1395 |
5.82e-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: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 955 QSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEk 1034
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIE---LEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1035 vksLNKLRLKYEATISdmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEEL---LAQLGRKEDELQAALLR 1111
Cdd:pfam05557 77 ---LNRLKKKYLEALN---KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTnseLEELQERLDLLKAKASE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1112 AEEEGGARAQLLKSLREAQAGLAEAQEDLE-----AERVARAKAEKQR-RDLGEELEALRGELEdTLDSTNAQQELrskR 1185
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqeqdSEIVKNSKSELARiPELEKELERLREHNK-HLNENIENKLL---L 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1186 EQEVTELKKALE--EESRAHEVSMqELRQRHSQALVEMAEQLEQ-----------ARRGKGVWEKTRLSLEAEVSELKAE 1252
Cdd:pfam05557 227 KEEVEDLKRKLEreEKYREEAATL-ELEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1253 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSErarsEAAEKLQRA-----------QAELESVSTALSEAESkAIRLGK 1321
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHK----ALVRRLQRRvllltkerdgyRAILESYDKELTMSNY-SPQLLE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1322 ELSSAESQLHDTQeLLQEETRAKL--------ALGSRVRALEAEAAGLREQMEEEVVARERAG-----RELQSTQAQLSE 1388
Cdd:pfam05557 381 RIEEAEDMTQKMQ-AHNEEMEAQLsvaeeelgGYKQQAQTLERELQALRQQESLADPSYSKEEvdslrRKLETLELERQR 459
|
....*..
gi 28801584 1389 WRRRQEE 1395
Cdd:pfam05557 460 LREQKNE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1119 |
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 28801584 861 TRQDEVLQARAQELQkvqelqqqsaREVGELQGRVAQLEEERTRLAEQLRAEAELCS---------EAEETRARLAARKQ 931
Cdd:COG4913 609 RAKLAALEAELAELE----------EELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 932 ELEL---VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQklQLEKVTTEAKMKKFEEDLLLLEDQNS 1008
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD--ELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1009 KLSKE------RRLLEERLAEFSSQAAEEEEK-VKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRrldgesselq 1081
Cdd:COG4913 757 AALGDaverelRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE---------- 826
|
250 260 270
....*....|....*....|....*....|....*....
gi 28801584 1082 EQMVEQKQRAEELLAQL-GRKEDELQAALLRAEEEGGAR 1119
Cdd:COG4913 827 DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1027-1303 |
7.68e-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: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1027 QAAEEEEKVKSlNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSelQEQMVEQKQRAEELLAQLGRKEDELQ 1106
Cdd:pfam17380 288 QQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1107 AALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGE---ELEALRGELEDTldstnAQQELRS 1183
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 KREQEVTELKKA-LEEESRAHEvsMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSslqtsrqE 1262
Cdd:pfam17380 440 LEEERAREMERVrLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI-------E 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28801584 1263 GEQKRRRLESQLQEVQGRSSDSERARSeaAEKLQRAQAELE 1303
Cdd:pfam17380 511 EERKRKLLEKEMEERQKAIYEEERRRE--AEEERRKQQEME 549
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1173-1394 |
7.75e-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: 7.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1173 DSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSqaLVEMAEQLEQarrgkgvwektrlsLEAEVSELKAE 1252
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1253 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSD--SERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQl 1330
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1331 hdtqeLLQEETRAKLALGSRVRALEAEAAGLREQMEEevvARERAgRELQSTQAQLSEWRRRQE 1394
Cdd:COG3206 307 -----LQQEAQRILASLEAELEALQAREASLQAQLAQ---LEARL-AELPELEAELRRLEREVE 361
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
992-1699 |
8.04e-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: 54.59 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 992 KMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAaeeEEKVKSLNKLRLKYEATISDMEDRLKK----EEKGRQELE 1067
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCT---PCMPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1068 KLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1148 AKAEKQRRDLGEE---LEALRGELEDTLDSTNAQQELRSKREQEVTELK--KALEEESRAHEVSMQELRQ-----RHSQA 1217
Cdd:TIGR00618 331 AAHVKQQSSIEEQrrlLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQhiHTLQQQKTTLTQKLQSLCKeldilQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1218 LVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTS--------RQEGEQKRRRLESQLQEVQGRSSDSERARS 1289
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihLQESAQSLKEREQQLQTKEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1290 EAAEKLQRAQAELESVSTALSEAESKAIRLGkelssaesQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEv 1369
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDID--------NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASL- 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1370 vaRERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDL 1449
Cdd:TIGR00618 562 --KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQ 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1450 GQQkQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDR--ERIEAEGREREARALSLTraleeeqEAREELERQNRALRAELE 1527
Cdd:TIGR00618 640 ELA-LKLTALHALQLTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLT-------YWKEMLAQCQTLLRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1528 ALLSSKddvgKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQL 1607
Cdd:TIGR00618 712 HIEEYD----REFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1608 AKQLRdaevERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL----KKMQVQMKELWREVEETRSSRDE 1683
Cdd:TIGR00618 788 QFFNR----LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRleekSATLGEITHQLLKYEECSKQLAQ 863
|
730
....*....|....*.
gi 28801584 1684 MFTLSRENEKKLKGLE 1699
Cdd:TIGR00618 864 LTQEQAKIIQLSDKLN 879
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
864-1115 |
8.24e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.16 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 864 DEVLQArAQELQKVQ--ELQQQSAREVGelqGRVAQLEEERTRLAEQLRAEAELCSEAEETR-----ARLAARKQELELV 936
Cdd:PRK05771 19 DEVLEA-LHELGVVHieDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 937 VTELEARVGEEEECSRQLQSEKKRLQQHIQELE---------------SHLEAEEGARQKLQLEKVTTEAKMKKFEE--- 998
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYist 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 999 ----DLLLLEDQNSKLSKERRLLEErlAEFSSQAAEEEEKVKSLnklrlkyeatISDMEDRLKKEEKGRQ----ELEKLK 1070
Cdd:PRK05771 175 dkgyVYVVVVVLKELSDEVEEELKK--LGFERLELEEEGTPSEL----------IREIKEELEEIEKEREslleELKELA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1071 RRLDGESSELQEQMVEQKQRAEELLAQLG-------------RKEDELQAALLRAEEE 1115
Cdd:PRK05771 243 KKYLEELLALYEYLEIELERAEALSKFLKtdktfaiegwvpeDRVKKLKELIDKATGG 300
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1159-1870 |
1.01e-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: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1159 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWE-K 1237
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1238 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAeskAI 1317
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREA---RD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1318 RLGKELSSA----ESQLHDTQ-----ELLQEETRAKLALGS-RVRALEAEAAG-LREQMEEEVVARERAGRELQSTQAQL 1386
Cdd:pfam12128 408 RQLAVAEDDlqalESELREQLeagklEFNEEEYRLKSRLGElKLRLNQATATPeLLLQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1387 SewrRRQEEEAAvleageearrraareaetLTQRLAEKTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRK 1465
Cdd:pfam12128 488 E---RLQSELRQ------------------ARKRRDQASEALRQASRRLEERQSALDELeLQLFPQAGTLLHFLRKEAPD 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1466 FDQLLAE--EKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVgknvheL 1543
Cdd:pfam12128 547 WEQSIGKviSPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREK------Q 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1544 ERARKAAEQAASDLRTQVTELEDELTAAEDAKL---RLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEverde 1620
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD----- 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1621 eRKQRALamaarkkleleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEETRSSrdemftlsrenekKLKGLEA 1700
Cdd:pfam12128 696 -KKHQAW-------------------------LEEQKEQKREARTEKQAYWQVVEGALDA-------------QLALLKA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1701 EVLRLQEELAASDRARRQaQQDRDEMAEEVASGNLSKAATleEKRQLEGRLSQLEEELEEEQNNSELLKDHYR----KLV 1776
Cdd:pfam12128 737 AIAARRSGAKAELKALET-WYKRDLASLGVDPDVIAKLKR--EIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1777 LQVESLTTELSAER----SFSAKAESGRQQLERQIQELRA---RLGEEDAGARARQKMLIaalESKLAQAEEQLEQESRE 1849
Cdd:pfam12128 814 TQLSNIERAISELQqqlaRLIADTKLRRAKLEMERKASEKqqvRLSENLRGLRCEMSKLA---TLKEDANSEQAQGSIGE 890
|
730 740
....*....|....*....|.
gi 28801584 1850 RILSGKLVRRAEKRLKEVVLQ 1870
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVKK 911
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1653-1943 |
1.56e-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: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1653 KEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAasdrarRQAQQDRDEMAEEVAS 1732
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ------LRVKEKIGELEAEIAS 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1733 GNLSKAATLEEKRQLEGRLSQleeeleeeqnnselLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRA 1812
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAK--------------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1813 RLGEEDAGARArqkmliaaLESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRL 1892
Cdd:TIGR02169 372 ELEEVDKEFAE--------TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1893 KQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
862-1392 |
1.60e-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: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 862 RQDEVLQARAQELQKvqELQQQSAREVG---ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL--- 935
Cdd:COG3096 525 EQRLRQQQNAERLLE--EFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 936 -------VVTELEARVGEEEECSRQLQSEKKRLQQHIQELEshLEAEEGARQKLQLEKVTTEAKMKKFEED--LLLLEDq 1006
Cdd:COG3096 603 awlaaqdALERLREQSGEALADSQEVTAAMQQLLEREREAT--VERDELAARKQALESQIERLSQPGGAEDprLLALAE- 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1007 nsklskerRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEdRLKKEEKGRQE-------LEKLKRRLDGESSE 1079
Cdd:COG3096 680 --------RLGGVLLSEIYDDVTLEDAPYFSALYGPARHAIVVPDLS-AVKEQLAGLEDcpedlylIEGDPDSFDDSVFD 750
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1080 LQEQ----MVEQKQRAEEL-----LAQLGRKEDELQAALLRAEEEGGAR--AQLLKSLREAQAgLAEAQEDLEAERVARA 1148
Cdd:COG3096 751 AEELedavVVKLSDRQWRYsrfpeVPLFGRAAREKRLEELRAERDELAEqyAKASFDVQKLQR-LHQAFSQFVGGHLAVA 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1149 KAEkqrrDLGEELEAL---RGELEDTLDSTNAQ-QELRSKREQ---EVTELKKALeeeSRAHEVSMQELRQRhSQALVEM 1221
Cdd:COG3096 830 FAP----DPEAELAALrqrRSELERELAQHRAQeQQLRQQLDQlkeQLQLLNKLL---PQANLLADETLADR-LEELREE 901
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1222 AEQLEQARRGKGVWEKTRLSLEAEVSELK---AELSSLQTSRQEGEQKRRRLESQ---LQEVQGRS-----SDSERARSE 1290
Cdd:COG3096 902 LDAAQEAQAFIQQHGKALAQLEPLVAVLQsdpEQFEQLQADYLQAKEQQRRLKQQifaLSEVVQRRphfsyEDAVGLLGE 981
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1291 AA-------EKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLR 1362
Cdd:COG3096 982 NSdlneklrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeAEERARIRR 1061
|
570 580 590
....*....|....*....|....*....|....
gi 28801584 1363 EQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1392
Cdd:COG3096 1062 DELHEELSQnrsrRSQLEKQLTRCEAEMDSLQKR 1095
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
857-1235 |
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 28801584 857 LLQVTRQDEVLQARAQELQKVQELQQQSARE------VGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:pfam09731 72 VSAVTGESKEPKEEKKQVKIPRQSGVSSEVAeeekeaTKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NS 1008
Cdd:pfam09731 152 KDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHldNV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1009 KLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQK 1088
Cdd:pfam09731 232 EEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1089 QRAEELLAQlgrkedelqaallRAEEEGGARAQLLKSLREAQAgLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1168
Cdd:pfam09731 312 KHIERALEK-------------QKEELDKLAEELSARLEEVRA-ADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1169 EDTLDSTNAQQELRSKREQEvTELKKALEEESRAHEVSMQELRQR---HSQALVEMAEQLEQARRGKGVW 1235
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQLW 446
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1016-1305 |
2.44e-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: 52.72 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1016 LLEERLAEFSSQAAEEEEkvksLNKLRLKyeATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1095
Cdd:pfam05667 208 LLERNAAELAAAQEWEEE----WNSQGLA--SRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1096 AQLGRKEDELQA-----------ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRrdLGEELE 1162
Cdd:pfam05667 282 SSFSGSSTTDTGltkgsrfthteKLQFTNEAPAATSSPPTKVETEEELQQQREEELEElqEQLEDLESSIQE--LEKEIK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1163 ALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAhEVSMQELR---QRHSQALVEMAEQleqarrgkgvWEKTR 1239
Cdd:pfam05667 360 KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDA-EENIAKLQalvDASAQRLVELAGQ----------WEKHR 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1240 LSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVqgrssdSERARSeAAEKLQRAQAELESV 1305
Cdd:pfam05667 429 VPLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEV------AEEAKQ-KEELYKQLVAEYERL 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1282-1500 |
2.54e-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: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1282 SDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGL 1361
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1362 REQMEEEVVARERAGR----ELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRR 1437
Cdd:COG4942 103 KEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28801584 1438 LQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALS 1500
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
855-1167 |
2.96e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 855 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERT-RLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELV----------VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMKKF 996
Cdd:pfam02029 105 ENNEEEensswekeekRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 997 EEDLLLLEDQNSKLSKERRLLEERlaefSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGE 1076
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVK----SQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1077 SSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggaraqllkslreaqaglaeaQEDLEAERVARAKAEKQRRD 1156
Cdd:pfam02029 261 ESEEFEKLRQKQQEAELELEELKKKREERRK--LLEEEE---------------------QRRKQEEAERKLREEEEKRR 317
|
330
....*....|.
gi 28801584 1157 LGEELEALRGE 1167
Cdd:pfam02029 318 MKEEIERRRAE 328
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
858-1393 |
3.12e-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: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 858 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQ------GRVAQLEEER-TRLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRdekkglGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELELVVTELEarVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVT-------TEAKMKKFEE----- 998
Cdd:TIGR00606 478 QELRKAERELS--KAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmemlTKDKMDKDEQirkik 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 999 ----DLLL-----------LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKK---EE 1060
Cdd:TIGR00606 556 srhsDELTsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDvcgSQ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1061 KGRQELEKLKRRLDGES---------SELQEQMVEQK-----------QRAEELLAQLGRKEDELQAALLRAEEEGGARA 1120
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSkqramlagaTAVYSQFITQLtdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1121 QLLKSL---REAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDT---LDSTNAQQELRSKREQEVT--- 1190
Cdd:TIGR00606 716 SELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKlQKVNRDIQRLKNDIEEQetlLGTIMPEEESAKVCLTDVTime 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1191 ELKKALEEESRAHE------------VSMQELRQR---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1255
Cdd:TIGR00606 796 RFQMELKDVERKIAqqaaklqgsdldRTVQQVNQEkqeKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQ 875
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1256 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE------AAEKLQRAQAEL-ESVSTALSEAESKAIRLGKELSSAES 1328
Cdd:TIGR00606 876 IGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHG 955
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1329 QLHDTQELLQEETRAKLalgsrvRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQ 1393
Cdd:TIGR00606 956 YMKDIENKIQDGKDDYL------KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1093 |
3.25e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 852 IKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERtrlaeqlraeaelcSEAEETRARLAARKQ 931
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL--------------DELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 932 ELEL-VVTELEARVGEEEECSRQ---LQSEKKRLQQHIQELESHLEAEEGARQKLQLEKvtteakmKKFEEDLLLLEDQN 1007
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETE-------KRLEELRKELEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1008 SKLSKER-RLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgESSELQEQMVE 1086
Cdd:PRK03918 654 KKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKK 732
|
....*..
gi 28801584 1087 QKQRAEE 1093
Cdd:PRK03918 733 YKALLKE 739
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1014-1196 |
4.43e-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: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1014 RRLLEerLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMveqkQRAEE 1093
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----KKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1094 LLAQlGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLD 1173
Cdd:COG1579 81 QLGN-VRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 28801584 1174 stnaqqELRSKREQEVTELKKAL 1196
Cdd:COG1579 160 ------ELEAEREELAAKIPPEL 176
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1064-1400 |
4.46e-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: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1064 QELEKLKRRLDGESSELQEQMVE-QKQRAE--ELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAGLAEAQEDL 1140
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAyGKLRRElaGLTRRLSAAEGELEELVARL-------AKLEAALREAEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1141 EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKA---LEEESRAHEVSMQELRQRHSQA 1217
Cdd:pfam19220 114 RDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERlalLEQENRRLQALSEEQAAELAEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1218 LVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQR 1297
Cdd:pfam19220 194 TRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1298 AQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALeAEAAGLREqmeeevVARERAGR 1377
Cdd:pfam19220 274 RDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML-TKALAAKD------AALERAEE 346
|
330 340
....*....|....*....|...
gi 28801584 1378 ELQSTQAQLSEWRRRQEEEAAVL 1400
Cdd:pfam19220 347 RIASLSDRIAELTKRFEVERAAL 369
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
927-1355 |
4.53e-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: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 927 AARKQELE---LVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGArqKLQLEKVTTEAKMKKfeedllll 1003
Cdd:pfam05701 28 AHRIQTVErrkLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEEL--KLNLERAQTEEAQAK-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1004 edQNSKLSKER-RLLEERLAEFSSQAAEEEEKVkslnkLRLKYEATISDMedRLKKEEKG--RQELEKLKRRLDGESSEL 1080
Cdd:pfam05701 98 --QDSELAKLRvEEMEQGIADEASVAAKAQLEV-----AKARHAAAVAEL--KSVKEELEslRKEYASLVSERDIAIKRA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1081 QEQMVEQKQ---RAEELLAQLGRKEDEL---QAALLRAEEE--GGARA------QLLKSLREAQAGLAEAQEDLEAERVA 1146
Cdd:pfam05701 169 EEAVSASKEiekTVEELTIELIATKESLesaHAAHLEAEEHriGAALAreqdklNWEKELKQAEEELQRLNQQLLSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1147 RAKAEKQRR---DLGEELEA---------LRGELEDTLDSTNAQQELRSKREqEVTELKKALEEES------RAHEVSMQ 1208
Cdd:pfam05701 249 KSKLETASAlllDLKAELAAymesklkeeADGEGNEKKTSTSIQAALASAKK-ELEEVKANIEKAKdevnclRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1209 ELRQRHSQALVEMaeqleqaRRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEvqgrssdserAR 1288
Cdd:pfam05701 328 SELEKEKAELASL-------RQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQ----------AA 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1289 SEAAEKLQRAQAELESVSTALSEAE-SKAirlgkELSSAESQLHDTQ-ELLQEETRAKLALGSrVRALE 1355
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEqAKA-----AASTVESRLEAVLkEIEAAKASEKLALAA-IKALQ 453
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
865-1388 |
4.79e-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: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 865 EVLQARA-------QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVV 937
Cdd:COG3096 406 DVQQTRAiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 938 TELEArvGEEEECSRQL---QSEKKRLQQHIQELESHL-EAEEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQNSKLs 1011
Cdd:COG3096 486 GEVER--SQAWQTARELlrrYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAEL- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1012 kerrllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLkRRLDGESSELQEQMVEQKQRA 1091
Cdd:COG3096 563 ------EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERL-REQSGEALADSQEVTAAMQQL 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1092 EELLAQLGRKEDELQAALLRAEEE-------GGARAQLLKSLREAQAG--LAEAQEDLEAE-------RVARAKAEKQRR 1155
Cdd:COG3096 636 LEREREATVERDELAARKQALESQierlsqpGGAEDPRLLALAERLGGvlLSEIYDDVTLEdapyfsaLYGPARHAIVVP 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1156 DLGEELEALRGeLEDTL--------------DSTNAQQEL-------------------------RSKREQEVTELKKAL 1196
Cdd:COG3096 716 DLSAVKEQLAG-LEDCPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAER 794
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1197 EEESRAHEVSMQELR--QRHSQALVE-MAEQLEQARRGKGvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQ 1273
Cdd:COG3096 795 DELAEQYAKASFDVQklQRLHQAFSQfVGGHLAVAFAPDP--EAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQ 872
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1274 LQEVQGRSS-------DSERARSEAAE----KLQRAQAELESVSTALSEAESKAIRL------GKELSSAESQLHDTQEL 1336
Cdd:COG3096 873 LQLLNKLLPqanlladETLADRLEELReeldAAQEAQAFIQQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRR 952
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1337 LQEETRAKLALGSRVRALE-AEAAG-----------LREQMEEEVVARERAGRELQSTQAQLSE 1388
Cdd:COG3096 953 LKQQIFALSEVVQRRPHFSyEDAVGllgensdlnekLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1033-1309 |
4.86e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.69 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1033 EKVKSLnklrlkyEATISDMEDRLK-KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1111
Cdd:pfam00038 18 DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1112 AEEEGGARaqllkslREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELED--------------------- 1170
Cdd:pfam00038 91 YEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEevrelqaqvsdtqvnvemdaa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1171 -TLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwekTRLSLEAEVSEL 1249
Cdd:pfam00038 164 rKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28801584 1250 KAELSSLQTSRQEGEQkrrRLESQLQEVQGRSSDSERARSEAAEKLQRAQAE---LESVSTAL 1309
Cdd:pfam00038 237 KKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEMARQLREyqeLLNVKLAL 296
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
863-1590 |
5.87e-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: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 943 RVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllledqnSKLSKERRLLEERLA 1022
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI------------ERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1023 EFSSQaaeEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesselqeqmveqkQRAEELLAQLGRKE 1102
Cdd:TIGR00606 416 DLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---------------QQLEGSSDRILELD 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1103 DELQAALlrAEEEGGARAQLLKSLREAQAGLAEAQEDLeaERVARAKAEKQrRDLGEELEALRGELEDTLDSTNAQQELR 1182
Cdd:TIGR00606 478 QELRKAE--RELSKAEKNSLTETLKKEVKSLQNEKADL--DRKLRKLDQEM-EQLNHHTTTRTQMEMLTKDKMDKDEQIR 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1183 SKREQEVTEL---------KKALEEESRAHEVSMQELRQRhsqaLVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAEL 1253
Cdd:TIGR00606 553 KIKSRHSDELtsllgyfpnKKQLEDWLHSKSKEINQTRDR----LAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1254 SSLQTSRQEgEQKRRRLESQLqevqgrssdsERARSEAAeKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDT 1333
Cdd:TIGR00606 629 FDVCGSQDE-ESDLERLKEEI----------EKSSKQRA-MLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1334 QELLQEETRaklALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraare 1413
Cdd:TIGR00606 697 ISDLQSKLR---LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK------------------ 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1414 AETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGRE 1493
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1494 REARalSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNvheLERARKAAEQAAsDLRTQVTELEDELTAAED 1573
Cdd:TIGR00606 836 HELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN---LQRRQQFEEQLV-ELSTEVQSLIREIKDAKE 909
|
730
....*....|....*..
gi 28801584 1574 AKLRLEVTVQALKAQHE 1590
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKE 926
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
897-1340 |
7.25e-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: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 897 QLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 976
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 977 gaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRL 1056
Cdd:TIGR04523 180 --KEKLNIQKNIDKIKNKLLKLELLLSNLK--KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1057 KKEekgRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKEDELQAalLRAEEEggarAQLLKSLREAqagLAEA 1136
Cdd:TIGR04523 256 NQL---KDEQNKIKKQL----SEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKE----QDWNKELKSE---LKNQ 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1137 QEDLEAERVARAKAEKQRRDLGEELEALRGELEDtLDSTNA--QQELRSKrEQEVTELKKALE---EESRAHEVSMQELR 1211
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTN-SESENSekQRELEEK-QNEIEKLKKENQsykQEIKNLESQINDLE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1212 QRHSQALV---EMAEQLEQARRGKGVWEK-------TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgRS 1281
Cdd:TIGR04523 398 SKIQNQEKlnqQKDEQIKKLQQEKELLEKeierlkeTIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS-RS 476
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1282 SDSERARSEAAEK-LQRAQAELESVSTALSEAESKAirlgKELSSAESQLHDTQELLQEE 1340
Cdd:TIGR04523 477 INKIKQNLEQKQKeLKSKEKELKKLNEEKKELEEKV----KDLTKKISSLKEKIEKLESE 532
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
941-1167 |
1.08e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllEDQNSKLSKERRLLEER 1020
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAefssQAAEEEEKVKSLNKL-----------RLKYEATISDMEDRLKKE-EKGRQELEKLKRRLDGESSELQEQMVEQK 1088
Cdd:COG3883 92 AR----ALYRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLEElKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1089 QRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGE 1167
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
894-1165 |
1.13e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.46 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 894 RVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV---VTELEA---RVGEEEEcsrqLQSEKKRLQqHIQE 967
Cdd:COG0497 149 AFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLrfqLEELEAaalQPGEEEE----LEEERRRLS-NAEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 968 LeshLEAEEGARQklqlekvtteakmkkfeedlLLLEDQNS---KLSKERRLLEeRLAEFSSQAAEEEEKVKSLnklrlk 1044
Cdd:COG0497 224 L---REALQEALE--------------------ALSGGEGGaldLLGQALRALE-RLAEYDPSLAELAERLESA------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1045 yEATISDMedrlkkeekgRQELEKLKRRLDGESSELQEqmVEQKQraeELLAQLGRK----EDELqaallraeeeggarA 1120
Cdd:COG0497 274 -LIELEEA----------ASELRRYLDSLEFDPERLEE--VEERL---ALLRRLARKygvtVEEL--------------L 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 28801584 1121 QLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:COG0497 324 AYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
893-1206 |
1.63e-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: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 893 GRVAQleEERtrlAEQLRAEAElcsEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEK--KRLQQHIQELES 970
Cdd:COG3096 779 GRAAR--EKR---LEELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAelAALRQRRSELER 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 971 HLEAEEGA--RQKLQLEKVTTEAKM-KKFEEDLLLLEDQNskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1047
Cdd:COG3096 851 ELAQHRAQeqQLRQQLDQLKEQLQLlNKLLPQANLLADET--LADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAV 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1048 TISDME--DRLKKE-EKGRQELEKLKRRLD---------------------GESSELQEQMVEQKQRAEELLAQLGrkeD 1103
Cdd:COG3096 929 LQSDPEqfEQLQADyLQAKEQQRRLKQQIFalsevvqrrphfsyedavgllGENSDLNEKLRARLEQAEEARREAR---E 1005
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1104 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV-----ARAKAEKQRRDLGEELEALRG---ELEDTLDST 1175
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSrrsQLEKQLTRC 1085
|
330 340 350
....*....|....*....|....*....|.
gi 28801584 1176 NAQQELRSKREQEVTELKKALEEESRAHEVS 1206
Cdd:COG3096 1086 EAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
853-1103 |
1.89e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.93 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 853 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREvgelqgrvaQLEEERTRLAEqlrAEAELCSEAEETRA-----RLA 927
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEK---------KLEQERLRWTE---AESKWISLAEELRTeldasRAL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 928 ARKQELELvvtELEARVGEEEECSRQL--QSEKKRLQQ-------HIQELESHLEAEEGARQklqLEKVTTEAKMKKFEE 998
Cdd:PLN03188 1081 AEKQKHEL---DTEKRCAEELKEAMQMamEGHARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAES 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 999 DLL-LLEDQNSKL----SKERRLLEERLAEFSSQAAEEEEKVKSLNKL--RLK-YEATISDMEDRLKKEE----KGRQEL 1066
Cdd:PLN03188 1155 KFInALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQI 1234
|
250 260 270
....*....|....*....|....*....|....*..
gi 28801584 1067 EKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKED 1103
Cdd:PLN03188 1235 DKLKRKHENEISTLNQLVAESRLPKEAIRPACNDDCM 1271
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
954-1583 |
1.90e-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: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 954 LQSEKKRLQQHIQELESHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERRLLEERLAEFSSQAAEEEE 1033
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1034 KVKSLNKLRLKYEATISDMEDRLKKEEKGRQELeklkrRLDGESS------ELQEQMVEQKQRAEELLAQLGRKEDELQA 1107
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1108 ALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE---LRSK 1184
Cdd:pfam05483 245 LLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEdlqIATK 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1185 REQEVTELKKALEEESrahevsmQELRQRHSQALVEMaeqleqarrgkgvwEKTRLSLEaevsELkaelssLQTSRQEGE 1264
Cdd:pfam05483 325 TICQLTEEKEAQMEEL-------NKAKAAHSFVVTEF--------------EATTCSLE----EL------LRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1265 QKRRRLESQLQEVQGRSSDSErarsEAAEKLQRAQAELESVSTALSEAESkairlgkeLSSAESQLHDTQELLQEETRAK 1344
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEK--------LLDEKKQFEKIAEELKGKEQEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1345 LALgsrVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAvleageearrraareaeTLTQRLAEK 1424
Cdd:pfam05483 442 IFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTA-----------------HCDKLLLEN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1425 TEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRA 1504
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1505 LEEEQEAREELERQNRALRAELEallsskdDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEdakLRLEVTVQ 1583
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIE-------NKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE---LELASAKQ 650
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1049-1233 |
1.99e-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: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1049 ISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEeggARAQL--LKSL 1126
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1127 REAQAglaeAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEEESRAHEVS 1206
Cdd:COG1579 89 KEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 28801584 1207 MQELRQRHSQALVEMAEQL----EQARRGKG 1233
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1287-1503 |
2.06e-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: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1287 ARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1366
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1367 EEvvaRERAGRELQSTQAQlsewRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDAT 1446
Cdd:COG4942 101 AQ---KEELAELLRALYRL----GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1447 VDLgqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTR 1503
Cdd:COG4942 174 AEL---EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1003-1230 |
2.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1003 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKvksLNKLRLKYEatISDMEDRLKKEEkgrQELEKLKRRLdgesSELQE 1082
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNG--LVDLSEEAKLLL---QQLSELESQL----AEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1083 QMVEQKQRAEELLAQLGRKEDELQAALlraeeEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELE 1162
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1163 AlrgELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELR--QRHSQALVEMAEQLEQARR 1230
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 ... |
1212-1899 |
2.47e-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: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1212 QRHSQALVEMAEQLEQARRgkgvweKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARS-E 1290
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKK------KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1291 AAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLREQMEEEV 1369
Cdd:pfam02463 227 LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKlLAKEEEELKSELLKLE 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1370 VARERAGRELQSTQAQLsewrrrQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDL 1449
Cdd:pfam02463 307 RRKVDDEEKLKESEKEK------KKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1450 GQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEAL 1529
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1530 LSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAK 1609
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1610 QLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKE-LWREVEETRSSRDEMFTLS 1688
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1689 RENEKKLKGLEAEVLRLQE-ELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSEL 1767
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKEsAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1768 LKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKlaqaEEQLEQES 1847
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE----LSLKEKEL 776
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1848 RERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQL 1899
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1069-1899 |
2.61e-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: 49.58 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1069 LKRRLDGESSELQEQM-VEQKQRAEELLAQLGRKEDELQAALLRAEEE---------GGARAQLLKSLREAQAGLAEAQE 1138
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLyLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtftrvvllpQGEFAQFLKAKSKEKKELLMNLF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1139 DLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrahevsMQELRQRHSQaL 1218
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA-------LQQTQQSHAY-L 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1219 VEMAEQLEQARRgkgvWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLesqlqevqgRSSDSERARSEAAEKLQRA 1298
Cdd:TIGR00618 246 TQKREAQEEQLK----KQQLLKQLRARIEELRAQEAVLEETQERINRARKAA---------PLAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1299 QAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEEtraklalgSRVRALEAEAAGLREQMEEEVVARERAgRE 1378
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE--------IHIRDAHEVATSIREISCQQHTLTQHI-HT 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1379 LQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLST 1458
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1459 LEKKQRKFDQLLAEEKAAVLRavedreriEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGK 1538
Cdd:TIGR00618 464 SAQSLKEREQQLQTKEQIHLQ--------ETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQ 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1539 NVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKA------QHERDLQGRDDAGEERRRQLAKQLR 1612
Cdd:TIGR00618 536 TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdipnlqNITVRLQDLTEKLSEAEDMLACEQH 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1613 DAEVERDEERKQRALAMAARKKLeleleelkaqtsaagqgKEEAVKQLKKMQVQMKELWREVEET-RSSRDEMFTLSREN 1691
Cdd:TIGR00618 616 ALLRKLQPEQDLQDVRLHLQQCS-----------------QELALKLTALHALQLTLTQERVREHaLSIRVLPKELLASR 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1692 EKKLKGLEAEVLRL---QEELAASDRARRQAQQDRDEMAEEVasgNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSell 1768
Cdd:TIGR00618 679 QLALQKMQSEKEQLtywKEMLAQCQTLLRELETHIEEYDREF---NEIENASSSLGSDLAAREDALNQSLKELMHQA--- 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1769 KDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEedagararqkmliaaleskLAQAEEQLEQESR 1848
Cdd:TIGR00618 753 RTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------------------LKTLEAEIGQEIP 813
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1849 ERILsgklvrraEKRLKEVVLQVDEErrvadQVRDQLEKSNLRLKQLKRQL 1899
Cdd:TIGR00618 814 SDED--------ILNLQCETLVQEEE-----QFLSRLEEKSATLGEITHQL 851
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
865-1276 |
2.64e-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: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 865 EVLQARAQELQKVQELQQQS-AREVGELQgrvaQLEEERTRLAEQLraeaeLCSEAEETRA---RLAARKQELELVVTEL 940
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEEElTRKIQPSD----SLEPEFPKKCRSL-----LNRWREKVFAlmvQLKAQDLEHRDSVKQL 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 EARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIW 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1021 LAEFSSQAAEEEEKVKSLNKlRLKYEA----TISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLA 1096
Cdd:pfam07111 417 LETTMTRVEQAVARIPSLSN-RLSYAVrkvhTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1097 QLGRKEDELQAALLRAEEEGGA-RAQLLKSLREAQAGLAEAQEDLEAervarakaekqrrdLGEELE-ALRGELEDTLDS 1174
Cdd:pfam07111 496 ELQLSAHLIQQEVGRAREQGEAeRQQLSEVAQQLEQELQRAQESLAS--------------VGQQLEvARQGQQESTEEA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1175 TNAQQELRSKRE-------QEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAE-QLEQARRGKGVWEKTRLSLEAEv 1246
Cdd:pfam07111 562 ASLRQELTQQQEiygqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEAR- 640
|
410 420 430
....*....|....*....|....*....|
gi 28801584 1247 selKAELSSLQTSRQEGEQKRRRLESQLQE 1276
Cdd:pfam07111 641 ---KEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1347-1863 |
2.78e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1347 LGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEeaavleageearrraareAETLTQRLAEKTE 1426
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE------------------LETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1427 AVERLerarrrlQQELDDATVDLGQQKQLLSTLEKKQrkfDQLLAEekAAVLRAveDRERIEAEGREREARALSLTRALE 1506
Cdd:PRK02224 266 TIAET-------EREREELAEEVRDLRERLEELEEER---DDLLAE--AGLDDA--DAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1507 EEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALK 1586
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1587 AQHERDLQGRDDAGE------------ERRRQLAKQLRDA----EVERDEERKQRALAMAARKKLELELEELKAQTSAAG 1650
Cdd:PRK02224 412 DFLEELREERDELREreaeleatlrtaRERVEEAEALLEAgkcpECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1651 QGKEEAVKQLKkmqvQMKELWREVEETRSSRDEMFTLSRENEKKL--KGLEAEVLRLQ-EELAASDRARRQAQQDRDEMA 1727
Cdd:PRK02224 492 EEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIeeKRERAEELRERaAELEAEAEEKREAAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1728 EEVAsgnlSKAATLEEKRQ-LEGRLSQLeeeleeeqnnsellkDHYRKLVLQVESLTTELSAERS-FSAKAESGRQQLER 1805
Cdd:PRK02224 568 EEAR----EEVAELNSKLAeLKERIESL---------------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER 628
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1806 qIQELRAR---LGEEDAGARarqkmlIAALESKLAQAEEQLEQesreriLSGKLVRRAEKR 1863
Cdd:PRK02224 629 -LAEKRERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREER 676
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1177-1398 |
3.09e-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: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1177 AQQELRSKREQEVTELKKALEEESRAHEvSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSL 1256
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1257 QTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQEL 1336
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1337 LQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAA 1398
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1519-1943 |
3.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1519 NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHE-RDLQGRD 1597
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1598 DAGEERRRQLAKQLRD-AEVERDEERKQRALAMAARKKLELELeelkAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEE 1676
Cdd:COG4717 149 EELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATE----EELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1677 TRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEE 1756
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1757 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKaesgrqQLERQIQELRARLgeEDAGARARQKMLIAALESKL 1836
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELL------DRIEELQELLREA--EELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1837 AQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNL--RLKQLKRQLEEAEEEASRAQAGRR 1914
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|.
gi 28801584 1915 RLQRELEDVTESAE--SMNREVTTLRNRLRR 1943
Cdd:COG4717 457 ELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
904-1229 |
3.43e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 904 RLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVgEEEECSrqLQSEKKRLQQhiqELESHLEAeegARQKLQ 983
Cdd:PLN03188 898 RLVQQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFL-EEELAS--LMHEHKLLKE---KYENHPEV---LRTKIE 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 984 LEKVTTEAK-MKKF----EEDLLLLEDQNSKLS-------------KERRLLEERLAEFSSQA--------AEEEEKVKS 1037
Cdd:PLN03188 969 LKRVQDELEhYRNFydmgEREVLLEEIQDLRSQlqyyidsslpsarKRNSLLKLTYSCEPSQApplntipeSTDESPEKK 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1038 LNKLRLKYEATISD---MEDRLKKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQKQRAEELLAQLGRKEDELQA 1107
Cdd:PLN03188 1049 LEQERLRWTEAESKwisLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYADLEEKHIQLLA 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1108 ALLRAEE------EGGARAqllkSLREAQAGLAEAqedLEAERVA-RAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:PLN03188 1129 RHRRIQEgiddvkKAAARA----GVRGAESKFINA---LAAEISAlKVEREKERRYLRDENKSLQAQLRDTAEAVQAAGE 1201
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1181 L--RSKREQE--VTELKKALEEESRAHEV--SMQELRQRHSQALVEMAEQLEQAR 1229
Cdd:PLN03188 1202 LlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESR 1256
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1163 |
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 28801584 1003 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgRQELEKLKRRLDGESSELQE 1082
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYEALQKEIES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1083 QMVEQKQRAEELLAQLGRKEdELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAErvaRAKAEKQRRDLGEELE 1162
Cdd:COG1579 101 LKRRISDLEDEILELMERIE-ELEEELAELEAE---LAELEAELEEKKAELDEELAELEAE---LEELEAEREELAAKIP 173
|
.
gi 28801584 1163 A 1163
Cdd:COG1579 174 P 174
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
952-1098 |
3.60e-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: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 952 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL---------SKERRLLEERLA 1022
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1023 EFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKgrqELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1098
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEA---ELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-976 |
3.71e-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: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 856 PLLQVTRQDEVLQArAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 935
Cdd:COG4942 121 PLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 28801584 936 VVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEE 976
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1043-1164 |
3.91e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1043 LKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLgrkEDELQAALLRAEEEGgarAQL 1122
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 28801584 1123 LKSLREAQAGLAEAQedleaervARAKAEKQRRDLGEELEAL 1164
Cdd:PRK00409 590 IKELRQLQKGGYASV--------KAHELIEARKRLNKANEKK 623
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1072-1229 |
4.00e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.04 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1072 RLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAE 1151
Cdd:PRK09039 57 RLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1152 KQRRDLGEELEALR---GELEDTLDstnaqqelrskreqevtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQA 1228
Cdd:PRK09039 137 AQVELLNQQIAALRrqlAALEAALD---------------------ASEKRDRESQAKIADLGRRLNVALAQRVQELNRY 195
|
.
gi 28801584 1229 R 1229
Cdd:PRK09039 196 R 196
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
947-1097 |
4.29e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 947 EEECSRQLQSEKKRLQQHIQELEshLEA-EEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQnskLSKERRLLEERLAE 1023
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEAL--LEAkEEIHKLRNEFEKELRErrNELQKLEKRLLQKEEN---LDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1024 FSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLK------KEEKGRQELEKLKRRLDGESSELQEQMVEQ-----KQRAE 1092
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEEakeeaDKKAK 191
|
....*
gi 28801584 1093 ELLAQ 1097
Cdd:PRK12704 192 EILAQ 196
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
860-1313 |
4.75e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.67 E-value: 4.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 860 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAElcSEAEETRARLAArkqELELVVTE 939
Cdd:NF041483 436 VELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAK--ADADELRSTATA---ESERVRTE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 940 LEARVG----EEEECSRQLQSEKKRLQQHIQEL--ESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsklske 1013
Cdd:NF041483 511 AIERATtlrrQAEETLERTRAEAERLRAEAEEQaeEVRAAAERAARELREETERAIAARQAEAAEELTRLHTE------- 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1014 rrlLEERLAefssqAAEEEEKVKSLNKLRLKYEATisdmedrlkkEEKGRQELEKLKRRldgesSELQEQMVEQKQR-AE 1092
Cdd:NF041483 584 ---AEERLT-----AAEEALADARAEAERIRREAA----------EETERLRTEAAERI-----RTLQAQAEQEAERlRT 640
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1093 ELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArAKAEKQRRDLGEELEALRGELEDTL 1172
Cdd:NF041483 641 EAAADASAARAEGENVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERVG-TEAAEALAAAQEEAARRRREAEETL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1173 DS--TNAQQELRSKREQEVTELKKALE--EESRAHEVSMQELRQRHSQALVEMAEQLEQARRGK--GVWEKTrlslEAEV 1246
Cdd:NF041483 720 GSarAEADQERERAREQSEELLASARKrvEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSvaGLQEQA----EEEI 795
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1247 SELK--AELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELE-SVSTALSEAE 1313
Cdd:NF041483 796 AGLRsaAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAKALAErTVSEAIAEAE 865
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
863-1154 |
4.77e-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: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAAR-----KQELELVV 937
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEErekteKLKVEEEK 792
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 938 TELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEA--EEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1015
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQEL 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1016 LLEERLAEFSSQAAEEEEKVKSLNKLRlkyeatisdmEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1095
Cdd:pfam02463 873 LLKEEELEEQKLKDELESKEEKEKEEK----------KELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1096 AQlgRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR 1154
Cdd:pfam02463 943 EE--ADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
862-1201 |
4.91e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 862 RQDEVLQARAQELQKVQELQQQSAREVGELQGRVaQLEEERTRLAEQLRAEAElcseaeETRARLAARKQELELVVTELE 941
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMI-QNAEKNILLLNQARLQAL------EDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 942 ARVGEEEECSRQLQSEKKrlqqHIQELESHLEAeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1021
Cdd:PLN02939 177 MRLSETDARIKLAAQEKI----HVEILEEQLEK---LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1022 AEFssqaAEEEEKVKSLNKLRLKYEATISDMEDRLkkeekgrqeleklkrrldgesSELQEQMVEQKQRAEELLAQlgrK 1101
Cdd:PLN02939 250 IEV----AETEERVFKLEKERSLLDASLRELESKF---------------------IVAQEDVSKLSPLQYDCWWE---K 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1102 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRdLGEELEALRGELEDTLDSTNAQQEL 1181
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQL 380
|
330 340
....*....|....*....|
gi 28801584 1182 RSKREQEVTELKKALEEESR 1201
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESK 400
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1030-1143 |
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 28801584 1030 EEEEKV----KSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDgesSELQEQMVEQKQRAEELLAQLgRKEDEL 1105
Cdd:PRK00409 513 EDKEKLneliASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ---EEEDKLLEEAEKEAQQAIKEA-KKEADE 588
|
90 100 110
....*....|....*....|....*....|....*...
gi 28801584 1106 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE 1143
Cdd:PRK00409 589 IIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
897-1295 |
5.26e-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: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 897 QLEEERTRLAEQL-----RAEAElcSEAEETRARLAARKQELELvvtELEARVGEEEECSRQLQSEKKRLQQHIQELESH 971
Cdd:pfam15818 1 QLLDFKTSLLEALeelrmRREAE--TQYEEQIGKIIVETQELKW---QKETLQNQKETLAKQHKEAMAVFKKQLQMKMCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 972 LEAEEGarqKLQLEKVTTEAKMKKFEEDLLLLedQNSKLSKERRLLE-ERLAEFSSQAAEEEEKvkSLNKLRlKYEATIS 1050
Cdd:pfam15818 76 LEEEKG---KYQLATEIKEKEIEGLKETLKAL--QVSKYSLQKKVSEmEQKLQLHLLAKEDHHK--QLNEIE-KYYATIT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1051 DMEDRLK----KEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQaalLRAEEEggaraQLLKSL 1126
Cdd:pfam15818 148 GQFGLVKenhgKLEQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQ---YKMGEE-----NINLTI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1127 REAQagLAEAQEDLEAERVARAKaekqrrdLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELK---KALEEESRAH 1203
Cdd:pfam15818 220 KEQK--FQELQERLNMELELNKK-------INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEaelKALKENNQTL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1204 EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSR--------QEGEQKRRRLESQLQ 1275
Cdd:pfam15818 291 ERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHiklqehynKLCNQKKFEEDKKFQ 370
|
410 420
....*....|....*....|
gi 28801584 1276 EVQGRSSDSERARSEAAEKL 1295
Cdd:pfam15818 371 NVPEVNNENSEMSTEKSENL 390
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
849-1043 |
5.46e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 849 RLFIKVKPLLQVTRQD----EVLQARAQELQKVQELQQQSAREVGE--------------------------LQGRVAQL 898
Cdd:PRK04863 918 NALAQLEPIVSVLQSDpeqfEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyedaaemlaknsdlnekLRQRLEQA 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 899 EEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE-----EEECSRQLQSEKKRLQQHIQELESHLE 973
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANRSRRN 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 974 AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSK------------ERRLLEERLAEFSSQAAEEEEKvKSLN 1039
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQvvNAKAGWcavlrlvkdngvERRLHRRELAYLSADELRSMSD-KALG 1156
|
....
gi 28801584 1040 KLRL 1043
Cdd:PRK04863 1157 ALRL 1160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1111-1452 |
6.37e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1111 RAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVT 1190
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1191 ELKKALEEESRAHEVSMQELRQRhSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRL 1270
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1271 ESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSR 1350
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1351 VRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVER 1430
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340
....*....|....*....|..
gi 28801584 1431 LERARRRLQQELDDATVDLGQQ 1452
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQ 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1013-1206 |
7.22e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1013 ERRLLEERLAEFSSQAAEEEEKVKSLNKlrlKYEATISDMEDRLKKEEKGRQELEKLKRRLDgessELQEQMVEQKQRAE 1092
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA---ELEELNEEYNELQAELEALQAEIDKLQAEIA----EAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1093 ELLAQLGRKEDELQ--AALLRAEEEG-------------GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDL 1157
Cdd:COG3883 90 ERARALYRSGGSVSylDVLLGSESFSdfldrlsalskiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 28801584 1158 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVS 1206
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1254-1464 |
8.23e-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: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1254 SSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSE---------AAEKLQRAQAELESVSTALSEAESKAIRLGKELS 1324
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1325 SAESQLHDTQELLQE--ETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLsewrrrQEEEAAVLEA 1402
Cdd:COG3206 244 ALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQL------QQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1403 GEEARRRAAREAETLTQRLAEKTEAVerleRARRRLQQELDDATVDLGQQKQLLSTLEKKQR 1464
Cdd:COG3206 318 LEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1047-1364 |
8.66e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 8.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1047 ATISDME---DRLKKEEKGRQELEKLKRRLDGESSELQEqmveqkqrAEELLAQLGRKEDELQAALLRAEEeggaRAQLL 1123
Cdd:PRK11281 60 LVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQ--------AQAELEALKDDNDEETRETLSTLS----LRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1124 KSLREAQAGLAEAQEDLEaervarakaekqrrDLGEELEALRGELEdtldstNAQQEL--RSKREQEVTELKKALEEESR 1201
Cdd:PRK11281 128 SRLAQTLDQLQNAQNDLA--------------EYNSQLVSLQTQPE------RAQAALyaNSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1202 AHEVSMQELRQRHsQALVEMaeQLEQARRgkgvwektrlslEAEVSELKAELssLQTSRQEGEQKRRRLESQLQEVQGRS 1281
Cdd:PRK11281 188 ALRPSQRVLLQAE-QALLNA--QNDLQRK------------SLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1282 SDSERARSEA-AEKLQRAQAELESVSTALSEAESKA-IRLGKELSSAESQLHdtqELLQEETRAKLALGsrvRALEAEAA 1359
Cdd:PRK11281 251 NSKRLTLSEKtVQEAQSQDEAARIQANPLVAQELEInLQLSQRLLKATEKLN---TLTQQNLRVKNWLD---RLTQSERN 324
|
....*
gi 28801584 1360 gLREQ 1364
Cdd:PRK11281 325 -IKEQ 328
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
857-1136 |
9.60e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 9.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEVLQARAQELQKVQELQ------QQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaeetrarlaark 930
Cdd:COG0497 137 LLDPDAQRELLDAFAGLEELLEEYReayrawRALKKELEELRADEAERARELDLLRFQL--------------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 931 QELElvvtELEARVGEEEEcsrqLQSEKKRLQ------QHIQELESHLEAEEG--------ARQKLQlEKVTTEAKMKKF 996
Cdd:COG0497 196 EELE----AAALQPGEEEE----LEEERRRLSnaeklrEALQEALEALSGGEGgaldllgqALRALE-RLAEYDPSLAEL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 997 EEDL----LLLEDQNSKLSKERRLLE---ERLAEFssqaaeeEEKVKSLNKLRLKYEATISDMedrLKKEEKGRQELEKL 1069
Cdd:COG0497 267 AERLesalIELEEAASELRRYLDSLEfdpERLEEV-------EERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1070 krrldgesselqeqmveqkQRAEELLAQLGRKEDELQAALLRAeeeggarAQLLKSLREAQAG-LAEA 1136
Cdd:COG0497 337 -------------------ENSDERLEELEAELAEAEAELLEA-------AEKLSAARKKAAKkLEKA 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1498-1738 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1498 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLR 1577
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1578 LEVTVQALKAQHerdlqgrddagEERRRQLAKQLR---------------DAEVERDEERKQRALAMAARKKLELELEEL 1642
Cdd:COG4942 88 LEKEIAELRAEL-----------EAQKEELAELLRalyrlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1643 KAQTSAAGQgKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQD 1722
Cdd:COG4942 157 ADLAELAAL-RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*.
gi 28801584 1723 RDEMAEEVASGNLSKA 1738
Cdd:COG4942 236 AAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1706-1948 |
1.61e-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: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1706 QEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTE 1785
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1786 LSAERSFSAKAESGRQQLERQiQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLK 1865
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1866 EVVLQVDEERRVADQVRDQLEKsnlRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1945
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 28801584 1946 LTF 1948
Cdd:COG4942 255 LPW 257
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
857-1082 |
1.97e-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: 45.96 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEER---TRLAEQLRAEAE----------LCSEAEETR 923
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLlelTRVNELLKAKFSedgtqkkmssLSMELMKLR 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 924 ARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE 998
Cdd:pfam15905 166 NKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLleyitELSCVSEQVEKYKLDI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 999 DLL--LLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKeekgrqELEKLKRRLDGE 1076
Cdd:pfam15905 246 AQLeeLLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNA------ELEELKEKLTLE 319
|
....*.
gi 28801584 1077 SSELQE 1082
Cdd:pfam15905 320 EQEHQK 325
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
940-1194 |
2.09e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 940 LEARVGEEEECSRQLQSEKKRLQQHI---QELESHLEAEEGAR-QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR 1015
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIktyNKNIEEQRKKNGENiARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1016 LLEERLAEFSSQAAEEEEKVKSLNKLRLKYE---------ATISDMEDRLkkeEKGRQELEKLKRRLDgessELQEQMVE 1086
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQISEGPDRI---TKIKDKLKELQHSLE----KLDTAIDE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1087 QKQRAEElLAQLGRKEDELQAALlraEEEGGARAQLLKSLREAQAglaeAQEDLEAERVARAkaekqrrdlgEELEALRG 1166
Cdd:PHA02562 325 LEEIMDE-FNEQSKKLLELKNKI---STNKQSLITLVDKAKKVKA----AIEELQAEFVDNA----------EELAKLQD 386
|
250 260
....*....|....*....|....*...
gi 28801584 1167 ELEDtLDSTNAQQELRSKREQEVTELKK 1194
Cdd:PHA02562 387 ELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1660-1966 |
2.13e-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: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1660 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAA 1739
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1740 TLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDA 1819
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1820 GARARQKMlIAALESKLAQAE------EQLEQE---SRERI-LSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSN 1889
Cdd:pfam07888 207 QVLQLQDT-ITTLTQKLTTAHrkeaenEALLEElrsLQERLnASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1890 LRLKQLKRQLeeaEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRgpltftTRTVRQVFRLEEGVASD 1966
Cdd:pfam07888 286 LQLADASLAL---REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE------ERMEREKLEVELGREKD 353
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
670-694 |
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 28801584 670 YKESLSRLMATLSNTNPSFVRCIVP 694
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
923-1194 |
2.32e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 923 RARLAARKQELELVVTEL-EARVGEEEECSRQLQSEKKR--------LQQHIQELESHLEAEEGarqklqLEKVTTEAKM 993
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALhELGVVHIEDLKEELSNERLRklrslltkLSEALDKLRSYLPKLNP------LREEKKKVSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 994 KKFEEdllLLEDQNSKLSK-ERRL--LEERLAEFssqaaEEEEKVKSLNKLRLKYEATIsDMEDRLKKEEK------GRQ 1064
Cdd:PRK05771 82 KSLEE---LIKDVEEELEKiEKEIkeLEEEISEL-----ENEIKELEQEIERLEPWGNF-DLDLSLLLGFKyvsvfvGTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1065 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAE------EEGGARAQLLKSLREAQAGLaeaqe 1138
Cdd:PRK05771 153 PEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGferlelEEEGTPSELIREIKEELEEI----- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1139 dleaervarakaEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKK 1194
Cdd:PRK05771 228 ------------EKERESLLEELKELAKKYLEELLALYEYLEIELERAEALSKFLK 271
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1707-1943 |
2.41e-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: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1707 EELAASDRARRQAQQDRDEMaeEVASGNLSKA-ATLEEKRQLEGRLSQLEEELEEEQNNSELLKD-HYRKLVLQVESLTT 1784
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEEL--EEVEENIERLdLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1785 ELSAERSFSAKAESGRQQLERQIQELRARLGE----------------EDAGARARQKML-----IAALESKLAQAEEQL 1843
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTEEISELEKRLEEieqlleelnkkikdlgEEEQLRVKEKIGeleaeIASLERSIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1844 EQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDV 1923
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260
....*....|....*....|
gi 28801584 1924 TESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02169 398 KREINELKRELDRLQEELQR 417
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1579 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 980 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKlrlkyEATISDMEDRLKKE 1059
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNS-----DLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1060 EKGR--QELEKLKRRLDgESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEggaRAQLLKSLREAQAGLAEAQ 1137
Cdd:TIGR04523 118 QKNKleVELNKLEKQKK-ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE---LNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1138 EDLEAER----VARAKAEKQRRDLGE--ELEALRGELEDTLdstnaqQELRSKREQEVTELKKALEEESRAHEVSMQELR 1211
Cdd:TIGR04523 194 NKLLKLElllsNLKKKIQKNKSLESQisELKKQNNQLKDNI------EKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1212 QrhsqaLVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQTSRQEGEQKrrRLESQLQEVQGRSSDSERARSEA 1291
Cdd:TIGR04523 268 Q-----LSEKQKELEQN-------NKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQN 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1292 AEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAE---AAGLREQMEEE 1368
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnQEKLNQQKDEQ 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1369 VVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERL----ERARRRLQQELDD 1444
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKS 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1445 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNR--AL 1522
Cdd:TIGR04523 494 KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieEL 573
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1523 RAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLE 1579
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
868-1396 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 868 QARAQELQKVQELQQQS------------AREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELEL 935
Cdd:pfam07111 136 EGSQRELEEIQRLHQEQlssltqaheealSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 936 VVTELEA---RVGEE---EECSRQLQSEKKRLQQHIQELESHleaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsk 1009
Cdd:pfam07111 216 QVTLVESlrkYVGEQvppEVHSQTWELERQELLDTMQHLQED-------RADLQATVELLQVRVQSLTHMLALQEEE--- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1010 lskerrlLEERLAEFSSQAAEEEEKVKSLnkLRLKYEATISDMEDRLKKEEKGRQELEKLKrrldGESSELQEQMVEQKQ 1089
Cdd:pfam07111 286 -------LTRKIQPSDSLEPEFPKKCRSL--LNRWREKVFALMVQLKAQDLEHRDSVKQLR----GQVAELQEQVTSQSQ 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1090 RaeellaqlgrkedelQAALLRAEEEGGARAQLLK-SLREAQAGLAEAQEdleaervARAKAEKQRRDLGEELEALRGEL 1168
Cdd:pfam07111 353 E---------------QAILQRALQDKAAEVEVERmSAKGLQMELSRAQE-------ARRRQQQQTASAEEQLKFVVNAM 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1169 EDTLDSTNAQQELRSKREQEVTELKKALEEESR---------AHEVSMQELRQRHS-------QALVEMAEQLEQARRgk 1232
Cdd:pfam07111 411 SSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRkvhtikglmARKVALAQLRQESCpppppapPVDADLSLELEQLRE-- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1233 gvwEKTRLSLEAEVSELKAElSSLQTSRQEGEQKRRRLESQLQEVQgrssdserarseaaEKLQRAQAELESVSTALSEA 1312
Cdd:pfam07111 489 ---ERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLE--------------QELQRAQESLASVGQQLEVA 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1313 eskaiRLGKELSSAESQlHDTQELLQEETRAKLALGSRVRALEAEaagLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1392
Cdd:pfam07111 551 -----RQGQQESTEEAA-SLRQELTQQQEIYGQALQEKVAEVETR---LREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
....
gi 28801584 1393 QEEE 1396
Cdd:pfam07111 622 ATQE 625
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1738-1943 |
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 28801584 1738 AATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEe 1817
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1818 dagARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKR 1897
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 28801584 1898 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
890-1194 |
2.95e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 890 ELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE 969
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 970 SHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1049
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1050 SDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELlaqlgRKEdelqaallraeeeggaraqllksLREA 1129
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADEL-----RKE-----------------------ADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1130 QAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLdSTNAQQELRSKREQEVTELKK 1194
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEEIFEKLKK 278
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
956-1730 |
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 28801584 956 SEKKRLQQHIQELES---HLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1032
Cdd:TIGR00606 166 SEGKALKQKFDEIFSatrYIKALETLRQVRQ----TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1033 EKVKSLNKLRLKYE------ATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQ 1106
Cdd:TIGR00606 242 SYENELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1107 AALLRAEEEGGARAQLLkSLREAQAGLAEAQEDLEAERVaraKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKre 1186
Cdd:TIGR00606 322 VDCQRELEKLNKERRLL-NQEKTELLVEQGRLQLQADRH---QEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF-- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1187 qeVTELKKALEEESRAHEVSMQELRQRHSQALvEMAEQLEQARRGKG-VWEKTRLSLEAEVSELKAELSSLQTSRQ---- 1261
Cdd:TIGR00606 396 --HTLVIERQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKGLGrTIELKKEILEKKQEELKFVIKELQQLEGssdr 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1262 --EGEQKRRRLESQLQEVQGRSSDSERARSEAAekLQRAQAELESVSTALSE----------AESKAIRLGKELSSAESQ 1329
Cdd:TIGR00606 473 ilELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKDEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1330 LHDTQELLQEETRAKLALGSRVRALEAEAAGLRE---QMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEA 1406
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1407 RRRAAREAETLtQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQ----LLSTLEKKQRKFDQLLAEEKAAVLRAVE 1482
Cdd:TIGR00606 631 VCGSQDEESDL-ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1483 DRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS----KDDVGKNVHELERArKAAEQAASDLR 1558
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDiqrlKNDIEEQETLLGTI-MPEEESAKVCL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1559 TQVTELEDELTAAEDAKLRLEVTVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERD--EERKQRALAMAARKKL 1635
Cdd:TIGR00606 789 TDVTIMERFQMELKDVERKIAQQAAKLQGSDlDRTVQQVNQEKQEKQHELDTVVSKIELNRKliQDQQEQIQHLKSKTNE 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1636 ELELEELKAQTSAAGQGKEEavkQLKKMQVQMKELWREVEEtrsSRDEMFTLSRENEKKLKGLEAEVLRLQEElaasdra 1715
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEE---QLVELSTEVQSLIREIKD---AKEQDSPLETFLEKDQQEKEELISSKETS------- 935
|
810
....*....|....*
gi 28801584 1716 RRQAQQDRDEMAEEV 1730
Cdd:TIGR00606 936 NKKAQDKVNDIKEKV 950
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
892-1059 |
3.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 892 QGRVAQLEEERTRLAEQLRAEAELCSEAEETRArlaarKQELELVVTELEARVGEEEecsRQLQSEKKRLQQHIQELESH 971
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA-----KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 972 LEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLeERLAEFSSQAAEEE--EKVKSlnklRLKYEA-- 1047
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEK---KEEELEELIEEQLQEL-ERISGLTAEEAKEIllEKVEE----EARHEAav 173
|
170
....*....|..
gi 28801584 1048 TISDMEDRLKKE 1059
Cdd:PRK12704 174 LIKEIEEEAKEE 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
865-1392 |
3.85e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 865 EVLQARAQEL-QKVQELQQQ--SAREVGELQGRVAQL------EEERTRLAEQLRaeaELCSEAEETRArLAARKQELEL 935
Cdd:PRK04863 445 EEFQAKEQEAtEELLSLEQKlsVAQAAHSQFEQAYQLvrkiagEVSRSEAWDVAR---ELLRRLREQRH-LAEQLQQLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 936 VVTELEARVGEEEECSRQLQSEKKRLQQHIQ---ELESHLEAEEGARQKLQLEKVTTEAK---MKKFEEDLLLLEDQNSK 1009
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrmaLRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1010 LSKERRLLEERLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQeqmveqkQ 1089
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDV-------TEYMQQLLERERELTVERDELAARKQALDEEIERLS-------Q 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1090 RAEELLAQLGRKEDELQAALLrAE-------EE--------GGARAQL----LKSLREAQAGLAEAQEDL---------- 1140
Cdd:PRK04863 667 PGGSEDPRLNALAERFGGVLL-SEiyddvslEDapyfsalyGPARHAIvvpdLSDAAEQLAGLEDCPEDLyliegdpdsf 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1141 -----EAERVARAKAEKQ-----------------RRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKALEE 1198
Cdd:PRK04863 746 ddsvfSVEELEKAVVVKIadrqwrysrfpevplfgRAAREKRIEQLRAEREEL-------AERYATLSFDVQKLQRLHQA 818
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1199 ESR---AH---------EVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSL------------------------ 1242
Cdd:PRK04863 819 FSRfigSHlavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladrvee 898
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1243 ------EAEV------------SELKAELSSLQTSRQEGEQKRRR---LESQLQEVQGRS---------------SDSER 1286
Cdd:PRK04863 899 ireqldEAEEakrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDyqqAQQTQRDAKQQAfaltevvqrrahfsyEDAAE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1287 ARSEAAE-------KLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEA 1358
Cdd:PRK04863 979 MLAKNSDlneklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgAEERA 1058
|
650 660 670
....*....|....*....|....*....|....*...
gi 28801584 1359 AGLREQMEEEVVA----RERAGRELQSTQAQLSEWRRR 1392
Cdd:PRK04863 1059 RARRDELHARLSAnrsrRNQLEKQLTFCEAEMDNLTKK 1096
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
917-1148 |
4.16e-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: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 917 SEAEETRARLAARKQELELVVTELEArvgeeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF 996
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDA-----------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 997 EEDL----LLLEDQNSKLSKERRLLE--------ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQ 1064
Cdd:COG3883 85 REELgeraRALYRSGGSVSYLDVLLGsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1065 ELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAER 1144
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
....
gi 28801584 1145 VARA 1148
Cdd:COG3883 245 SAAG 248
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1136-1347 |
4.92e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1136 AQEDLEAERVARAKAEKQRRDLGEELealRGELEdtldstnAQQELRSKREQEVTELKKALEEESRAHEVSMQ------- 1208
Cdd:PLN03188 1045 PEKKLEQERLRWTEAESKWISLAEEL---RTELD-------ASRALAEKQKHELDTEKRCAEELKEAMQMAMEgharmle 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1209 ---ELRQRHSQALVEMAEQLE--------QARRG-KGVWEKTRLSLEAEVSELKAElsslqtsrqeGEQKRRRLESQLQE 1276
Cdd:PLN03188 1115 qyaDLEEKHIQLLARHRRIQEgiddvkkaAARAGvRGAESKFINALAAEISALKVE----------REKERRYLRDENKS 1184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1277 VQGRSSDSERARSEAAEKLQRAQAELESVSTALS---EAESKAIRLGKELSSA----ESQLHDTQELLQEETRAKLAL 1347
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKramDAEQEAAEAYKQIDKLkrkhENEISTLNQLVAESRLPKEAI 1262
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
865-1166 |
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 28801584 865 EVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARV 944
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 945 GEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEF 1024
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1025 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1104
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1105 LQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1166
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1129-1385 |
6.30e-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: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1129 AQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEesrahevsmq 1208
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1209 eLRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAE-VSELkaeLSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERA 1287
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDF---LDRLSALSKIADADADLLEELKADKA----ELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1288 RSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEE 1367
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*...
gi 28801584 1368 EVVARERAGRELQSTQAQ 1385
Cdd:COG3883 229 AAAAAAAAAAAAAAAASA 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
867-1366 |
6.33e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 867 LQARAQELQKVQELQQQSAREVGELQGRVAQLEE-ERTRLAEQLRAEAELCSEAEEtrarlaarKQELELVVTELEArvg 945
Cdd:PRK01156 178 LRAEISNIDYLEEKLKSSNLELENIKKQIADDEKsHSITLKEIERLSIEYNNAMDD--------YNNLKSALNELSS--- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 946 eeeecsrqLQSEKKRLQQHIQELESHLEAEEGARQKL-----QLEKVTTEAKMKKFEE---------DLL----LLEDQN 1007
Cdd:PRK01156 247 --------LEDMKNRYESEIKTAESDLSMELEKNNYYkeleeRHMKIINDPVYKNRNYindyfkyknDIEnkkqILSNID 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1008 SKLSKERRLLE--ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV 1085
Cdd:PRK01156 319 AEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1086 EQKQRAEELLAQLgrkeDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV--------ARAKAEKQRRDL 1157
Cdd:PRK01156 399 IQEIDPDAIKKEL----NEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlGEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1158 GEELEALRGEL--------------------------EDTLDSTNAQQELRSKREQ------EVTELK----KALEEESR 1201
Cdd:PRK01156 475 NEKKSRLEEKIreieievkdidekivdlkkrkeylesEEINKSINEYNKIESARADledikiKINELKdkhdKYEEIKNR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1202 AHEVSMQELRQRHSQALVEMAE----QLEQARRGKGVWEKTRLSLEAEVSELKAEL----SSLQTSRQEGEQKRRRLESQ 1273
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNALAVisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFpddkSYIDKSIREIENEANNLNNK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1274 LQEVQGRSSDSERARsEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRA 1353
Cdd:PRK01156 635 YNEIQENKILIEKLR-GKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570
....*....|...
gi 28801584 1354 LEAEAAGLREQME 1366
Cdd:PRK01156 714 LSDRINDINETLE 726
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1602-1925 |
6.45e-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: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1602 ERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMkelwREVEETRSSR 1681
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1682 DEMftlsRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAsgNLSKAATLEEKR-----QLEGRLSQLEE 1756
Cdd:COG3096 354 EDL----EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQTRaiqyqQAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1757 ELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQKMLIAALE 1833
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1834 SKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEksnlrlkQLKRQLEEAEEEASRAQAGR 1913
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQR 580
|
330
....*....|..
gi 28801584 1914 RRLQRELEDVTE 1925
Cdd:COG3096 581 SELRQQLEQLRA 592
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
896-1255 |
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 28801584 896 AQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAE 975
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 976 EGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDR 1055
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1056 LKKEEKGRQELEKLKRRldgesSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE 1135
Cdd:COG4372 166 LAALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1136 AQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHS 1215
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 28801584 1216 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1255
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
875-1155 |
8.68e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 875 QKVQELQQqsarEVGELQGRVAQLEEERTRLAEQLRAEAELCSEA----EETRARLAARKQELELV---VTELEARVGEE 947
Cdd:PRK11637 47 DQLKSIQQ----DIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrklRETQNTLNQLNKQIDELnasIAKLEQQQAAQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 948 EE-CSRQLQSeKKRLQQHiQELESHLEAEEGARQK--LQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERLAEF 1024
Cdd:PRK11637 123 ERlLAAQLDA-AFRQGEH-TGLQLILSGEESQRGEriLAYFGYLNQARQETIAE----LKQTREELAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1025 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrqeleklkrrldgesselQEQMVEQKQraeellaqlgrKEDE 1104
Cdd:PRK11637 197 KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD---------------------QQQLSELRA-----------NESR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 28801584 1105 LQAALLRAEEEGGARAQllkslREAQaglaeaqedlEAERVARAKAEKQRR 1155
Cdd:PRK11637 245 LRDSIARAEREAKARAE-----REAR----------EAARVRDKQKQAKRK 280
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1238-1622 |
8.70e-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: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1238 TRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERARSEAAEKLQRAQAELESVStALSEAESKAI 1317
Cdd:COG5185 185 TLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKA----KEIINIEEALKGFQDPESELEDLA-QTSDKLEKLV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1318 RLGKELSsaESQLHDTQELLQeetraklalgsRVRALEAEAAGLREQMEEEVVARERAG---RELQSTQAQLSEWRRRQE 1394
Cdd:COG5185 260 EQNTDLR--LEKLGENAESSK-----------RLNENANNLIKQFENTKEKIAEYTKSIdikKATESLEEQLAAAEAEQE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1395 EEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDlgqqkQLLSTLEKKQRKFDQLLAEEK 1474
Cdd:COG5185 327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELD-----SFKDTIESTKESLDEIPQNQR 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1475 AA---VLRAVEDRERIEAEGREREARALsltraleeeqearEELERQNRALRAELEALLSSKDDVGKNVHELERAR--KA 1549
Cdd:COG5185 402 GYaqeILATLEDTLKAADRQIEELQRQI-------------EQATSSNEEVSKLLNELISELNKVMREADEESQSRleEA 468
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28801584 1550 AEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEER 1622
Cdd:COG5185 469 YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1012-1227 |
8.98e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.30 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1012 KERRLLEERLAEFSSQAAEEEEK-------VKSLNKLRLKyeatiSDMEDRLKKE-------EKGRQELEKLKRRLDGES 1077
Cdd:COG0497 165 RAWRALKKELEELRADEAERAREldllrfqLEELEAAALQ-----PGEEEELEEErrrlsnaEKLREALQEALEALSGGE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1078 SELQEQMveqkQRAEELLAQLGRKEDELQAALLRAEEeggARAQLlkslREAQAGLAEAQEDLEA---------ERVARA 1148
Cdd:COG0497 240 GGALDLL----GQALRALERLAEYDPSLAELAERLES---ALIEL----EEAASELRRYLDSLEFdperleeveERLALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1149 KAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEEsrAHEVSmqELRQRHSQALVE-MAEQLE 1226
Cdd:COG0497 309 RRLARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEA--AEKLS--AARKKAAKKLEKaVTAELA 384
|
.
gi 28801584 1227 Q 1227
Cdd:COG0497 385 D 385
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1104-1276 |
8.99e-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: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1104 ELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtlDSTNAQQELRS 1183
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK---KYEEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 KREQEvtelkkALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEG 1263
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|...
gi 28801584 1264 EQKRRRLESQLQE 1276
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
872-1155 |
9.71e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 872 QELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRaeaELCSEAEETRARlaaRKQELELVvtelearvgeeeecs 951
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK---ELREEAQELREK---RDELNEKV--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 952 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEE 1031
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1032 EEKVKSLNKLRLKyeatISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLR 1111
Cdd:COG1340 149 LEKAKKALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 28801584 1112 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1155
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1216-1350 |
1.08e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1216 QALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLqtsrqegEQKRRRLESQLQEVQGrssdserARSEAAEKL 1295
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-------EAERSRLQALLAELAG-------AGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1296 QRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ------EETRAKLA-LGSR 1350
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDasekrdRESQAKIAdLGRR 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1417-1626 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1417 LTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREA 1496
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1497 RALSLTRALEEEQEAREELERQ----NRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAE 1572
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1573 DAKLRLEVTVQALKAQhERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA 1626
Cdd:COG4942 192 ALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
900-1297 |
1.23e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 900 EERTRLAEQLRAEAELCSEAEETRARLAARKQELelvvTELEARVGEEEEC-SRQLQSEKKRLQQHIQEleshleAEEGA 978
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSEL----KPSGQGGLDEEEAfLDRTAKREERRQKRLQE------ALERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 979 RQklqLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLlEERLAEfssqAAEEEEKVKSLNKLRLKYEATISDMEDRLKK 1058
Cdd:pfam02029 87 KE---FDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQAEEEGEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1059 EEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQE 1138
Cdd:pfam02029 159 EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1139 DLEAERVARAKAEKQRRDLGEelealrgeledtldstnaqqelrsKREQEvtelkkaleeesrahevsMQELRQRHSQAL 1218
Cdd:pfam02029 239 EAEVFLEAEQKLEELRRRRQE------------------------KESEE------------------FEKLRQKQQEAE 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 28801584 1219 VEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAelsslqtsrQEGEQKRRRLEsqlqevqgrssDSERARSEAAEKLQR 1297
Cdd:pfam02029 277 LELEELKKKREERRKLLEEEEQRRKQEEAERKL---------REEEEKRRMKE-----------EIERRRAEAAEKRQK 335
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
882-1170 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 882 QQSAREVGELQGRVAQLEEERTRLAEQLRAeaelcseaeeTRARLAARKQELELVV----TELEARVGEEEECSRQLQSE 957
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQ----------LKEQLQLLNKLLPQANlladETLADRLEELREELDAAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 958 KKRLQQH---IQELESHLEA--------EEGARQKLQLEKVTTEAKMKKFE-------------EDLLLLEDQNSKLSKE 1013
Cdd:COG3096 909 QAFIQQHgkaLAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1014 rrlLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLkkeEKGRQELEKLKRRLD---------------GESS 1078
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEelgvqadaeaeerarIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1079 ELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAE-----AQEDLEAERVARA----K 1149
Cdd:COG3096 1063 ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAvlrlaRDNDVERRLHRRElaylS 1142
|
330 340
....*....|....*....|.
gi 28801584 1150 AEKQRRDLGEELEALRGELED 1170
Cdd:COG3096 1143 ADELRSMSDKALGALRLAVAD 1163
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
873-1051 |
1.27e-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: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 873 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcSEAEETRARLAARKQELELVVTELEARVGEEEECSR 952
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARL-------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 953 QLQSEKKrLQQHIQELESHleaeegARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1032
Cdd:COG1579 84 NVRNNKE-YEALQKEIESL------KRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*....
gi 28801584 1033 EKVKSLNKLRLKYEATISD 1051
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1102-1377 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1102 EDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQEL 1181
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1182 RSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRgkgvwektrlSLEAEVSELKAELSSLQTSRQ 1261
Cdd:COG3883 95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKA----------ELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1262 EGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEET 1341
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
250 260 270
....*....|....*....|....*....|....*.
gi 28801584 1342 RAKLALGSRVRALEAEAAGLREQMEEEVVARERAGR 1377
Cdd:COG3883 245 SAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1941 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1653 KEEAVKQLKKMQVQMKELWREVEETRSSR----DEMFTLSRENEKKLKGLEAEVLRLQEElaasDRARRQAQQDRDEMAE 1728
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1729 EVasgnlSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQ 1808
Cdd:pfam17380 373 EI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1809 ELRARLGEEDagaRARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRA-EKRLKEVVLQVDEERRVADQVRDQLEK 1887
Cdd:pfam17380 448 MERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1888 snlrlkqlkRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1941
Cdd:pfam17380 525 ---------RQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
859-1139 |
1.38e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:COG4372 60 ELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 939 ELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1018
Cdd:COG4372 140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1019 ERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQL 1098
Cdd:COG4372 220 LLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA 299
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 28801584 1099 GRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQED 1139
Cdd:COG4372 300 LLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1057-1313 |
1.39e-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: 43.26 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1057 KKEEKGRQELEKLKRrLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREaqagLAEA 1136
Cdd:pfam15905 63 KKSQKNLKESKDQKE-LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLE----LTRV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1137 QEDLEAeRVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEV-TELKKALEEESRAHE--VSMQELRQR 1213
Cdd:pfam15905 138 NELLKA-KFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTqKNLEHSKGKVAQLEEklVSTEKEKIE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1214 ---HSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQK-RRRLESQLQEVQGRSSDSERARS 1289
Cdd:pfam15905 217 eksETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQElSKQIKDLNEKCKLLESEKEELLR 296
|
250 260
....*....|....*....|....
gi 28801584 1290 EAAEKLQRAQAELESVSTALSEAE 1313
Cdd:pfam15905 297 EYEEKEQTLNAELEELKEKLTLEE 320
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1076-1530 |
1.44e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1076 ESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAgLAEAQEDLEAERVAR---AKAEK 1152
Cdd:COG3899 763 EAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALA-LAERLGDRRLEARALfnlGFILH 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1153 QRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGK 1232
Cdd:COG3899 842 WLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARL 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1233 GVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELEsvsTALSEA 1312
Cdd:COG3899 922 AAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALE---AAAAAL 998
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1313 ESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRR 1392
Cdd:COG3899 999 LALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAA 1078
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1393 QEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAE 1472
Cdd:COG3899 1079 AAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLA 1158
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1473 EKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1530
Cdd:COG3899 1159 LALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
857-1125 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELV 936
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 937 VTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL-LEDQNSKLSKERR 1015
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLkYEEEPEELLLEEA 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1016 LLEERLAEFSSQaaEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELL 1095
Cdd:pfam02463 946 DEKEKEENNKEE--EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
250 260 270
....*....|....*....|....*....|
gi 28801584 1096 AQLGRKEDELQAalLRAEEEGGARAQLLKS 1125
Cdd:pfam02463 1024 ELFVSINKGWNK--VFFYLELGGSAELRLE 1051
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1208-1380 |
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 28801584 1208 QELRQRHSqalvemAEQLEQARRGkgvwektRLSLEAEVSELKAElsslqtsrqegEQKRRRLESQLQEVQGRSSDSERA 1287
Cdd:PTZ00491 664 QEAAARHQ------AELLEQEARG-------RLERQKMHDKAKAE-----------EQRTKLLELQAESAAVESSGQSRA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1288 RSEAaeklqRAQAELESVSTALSEAE--SKAIRLGKELSSAESQLHDTQELLQEETRAKLALgSRVRAL-EAEAAGLREQ 1364
Cdd:PTZ00491 720 EALA-----EAEARLIEAEAEVEQAElrAKALRIEAEAELEKLRKRQELELEYEQAQNELEI-AKAKELaDIEATKFERI 793
|
170 180
....*....|....*....|
gi 28801584 1365 ME----EEVVARERAGRELQ 1380
Cdd:PTZ00491 794 VEalgrETLIAIARAGPELQ 813
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1778-1921 |
1.63e-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: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1778 QVESLTTELSAERSFSAKAESGRQQLERQIQelrarlGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLV 1857
Cdd:COG3206 220 QLSELESQLAEARAELAEAEARLAALRAQLG------SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV 293
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 28801584 1858 RRAEKRLKEVVLQVDEE-RRVADQVRDQLEKSNLRLKQLKRQLEE---AEEEASRAQAGRRRLQRELE 1921
Cdd:COG3206 294 IALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQleaRLAELPELEAELRRLEREVE 361
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1256-1887 |
1.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1256 LQTSRQEGEQKRRRLESQLQevqgrssdserARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHD--- 1332
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIK-----------RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKElee 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1333 TQELLQEETRAKLALGSRVRALEAEAAGLREQMEEevvaRERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAR 1412
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEE----LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1413 EAETLTqRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFdqllaeEKAAVLRAVEDRERIEAEGR 1492
Cdd:PRK03918 312 IEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY------EEAKAKKEELERLKKRLTGL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1493 EREAralsltraleeeqeareelerqnraLRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDeltaae 1572
Cdd:PRK03918 385 TPEK-------------------------LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK------ 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1573 dAKLRLEVTVQALKAQHERDLQGRDDAG-----------EERRRQLAKQLRDAEVERDEERKQRALAMAARKKlelelee 1641
Cdd:PRK03918 434 -AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiEEKERKLRKELRELEKVLKKESELIKLKELAEQL------- 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1642 lkaqtsaagqgkEEAVKQLKKMQVQ-MKELWREVEETRSsrdemftLSRENEKKLKGLEAEVLRLQE---ELAASDRARR 1717
Cdd:PRK03918 506 ------------KELEEKLKKYNLEeLEKKAEEYEKLKE-------KLIKLKGEIKSLKKELEKLEElkkKLAELEKKLD 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1718 QAQQDRDEMAEEVASGNLSKAATLEEK-RQLEGRLSQLEEELEEEQNNSELLKdhyrklvlQVESLTTELSAERSFSAKA 1796
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERlKELEPFYNEYLELKDAEKELEREEK--------ELKKLEEELDKAFEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1797 ESGRQQLERQIQELRARLGEEDAgARARQKMLiaALESKLAqaeeqleqesrerilsgklvrRAEKRLKEVVLQVDEERR 1876
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEEY-EELREEYL--ELSRELA---------------------GLRAELEELEKRREEIKK 694
|
650
....*....|.
gi 28801584 1877 VADQVRDQLEK 1887
Cdd:PRK03918 695 TLEKLKEELEE 705
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
863-1107 |
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 28801584 863 QDEVLQARAQELQKV--QELQQQSARevgeLQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVvtel 940
Cdd:pfam13166 262 GQPLPAERKAALEAHfdDEFTEFQNR----LQKLIEKVESAISSLLAQLPAVSDLASLLSAFELDVEDIESEAEVL---- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 941 earvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAK--MKKFEEDLLLLEDQNSKLSKERRLLE 1018
Cdd:pfam13166 334 ----------NSQLDGLRRALEAKRKDPFKSIELDSVDAKIESINDLVASINelIAKHNEITDNFEEEKNKAKKKLRLHL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1019 erLAEFSSQAAEEEEKVKSLnklrlkyEATISDMEDRLKKEEKgrqELEKLkrrlDGESSELQEQMVEQKQRAEE---LL 1095
Cdd:pfam13166 404 --VEEFKSEIDEYKDKYAGL-------EKAINSLEKEIKNLEA---EIKKL----REEIKELEAQLRDHKPGADEinkLL 467
|
250
....*....|..
gi 28801584 1096 AQLGRKEDELQA 1107
Cdd:pfam13166 468 KAFGFGELELSF 479
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1439-1700 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1439 QQELDDATVDLGQQKQLLSTLEKKQRKFDQ---LLAEEKAAVLRAVEDRERIEAEGREREAR-------ALSLTRALEEE 1508
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRqaaIYAEQERMAMERERELERIRQEERKRELErirqeeiAMEISRMRELE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1509 QEAREELErQNRALRAELEALLSSK-------DDVGKNVHELERARKAAEQAAS-DLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam17380 382 RLQMERQQ-KNERVRQELEAARKVKileeerqRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQQ 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1581 TVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQ 1659
Cdd:pfam17380 461 QVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 28801584 1660 LKKMQVQMKE------LWREVEETRSSRD------EMFTLSRENEKKLKGLEA 1700
Cdd:pfam17380 541 ERRKQQEMEErrriqeQMRKATEERSRLEamererEMMRQIVESEKARAEYEA 593
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1129-1400 |
1.93e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1129 AQAGLAEAQEDL--EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQevtelkkaleeesrahevs 1206
Cdd:PRK11281 24 SAFARAASNGDLptEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQ------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1207 mqeLRQRHSQAlvemAEQLEQARRgkgvwEKTRLSlEAEVSELKAELSSLQTsrqegeqkrRRLESQLQEVQgrssdser 1286
Cdd:PRK11281 85 ---LKQQLAQA----PAKLRQAQA-----ELEALK-DDNDEETRETLSTLSL---------RQLESRLAQTL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1287 arseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQM 1365
Cdd:PRK11281 135 ------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQN 208
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 28801584 1366 EEEvvARERAGRE-LQST-QAQ---LSEWRRRQEEEAAVL 1400
Cdd:PRK11281 209 DLQ--RKSLEGNTqLQDLlQKQrdyLTARIQRLEHQLQLL 246
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1071-1695 |
2.02e-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: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1071 RRLDGESSELQEQMVEQKQRAEELLAQLgrkedelqAALLRAEEEGGARAQllkSLREAQAGlaeaqedleAERVARAKA 1150
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMEL--------DALAVAEKAGQAEAE---GLRAALAG---------AEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1151 EKQRRDLgEELEALrgeledtldstnaQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARR 1230
Cdd:pfam07111 136 EGSQREL-EEIQRL-------------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1231 GKGVWEKTRLSLEAEVSELKA------ELSSLQTSRQEGEQKRRRLESQLQEVQgrssdSERARSEAAEKLqrAQAELES 1304
Cdd:pfam07111 202 LRKQLSKTQEELEAQVTLVESlrkyvgEQVPPEVHSQTWELERQELLDTMQHLQ-----EDRADLQATVEL--LQVRVQS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1305 VSTALSEAESKAIRLGKELSSAESQL-HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVvareragrelqstq 1383
Cdd:pfam07111 275 LTHMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQV-------------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1384 AQLSEWRRRQEEEAAVLEageearrraareaetltQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKK- 1462
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQ-----------------RALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQl 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1463 ----------QRKFDQLLAEEKAAVLRAVEDRERIEAEGRERE------ARALSLTRALEEEQEAREELERQNRALRAEL 1526
Cdd:pfam07111 404 kfvvnamsstQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglmARKVALAQLRQESCPPPPPAPPVDADLSLEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1527 EALLSSKDDVGKNV--------HELERARKAAEQAASDLRTQVTELEDELTAAEDA----KLRLEVTVQA---------- 1584
Cdd:pfam07111 484 EQLREERNRLDAELqlsahliqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvGQQLEVARQGqqesteeaas 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1585 ----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVK-Q 1659
Cdd:pfam07111 564 lrqeLTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKeE 643
|
650 660 670
....*....|....*....|....*....|....*.
gi 28801584 1660 LKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKL 1695
Cdd:pfam07111 644 GQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
881-1068 |
2.32e-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: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 881 QQQSAREVGELQGRVAQLEEERTRLAEQLraeAELCSEAEETRARLAARKQELElvvtelearvgeeeecsrQLQSEKKR 960
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELE------------------DLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 961 LQQHIQELESHLEaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKS--- 1037
Cdd:COG1579 64 LELEIEEVEARIK-----KYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAElea 138
|
170 180 190
....*....|....*....|....*....|..
gi 28801584 1038 -LNKLRLKYEATISDMEDRLKKEEKGRQELEK 1068
Cdd:COG1579 139 eLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1109-1585 |
2.46e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1109 LLRAEEEGGARAQLLKSLRE-AQAGLAEAQEDLEAER---------VARAKAEKQRRDLGEELEALRGELEDTLDstnAQ 1178
Cdd:COG3903 456 LEVEGGGGGPRYRLLETVREyAAERLAEAGERAAARRrhadyylalAERAAAELRGPDQLAWLARLDAEHDNLRA---AL 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1179 QELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQT 1258
Cdd:COG3903 533 RWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1259 SRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1338
Cdd:COG3903 613 AAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAA 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1339 EETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLT 1418
Cdd:COG3903 693 ALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAAL 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1419 QRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEkkqrkfDQLLAEEKAAVLRAVEDRERIEAEGREREARA 1498
Cdd:COG3903 773 AALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAA------ALAAAAAAAAAAAAALAAALAAAAAAAAAAAA 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1499 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRL 1578
Cdd:COG3903 847 AAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAA 926
|
....*..
gi 28801584 1579 EVTVQAL 1585
Cdd:COG3903 927 AAAAAAA 933
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
920-1086 |
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 28801584 920 EETRARLAARKQELELVVTELEARvgeeeecSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKF--- 996
Cdd:PHA02562 205 EEQRKKNGENIARKQNKYDELVEE-------AKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFqkv 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 997 -------------------EEDLLL-LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA---TISDME 1053
Cdd:PHA02562 278 ikmyekggvcptctqqiseGPDRITkIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTnkqSLITLV 357
|
170 180 190
....*....|....*....|....*....|...
gi 28801584 1054 DRLKKEEKGRQELEKLKRRLDGESSELQEQMVE 1086
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
865-984 |
3.32e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 865 EVLQARAQELQKVQElqqQSAREVGELQGRVAQLEEERTRLAEQLRA-EAELCSEAEET-RARLAARKQELELVVTELEA 942
Cdd:PRK00409 519 NELIASLEELERELE---QKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 28801584 943 RVGEEEEC--SRQLQSEKKRLQQHIQELESHLEAEEGARQKLQL 984
Cdd:PRK00409 596 LQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1025-1150 |
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 28801584 1025 SSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDE 1104
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 28801584 1105 LQAAlLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaERVARAKA 1150
Cdd:COG2433 457 ERRE-IRKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
915-1255 |
3.63e-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: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 915 LCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE--SHLEAEEGARQKLQLEKVTTEAK 992
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIkrKKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 993 MKKFEEDLlllEDQNSKLSKERRllEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEekgrQELEKLKRR 1072
Cdd:pfam13166 167 LREIEKDN---FNAGVLLSDEDR--KAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGKS----SAIEELIKN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1073 LD-----GESSELQEQMVEQ---------KQRAEELLAQLGRKEDELQAALLR-AEEEGGARAQLLKSLreaQAGLAEAQ 1137
Cdd:pfam13166 238 PDladwvEQGLELHKAHLDTcpfcgqplpAERKAALEAHFDDEFTEFQNRLQKlIEKVESAISSLLAQL---PAVSDLAS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1138 EDLEAERvARAKAEKQRRDLGEELEALRGELE-----------------------DTLDSTNAQQELRSKREQEVTELKK 1194
Cdd:pfam13166 315 LLSAFEL-DVEDIESEAEVLNSQLDGLRRALEakrkdpfksieldsvdakiesinDLVASINELIAKHNEITDNFEEEKN 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1195 ALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSS 1255
Cdd:pfam13166 394 KAKKKLRLHLVEeFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
886-1071 |
3.95e-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: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 886 REVGELQGRVAQLEEERTRLAEQ---LRAE-AELCSEAEETRARLAARKQELELVVTELEARVGEEEECSR------QLQ 955
Cdd:COG2433 399 REKEHEERELTEEEEEIRRLEEQverLEAEvEELEAELEEKDERIERLERELSEARSEERREIRKDREISRldreieRLE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 956 SEKKRLQQHIQELESHLEAEEGARQKLQ---------LEKVTTEA------KMKKFEEDLLLLEDQNSKLSKERRLLEE- 1019
Cdd:COG2433 479 RELEEERERIEELKRKLERLKELWKLEHsgelvpvkvVEKFTKEAirrleeEYGLKEGDVVYLRDASGAGRSTAELLAEa 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1020 ------RLAEFSSQAAE------------EEEKVKSLNKL----RLKYEATISDMEDRLKKEEKgRQELEKLKR 1071
Cdd:COG2433 559 gpraviVPGELSEAADEvlfeegipvlpaEDVTIQEVDDLavvdEEELEAAIEDWEERAEERRR-EKKAEMLER 631
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
873-1316 |
4.47e-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: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 873 ELQKVQELQQQSAREVGELQGRVAQLEEERTRLA---EQLRAEAELCSEAEETRARLAARKQELELVVTELearvgeeEE 949
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQL-------QE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 950 CSRQLQSEKKRLQQHIQELESHLeAEEGARQKlQLEKVTTEAKMKKFEEDllLLEDQNSKLSKERRLLE------ERLAE 1023
Cdd:pfam05622 74 ENFRLETARDDYRIKCEELEKEV-LELQHRNE-ELTSLAEEAQALKDEMD--ILRESSDKVKKLEATVEtykkklEDLGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1024 FSSQaaeeeekVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLdgesSELQEQMVEQKQRAEELLAQLGRKED 1103
Cdd:pfam05622 150 LRRQ-------VKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1104 ELqAALLRAEEeggaraqllkSLREAQAGLAEAQEDLEAervarakAEKQRRDLGEElEALRGELEDTLDSTNAqqelrs 1183
Cdd:pfam05622 219 KL-EALQKEKE----------RLIIERDTLRETNEELRC-------AQLQQAELSQA-DALLSPSSDPGDNLAA------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1184 krEQEVTELKKALEEESraHEVSMQELRQRHS--QALVEMAEQLEQARRGK-GVWEKTRLSLEaEVSELKAELSSLQTSR 1260
Cdd:pfam05622 274 --EIMPAEIREKLIRLQ--HENKMLRLGQEGSyrERLTELQQLLEDANRRKnELETQNRLANQ-RILELQQQVEELQKAL 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1261 QEGEQKRRrlesqlqevqgRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKA 1316
Cdd:pfam05622 349 QEQGSKAE-----------DSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ 393
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1104-1395 |
4.85e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1104 ELQAALLRAEEE---GGARAQLLKSLREAQAGLAEAQEDLEAERVARakaekqRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:NF041483 82 QIQADQLRADAErelRDARAQTQRILQEHAEHQARLQAELHTEAVQR------RQQLDQELAERRQTVESHVNENVAWAE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1181 -LRSKREQEVtelkKALEEESRAhevsmqELRQRHSQALVEMAEQLEQARRgkgvwektRLSLEAEVSELKAElSSLQTS 1259
Cdd:NF041483 156 qLRARTESQA----RRLLDESRA------EAEQALAAARAEAERLAEEARQ--------RLGSEAESARAEAE-AILRRA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1260 RQEGEQKRRRLESQLQEV-----QGRSS---DSERAR--------------SEAAEKLQRAQAELESVstaLSEAESKAi 1317
Cdd:NF041483 217 RKDAERLLNAASTQAQEAtdhaeQLRSStaaESDQARrqaaelsraaeqrmQEAEEALREARAEAEKV---VAEAKEAA- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1318 rlGKELSSAESQ--------LHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAgRELQSTQAQLSEW 1389
Cdd:NF041483 293 --AKQLASAESAneqrtrtaKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKART-VAAEDTAAQLAKA 369
|
....*.
gi 28801584 1390 RRRQEE 1395
Cdd:NF041483 370 ARTAEE 375
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
902-1060 |
5.09e-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: 41.86 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 902 RTRLAEQLRAEAELCSEAEETRARLAARKQELElvvteleARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQK 981
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERA-------EKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 982 LQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----------RRLLEERLAEFSSQAAE--EEEKVKSLNKLRLKYEATI 1049
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEaeraeaekqrQKELEMQLAEEQKRLMEmaEEERLEYQRQKQEAEEKAR 491
|
170
....*....|.
gi 28801584 1050 SDMEDRLKKEE 1060
Cdd:pfam15709 492 LEAEERRQKEE 502
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
869-1154 |
5.15e-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: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 869 ARAQELQKVQELQQQsarevgelqgrvAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEE 948
Cdd:pfam15558 15 ARHKEEQRMRELQQQ------------AALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE----QRKARLGREE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 949 EcsRQLQSEKKRLQQHIQELESHLEAEEGARQKlQLEKVTTEAKMKKFEEDLLLLED---QNSKLSKERRLLEERLAEFS 1025
Cdd:pfam15558 79 R--RRADRREKQVIEKESRWREQAEDQENQRQE-KLERARQEAEQRKQCQEQRLKEKeeeLQALREQNSLQLQERLEEAC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1026 S----QAAEEEEKVKSLN-KLRLKYEATISDMEDRLKKEEKGRQ-ELEKLKRRldgeSSELQEQMVEQkqRAEELLAQLG 1099
Cdd:pfam15558 156 HkrqlKEREEQKKVQENNlSELLNHQARKVLVDCQAKAEELLRRlSLEQSLQR----SQENYEQLVEE--RHRELREKAQ 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 28801584 1100 RKEDELQAALLRAEEEGGARAQLLKSLREAqAGLAEAQEDLEAERVARAKAEKQR 1154
Cdd:pfam15558 230 KEEEQFQRAKWRAEEKEEERQEHKEALAEL-ADRKIQQARQVAHKTVQDKAQRAR 283
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
866-1327 |
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 28801584 866 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 945
Cdd:COG5278 70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 946 EEEECsRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1025
Cdd:COG5278 150 LMDEI-RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1026 SQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDEL 1105
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1106 QAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKR 1185
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1186 EQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQ 1265
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 28801584 1266 KRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAE 1327
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
1237-1388 |
5.79e-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: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1237 KTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQevqgrssdSERARSEAA----EKLQRAQAELESvstALSEA 1312
Cdd:pfam14915 56 KTVFQYNGQLNVLKAENTMLNSKLENEKQNKERLETEVE--------SYRSRLAAAiqdhEQSQTSKRDLEL---AFQRE 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 28801584 1313 ESKAIRLGKELSSAESQLHDTQELL-QEETRAKlalgSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSE 1388
Cdd:pfam14915 125 RDEWLRLQDKMNFDVSNLRDENEILsQQLSKAE----SKANSLENELHRTRDALREKTLLLESVQRDLSQAQCQKKE 197
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1128-1338 |
5.79e-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: 40.96 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1128 EAQAGLAEAQEDLEAERVARAKAEKQRRDLgeELEALRGELEDTLdstNAQQELRSKREQEVTELKKALEEESRAHE-VS 1206
Cdd:pfam17045 27 EGQTRALETRLDIREEELLSARNTLERKHK--EIGLLRQQLEELE---KGKQELVAKYEQQLQKLQEELSKLKRSYEkLQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1207 MQELRQRHSQA---------LVEMAEQLEQARRGKGVWEKTRL-------SLEAEVSELKAELSSLQTS--RQEGEQKRR 1268
Cdd:pfam17045 102 RKQLKEAREEAksreedrseLSRLNGKLEEFRQKSLEWEQQRLqyqqqvaSLEAQRKALAEQSSLIQSAayQVQLEGRKQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1269 RLESQLQEVQGRSSDSERARseaaEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQ 1338
Cdd:pfam17045 182 CLEASQSEIQRLRSKLERAQ----DSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1788-1880 |
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 28801584 1788 AERSFSAKAESGRQQLERQIQELRAR--LGEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ESRERILSGKLVRRA 1860
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|
gi 28801584 1861 EKRLKEVVLQVDEERRVADQ 1880
Cdd:PRK11448 223 DQAAKRLELSEEETRILIDQ 242
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
880-1148 |
6.58e-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: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 880 LQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEARVGEEEecSRQLQSEKK 959
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQKNGLVDLSEEAKLLLQQ--LSELESQLA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 960 RLQQHIQELESHLEAeegARQKLQLEKVTTEAkmkkfeedlLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLn 1039
Cdd:COG3206 230 EARAELAEAEARLAA---LRAQLGSGPDALPE---------LLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIAL- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1040 klrlkyeatisdmedrlkkeekgRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGAR 1119
Cdd:COG3206 297 -----------------------RAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL 353
|
250 260
....*....|....*....|....*....
gi 28801584 1120 AQLLKSLREAQAGLAEAQEDLEAERVARA 1148
Cdd:COG3206 354 RRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
919-1041 |
6.75e-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: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 919 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLE----KVTTEAKMK 994
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERElseaRSEERREIR 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 28801584 995 KfEEDLLLLEDQNSKLSKERRLLEERLAEFSsqaaEEEEKVKSLNKL 1041
Cdd:COG2433 463 K-DREISRLDREIERLERELEEERERIEELK----RKLERLKELWKL 504
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
849-957 |
7.03e-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: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 849 RLFIKVKP--LLQVTRQDEVLQARAQELQKvqELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARL 926
Cdd:COG0542 403 RMEIDSKPeeLDELERRLEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 28801584 927 AARKQELELVVTELEARVGEEEECSRQLQSE 957
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1168 |
7.03e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 857 LLQVTRQDEV--LQARAQELQKVQELQQQSAREVGELQGRV------AQLEEERTRLAEQLRAEAELCSEAEETRARLAA 928
Cdd:PRK04863 790 QLRAEREELAerYATLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 929 RKQELELV-----------VTELEARVGEEEECSRQLQSEKKRLQQH-------------IQELESHLEAEEgaRQKLQL 984
Cdd:PRK04863 870 AKEGLSALnrllprlnllaDETLADRVEEIREQLDEAEEAKRFVQQHgnalaqlepivsvLQSDPEQFEQLK--QDYQQA 947
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 985 EKVTTEAKMKKF--------------EEDLLLLE---DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEA 1047
Cdd:PRK04863 948 QQTQRDAKQQAFaltevvqrrahfsyEDAAEMLAknsDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKS 1027
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1048 TISDMEDRLKKEEkgrQELEKLKRRLDGE--------SSELQEQMVEQKQRAEELLAQLGRKEDELQAallraeeeggar 1119
Cdd:PRK04863 1028 SYDAKRQMLQELK---QELQDLGVPADSGaeerararRDELHARLSANRSRRNQLEKQLTFCEAEMDN------------ 1092
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 28801584 1120 aqLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1168
Cdd:PRK04863 1093 --LTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRREL 1139
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1029-1375 |
7.23e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1029 AEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAA 1108
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1109 LLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1188
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1189 VTELKKALEEESRAHEVS-MQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKR 1267
Cdd:COG4372 166 LAALEQELQALSEAEAEQaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1268 RRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLAL 1347
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*...
gi 28801584 1348 GSRVRALEAEAAGLREQMEEEVVARERA 1375
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1241-1352 |
7.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1241 SLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGR-SSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRL 1319
Cdd:PRK00409 524 SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEeDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAS 603
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 28801584 1320 GK--ELSSAESQLHDTQELLQE------ETRAKLALGSRVR 1352
Cdd:PRK00409 604 VKahELIEARKRLNKANEKKEKkkkkqkEKQEELKVGDEVK 644
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
952-1209 |
7.99e-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: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 952 RQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKfeedlllLEDQNSKLSKERRLLEERLAEFSSQaaee 1031
Cdd:pfam15905 83 RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------LEKQLLELTRVNELLKAKFSEDGTQ---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1032 eEKVKSLN----KLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMV-------EQKQRAEELLAQLgr 1100
Cdd:pfam15905 152 -KKMSSLSmelmKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVstekekiEEKSETEKLLEYI-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1101 keDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArakAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:pfam15905 229 --TELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
|
250 260
....*....|....*....|....*....
gi 28801584 1181 LRSKreqEVTELKKALEEESRAHEVSMQE 1209
Cdd:pfam15905 304 TLNA---ELEELKEKLTLEEQEHQKLQQK 329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1120-1942 |
8.27e-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: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1120 AQLLKSLREAQAGLAEAQEDLEaeRVARAKAEKQRR--DLGEELEALRGELEDTLDSTnAQQELRSKREQEVTELKKALE 1197
Cdd:COG3096 288 LELRRELFGARRQLAEEQYRLV--EMARELEELSAResDLEQDYQAASDHLNLVQTAL-RQQEKIERYQEDLEELTERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1198 EESrahevsmqelrqrhsQALVEMAEQLEQArrgkgvwEKTRLSLEAEVSELKAELSSLQtsRQEGEQKRRRLESQ---- 1273
Cdd:COG3096 365 EQE---------------EVVEEAAEQLAEA-------EARLEAAEEEVDSLKSQLADYQ--QALDVQQTRAIQYQqavq 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1274 -LQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKairlgkelssaesqLHDTQELLQEETRAKLALGSRVR 1352
Cdd:COG3096 421 aLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQK--------------LSVADAARRQFEKAYELVCKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1353 ALEAEAAGlreqmeeeVVARE--RAGRELQSTQAQLSEWRRRQEEeaavleageearrraareaetLTQRLAEKTEAVER 1430
Cdd:COG3096 487 EVERSQAW--------QTAREllRRYRSQQALAQRLQQLRAQLAE---------------------LEQRLRQQQNAERL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1431 LERARRRLQQELDDATvdlgQQKQLLSTLEKKQRKFDQLLAEekaavlrAVEDRERIEAEGREREARALSLTRALEEEqe 1510
Cdd:COG3096 538 LEEFCQRIGQQLDAAE----ELEELLAELEAQLEELEEQAAE-------AVEQRSELRQQLEQLRARIKELAARAPAW-- 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1511 areelerqnRALRAELEALlsskddvgknvHELERARKAAEQAASDLRTQVTELEDELTAAEDaklRLEVTVQALKAQHE 1590
Cdd:COG3096 605 ---------LAAQDALERL-----------REQSGEALADSQEVTAAMQQLLEREREATVERD---ELAARKQALESQIE 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1591 RDLQGrDDAGEERRRQLAKQL---------------------------RDAEVERDEERKQRALAmaARKKLELELEELK 1643
Cdd:COG3096 662 RLSQP-GGAEDPRLLALAERLggvllseiyddvtledapyfsalygpaRHAIVVPDLSAVKEQLA--GLEDCPEDLYLIE 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1644 AQTSAAGQGKEEAVKQLKKMQVQMKElwREVEETRSSRDEMFTlSRENEKKLKGLEAEVLRLQEELAASdRARRQAQQDR 1723
Cdd:COG3096 739 GDPDSFDDSVFDAEELEDAVVVKLSD--RQWRYSRFPEVPLFG-RAAREKRLEELRAERDELAEQYAKA-SFDVQKLQRL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1724 DEMAEEVASGNLSKA---------ATLEEKR-QLEGRLSQLEEELEEEQNNSELLKDHY---RKLVLQVESLTTELSAER 1790
Cdd:COG3096 815 HQAFSQFVGGHLAVAfapdpeaelAALRQRRsELERELAQHRAQEQQLRQQLDQLKEQLqllNKLLPQANLLADETLADR 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1791 SFSAKAESGR-QQLERQIQELRARLGEEDAgararqkmLIAALESKLAQaEEQLEQESRERILSGKLVRRAEKRLKEVVl 1869
Cdd:COG3096 895 LEELREELDAaQEAQAFIQQHGKALAQLEP--------LVAVLQSDPEQ-FEQLQADYLQAKEQQRRLKQQIFALSEVV- 964
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28801584 1870 qvdeERRVA---DQVRDQLEKSNLRLKQLKRQLEeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLR 1942
Cdd:COG3096 965 ----QRRPHfsyEDAVGLLGENSDLNEKLRARLE-------QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRD 1029
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
864-1121 |
9.02e-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: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 864 DEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLraeaelcseaEETRARLAARKQELELVVTELEAR 943
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL----------EALQAEIDKLQAEIAEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 944 VGEEEECSRQLQsekkRLQQHIQELESHLEAE--EGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1021
Cdd:COG3883 85 REELGERARALY----RSGGSVSYLDVLLGSEsfSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1022 AEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRK 1101
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260
....*....|....*....|
gi 28801584 1102 EDELQAALLRAEEEGGARAQ 1121
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 ... |
1071-1220 |
9.20e-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: 9.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28801584 1071 RRLDGESSELQEQM---VEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:pfam00529 54 TDYQAALDSAEAQLakaQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28801584 1148 AKAEKQRRDLgEELEALRGELEDTLDSTNAQQE-LRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVE 1220
Cdd:pfam00529 134 PIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLD 206
|
|
| |
