|
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 ... |
119-788 |
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: 1325.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFS 358
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 359 HEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 438
Cdd:cd14930 241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 439 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 518
Cdd:cd14930 321 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 519 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLH 598
Cdd:cd14930 401 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 599 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 678
Cdd:cd14930 481 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 679 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 758
Cdd:cd14930 561 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 327478526 759 DGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14930 641 DGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-788 |
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: 1299.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETLESLRVLGF 357
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 437
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 438 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 517
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 518 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 597
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 598 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 675
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 676 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 755
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 327478526 756 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
119-788 |
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: 1278.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQETLESLRVL 355
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 435
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 436 ADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 515
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 516 EEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK-FQRPRHLRDQADF 594
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 595 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMFRTVGQLY 674
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 675 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 754
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 327478526 755 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
865-1945 |
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: 1201.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 865 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL 944
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 945 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDR 1024
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1025 LAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGR 1104
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1105 KEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1184
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1185 LRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTAR 1264
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1265 QEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1344
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1345 TRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQR 1424
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1425 LAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALS 1504
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1505 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEV 1584
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1585 TVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQL 1664
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1665 RKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAI 1744
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1745 LEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAG 1824
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1825 ARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1904
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 327478526 1905 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1945
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-788 |
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: 1166.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 274
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 275 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLR 353
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 433
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD 593
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQ 672
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 673 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 752
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 327478526 753 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
119-788 |
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: 1128.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 269
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 270 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 348
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 349 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 428
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 429 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 508
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 509 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHL 588
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 589 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 668
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 327478526 749 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-788 |
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: 1113.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGF 357
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 437
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 438 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 517
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 518 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 597
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 598 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYK 675
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 676 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 755
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 327478526 756 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-788 |
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: 1102.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG----VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 274
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 275 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETLESLR 353
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 433
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD 593
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQL 673
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 674 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 753
Cdd:cd15896 561 YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 640
|
650 660 670
....*....|....*....|....*....|....*
gi 327478526 754 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd15896 641 PKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
119-788 |
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: 1101.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVLGF 357
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 437
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 438 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 517
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 518 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVL 597
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 598 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 675
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 676 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 755
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 327478526 756 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
108-788 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1077.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 108 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 187
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 188 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 267
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGS----GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 268 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELF 345
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiDGiDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 346 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 425
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 426 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 505
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 506 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 585
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 586 RhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGPPGGRPRRG 665
Cdd:pfam00063 475 R-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 666 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 745
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 327478526 746 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
100-800 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1003.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 100 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 179
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 180 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpGELERQLLQANPILEAFGNAKTVKNDNS 259
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 260 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 338
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTvD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 339 GQE-RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT-AAQKLCRLLGLGVTDFSRALL 416
Cdd:smart00242 235 GIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 417 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCIN 496
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 497 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQ 576
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 577 GGHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGdg 656
Cdd:smart00242 471 KKHPHFSKPK-KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS-----NAGSKK-- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 657 ppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 736
Cdd:smart00242 543 ---------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327478526 737 LFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 800
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
98-1175 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 914.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 98 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 177
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 178 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkEPGVPGELERQLLQANPILEAFGNAKTVKND 257
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-----STVEISSIEKQILATNPILEAFGNAKTVRND 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 258 NSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS 337
Cdd:COG5022 214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 338 PGQ--ERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 415
Cdd:COG5022 294 IDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 416 LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCI 495
Cdd:COG5022 373 VKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 496 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKSFVEKVAQ- 574
Cdd:COG5022 452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQr 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 575 -EQGGHPKFQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVgleqvssl 653
Cdd:COG5022 530 lNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 654 gdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP 733
Cdd:COG5022 600 ---------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 734 NRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVS 809
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 810 FQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVLQARAQELQKVQ--ELQQQ 887
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQktIKREK 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 888 SAREvgelqgrvaQLEEERARLAEQLRAEAELCaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQ 967
Cdd:COG5022 831 KLRE---------TEEVEFSLKAEVLIQKFGRS---------LKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 968 HIQELeahleaeegARQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERKLLEDRlaEFSSQAAEEEEKVKSLNKLR 1046
Cdd:COG5022 893 SISSL---------KLVNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLH 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1047 L---KYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQ--QRAEELRAQLGRKEEELQAALARAEDEGG 1121
Cdd:COG5022 961 EvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSASKIISSEST 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 1122 ARAQLLKSlreaqaALAEAQEDLESERV-ARTKAEKQRRDLGEELEALRGELEDT 1175
Cdd:COG5022 1041 ELSILKPL------QKLKGLLLLENNQLqARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
119-788 |
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: 841.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RELFQETLES 351
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 352 LRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIefEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 508
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 509 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHL 588
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 589 RDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppggrprrgmfr 668
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 tvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd00124 519 -----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 327478526 749 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
119-788 |
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 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 272
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 273 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 350
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 351 SLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 430
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 431 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 509
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHH 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 510 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR-- 586
Cdd:cd14927 399 MFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRpd 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 587 -HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRG 665
Cdd:cd14927 476 kKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 666 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 745
Cdd:cd14927 553 SFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 327478526 746 EILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14927 633 RILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
120-788 |
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: 756.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 355
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd14913 242 GFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTVD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd14913 321 QVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRDQA 592
Cdd:cd14913 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGRA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 593 D--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 670
Cdd:cd14913 476 EahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 671 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd14913 550 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 327478526 751 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
119-788 |
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: 743.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 356
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 436
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 437 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 516
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 517 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLR---DQA 592
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 593 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRRGMFRTVGQ 672
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKGGGFATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 673 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 752
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*.
gi 327478526 753 IpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
119-788 |
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: 711.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQETLESLRVLG 356
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 436
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 437 DFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 516
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 517 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD---QA 592
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGkgpEA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 593 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRRGMFRTVGQ 672
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRGSSFMTVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 673 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 752
Cdd:cd14934 544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
650 660 670
....*....|....*....|....*....|....*.
gi 327478526 753 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14934 624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
120-788 |
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: 707.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGrkEPGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQETLESLRVLG 356
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 436
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 437 DFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 515
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 516 EEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK--FQRPRhlRDQAD 593
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR--FSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrgmfRTVGQL 673
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------------KTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 674 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 753
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....*
gi 327478526 754 PKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01380 596 WLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
120-788 |
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: 694.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVL 355
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATDNAFDVL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd14917 242 GFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd14917 321 QVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD-- 590
Cdd:cd14917 399 EQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGkp 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 591 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRTV 670
Cdd:cd14917 476 EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 671 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd14917 550 SALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 327478526 751 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14917 630 AAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
119-788 |
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: 691.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA---LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 357
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 437
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 438 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 516
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 517 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD--QAD 593
Cdd:cd14929 396 EYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKkfEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrgmFRTVGQL 673
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS---FQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 674 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 753
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 327478526 754 PKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14929 627 PKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
121-788 |
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: 676.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 200
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 201 GAGKTENTKKVIQYLAHVA-SSPKGRKEPG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAvTGEKKKEESGkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRVLG 356
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIDILG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 435
Cdd:cd14918 243 FTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 436 ADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 514
Cdd:cd14918 322 VYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 515 QEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRDQAD 593
Cdd:cd14918 400 QEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKAE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 --FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRGMFRTVG 671
Cdd:cd14918 477 ahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 672 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 751
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 327478526 752 AIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14918 631 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
120-788 |
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: 675.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 276
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 277 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLRV 354
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLATDSAFDV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 433
Cdd:cd14916 242 LGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 512
Cdd:cd14916 321 QQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 513 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHL--R 589
Cdd:cd14916 399 LEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVkgK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 590 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRprrgmFRT 669
Cdd:cd14916 476 QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-----FQT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 670 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 749
Cdd:cd14916 551 VSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 327478526 750 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14916 631 PAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
120-788 |
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: 674.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 275
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 276 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETLESLR 353
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATDSAID 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 432
Cdd:cd14912 242 ILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 433 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 511
Cdd:cd14912 321 VEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRHLRD 590
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKVVKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 591 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRGMFR 668
Cdd:cd14912 476 KAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKGSSFQ 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14912 553 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 327478526 749 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
120-788 |
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: 669.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 275
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 276 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 353
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDSAIE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 432
Cdd:cd14910 242 ILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 433 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 511
Cdd:cd14910 321 VQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 590
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 591 --QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRRGMFR 668
Cdd:cd14910 476 kvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14910 551 TVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 327478526 749 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14910 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-788 |
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: 667.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGRKE--PG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 276
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 277 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------ERELFQETL 349
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 350 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 428
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 429 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 507
Cdd:cd14923 316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 508 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 586
Cdd:cd14923 394 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 587 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPGGRPRR 664
Cdd:cd14923 471 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 665 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 744
Cdd:cd14923 547 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 327478526 745 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14923 627 YRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-788 |
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: 664.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 275
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 276 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLESLR 353
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATDSAVD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 432
Cdd:cd14915 242 ILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 433 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 511
Cdd:cd14915 321 VQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRHLRD 590
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAKG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 591 QAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRRGMFR 668
Cdd:cd14915 476 KAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14915 551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 327478526 749 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14915 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
120-788 |
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: 636.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYI 276
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 277 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETLESLRV 354
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDYVQKAQ 431
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFA-EDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 432 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFnhTMF 511
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQRPR-H 587
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSgH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 588 LRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggrprrGM 666
Cdd:cd01378 468 FELrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK------------KR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 667 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 746
Cdd:cd01378 531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 327478526 747 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
120-788 |
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: 631.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 279
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 280 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLESLRVLGF 357
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 437
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 438 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 517
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 518 YQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRprhlRDQADFSVL 597
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----ERGGAFTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 598 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKES 677
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 678 LSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGF 757
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SAS 616
|
650 660 670
....*....|....*....|....*....|.
gi 327478526 758 MDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01383 617 QDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
120-788 |
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: 626.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 279
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 280 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVL 355
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKR-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 514
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 515 QEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADF 594
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 595 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLY 674
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGKPTVGDTF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 675 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 754
Cdd:cd14883 548 KHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARS 627
|
650 660 670
....*....|....*....|....*....|....
gi 327478526 755 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14883 628 ADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
119-788 |
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: 598.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVAsspkGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQHS-----WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQETLESLRVLG 356
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALK--RERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEatVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 512
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 513 LEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHlRDQ 591
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS-DLN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 592 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPrrgmfrTVG 671
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP------TLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 672 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 751
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 327478526 752 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01381 612 IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
119-788 |
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: 591.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQETLESLRVL 355
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGRD-YVQKAQ 431
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTPDgIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 432 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 511
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQ 591
Cdd:cd01384 394 KMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 592 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPRRGM-FRTV 670
Cdd:cd01384 469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTSSSSkFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 671 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 327478526 751 NAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 788
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 ... |
119-788 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 563.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETLESLRVLGF 357
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 SHEEIISMLRMVSAVLQFGNIALKRERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRIKVGRDYVQ 428
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGGAKGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 429 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 506
Cdd:cd01382 299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 507 NHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPR 586
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 587 ------H--LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQVSSLGDGPP 658
Cdd:cd01382 452 ksklkiHrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFESSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 659 GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 738
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 327478526 739 QEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
119-788 |
8.92e-178 |
|
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: 555.54 E-value: 8.92e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 193
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 194 ILCTGESGAGKTENTKKVIQYLAHVAS-----SPKGRKEPGVPGE-----LERQLLQANPILEAFGNAKTVKNDNSSRFG 263
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgASGEGEAASEAIEqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 264 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 342
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 343 ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 419
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 420 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 500 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 569
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 570 ------EKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 643
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 644 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 723
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 724 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
119-788 |
1.48e-174 |
|
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: 546.30 E-value: 1.48e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL----------FQET 348
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvddvadFEEV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 349 LESLRVLGFSHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKV-GR 424
Cdd:cd14872 222 VLAMEQLGFDDADINNVMSLIAAILKLGNIefaSGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 425 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 504
Cdd:cd14872 302 DPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 505 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQR 584
Cdd:cd14872 382 HFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVY 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 585 PRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdgppggrPRR 664
Cdd:cd14872 459 AEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------------DQK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 665 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 744
Cdd:cd14872 521 TSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKR 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 327478526 745 YEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 788
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 ... |
120-788 |
5.06e-167 |
|
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: 525.30 E-value: 5.06e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 279
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR--------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 280 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELFQETLESLR 353
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQ----ATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 507
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 508 HTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPkFQRPR 586
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 587 hlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgppggrprrgm 666
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 667 frTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 746
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 327478526 747 ILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 788
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
119-788 |
5.04e-166 |
|
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: 523.55 E-value: 5.04e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIVG 278
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQETLESLRVLG 356
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 433
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQAD 593
Cdd:cd01387 391 EQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--MPLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 594 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRGmfRTVGQL 673
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT--PTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 674 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 753
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 327478526 754 PKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 788
Cdd:cd01387 623 PRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
119-788 |
1.12e-163 |
|
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: 516.17 E-value: 1.12e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE--------RELFQETL 349
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 350 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 505
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 506 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 585
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 586 RHlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgppggrprrg 665
Cdd:cd14897 470 PG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 666 mfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 745
Cdd:cd14897 522 ------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRY 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 327478526 746 EILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 788
Cdd:cd14897 596 KEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
119-786 |
1.05e-162 |
|
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: 514.34 E-value: 1.05e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 190
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 191 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 268
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 269 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQER------ 342
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCYDRrdgvdd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 343 -ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIA-LKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI 420
Cdd:cd14901 237 sVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 421 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFEQLCINYTN 499
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 500 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGH 579
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 580 PKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSlgdgppg 659
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 660 grprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 739
Cdd:cd14901 531 ---------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHD 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 327478526 740 EFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 786
Cdd:cd14901 602 AFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
119-788 |
1.79e-161 |
|
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: 511.24 E-value: 1.79e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 355
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 433
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 513
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 514 EQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGGHPKFQR----PRHLR 589
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 590 DQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMfRT 669
Cdd:cd14903 463 TQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT-TT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 670 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 749
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 327478526 750 PNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 788
Cdd:cd14903 620 PEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
119-788 |
9.64e-161 |
|
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: 510.38 E-value: 9.64e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLahVASSPKGRKEpGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGS-GV----EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQETLESLRVLG 356
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 510
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 511 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhLRD 590
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ-VME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 591 QAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL----------------- 653
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 654 -GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 714
Cdd:cd01385 541 aGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327478526 715 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
119-788 |
4.14e-160 |
|
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: 507.03 E-value: 4.14e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 355
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKrerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 435
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 436 ADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 515
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 516 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQadFS 595
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNN--FG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 596 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMFRTVGQLYK 675
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRRPTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 676 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 755
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|...
gi 327478526 756 GFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14873 621 EDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
119-750 |
4.26e-158 |
|
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: 502.30 E-value: 4.26e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD------ 271
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSklkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 272 ---VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKADLLL-EPCS 325
Cdd:cd14888 155 msgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISIDMSSfEPHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 326 HYRFLT-NGPSSSPG-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL--- 400
Cdd:cd14888 235 KFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 401 CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIA 480
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 481 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWF 560
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 561 PKATDKSFVEKVAQEQGGHPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKd 640
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 641 vegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 720
Cdd:cd14888 549 -----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 327478526 721 VLEGIRICRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
119-788 |
1.67e-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: 497.36 E-value: 1.67e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 191
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 192 QSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 267
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 268 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQEREL-F 345
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDDATeF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 346 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNiaLKRERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLTPRIK 421
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 422 VGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQLNSFE 491
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 492 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDKSFVE 570
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 571 KVAQEQ-GGHPKFQRPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleq 649
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 650 vsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 729
Cdd:cd14892 536 -----------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 730 QGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 788
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
119-788 |
5.71e-150 |
|
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: 479.91 E-value: 5.71e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 189
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 190 EDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE-----------LERQLLQANPILEAFGNAKTVKNDN 258
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 259 SSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNGPSS 336
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 337 SPGQER----ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RERNTDQATMPDNTAA-QKLCRLLGLGVTD 410
Cdd:cd14907 241 CYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 411 FSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIAGFE 483
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 484 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEECWFP 561
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 562 KATDKSFVEKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDV 641
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 642 EGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGV 721
Cdd:cd14907 557 DG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 722 LEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 788
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
121-788 |
5.59e-143 |
|
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: 460.14 E-value: 5.59e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 196
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 197 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYI 276
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 277 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELFQETLESLR 353
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 354 VLGFSHEEIISMLRMVSAVLQFGNIALkrERNTDQA---TMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 430
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 431 QTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 506
Cdd:cd14889 310 HTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLANEQLQYFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 507 NHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPR 586
Cdd:cd14889 388 NHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSR 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 587 hlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGM 666
Cdd:cd14889 465 --SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 667 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 746
Cdd:cd14889 543 KQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYK 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 327478526 747 IL--TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 788
Cdd:cd14889 623 ILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
120-748 |
7.54e-137 |
|
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: 441.67 E-value: 7.54e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 185
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 186 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSP-KGRKEPGVPGE-LERQLLQANPILEAFGNAKTVKNDNSSR 261
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNlAASVSMGKSTSgIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 262 FGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngpssspgqe 341
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 342 RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAAQKL------CRLLGLGVTDFSRA 414
Cdd:cd14900 218 RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEKA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 415 LLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFEIFQLNSF 490
Cdd:cd14900 298 LSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 491 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVE 570
Cdd:cd14900 378 EQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 571 KVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQstdrltaeiwkdvegivglEQV 650
Cdd:cd14900 455 KLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ-------------------EAV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 651 SslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 730
Cdd:cd14900 508 D--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARA 572
|
650
....*....|....*...
gi 327478526 731 GFPNRILFQEFRQRYEIL 748
Cdd:cd14900 573 GFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
119-788 |
1.59e-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: 442.07 E-value: 1.59e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAHVASspkGRKEPGVPgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQETLESLRV 354
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 434
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMFD-KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 435 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 514
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 515 QEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGGHPKFQRPRHLRDQ 591
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 592 adFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPRrgmfRTVG 671
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP----KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 672 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 751
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 327478526 752 AIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 788
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
119-788 |
4.36e-133 |
|
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: 431.78 E-value: 4.36e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 191
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 192 QSILCTGESGAGKTENTKKVIQYLAH------------VASSPKGRKEPGVpgELERQLLQANPILEAFGNAKTVKNDNS 259
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 260 SRFGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSS 337
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 338 PG-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQ-----ATMPDNTAAQKLCRLLGLGVTDF 411
Cdd:cd14891 234 DNiDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEgeaeiASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 412 SRALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NS 489
Cdd:cd14891 313 EKVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkND 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 490 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATD 565
Cdd:cd14891 391 FEQLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 566 KSFVEKVAQEQGGHPKFQRPrHLRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegi 644
Cdd:cd14891 464 AKLNETLHKTHKRHPCFPRP-HPKDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 645 vgleqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 724
Cdd:cd14891 528 ---------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 725 IRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14891 581 CEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
119-750 |
2.61e-129 |
|
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: 423.92 E-value: 2.61e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 188
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 189 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPG-ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 267
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 268 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPGQER---- 342
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARKRAVadky 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 343 -ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTP 418
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 419 RIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFEIFQLNSF 490
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 491 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE 570
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 571 KVAQEQGGhpkfqrprhlRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQV 650
Cdd:cd14902 478 KFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 651 SSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 727
Cdd:cd14902 539 DSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650 660
....*....|....*....|...
gi 327478526 728 CRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
117-834 |
7.47e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 423.29 E-value: 7.47e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 117 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 196 CTGESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 275
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMD----LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 276 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRV 354
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALK-RERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVEIEgKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 508
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 509 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhl 588
Cdd:PTZ00014 499 IVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAK-- 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 589 RDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdgppggrprr 664
Cdd:PTZ00014 574 VDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL-------------- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 665 gmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 744
Cdd:PTZ00014 640 -----IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQ 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 745 YEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEERDLKVTDIIVSFQAAARGYLARR 821
Cdd:PTZ00014 715 FKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKR 794
|
730
....*....|....*..
gi 327478526 822 AFQKR----QQQQSALR 834
Cdd:PTZ00014 795 KVRKNikslVRIQAHLR 811
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
119-788 |
4.82e-127 |
|
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: 416.23 E-value: 4.82e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 188
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 189 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 265
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 266 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTNG--PS 335
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQGgaPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 336 SSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQK----LCRLLGLGVTDF 411
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 412 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSF 490
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 491 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFV 569
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 570 EKV--------AQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLM-KNMDPLNdnvaallhqstdrLTAEIwkd 640
Cdd:cd14908 477 SRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTADS--- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 641 vegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 720
Cdd:cd14908 541 -------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 721 VLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL----YR 779
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQ 673
|
....*....
gi 327478526 780 VGQSKIFFR 788
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
119-788 |
4.30e-126 |
|
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: 412.25 E-value: 4.30e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIVG 278
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR--------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 356
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRDYVQKAQTK 433
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 434 EQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 511
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 512 VLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQ 591
Cdd:cd14896 390 AQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQ--LPL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 592 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrprrgmfrTVG 671
Cdd:cd14896 465 PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------------TLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 672 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpN 751
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-S 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 327478526 752 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
119-786 |
5.19e-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: 400.52 E-value: 5.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRInfDVA--GY 275
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMD----LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL--DVAseGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 276 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRV 354
Cdd:cd14876 152 IRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFEEVLESLKS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALKRErntDQATMPDntAA----------QKLCRLLGLGVTDFSRALLTPRIKVGR 424
Cdd:cd14876 232 MGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 425 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 503
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 504 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 583
Cdd:cd14876 385 KNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 584 RPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrpr 663
Cdd:cd14876 462 PAKVDSNI-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL---------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 664 rgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 743
Cdd:cd14876 531 ------IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLY 604
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 327478526 744 RYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 786
Cdd:cd14876 605 QFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
119-784 |
7.56e-122 |
|
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: 402.44 E-value: 7.56e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 196
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 197 TGESGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 274
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 275 YIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TNGPSSSP 338
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 339 GQEREL---FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQAT--MPDNTAA-QKLCRLLGLGVTDFS 412
Cdd:cd14906 241 NNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 413 RALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFLGILDIA 480
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 481 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWF 560
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 561 PKATDKSFVEKVAQEQGGHPK-FQRPrhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwk 639
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQyYQRT---LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL------ 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 640 dvegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCN 719
Cdd:cd14906 549 ----KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNV 622
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 720 GVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 784
Cdd:cd14906 623 GVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
120-749 |
1.02e-119 |
|
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: 396.25 E-value: 1.02e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 187
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 188 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGElerQLLQANPILEAFGNAKTVKNDNSSR 261
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 262 FGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNG- 333
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 334 --PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQ-------------ATMPDNTA 396
Cdd:cd14895 232 cyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEdngaasapcrlasASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 397 AQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR-----SPR 468
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalNPN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 469 QGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIEr 543
Cdd:cd14895 392 KAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 544 pANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDN 621
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 622 VAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHE 701
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 327478526 702 KRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 749
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
119-788 |
9.88e-119 |
|
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: 392.83 E-value: 9.88e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgelerqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIV 277
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEK--------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---FQETLESL 352
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaFSKLQAAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 353 RVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL------------LTPRI 420
Cdd:cd01386 231 KTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 421 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN---------SFE 491
Cdd:cd01386 311 QESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 492 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLALLDEECW 559
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 560 FPKATDKSFVEKV--AQEQGGHPKFQRPRHLRDQA-DFSVLHYAGK--VDYKANEWLMK-NMDPLNDNVAALLHQSTDRL 633
Cdd:cd01386 467 YPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 634 TAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--- 710
Cdd:cd01386 547 AAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStss 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 711 -----------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELD 774
Cdd:cd01386 596 paagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 327478526 775 PNLYRVGQSKIFFR 788
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
119-750 |
1.37e-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: 374.19 E-value: 1.37e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 194
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 195 LCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAG 274
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 275 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELFQETLESLRV 354
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCFEVTREAMLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 355 LGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV--QK 429
Cdd:cd14880 238 LGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 509
Cdd:cd14880 318 PCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 510 MFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGGHPKFQRPRhL 588
Cdd:cd14880 398 YLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK-L 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 589 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrPRRGMFR 668
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG---------QSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
..
gi 327478526 749 TP 750
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 ... |
119-788 |
4.10e-112 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 372.30 E-value: 4.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 192
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 193 SILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 272
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 273 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETLE 350
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 351 SLRVLgFSHEEIISMLRMVSAVLQFGNIALKRERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYV 427
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 428 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 505
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 506 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAqeqgghpkfqrp 585
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK------------ 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 586 RHLRD---------QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdg 656
Cdd:cd14886 454 SKIKNnsfipgkgsQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMK------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 657 ppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 736
Cdd:cd14886 527 ----------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYND 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 327478526 737 LFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14886 597 TFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
119-788 |
2.50e-105 |
|
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: 353.35 E-value: 2.50e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 195
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 196 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKEpgVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 271
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQRS--IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 272 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPSSSPGQERE 343
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 344 LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLtprIKVG 423
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 424 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQLCINYTNE 500
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 501 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGG-H 579
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 580 PKFQRPRH-LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgpp 658
Cdd:cd14875 470 PYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 659 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 738
Cdd:cd14875 539 ----------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 739 QEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 788
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
119-745 |
7.55e-101 |
|
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: 342.08 E-value: 7.55e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 185
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---------LERQLLQANPILEAFGNAKTVKN 256
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 257 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 330
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 331 TNGPSSSPG---QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-----KRERNT--DQATMPDNTAA--- 397
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 398 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 467
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 468 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 541
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 542 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPL 618
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 619 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 696
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 327478526 697 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 745
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
120-752 |
5.22e-98 |
|
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: 329.17 E-value: 5.22e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 199
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLA-HVASSPKgrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvaGYIVG 278
Cdd:cd14898 78 SGSGKTENAKLVIKYLVeRTASTTS----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLESLRVLGFS 358
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 359 HEEIISMLRMvsAVLQFGNIALKRERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 438
Cdd:cd14898 220 NFKSIEDCLL--GILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 439 ALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 518
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 519 QREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGhpkfqrprHLRDQAD--FSV 596
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNG--------FINTKARdkIKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 597 LHYAGKVDYKANEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKE 676
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL-----------------VKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 677 SLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 752
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
119-788 |
1.80e-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: 329.30 E-value: 1.80e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 270
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 271 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqeRELFQETLE 350
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD---------LRRITAAMK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 351 SLRVLGFSHEEIISMLrmvSAVLQFGNIALKRERNTDQATMPDNTA--------AQKLCRLL-------GLGVTDFSRAL 415
Cdd:cd14887 226 TVGIGGGEQADIFKLL---AAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 416 LT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR------- 468
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 469 ------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI---------PWTF-LD 529
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsafPFSFpLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 530 FGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQEQGGHPKF--QRPRHL 588
Cdd:cd14887 463 STLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYknITPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 589 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGGRPRRGMFR 668
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 669 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 748
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 327478526 749 TPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 788
Cdd:cd14887 687 LPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
116-787 |
1.57e-93 |
|
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: 318.34 E-value: 1.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 116 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 185
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGK 264
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 265 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-----PSSSPG 339
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgchplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 340 QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDqATMPDNTAA-QKLCRLLGLGVTDFsRALL 416
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 417 TPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEifQL---- 487
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--NRsstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 488 -NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC-WFPKATD 565
Cdd:cd14879 384 gNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 566 KSFVEKVAQEQGGHPKFQRPRHLRDQAD---FSVLHYAGKVDYKANEWLMKNMDPLndnvaallhqSTDRLTaeiwkdve 642
Cdd:cd14879 461 EQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 643 givgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVL 722
Cdd:cd14879 523 -----------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 723 EGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 787
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
119-788 |
4.18e-93 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 317.53 E-value: 4.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 196 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DVAG 274
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 275 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELFQETL---- 349
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLNREKLavlk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 350 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 506
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 507 NHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----FPK------ 562
Cdd:cd14878 393 NEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnLPKklqsll 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 563 -ATDKSFVEKVAQEQGGHPKFqrprhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKd 640
Cdd:cd14878 461 eSSNTNAVYSPMKDGNGNVAL------KDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 641 vegivgleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 720
Cdd:cd14878 534 ----------SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIG 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327478526 721 VLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 788
Cdd:cd14878 590 VLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
119-788 |
1.83e-85 |
|
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: 294.62 E-value: 1.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESLRVLGF 357
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 358 sHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 432
Cdd:cd14937 228 -HDMKDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 433 KEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 512
Cdd:cd14937 307 VEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 513 LEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRD-Q 591
Cdd:cd14937 386 KETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--KDiN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 592 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppggRPRRGMFRtv 670
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG------RKNLITFK-- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 671 gqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEILTP 750
Cdd:cd14937 525 ---YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDY 600
|
650 660 670
....*....|....*....|....*....|....*...
gi 327478526 751 NAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 788
Cdd:cd14937 601 STSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
119-740 |
4.20e-81 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 282.95 E-value: 4.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 270
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-------ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 271 D---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL---------- 330
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 331 ----------TNGPSSSPGQEREL-FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrerntdqatmpdntAAqk 399
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK--------------AA-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 400 lCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-----------DRSPR 468
Cdd:cd14884 298 -AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdnEDIYS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 469 QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDLIERpanpp 548
Cdd:cd14884 377 INEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 549 gLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGGHPKFQRPRHLRDQAD---------FSVLHYAGKVDYKANE 609
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYGFVLNHDADGTAkkqnikkniFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 610 WLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRLMATLSNTN 689
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 327478526 690 PSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 740
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
120-787 |
1.19e-71 |
|
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: 253.88 E-value: 1.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 192
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 193 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFdV 272
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV-T 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 273 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQEREL-FQETL 349
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAArFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 350 ESLRVLGFSHEEIIsmlRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 429
Cdd:cd14881 222 ACLGILGIPFLDVV---RVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 430 AQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQLCINYTNEK 501
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 502 LQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKVAQEQGGHP 580
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 581 KFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSSLGdgppgg 660
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCNFG------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 661 rprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 740
Cdd:cd14881 503 ------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 741 FRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 787
Cdd:cd14881 577 FNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
120-748 |
1.75e-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: 247.73 E-value: 1.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 200 SGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 279
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--------GNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 280 NIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER----------ELFQE 347
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 348 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKreRNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 427
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 428 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 505
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 506 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQGGHPKfqr 584
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 585 prhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdgppggrprr 664
Cdd:cd14882 462 ---KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 665 gmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 740
Cdd:cd14882 521 ---RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
....*...
gi 327478526 741 FRQRYEIL 748
Cdd:cd14882 598 FLRRYQFL 605
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
119-753 |
1.17e-67 |
|
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: 242.08 E-value: 1.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 197
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 198 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDvAGYIV 277
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVT-------TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 278 GANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETLESLRVL 355
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 356 GFSHEEIISMLRMVSAVLQFGNIALKRERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKVGrdyvqKA 430
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSEDG-----TT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 431 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 510
Cdd:cd14874 293 IDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 511 FVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHlR 589
Cdd:cd14874 371 FHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-K 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 590 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggrprrgmfrt 669
Cdd:cd14874 448 ERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS------------------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 670 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 749
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 327478526 750 PNAI 753
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
120-788 |
2.10e-65 |
|
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: 236.53 E-value: 2.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 278
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSK-----YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 279 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQETLESLRVLG 356
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 357 FSHEEIISMLRMVSAVLQFGNIALKRERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAqtkeqa 436
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 437 dfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 516
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 517 EYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGGHPKF-QRPRhlrdqaDF 594
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPN------KF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 595 SVLHYAGKVDYKANEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGMFRTVGQLY 674
Cdd:cd14905 445 GIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQMFDAKNTAK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 675 KESLS--RLMATLSNTNPS-----------------------------------------------FVRCIVPNHEKRAG 705
Cdd:cd14905 512 KSPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIKPNSKKTHL 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 706 KLEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALELDPNLYRV 780
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQV 665
|
....*...
gi 327478526 781 GQSKIFFR 788
Cdd:cd14905 666 GNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
122-746 |
5.68e-64 |
|
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: 233.71 E-value: 5.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 122 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 191
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 192 QSILCTGESGAGKTENTKKVIQYLAHVASS----PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 267
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 268 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSPGQER 342
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 343 ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-------KRERNTDQATMPDNTAaqklCRLLGLGVTDFSRAL 415
Cdd:cd14893 244 RDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQS----CALKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 416 LTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPR------- 468
Cdd:cd14893 320 LEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsnivins 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 469 QGasfLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQPCID 539
Cdd:cd14893 400 QG---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 540 LIERPanPPGLLALLDEECWFPKATDKSFVEK---VAQEQGGhpkFQRPRHLRDQAD------------FSVLHYAGKVD 604
Cdd:cd14893 477 LFEDK--PFGIFDLLTENCKVRLPNDEDFVNKlfsGNEAVGG---LSRPNMGADTTNeylapskdwrllFIVQHHCGKVT 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 605 YKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYKESLS 679
Cdd:cd14893 552 YNGKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSARESKN 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 680 --------------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 745
Cdd:cd14893 624 itdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
.
gi 327478526 746 E 746
Cdd:cd14893 704 K 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
141-275 |
9.32e-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: 197.18 E-value: 9.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 141 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 219
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 220 SS--PKGRKEPGVP-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 275
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 ... |
120-786 |
6.41e-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: 196.98 E-value: 6.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 199 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPG-----------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFG 263
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEednihneentdYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 264 KFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERE 343
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 344 -LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI---------ALKRERNTDQATMPDNTAAQKL------------- 400
Cdd:cd14938 241 gKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkkSLLMGKNQCGQNINYETILSELensedigldenvk 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 401 -----CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASF 473
Cdd:cd14938 321 nlllaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 474 LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLLAL 553
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLFSL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 554 LDEECwFPKATDKSFVEKVAQEQGGH-PKF-QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTD 631
Cdd:cd14938 479 LENVS-TKTIFDKSNLHSSIIRKFSRnSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 632 RLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNHEK 702
Cdd:cd14938 558 EYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNESK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 703 RA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYRVG 781
Cdd:cd14938 635 RElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWMIG 706
|
....*
gi 327478526 782 QSKIF 786
Cdd:cd14938 707 NNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1184-1814 |
1.90e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.97 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1184 ELRSKREQEVTELKKTLEEETRIhEAAVQELRQRhgqaLGELAEQLEQARRGKG-AWEKTRLALEA---EVSELRAELSS 1259
Cdd:COG1196 169 KYKERKEEAERKLEATEENLERL-EDILGELERQ----LEPLERQAEKAERYRElKEELKELEAELlllKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1260 LQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQE 1339
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1340 LLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAE 1419
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1420 ALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraeaegreRE 1499
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA---------------EL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1500 ARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAAnDLRAQVTELEDELTAAEDAK 1579
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1580 LRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEE 1659
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1660 AVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL 1739
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 1740 SKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERsfsAKAESGRQQLERQIQEL 1814
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL---EELERELERLEREIEAL 779
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
238-729 |
6.59e-26 |
|
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: 116.77 E-value: 6.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 238 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDECSFHIFYQ 306
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 307 LLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGFSHEEIISMLRMVS 370
Cdd:cd14894 329 MVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 371 AVLQFGNIALKRERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALEALA 444
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 445 KATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQqlfnh 508
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 509 tmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQEQGG 578
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 579 H-PKFQR-----PRH---LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVGL 647
Cdd:cd14894 638 RlPEPPRvlsnaKRHtpvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlGWSPN 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 648 EQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 727
Cdd:cd14894 718 TNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEI 793
|
..
gi 327478526 728 CR 729
Cdd:cd14894 794 CR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1068-1700 |
7.66e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 7.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1068 QELEKLKRRLDGESSELQEQmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1147
Cdd:COG1196 216 RELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1148 RVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAE 1227
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1228 QLEQARRGKGAWEKtRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELE 1307
Cdd:COG1196 374 LAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1308 NVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQ 1387
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1388 AQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKtETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQ 1467
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1468 RKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddvgksvhel 1547
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE------------- 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1548 eracRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEErK 1627
Cdd:COG1196 679 ----AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA-L 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1628 QRTLAVAARKKLEGELEELKAQMASAG-------QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqNRESEKRLK 1700
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEEI---DRETRERFL 830
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
892-1459 |
1.84e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.95 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 892 VGELQGRVAQLEEErARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEEcsRQMQTEKKRLQQHIQE 971
Cdd:COG1196 195 LGELERQLEPLERQ-AEKAERYR--------------ELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 972 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEA 1051
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1052 TIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLR 1131
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1132 EAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV 1211
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1212 QELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVS---ELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDG 1288
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1289 ERARAEAAEKLQRAQAELENVSGALNEAEsktirlskELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQ 1368
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVAS--------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1369 LEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDD 1448
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570
....*....|.
gi 327478526 1449 ATMDLEQQRQL 1459
Cdd:COG1196 730 LEAEREELLEE 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1151-1729 |
5.60e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.41 E-value: 5.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1151 RTKAEKqRRDLGEELEALRGELE-DTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQL 1229
Cdd:COG1196 209 AEKAER-YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1230 EQARRgkgawektrlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV 1309
Cdd:COG1196 288 AEEYE-----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1310 SGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLeeeaaareragrelQTAQAQ 1389
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--------------ERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1390 LSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1469
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1470 FDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDdvGKSVHELER 1549
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1550 ACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQR 1629
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1630 TLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRL 1709
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580
....*....|....*....|
gi 327478526 1710 QEELAASDRARRQAQQDRDE 1729
Cdd:COG1196 741 LLEEEELLEEEALEELPEPP 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
994-1715 |
1.79e-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: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 994 EAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKL 1073
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1074 KRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTK 1153
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1154 AEKQRRDLGEELEALRGELEDTldSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRqRHGQALGELAEQLEQAR 1233
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1234 RgkgawekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERA--RAEAAEKLQRAqaeLENVSG 1311
Cdd:TIGR02168 475 Q-------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLseLISVDEGYEAA---IEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1312 AlneaesktiRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLS 1391
Cdd:TIGR02168 545 G---------RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1392 EW-------RRRQEEEAGALEAGEEARRRAAREAEALTQ--------RLAEKTETVdRLERGR--RRLQQELDDATMDLE 1454
Cdd:TIGR02168 616 KAlsyllggVLVVDDLDNALELAKKLRPGYRIVTLDGDLvrpggvitGGSAKTNSS-ILERRReiEELEEKIEELEEKIA 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1455 QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1534
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1535 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEERRRQLAKQ 1614
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSED 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1615 LRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqnre 1694
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------ 927
|
730 740
....*....|....*....|.
gi 327478526 1695 sEKRLKGLEAEVLRLQEELAA 1715
Cdd:TIGR02168 928 -ELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1057-1890 |
4.99e-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: 104.37 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1057 EDRLRKEEKGRQELEKLKRRLDGESSELQEQmVEQQQRAEELRAQLgrkeEELQAALAraedeggarAQLLKSLREAQAA 1136
Cdd:TIGR02168 178 ERKLERTRENLDRLEDILNELERQLKSLERQ-AEKAERYKELKAEL----RELELALL---------VLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1137 LAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDStnAQQELrskreQEVTELKKTLEEETRIHEAAVQELRQ 1216
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--LQKEL-----YALANEISRLEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1217 RhgqaLGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAA 1296
Cdd:TIGR02168 317 Q----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1297 EKLQRAQAELENVSGALNEAESKTIRLSKELSS-----TEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE 1371
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEEllkklEEAELKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1372 EAAARERAGRELQTAQAQLSEWRRRQEEEAGaLEAGEEARRRAAREAEALTQRLAEKTETVDRLER-----GRRRLQQEL 1446
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEG-FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAaieaaLGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1447 DDatmDLEQQRQLVSTLEKK-----------QRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEA 1515
Cdd:TIGR02168 552 VE---NLNAAKKAIAFLKQNelgrvtflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1516 REELERQNRALRAELEALLSSKD-----------------------------DVGKSVHELERACRVAEQAANDLRAQVT 1566
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1567 ELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEEL 1646
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1647 KAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQD 1726
Cdd:TIGR02168 788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1727 RDEMADEVAngnlskaAILEEKRQLEGRLgqleeeleeeqsnsELLNDRYRKLLLQVESLttelsaersfsakaESGRQQ 1806
Cdd:TIGR02168 868 IEELESELE-------ALLNERASLEEAL--------------ALLRSELEELSEELREL--------------ESKRSE 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1807 LERQIQELRGRLGEEDAgARARHKMTIAALESKLAqAEEQLEQETrerilsgklvrrAEKRLKEVVLQVEEERRVADQLR 1886
Cdd:TIGR02168 913 LRRELEELREKLAQLEL-RLEGLEVRIDNLQERLS-EEYSLTLEE------------AEALENKIEDDEEEARRRLKRLE 978
|
....
gi 327478526 1887 DQLE 1890
Cdd:TIGR02168 979 NKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
871-1399 |
5.95e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 5.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 871 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGE 950
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 951 EEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS 1030
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1031 QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQ 1110
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1111 AALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR----------------RDLGEELEALRGEL-- 1172
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeAALEAALAAALQNIvv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1173 EDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARrgkgawektRLALEAEVSE 1252
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------YYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1253 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1332
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 1333 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1399
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1292-1904 |
6.15e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.86 E-value: 6.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1292 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKElsstEAQLHDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQle 1370
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQ----AEKAERYRELKEELKELEAELlLLKLRELEAELEELEAE-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1371 eeaaareragreLQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1450
Cdd:COG1196 248 ------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1451 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1530
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1531 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRrQ 1610
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-L 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1611 LAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1690
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1691 QNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE--MADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1768
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1769 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1848
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1849 QETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1904
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1148-1947 |
6.06e-21 |
|
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: 100.90 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1148 RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKTLEEETRIhEAAVQ 1212
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEELQEE-LKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1213 ELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERAR 1292
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1293 AEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA-------KLALGSRVRAMEAEAAGL 1365
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1366 REQLEEEAAARERAGRELQTAQaqLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQE 1445
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1446 LDDATMDLEQQRQL---VSTLEKKQRKF--------DQLLAEEK-----AAVLRAVEERERAEAEGREREARAlSLTRAL 1509
Cdd:TIGR02168 491 LDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIA-FLKQNE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1510 EEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAK-LRLEVTVQA 1588
Cdd:TIGR02168 570 LGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1589 LktqhERDLQGRD--EAGEERRRQLAKQLRDAEVERDEERKQR-----TLAVAARKKLEGELEELKAQMASAGQGKEEAV 1661
Cdd:TIGR02168 650 L----DGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEEleekiAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1662 KQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVangNLSK 1741
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL---KALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1742 AAILEEKRQLEgrlgqleeeleeeqsnseLLNDRYRKLLLQVESLTTELSAersfsakaesgrqqLERQIQELRGRLGEE 1821
Cdd:TIGR02168 803 EALDELRAELT------------------LLNEEAANLRERLESLERRIAA--------------TERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1822 dAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1901
Cdd:TIGR02168 851 -SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 327478526 1902 QLEEAEEEASR-AQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:TIGR02168 930 RLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1522-1992 |
4.39e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1522 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRD 1601
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1602 EAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEET 1681
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1682 RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEE 1761
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1762 LEEEQSNSELLNDRYRKLLLQVESLT----TELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALE 1837
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAarllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1838 SKLAQaEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR--VKQLKRQLEEAEEEASRAQA 1915
Cdd:COG1196 545 AAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1916 GRRRLQRELEDVTESAESMN---REVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQPGSGPSPEPEGSPPA 1992
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAgrlREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1022-1752 |
8.48e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 90.51 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1022 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEaTIADMEDRLRKEE-----KGRQELEKLKRRLDGESSELQEQMVEQQQRAE 1096
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1097 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTK-AEKQRRDLGEELEALRGELEDT 1175
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1176 LDSTNAQQELRSKREQEVTELKKTLEE-ETRIHE--AAVQELRQRHGQalgeLAEQLEQARRGKGAWEKTRLALEAEVSE 1252
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDlRAELEEvdKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1253 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1332
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1333 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE-EAAARERAGRELQ--------TAQAQLSEWRRRQEEEAGA 1403
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEVAAGNRLNnvvveddaVAKEAIELLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1404 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATM--DLEQQRQLVS-----TLEKKqrkfdqlLAE 1476
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRLMGkyrmvTLEGE-------LFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1477 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQ 1556
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1557 AANDLRAQVTELEDELTAAEDAKLRLEVTVQAL---KTQHERDL-QGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLA 1632
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELearIEELEEDLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1633 VAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQ-------NRESEKRLKGLEAE 1705
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaaLRDLESRLGDLKKE 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 327478526 1706 VLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1752
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
952-1752 |
2.44e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 952 EECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RKLLEDRLAE 1027
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1028 FSSQA-----AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEklkrrldgesselqEQMVEQQQRAEELRaql 1102
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED--------------AKKAEAVKKAEEAK--- 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1103 gRKEEELQaalaRAEDEggaraqllkSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeelealRGELEDTLDSTNAQ 1182
Cdd:PTZ00121 1237 -KDAEEAK----KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1183 QELRSKREQEVTELKKTLEEETRIHEAAVQ-ELRQRHGQALGELAEQLEQARRGKGAWEKTRlALEAEVSELRAELSSLQ 1261
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA-ADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1262 TARQEGEQRrrrlELQLQEVQGRAGDGERARAE----AAEKLQRAQAELENVSGALNEAESKtiRLSKELSSTEAQLHDA 1337
Cdd:PTZ00121 1373 KEEAKKKAD----AAKKKAEEKKKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1338 QELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAARE 1417
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1418 AealtqRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraEAEGRE 1497
Cdd:PTZ00121 1527 A-----KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA---------KKAEEA 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1498 REARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAED 1577
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1578 AKLRLEVTVQALKTQHERDLQGRDEAGEER-----RRQLAKQLRDAEVERDEERKQRTLAVAARKklEGELEELKAQMAS 1652
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEEAK 1750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1653 AGQGKEEAVKQLRKMQAQMKELWREVEET---RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE 1729
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820
....*....|....*....|...
gi 327478526 1730 MADEVAngnLSKAAILEEKRQLE 1752
Cdd:PTZ00121 1831 AIKEVA---DSKNMQLEEADAFE 1850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1605-1915 |
4.39e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1605 EERRRQLAKQLRDA----EVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEE 1680
Cdd:COG1196 199 ERQLEPLERQAEKAeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1681 TRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEE 1760
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1761 ELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRlgeedagaRARHKMTIAALESKL 1840
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 1841 AQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQA 1915
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1473 |
1.12e-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: 86.66 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 862 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVV 941
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 942 SELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLL 1021
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1022 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLD---GESSELQEQMVEQQQRAEEL 1098
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVEEVLKASIQGVHGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1099 RAQLGRKEEELQAALARA----------EDEGGARA--QLLKSLREAQAA----LAEAQEDLESERVARTKAEKQRRDLG 1162
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAKEaiELLKRRKAGRATflplNKMRDERRDLSILSEDGVIGFAVDLV 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1163 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV----QELRQRHGQALGELAEqLEQARRGKGA 1238
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE-LQRLRERLEG 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1239 WEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1318
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1319 KTIRLSKELSSTEAQL-----HDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEW 1393
Cdd:TIGR02169 766 RIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1394 -------RRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTL-EK 1465
Cdd:TIGR02169 846 keqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAK 925
|
....*...
gi 327478526 1466 KQRKFDQL 1473
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
863-1477 |
1.79e-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: 86.26 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 863 QVTRQDEVLQARAQEL-QKVQELQQQSAR---EVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELE 938
Cdd:TIGR02168 313 NLERQLEELEAQLEELeSKLDELAEELAEleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 939 LVVSELEARVGEEEecSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER 1018
Cdd:TIGR02168 393 LQIASLNNEIERLE--ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1019 KLLEDRLAEFSSQAAEEEEKVKSLNklrlkyeatiaDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEEL 1098
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLE-----------RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1099 RAQLG---------RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEkqrrDLGEELEALR 1169
Cdd:TIGR02168 540 EAALGgrlqavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK----DLVKFDPKLR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1170 GELE---------DTLDSTNAQQEL----------------------------------RSKREQEVTELKKTLEEETRI 1206
Cdd:TIGR02168 616 KALSyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAE 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1207 HEAAVQELRQrhgqALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAG 1286
Cdd:TIGR02168 696 LEKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1287 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR 1366
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1367 EQLEEEAAARERAGRELQTAQAQLSEW--RRRQEEEAGALEAGEEARrraareaeaLTQRLAEKTETVDRLERGRRRLQQ 1444
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEE---------LSEELRELESKRSELRRELEELRE 922
|
650 660 670
....*....|....*....|....*....|...
gi 327478526 1445 ELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEE 1477
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1542-1947 |
2.53e-14 |
|
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: 79.06 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1542 KSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAgEERRRQLAKQLRDAEVE 1621
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQED 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1622 RDEERKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLR-KMQAQMKELWREVEETRTSREEIFSQNRESEKR-L 1699
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1700 KGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKL 1779
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1780 LLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGK 1859
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1860 LVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVT 1939
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 327478526 1940 TLRNRLRR 1947
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1561-1976 |
2.92e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1561 LRAQVTELEDEltaAEDAKLRLEVTVQALKTQHERDLQgrdeageeRRRQLAKQLRDAEVERDEERKQRTLAVAARKKLE 1640
Cdd:COG1196 198 LERQLEPLERQ---AEKAERYRELKEELKELEAELLLL--------KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1641 GELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRAR 1720
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1721 RQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKA 1800
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1801 ESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1880
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1881 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAqAGRRRLQRELEDVTESAESMNREVTTLRNRlRRGPLTFTTRTVRQV 1960
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRATFLPLDKIRA 584
|
410
....*....|....*.
gi 327478526 1961 FRLEEGVASDEEAEEA 1976
Cdd:COG1196 585 RAALAAALARGAIGAA 600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1482 |
3.87e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 874 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL----EARV 948
Cdd:PTZ00121 1183 KAEEVRKAEELRKaEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 949 GEEEECSRQMQTEKKRLQQHIQELEAHLEAEEG--ARQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRL 1025
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1026 AEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgeSSELQEQMVEQQQRAEELRAqlgRK 1105
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKK---AA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1106 EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDLGEELEAlrGELEDTLDSTNAQQEL 1185
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KAEEAKKKAEEAKKA--DEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1186 RSKREQ---EVTELKKTLEEETRIHEA-------AVQELRQRHGQALGELAEQLEQARRG---KGAWEKTRLALEAEVSE 1252
Cdd:PTZ00121 1489 KKKAEEakkKADEAKKAAEAKKKADEAkkaeeakKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1253 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGAlnEAESKTIRLSKELSSTEA 1332
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1333 QlhDAQELLQEETRAKLALGSRVRAMEAEaaglreqleeeaAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARR 1412
Cdd:PTZ00121 1647 K--KAEELKKAEEENKIKAAEEAKKAEED------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1413 RAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDlEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1482
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1292-1977 |
6.36e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1292 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEaqlhDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQLE 1370
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1371 EEAAARERAGRELQTAQAQLSEWRRRQEEeagaleageearrrAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAt 1450
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIEELQKELYALANEISRLEQQKQILRERLANL- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1451 mdLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsLTRALEEEQEAREELERQNRALRAEL 1530
Cdd:TIGR02168 315 --ERQLEELEAQLEELESKLDELAEELAE-------------------------LEEKLEELKEELESLEAELEELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1531 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER----DLQGRDEAGEE 1606
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1607 RRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEavkqLRKMQAQMKELWreveetrtsre 1686
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALL----------- 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1687 eifsQNRESEKRLKGLEAEVLRLQEE----LAASDRARRQAQQDRDEMADEVA-----NGNLSKAAILEEK----RQLEG 1753
Cdd:TIGR02168 513 ----KNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDsikgTEIQG 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1754 RLGQLEEELEEEQSNSELL---NDRYRKLL-------LQVESLTT------ELSAERSF-----------------SAKA 1800
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLvkfDPKLRKALsyllggvLVVDDLDNalelakKLRPGYRIvtldgdlvrpggvitggSAKT 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1801 ESGRQQLERQIQELRGRLgEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1880
Cdd:TIGR02168 669 NSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1881 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQV 1960
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730
....*....|....*..
gi 327478526 1961 FRLEEGVASDEEAEEAQ 1977
Cdd:TIGR02168 828 SLERRIAATERRLEDLE 844
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
990-1870 |
9.04e-14 |
|
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: 77.32 E-value: 9.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 990 KVTTEAKMKKFEEDLLLLEDqnSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE 1069
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEE--AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1070 -LEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESER 1148
Cdd:pfam02463 220 eLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1149 VARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGELAEQ 1228
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKL----QEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1229 LEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEvqgRAGDGERARAEAAEKLQRAQAELEN 1308
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE---EKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1309 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEA-----------EAAGLREQLEEEAAARE 1377
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1378 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLE--- 1454
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaql 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1455 QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1534
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1535 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELT------AAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERR 1608
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1609 RQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMasagqgKEEAVKQLRKMQAQMKELWREVEETRTSREEI 1688
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL------KEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1689 FsqnrESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1768
Cdd:pfam02463 843 K----EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1769 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1848
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900
....*....|....*....|...
gi 327478526 1849 QETRERI-LSGKLVRRAEKRLKE 1870
Cdd:pfam02463 999 RLEEEKKkLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
932-1234 |
1.91e-13 |
|
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: 76.25 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 932 ARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKL---QLEKVTTEAKMKKFEEDLLLLE 1008
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1009 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLnklrlkyEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE-- 1086
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRErl 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1087 -----QMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1161
Cdd:TIGR02168 827 eslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 1162 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARR 1234
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1143-1961 |
4.96e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1143 DLESERVARTKAEkqRRDLGEELEALRGELEDtldstNAQQELRSKREQEVTELKKTLEEETRIHEA--AVQELRQRHGQ 1220
Cdd:PTZ00121 1049 DEDIDGNHEGKAE--AKAHVGQDEGLKPSYKD-----FDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1221 ALGELAEQLEQARRGkgawEKTRLALEAEVSELRAELSSLQTARqegeqrrrrlELQLQEVQGRAGDGERAR-AEAAEKL 1299
Cdd:PTZ00121 1122 KKAEDARKAEEARKA----EDARKAEEARKAEDAKRVEIARKAE----------DARKAEEARKAEDAKKAEaARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1300 QRAQaELENVSGALNEAESKtiRLSKELSSTEAQLHDAQELLQEETRAKLAlgsRVRAMEAEAAGLREQLEEEAAARERA 1379
Cdd:PTZ00121 1188 RKAE-ELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1380 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAtmdleqqRQL 1459
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA-------DAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1460 VSTLEKKQRKFDQLLAEEKAAvlraveereraeaegrerearalsltraleeeQEAREELERQNRALRAELEALLSSKDD 1539
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAA--------------------------------ADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1540 VGKSVHELERACRVAEQAANDLRA--QVTELEDELTAAEDAKLRLEVTVQA----LKTQHERDLQGRDEAGEERRRQLAK 1613
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKAdeakKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1614 QLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK--QLRKMQAQMK-ELWREVEETRTSREEifs 1690
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKaDEAKKAEEAKKADEA--- 1539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1691 qnRESEKRLKgleAEVLRLQEELAASDRARRQAQQDRDEmadEVANGNLSKAAIL---EEKRQLEGRLGQLEEELEEEQS 1767
Cdd:PTZ00121 1540 --KKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEE 1611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1768 NSELLNDRyrkllLQVESLTTElSAERSFSAKAESGRQQLERQIQELRGRlgEEDAGARARHKMTIAALESKlaQAEEQL 1847
Cdd:PTZ00121 1612 AKKAEEAK-----IKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKK--KAEEAK 1681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1848 EQETRERILSGKLVRRAE--KRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR----------QLEEAEEEASRAQA 1915
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeedkkkaeEAKKDEEEKKKIAH 1761
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 327478526 1916 GRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1961
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
890-1253 |
1.27e-12 |
|
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: 73.55 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 890 REVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHI 969
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALA--------------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 970 QELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKY 1049
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1050 EATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQL 1126
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1127 LKSLREAQAALAEAQEDLESERVA-RTKAEKQRRDLGEELEALRGELEDTLD----STNAQQELRSKREQEVTELKKTLE 1201
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIK 982
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 327478526 1202 EETRIHEAAVQELRQRHGQaLGELAEQLEQARRGKGAWEKTRLALEAEVSEL 1253
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
881-1365 |
3.06e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 881 VQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV---VSELEARVGEEEECSRQ 957
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 958 MQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1037
Cdd:PRK03918 271 LKKEIEELEEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1038 KVKSLNKLRLKYEAtiadMEDRLRKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQQQRAEElraQLGRKEEELQAALA 1114
Cdd:PRK03918 343 LKKKLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1115 RAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAE---------KQRRDLGEELEALRGELEDTLDSTNAQQEL 1185
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEytaelkrieKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1186 RskREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQ--LEQARRGKGAWEKTRLALEAEVSELRAELS 1258
Cdd:PRK03918 496 I--KLKELAEQLKELEEKLKKYnleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1259 SLQTARQEGE-QRRRRLELQLQEVQG------RAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSstE 1331
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--E 651
|
490 500 510
....*....|....*....|....*....|....
gi 327478526 1332 AQLHDAQELLQEETRAKLALGSRVRAMEAEAAGL 1365
Cdd:PRK03918 652 LEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
987-1733 |
7.00e-12 |
|
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: 71.25 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 987 QLEKVTTEaKMKKFEEDLLLLEDQNSK---LSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1063
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1064 EKgrqeleKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALAEAQED 1143
Cdd:TIGR02169 278 NK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1144 LESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQaLG 1223
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE-LA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1224 ELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGER------ARAEAAE 1297
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1298 KLQRAQAELENVSGALNEAESKTI--------------------RLSKELSSTEAQLHDAQELLQEE--TRAKLALGSRV 1355
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVaqlgsvgeryataievaagnRLNNVVVEDDAVAKEAIELLKRRkaGRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1356 RAMEAEAAGLREQLEEEAA------------------ARERAGRELQTAQAQLSEWRR-----RQEEEAGALEAGEEARR 1412
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1413 RAAREAEALTQRLAEKTETVDRLERGRRRLQQE--------------LDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEK 1478
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSElrrienrldelsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1479 AAVLRAVEERERAEAEGREREARALSLTRALEEEQEAReelerqnralrAELEALLSskddvgksvheleracrvaeqaa 1558
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----------NDLEARLS----------------------- 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1559 ndlRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKK 1638
Cdd:TIGR02169 790 ---HSRIPEIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1639 LEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREeifsqnrESEKRLKGLEAEVLRLQEELAASDR 1718
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIED 938
|
810
....*....|....*
gi 327478526 1719 ARRQAQQDRDEMADE 1733
Cdd:TIGR02169 939 PKGEDEEIPEEELSL 953
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
810-1346 |
8.23e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 810 FQAAARGYLARRAFQKRQQQQSALRVMqrncaaylKLRHWQWWRLFTKVKPLLQVTRQDEVlqaRAQELQKVQELQQ-QS 888
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE--------EERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKaEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 889 AREVGELQgrvaqlEEERARLAEQL-------RAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTE 961
Cdd:PTZ00121 1289 KKKADEAK------KAEEKKKADEAkkkaeeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 962 KKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKmKKFEEDLLLLEDQNSKLSK-------ERKLLEDRLAEFSSQAAE 1034
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAkkkadeaKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1035 EEEKVKSLNKlrlKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELR--AQLGRKEEELQAA 1112
Cdd:PTZ00121 1442 EAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1113 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeeLEALRGELEDTLDSTNAQQELRSKREQE 1192
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-----AEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1193 VTELKKTLEEETRIheaAVQELRQRHGQALGelAEQLEQARRGKGAWEKTRLALEAEV---SELRAELSSLQTARQEGEQ 1269
Cdd:PTZ00121 1594 IEEVMKLYEEEKKM---KAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 1270 RRRRLELQLQEVQgRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETR 1346
Cdd:PTZ00121 1669 KAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
866-1327 |
8.44e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 866 RQDEVLQARAQELQKVQELQQQsAREVGELQGRVAQLEEERARlAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 945
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKK-AEEDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 946 ARVGEE----EECSRQMQTEKKRLQQhiqeleahleaeegARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKLL 1021
Cdd:PTZ00121 1456 AKKAEEakkkAEEAKKADEAKKKAEE--------------AKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1022 EDRLAEfSSQAAEEEEKVKSLNKLRLKYEAtiadmeDRLRKEEKGRQELEKLKrrldgesselqeqmVEQQQRAEELRAQ 1101
Cdd:PTZ00121 1520 EAKKAD-EAKKAEEAKKADEAKKAEEKKKA------DELKKAEELKKAEEKKK--------------AEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1102 LGRKEEELQAAlaraedeggARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNA 1181
Cdd:PTZ00121 1579 ALRKAEEAKKA---------EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1182 QQELRSKREQEV--TELKKTLEEETRIHEAAVQELRQRHGQalgelAEQLEQARRGKGAWEKTRLALEAEVSelRAElsS 1259
Cdd:PTZ00121 1650 EELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKK--KAE--E 1720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1260 LQTARQEGEQRRRRLELQLQEVQGRAgdgERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1327
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1202 |
1.46e-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: 70.10 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 866 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 945
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIE----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 946 ARVGEEE-----ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKL 1020
Cdd:TIGR02169 779 EALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1021 LEDRLAEFSSQAAEeeekvkslnklrlkYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1100
Cdd:TIGR02169 859 LNGKKEELEEELEE--------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1101 QLGRKEEELqAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEELEALRG-------ELE 1173
Cdd:TIGR02169 925 KLEALEEEL-SEIEDPKGEDEEIPEEELSLE---------------------DVQAELQRVEEEIRALEPvnmlaiqEYE 982
|
330 340
....*....|....*....|....*....
gi 327478526 1174 DTLDSTNAQQELRSKREQEVTELKKTLEE 1202
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1184-1941 |
2.28e-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: 69.33 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1184 ELRSKREQEVTELKkTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTA 1263
Cdd:TIGR02169 167 EFDRKKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1264 RQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALNEAESKTIRLSKELSSTEAQLHDAQELLQ 1342
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1343 EETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRaareaeaLT 1422
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-------YR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1423 QRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLaEEKAAVLRAveereraeaegrereara 1502
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-EDKALEIKK------------------ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1503 lsLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTEL-------------- 1568
Cdd:TIGR02169 453 --QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaql 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1569 ------------------------EDELTAAEDAKLRLEVTVQALK-------TQHERDLQGRDEAG-----------EE 1606
Cdd:TIGR02169 531 gsvgeryataievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRATflplnkmRDERRDLSILSEDGvigfavdlvefDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1607 RRRQLAKQ-LRDAEVERDEERKQRTLAVAARKKLEGELEE---------------------LKAQMASAGQGKEEAVKQL 1664
Cdd:TIGR02169 611 KYEPAFKYvFGDTLVVEDIEAARRLMGKYRMVTLEGELFEksgamtggsraprggilfsrsEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1665 RKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQ----DRDEMAD---EVANG 1737
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienVKSELKEleaRIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1738 NLSKAAILEEKRQLEGRLGQLEEELEEEQSNSelLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGR 1817
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1818 LGEEDAgararhkmTIAALESKLAQAEEQLEQ-ETRERILSGKLVRRAEKRlKEVVLQVEEERRVADQLRDQLEKGNLRV 1896
Cdd:TIGR02169 849 IKSIEK--------EIENLNGKKEELEEELEElEAALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRL 919
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1897 KQLKRQLEEAEEEASRAQAGRRRLQRE------LEDVTESAESMNREVTTL 1941
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1075-1845 |
1.25e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1075 RRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKA 1154
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1155 EKQRRDLGEELEALRgELEDTLDSTNAQQELRSKREQEV---TELKKTlEEETRIHEA-AVQELRQRHGQALGELAEQLE 1230
Cdd:PTZ00121 1150 DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVrkaEELRKA-EDARKAEAArKAEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1231 QARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlqevqgrAGDGERARaeAAEKLQRAqaelENVS 1310
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA-----------AIKAEEAR--KADELKKA----EEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1311 GALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKlalgSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQl 1390
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK- 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1391 SEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERgRRRLQQELDDATMDLEQQRQLVSTLEKKQRKF 1470
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1471 DQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERA 1550
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1551 --CRVAEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVtvqalKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEE 1625
Cdd:PTZ00121 1525 deAKKAEEAkkADEAKkAEEKKKADELKKAEELKKAEEK-----KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1626 RKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK---ELWREVEETRTSREEIFSQNRESEKR---- 1698
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKkaee 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1699 LKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRK 1778
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 1779 LLLQVeslttelsaERSFSAKAESGRQQLERQIQElrgRLGEEDAGARARHKMTIAALESKLAQAEE 1845
Cdd:PTZ00121 1758 KIAHL---------KKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1553-1947 |
1.31e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1553 VAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEeRKQRtla 1632
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-RERR--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1633 vaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTsreEIFSQNRESEKRLKGLEAEVLRLQ-- 1710
Cdd:COG4913 361 ---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLErr 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1711 ------EELAASDRARRQAQQDRDEM----------ADE-------------------VANGNLSKAAILEEKRQLEGRL 1755
Cdd:COG4913 435 ksnipaRLLALRDALAEALGLDEAELpfvgelievrPEEerwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1756 GQLEEELEEEQSNSELLNDR--YRKLLLQVESLTTELSAE--RSFS-AKAESGRQ--QLERQIQE-----LRGRLGEEDA 1823
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRFDyVCVDSPEElrRHPRAITRagqvkGNGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1824 ----------GARARHKmtIAALESKLAQAEEQLEQ-ETRERILSGKL-----VRRAEKRLKEV------VLQVEEERRV 1881
Cdd:COG4913 595 rrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEALEAELdalqeRREALQRLAEYswdeidVASAEREIAE 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1882 ADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
929-1332 |
1.93e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.24 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 929 RLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLqlEKVTTEAK-MKKFEEDLLLL 1007
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--EKLEKEVKeLEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1008 EDQNSKLSKERKLLEDRLAEFSSQAAEE-------EEKVKSLNKLRLKYEATIAdMEDRLRKEEKGRQELEKLKRRLDGE 1080
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1081 SSELQEQMVEQQQRAEELRaQLGRKEEELQAALARAEDeggaRAQLLKSLREAQAalaeaqedlESERVARTKAEKQRRD 1160
Cdd:PRK03918 323 INGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKE---------ELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1161 LGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE---ETRIHEAAVQELRQRHGQALgelaeqLEQARRGKG 1237
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPVCGRELTEEHRKEL------LEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1238 AWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLEL--QLQEVQgragdgERARAEAAEKLQRAQAELENVSGALNE 1315
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELE------EKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410
....*....|....*..
gi 327478526 1316 AESKTIRLSKELSSTEA 1332
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE 553
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1066-1876 |
6.84e-10 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 64.37 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1066 GRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaalaeaqedle 1145
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR---------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1146 sERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKTLEEetriHEAAVQELRQrhgqalgeL 1225
Cdd:pfam15921 136 -ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMMLS----HEGVLQEIRS--------I 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1226 AEQLEQARrGKGAWEKTRLA------LEAEVSELraeLSSLQTARQEGEQRRRRLELQLqevqgragdgERARAEAAEK- 1298
Cdd:pfam15921 193 LVDFEEAS-GKKIYEHDSMStmhfrsLGSAISKI---LRELDTEISYLKGRIFPVEDQL----------EALKSESQNKi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1299 ---LQRAQAELENVsgaLNEAESKTIRLSKELSSTEAQLHDAQ---ELLQEETRAKLALGSR-VRAMEAEAAGLREQLEE 1371
Cdd:pfam15921 259 ellLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1372 EAAARERAGRELQT----AQAQLSEWRRRQEE---EAGALE-----------AGEEARRRAAREAEALTQRLAEKTETVD 1433
Cdd:pfam15921 336 AKRMYEDKIEELEKqlvlANSELTEARTERDQfsqESGNLDdqlqklladlhKREKELSLEKEQNKRLWDRDTGNSITID 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1434 RLERgrrrlqqELDDATMDLEQQRQLVSTLEKK-QRKFDQLLAEEKAavlraveereraeaegrerearalsltraleee 1512
Cdd:pfam15921 416 HLRR-------ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQG--------------------------------- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1513 qeaREELERQNRALRAELEallSSKDDVGKSVHEL---ERACRVAEQAANDLRAQVTELED--ELTAAEDAKLRLEVTVQ 1587
Cdd:pfam15921 456 ---KNESLEKVSSLTAQLE---STKEMLRKVVEELtakKMTLESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1588 ALKTQHerdLQGRDEageerrrqlakQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKM 1667
Cdd:pfam15921 530 LQELQH---LKNEGD-----------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1668 QAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEE 1747
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1748 KRQLEGRLGQLEEELEEEQsnsellndryRKLLLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRGRLG- 1819
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTT----------NKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDa 745
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 327478526 1820 --------EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE 1876
Cdd:pfam15921 746 lqskiqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
891-1254 |
2.32e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 891 EVGELQGRVAQLEEERARLAEQLRAEAELCAEAeetRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQ 970
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 971 eleahleaeegarqklqlEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEfsSQAAEEEEKVKSLNKLRLKYE 1050
Cdd:TIGR02169 752 ------------------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1051 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAqllksl 1130
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1131 reaqaalaeaqeDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAA 1210
Cdd:TIGR02169 886 ------------DLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1211 -----VQELRQRHGQALGELA-------EQLEQARRGKGAWEKTRLALEAEVSELR 1254
Cdd:TIGR02169 951 lsledVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
956-1254 |
2.82e-09 |
|
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: 62.45 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 956 RQMQTEKKRLQQH-IQELEAHLEAEEGARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKL----LEDRLAEF-- 1028
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1029 --SSQAAEEEEKVKSLNKLRLkyeatiadmeDRLRKEEKGRQELE---KLKRRLDGESSELQEQMVEQQQ-RAEELRA-- 1100
Cdd:pfam17380 365 irQEEIAMEISRMRELERLQM----------ERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQiRAEQEEArq 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1101 -QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEElealrgELEDTLDST 1179
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1180 NAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawEKTRL-ALEAEVSELR 1254
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE-----ERSRLeAMEREREMMR 579
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1527-1944 |
3.03e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1527 RAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEE 1606
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE-ELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1607 RrrqlakqLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSRE 1686
Cdd:PRK02224 329 R-------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1687 EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL----------SKAAILEEKRQ----LE 1752
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRErveeLE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1753 GRLGQLEEELEEEQSNSELLNDrYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKM- 1831
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAa 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1832 ------------TIAALESKLAQAEEQLEQ-ETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1898
Cdd:PRK02224 561 aeaeeeaeeareEVAELNSKLAELKERIESlERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 327478526 1899 LKRQLeeAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNR 1944
Cdd:PRK02224 639 LEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
876-1179 |
4.74e-09 |
|
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: 61.68 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 876 QELQKVQELQQQSAREVGElQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAA-----------RKQELELVVSEL 944
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKME-QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermameRERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 945 EAR----VGEEE---ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1017
Cdd:pfam17380 358 RKRelerIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1018 RKLLEDRLAEFSSQAAEEEEKVKSLNKLRlKYEATIADMEDRLRKEEKGRQELEKLKRR-LDGESSELQEQMVEQQQRae 1096
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERK-- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1097 elRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEEL---EALRGELE 1173
Cdd:pfam17380 515 --RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIvesEKARAEYE 592
|
....*.
gi 327478526 1174 DTLDST 1179
Cdd:pfam17380 593 ATTPIT 598
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1086-1856 |
5.44e-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: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1086 EQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQLLKSLREAqaalaeaqeDLESERVARTKAEKQRRDLGEEL 1165
Cdd:COG4913 228 DALVEHFDDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1166 EALRGELEDTldstnaqqelrskrEQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLA 1245
Cdd:COG4913 298 EELRAELARL--------------EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1246 LEAEVSELRAEL----SSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALN-EAESK 1319
Cdd:COG4913 364 LEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLeRRKSNiPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1320 TIR--LSKELSSTEAQLHDAQELLQ---EETR----AKLALGSRVRAM------EAEAAglreqleeEAAARERAGRELQ 1384
Cdd:COG4913 444 ALRdaLAEALGLDEAELPFVGELIEvrpEEERwrgaIERVLGGFALTLlvppehYAAAL--------RWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1385 TAQAQLS-EWRRRQEEEAGALEAGEEARRRAARE--AEALTQRLA-EKTETVDRLERGRRRLQQ-----------ELDDA 1449
Cdd:COG4913 516 YERVRTGlPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDyVCVDSPEELRRHPRAITRagqvkgngtrhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1450 TmDLEQQRQL-VSTLEKKQRKFDQL-LAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALR 1527
Cdd:COG4913 596 R-RIRSRYVLgFDNRAKLAALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1528 AELEALLSSKDDVGksvhELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDlqgRDEAGEER 1607
Cdd:COG4913 675 AELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1608 RRQLAKQLRDAEVERDEERkqrtlavaARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWR-EVEETRTSRE 1686
Cdd:COG4913 748 RALLEERFAAALGDAVERE--------LRENLEERIDALRARLN-------RAEEELERAMRAFNREWPaETADLDADLE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1687 EifsqNRESEKRLKGLEAEVL-RLQEELAasDRARRQAQQDRdemadevanGNLSkAAILEEKRQLEGRLGQleeeleee 1765
Cdd:COG4913 813 S----LPEYLALLDRLEEDGLpEYEERFK--ELLNENSIEFV---------ADLL-SKLRRAIREIKERIDP-------- 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1766 qsnselLNDRYRKL------LLQVESLTTELSAERSFsakaesgrqqlERQIQELRGRLGEEDAGARARHKMTIAALESK 1839
Cdd:COG4913 869 ------LNDSLKRIpfgpgrYLRLEARPRPDPEVREF-----------RQELRAVTSGASLFDEELSEARFAALKRLIER 931
|
810
....*....|....*..
gi 327478526 1840 LAQAEEQLEQETRERIL 1856
Cdd:COG4913 932 LRSEEEESDRRWRARVL 948
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1009-1246 |
1.69e-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: 59.01 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1009 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQM 1088
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1089 VEQQQR-AEELRAQLGRKEEELQAALARAEDEGGA--RAQLLKSL-REAQAALAEAQEDLESERVARTKAEKQRrdlgEE 1164
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLaPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1165 LEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1244
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
..
gi 327478526 1245 AL 1246
Cdd:COG4942 256 PW 257
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1308 |
2.00e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 871 LQARAQELQKVQELQQQSAREVGELQGRVAQLE---EERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEAR 947
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 948 VGEEEECSRqmqtEKKRLQQHIQELEAHLEAEEGARQKL----QLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLED 1023
Cdd:PRK03918 337 EERLEELKK----KLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1024 RLAEFSSQAAEEEEKVKSLNK-------------------LRLKYEATIADMEDRLR----KEEKGRQELEKLKRRLDGE 1080
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkeLLEEYTAELKRIEKELKeieeKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1081 S----------------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1144
Cdd:PRK03918 493 SeliklkelaeqlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1145 ES-ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRS---KREQEVTELKKTLEEETRIhEAAVQELRQRHGQ 1220
Cdd:PRK03918 573 AElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAET-EKRLEELRKELEE 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1221 ALGELAEQLEQARRGKgawektRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEaAEKLQ 1300
Cdd:PRK03918 652 LEKKYSEEEYEELREE------YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-------EKAKKE-LEKLE 717
|
....*...
gi 327478526 1301 RAQAELEN 1308
Cdd:PRK03918 718 KALERVEE 725
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1559-1941 |
2.35e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1559 NDLRAQVTELEDELTAAEDAKLRLEVTVQALK---TQHERDLQGRDEAGEERRrQLAKQLRDAEVERDEERKQRTLAVAA 1635
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIE-DLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1636 RKKLEGELEELKAQmASAGQGKEEAVKQLRK-MQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELA 1714
Cdd:PRK02224 288 LEELEEERDDLLAE-AGLDDADAEAVEARREeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1715 ASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAER 1794
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1795 SFSAKAESGR---------QQLERQ-----IQELRGRLGEEDAgARARHKMTIAALESKLAQAEEQLEQETRerilsgkl 1860
Cdd:PRK02224 440 ERVEEAEALLeagkcpecgQPVEGSphvetIEEDRERVEELEA-ELEDLEEEVEEVEERLERAEDLVEAEDR-------- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1861 VRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEE----ASRAQAGRRR---LQRELEDVTESAES 1933
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEAREEvaeLNSKLAELKERIES 590
|
....*...
gi 327478526 1934 MNREVTTL 1941
Cdd:PRK02224 591 LERIRTLL 598
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
926-1326 |
5.13e-08 |
|
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: 58.54 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 926 TRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1005
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1006 LLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKslnklrlKYEATIADMEDRLRKEEkgrqeleklKRRLDGESSELQ 1085
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSHSR---------IPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1086 EQMVEQQQRAEELRAQLGRKEEELQAalarAEDEggaraqllkslreaqaalaeaQEDLESERVArtkAEKQRRDLGEEL 1165
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEY----LEKE---------------------IQELQEQRID---LKEQIKSIEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1166 EALRGELEDtldsTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRLA 1245
Cdd:TIGR02169 857 ENLNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRKRLSELKAKLEA 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1246 LEAEVSELRAELSSLQTaRQEGEQRRRRLELQLQEVQgragdgerARAEAAEKLQ-RAQAELENVSGALNEAESKTIRLS 1324
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVE--------EEIRALEPVNmLAIQEYEEVLKRLDELKEKRAKLE 999
|
..
gi 327478526 1325 KE 1326
Cdd:TIGR02169 1000 EE 1001
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1015-1353 |
7.82e-08 |
|
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: 57.77 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1015 SKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQR 1094
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1095 AEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVartkaeKQRRDLGEELEALRGELED 1174
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1175 TLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawektrlaLEAEVSELR 1254
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-----------LEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1255 AELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAEsKTIRLSKELSSTEAQL 1334
Cdd:TIGR02169 882 SRLGDLK-------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSL 953
|
330
....*....|....*....
gi 327478526 1335 HDAQELLQEETRAKLALGS 1353
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP 972
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1351-1899 |
9.20e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1351 LGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEA---GALEAGEEARRRAAREAEALTQRLAE 1427
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1428 KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEEREraeaegrerearalSLTR 1507
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE--------------SLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1508 ALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ 1587
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1588 ALKTqherDLQGRDEAGEERRRQLA--------KQLRDAE-VERDEERKQRtlavaaRKKLEGELEELKAQMASAGQgKE 1658
Cdd:PRK02224 430 ELEA----TLRTARERVEEAEALLEagkcpecgQPVEGSPhVETIEEDRER------VEELEAELEDLEEEVEEVEE-RL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1659 EAVKQLRKMQAQMKELwrevEETRTSREEIFSQNRES--EKRLKgleAEVLRLQ-EELAASDRARRQAQQDRDEMADEVA 1735
Cdd:PRK02224 499 ERAEDLVEAEDRIERL----EERREDLEELIAERRETieEKRER---AEELRERaAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1736 ngnlskaailEEKRQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVESLTTELSAERS-FSAKAESGRQQLERqIQEL 1814
Cdd:PRK02224 572 ----------EEVAELNSKLAELKERIESL--------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER-LAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1815 RGR---LGEEDAGARarhkmtIAALESKLAQAEEQLEQetreriLSGKLVRRAEKR--LKEVVLQVEEERRVADQLRDQL 1889
Cdd:PRK02224 633 RERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREERddLQAEIGAVENELEELEELRERR 700
|
570
....*....|
gi 327478526 1890 EKGNLRVKQL 1899
Cdd:PRK02224 701 EALENRVEAL 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1013-1472 |
1.41e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1013 KLSKERKLLEdRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEkgRQELEKLKRRLDGESSELQEQMVEQQ 1092
Cdd:COG4913 246 DAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1093 QRAEELRAQL----GRKEEELQAALARAEDEGGARAQLLKSL----------------------REAQAALAEAQEDLES 1146
Cdd:COG4913 323 EELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaeefaalrAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1147 ERVARTKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQEVTELKKTLEEETRIHEAAVQ------ELRQR 1217
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAELPfvgeliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1218 ------------HGQALGEL--AEQLEQARRgkgAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQG 1283
Cdd:COG4913 473 eerwrgaiervlGGFALTLLvpPEHYAAALR---WVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1284 -----------------------------RAG-----------DGERARAE-------AAEKLQRAQAELENVSGALNEA 1316
Cdd:COG4913 550 wleaelgrrfdyvcvdspeelrrhpraitRAGqvkgngtrhekDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1317 ESKTIRLSKELSSTEAQLHDAQELLQ------------------EETRAKLALGS-RVRAMEAEAAGLREQLEEEAAARE 1377
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEyswdeidvasaereiaelEAELERLDASSdDLAALEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1378 RAGRELQTAQAQLSEWRRRQEEEAGALeaGEEARRRAAREAEALTQRLAEKTETvDRLERGRRRLQQELDDATmdlEQQR 1457
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALR---ARLN 783
|
570
....*....|....*
gi 327478526 1458 QLVSTLEKKQRKFDQ 1472
Cdd:COG4913 784 RAEEELERAMRAFNR 798
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1002-1734 |
2.51e-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: 56.13 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1002 EDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEeeKVKSLNKLRLKYEATIADMEDRLRK----EEKGRQELEKLKRRL 1077
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1078 DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQ 1157
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1158 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQevteLKKTLEEETRIHeaAVQELRQRHGQALGELAEQLEQARRGKG 1237
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI----SCQQHTLTQHIH--TLQQQKTTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1238 awekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAE 1317
Cdd:TIGR00618 411 ----TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1318 SKtirlskelssteAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLsewRRRQ 1397
Cdd:TIGR00618 487 RK------------KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV---YHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1398 EEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDdatMDLEQQRQLVSTLEKKQRKFDQLLA-E 1476
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---KLSEAEDMLACEQHALLRKLQPEQDlQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1477 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELER---ACRV 1553
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1554 AEQAANDLRAQVTELEDELTAAedaklrlevtvqalktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAV 1633
Cdd:TIGR00618 709 LETHIEEYDREFNEIENASSSL------------------GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1634 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK----RLKGLEAEVLRL 1709
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQ 850
|
730 740
....*....|....*....|....*
gi 327478526 1710 QEELAASDRARRQAQQDRDEMADEV 1734
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
992-1234 |
8.57e-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: 8.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 992 TTEAKMKKFEEDLLLLED-------QNSKLSKERKLLEDRLAEFS--SQAAEEEEKVKSLnklrlkyEATIADMEDRLRK 1062
Cdd:COG4913 607 DNRAKLAALEAELAELEEelaeaeeRLEALEAELDALQERREALQrlAEYSWDEIDVASA-------EREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1063 EEKGRQELEKLKRRLDG---ESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLlksLREAQAALAE 1139
Cdd:COG4913 680 LDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1140 AQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSK-------REQEVTELKKTLEEEtRIHEAAVQ 1212
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleSLPEYLALLDRLEED-GLPEYEER 835
|
250 260
....*....|....*....|....*
gi 327478526 1213 ELRQRH---GQALGELAEQLEQARR 1234
Cdd:COG4913 836 FKELLNensIEFVADLLSKLRRAIR 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1651-1891 |
1.00e-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: 53.23 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1651 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1730
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1731 adevangnlsKAAILEEKRQLEGRLGQLEEELEEEqsnsellndrYRKLLLQVESLTTELSAERSFSAKAESGRQQLErQ 1810
Cdd:COG4942 96 ----------RAELEAQKEELAELLRALYRLGRQP----------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1811 IQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQETRERilsGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLE 1890
Cdd:COG4942 155 LRADLAELAALRAELEAERA-ELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
.
gi 327478526 1891 K 1891
Cdd:COG4942 231 R 231
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1021-1828 |
1.06e-06 |
|
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: 53.97 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1021 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYE----ATIADMEDRLRKEEKGRQELEKLKRRldgesselqeqmveQQQRAE 1096
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRR--------------ESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1097 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR------------------ 1158
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrslgsa 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1159 -----RDLGEELEALRGEL---EDTLDSTNAqqELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGE---LAE 1227
Cdd:pfam15921 222 iskilRELDTEISYLKGRIfpvEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1228 QLE----QARRGKGAWEKTRLALEAEVSELRAELsslQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE------ 1297
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnld 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1298 -KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAAR 1376
Cdd:pfam15921 377 dQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1377 ERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1456
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1457 RQLVSTLEKKQRKFD--QLLAEEKAAVLRAVEERERAEAEGREREaralslTRALEEEQEAREELERQNRALRAELEALL 1534
Cdd:pfam15921 537 KNEGDHLRNVQTECEalKLQMAEKDKVIEILRQQIENMTQLVGQH------GRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1535 SSKDDVGKSVHELEraCRVAE----------------QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQ 1598
Cdd:pfam15921 611 ILKDKKDAKIRELE--ARVSDlelekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK----RNFR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1599 GRDEAGEERRRQLAKQLRDAEVERDEERKQ-----------RTLAVAARKKLEGELEELKAqMASAGQGKEEAVKQLRKM 1667
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghaMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1668 QAQMKElwrevEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELA----ASDRARRQAQQDRDEMADEVANGNLSK 1741
Cdd:pfam15921 764 KHFLKE-----EKNKLSQElsTVATEKNKMAGELEVLRSQERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1742 AAILEEKRQLEGRlGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAE-RSFSAKAESGRQQLERQIQELRGRLGE 1820
Cdd:pfam15921 839 LQHTLDVKELQGP-GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQLLQELRSVINE 917
|
....*...
gi 327478526 1821 EDAGARAR 1828
Cdd:pfam15921 918 EPTVQLSK 925
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
863-1478 |
1.28e-06 |
|
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: 53.82 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 863 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------ARLAEQLRAEAELCAEAEETRGRLAAR 933
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 934 KQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQleKVTTEAKMKKFEEDLLLLEDQ--- 1010
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQKTTLTQKlqs 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1011 -NSKLSKERKLLEDRLAEFSSQAAEEEEKV--KSLNKLRLKYEATIADMEDRLRKEEKGRQ-ELEKLKRRLDGESSELQ- 1085
Cdd:TIGR00618 398 lCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQt 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1086 -EQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLL-------KSLREAQAALAEAQEDLESERVARTKAEKQ 1157
Cdd:TIGR00618 478 kEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1158 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQLEQA 1232
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1233 RRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGA 1312
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1313 LNEAESKTIRLSKELSSTEAQLHDAQELLQE-ETRAKLALGSRVRAMEaeaaglreQLEEEAAARERAGRELQTAQAQLS 1391
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHF--------NNNEEVTAALQTGAELSHLAAEIQ 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1392 EWRRRQEEEAGALeageeaRRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFD 1471
Cdd:TIGR00618 789 FFNRLREEDTHLL------KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*..
gi 327478526 1472 QLLAEEK 1478
Cdd:TIGR00618 863 QLTQEQA 869
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1606-1929 |
1.48e-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: 53.80 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1606 ERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK------------- 1672
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqqekieryqedle 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1673 ELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARrQAQQDRdemadevangnlskaAIleEKRQLE 1752
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQTR---------------AI--QYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1753 GRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE---EDAGARARH 1829
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1830 KMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEkgnlrvkQLKRQLEEAEEE 1909
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQ 572
|
330 340
....*....|....*....|
gi 327478526 1910 ASRAQAGRRRLQRELEDVTE 1929
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRA 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
983-1752 |
1.71e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 983 RQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLR 1061
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1062 KEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEELRAqlgrKEEELQAALARaedeggaraqlLKSLREAQAALA 1138
Cdd:PRK03918 232 ELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1139 EAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQ---EVTELKKTLE--EETRIHEAAVQE 1213
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1214 LRQRH-GQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQegeqrrrrlelQLQEVQGRAGDGERAR 1292
Cdd:PRK03918 377 LKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-----------ELKKAKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1293 AEAAEK--LQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLalgsrVRAMEAEAAGLREqle 1370
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYNL--- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1371 eeaaareragrelqtaqaqlsewrrrqeeeagaleageearrraareaealtQRLAEKTETVDRLERGRRRLQQELDDAT 1450
Cdd:PRK03918 518 ----------------------------------------------------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1451 MDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLraveereraeaegrerearalsltraleeeqeareelerqnraLRAEL 1530
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDEL--EEELAEL-------------------------------------------LKELE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1531 EALLSSKDDVGKSVHELERACRvaeqAANDLRAQVTELEDELTAAEDAKLRLEvtvqalktQHERDLQGRDEAGEERRrq 1610
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYN----EYLELKDAEKELEREEKELKKLEEELD--------KAFEELAETEKRLEELR-- 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1611 laKQLRDAEVERDEERkqrtlavaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1690
Cdd:PRK03918 647 --KELEELEKKYSEEE---------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 327478526 1691 QNRESEkRLKGLEAEVLRLQEELAasDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1752
Cdd:PRK03918 716 LEKALE-RVEELREKVKKYKALLK--ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1021-1436 |
1.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1021 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1100
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1101 QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTN 1180
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1181 AQQELRSKREQEVTELKKTLEEETRIHEA-----------------AVQELRQRhgqaLGELAEQLEQARRGKGAWEK-- 1241
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRER----VEELEAELEDLEEEVEEVEErl 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1242 TRL----ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGD----GERARAEAAEKLQRAQAELENVS--- 1310
Cdd:PRK02224 499 ERAedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleaeAEEKREAAAEAEEEAEEAREEVAeln 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1311 ---GALNEAESKTIRLSKELSSTEAQLHDAQEL---------LQEETRAKLA-LGSRVRAMEAEAAGlreqleEEAAARE 1377
Cdd:PRK02224 579 sklAELKERIESLERIRTLLAAIADAEDEIERLrekrealaeLNDERRERLAeKRERKRELEAEFDE------ARIEEAR 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 327478526 1378 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLE 1436
Cdd:PRK02224 653 EDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1526-1947 |
2.02e-06 |
|
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: 53.20 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1526 LRAELEALLSSKDDvgkSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ------ALKTQHERDLQG 1599
Cdd:pfam15921 329 LRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHkrekelSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1600 RDEAGEERRRQLAKQL--RDAEVERDEerkqrTLAVAARKKLEGELEElkaQMAsAGQGKEEAVKQLRKMQAQM---KEL 1674
Cdd:pfam15921 406 RDTGNSITIDHLRRELddRNMEVQRLE-----ALLKAMKSECQGQMER---QMA-AIQGKNESLEKVSSLTAQLestKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1675 WREVEETRTSRE-----------EIFSQNRESEKRLKGLEAEV--------LRLQE-----------------------E 1712
Cdd:pfam15921 477 LRKVVEELTAKKmtlessertvsDLTASLQEKERAIEATNAEItklrsrvdLKLQElqhlknegdhlrnvqtecealklQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1713 LAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQsnseLLNDRYRKLLLQVESLTTELSA 1792
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLEL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1793 ERSFSAKAESGRQQLERQIQELRGRLGEEDAGARA----------------RHK-----MTIAALESKLAQAEEQLEQeT 1851
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNelnslsedyevlkrnfRNKseemeTTTNKLKMQLKSAQSELEQ-T 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1852 RERIlsgKLVRRAEKRLKEVVLQVEEERRVAdqlRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESA 1931
Cdd:pfam15921 712 RNTL---KSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
490
....*....|....*.
gi 327478526 1932 ESMNREVTTLRNRLRR 1947
Cdd:pfam15921 786 NKMAGELEVLRSQERR 801
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1068-1358 |
2.19e-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: 52.38 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1068 QELEKLKRRLdgesSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1147
Cdd:pfam19220 41 RELPQAKSRL----LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1148 RVARTKAEKQ-------RRDLGEELEALRGEL----EDTLDSTNAQQELRSKR---EQEVTELKKTLEE---ETRIHEAA 1210
Cdd:pfam19220 117 TAQAEALERQlaaeteqNRALEEENKALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1211 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQtarqegeqrrrrleLQLQEVQGRAGDGER 1290
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLR--------------MKLEALTARAAATEQ 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1291 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAM 1358
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
867-1259 |
5.43e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 867 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 946
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 947 RVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLA 1026
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1027 EFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqMVEQQQR--AEELRAQLGR 1104
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS-MAAQRDRtqAELHQARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1105 KEEELQAALAR-AEDEGGAR-AQLLKSLReaqaalaeAQEDLESERVARTKAEKQRRD--LGEEL---EALRGELEDTLD 1177
Cdd:pfam07888 282 AQLTLQLADASlALREGRARwAQERETLQ--------QSAEADKDRIEKLSAELQRLEerLQEERmerEKLEVELGREKD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1178 STNAQqelRSKREQEVTELKKTLEEETRiheaaVQELRQRHGQALGELAEQLEQaRRGKGAWEKTRLALEAEVSELRAEL 1257
Cdd:pfam07888 354 CNRVQ---LSESRRELQELKASLRVAQK-----EKEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDSPL 424
|
..
gi 327478526 1258 SS 1259
Cdd:pfam07888 425 SD 426
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
985-1344 |
5.71e-06 |
|
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: 51.50 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 985 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME---DRLR 1061
Cdd:COG5185 177 KKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1062 ---------KEEKGRQELEKLKR------RLDGESSELQEQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQl 1126
Cdd:COG5185 257 klveqntdlRLEKLGENAESSKRlnenanNLIKQFENTKEKIAEYTKSIDIKKATE-SLEEQLAAAEAEQELEESKRET- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1127 LKSLREAQAALAEAQEDLEsERVARTKAEKQRRDLGEELEALRGELEdtldstNAQQELRSKREqEVTELKKTLEEETRI 1206
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELSKSSEELD------SFKDTIESTKE-SLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1207 HEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlQEVQGRAG 1286
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1287 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1344
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
876-1208 |
7.20e-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: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 876 QELQKVQELQQQsarevgeLQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECS 955
Cdd:TIGR04523 398 SKIQNQEKLNQQ-------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 956 RQMQTEKKRLQQhiqeleahleaeegarqklQLEKVTTEAKMKkfeedllllEDQNSKLSKERKLLEDRLAEFSSQAAEE 1035
Cdd:TIGR04523 471 KVLSRSINKIKQ-------------------NLEQKQKELKSK---------EKELKKLNEEKKELEEKVKDLTKKISSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1036 EEKVKSLNKLRLKYEATIADMEDRLRK--EEKGRQELEKLKRRLDGESSEL---QEQMVEQQQRAEELRAQLGRKEEELQ 1110
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1111 AALARAEdeggaraQLLKSLREAQAALAEAQEDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTN----AQQELR 1186
Cdd:TIGR04523 603 KEIEEKE-------KKISSLEKELEKAKKENEKLSSI---IKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiikKIKESK 672
|
330 340
....*....|....*....|..
gi 327478526 1187 SKReQEVTELKKTLEEETRIHE 1208
Cdd:TIGR04523 673 TKI-DDIIELMKDWLKELSLHY 693
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1634-1870 |
7.77e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1634 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1713
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1714 AASDRAR-RQAQQDRDEMAdevangnLSKAAILEEKRQLEgrlgqleeeleeeqsnseLLNDRYRKLLLQVESLTTELSA 1792
Cdd:COG4942 107 AELLRALyRLGRQPPLALL-------LSPEDFLDAVRRLQ------------------YLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1793 ERSFSAKAESGRQQLERQIQELRGRLgEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKE 1870
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1554-1977 |
8.32e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1554 AEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDA----EVERDEER 1626
Cdd:PTZ00121 1274 AEEArkADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1627 KQRTLAVAARKKLEGEleELKAQMAsagQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK--RLKGlEA 1704
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAA--EKKKEEA---KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKK-KA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1705 EVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEgrlgqleeeLEEEQSNSELLNDRYRKLLLQVE 1784
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA--EEAKKAD---------EAKKKAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1785 SLTTELSAERSFSAKAESGRQQLE-RQIQELRGrlGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERIlsgKLVRR 1863
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEaKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1864 AEKRlKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRN 1943
Cdd:PTZ00121 1572 AEED-KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
410 420 430
....*....|....*....|....*....|....
gi 327478526 1944 RLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQ 1977
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1244-1469 |
9.41e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1244 LALEAEVSELRAELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1323
Cdd:COG4942 16 AAQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1324 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAME----AEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1399
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1400 EAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1469
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1524-1740 |
1.02e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1524 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEA 1603
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1604 GeerRRQLAKQLRDAEVERDEERKQRTLAVAAR------KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWRE 1677
Cdd:COG4942 117 G---RQPPLALLLSPEDFLDAVRRLQYLKYLAParreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 1678 VEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLS 1740
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
871-1361 |
1.07e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 871 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA-EQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVG 949
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 950 EEEECSRQMQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEdRLAEFS 1029
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAEQLRQNL--------EKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1030 SQAAEEEEKVKSLNKLR---LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA--QLGR 1104
Cdd:pfam05557 204 KELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1105 KEEELQAALARAEDEGGARAQLLKSLReaqaalaEAQEDLESE-RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ- 1182
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLE-------KARRELEQElAQYLKKIEDLNKKL-KRHKALVRRLQRRVLLLTKEr 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1183 ---QELRSKREQEVTELKKTLEEETRIHEAAvqELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSS 1259
Cdd:pfam05557 356 dgyRAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1260 LQTARQEGEQRRRRLELQLQEvqgragdGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKE-LSSTEAQLHDAQ 1338
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLETLE-------LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNpAAEAYQQRKNQL 506
|
490 500
....*....|....*....|...
gi 327478526 1339 ELLQEETRaklALGSRVRAMEAE 1361
Cdd:pfam05557 507 EKLQAEIE---RLKRLLKKLEDD 526
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1710-1952 |
1.19e-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: 49.76 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1710 QEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTE 1789
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1790 LSAERSFSAKAESGRQQLERQiQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLK 1869
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1870 EVVLQVEEERRVADQLRDQLEKgnlRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1949
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 327478526 1950 LTF 1952
Cdd:COG4942 255 LPW 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
806-1048 |
1.32e-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: 49.76 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 806 IIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKlrhwqwwrlfTKVKPLLQVTRQDEVLQARAQELQKVQELQ 885
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK----------EEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 886 QQSAREVGELQGRVAQLEEE----RARLAEQLRAEAELCAEAEETR-------GRLAARKQELELVVSELEARVGEEEEC 954
Cdd:COG4942 79 AALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 955 SRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAE 1034
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 327478526 1035 EEEKVKSLNKLRLK 1048
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1274-1727 |
1.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1274 LELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGS 1353
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1354 RVRAMEAEAagLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREA-EALTQRLAEKTETV 1432
Cdd:COG4717 131 YQELEALEA--ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1433 DRLERGRRRLQQELDDATMDLEQ-QRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEE 1511
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1512 EQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE----QAANDLRAQVTELEDELTAAEDAKLRLEvtVQ 1587
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspEELLELLDRIEELQELLREAEELEEELQ--LE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1588 ALKTQHERDLQGRDEAGEERRRQLAKQLRD-----AEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK 1662
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEyqelkEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 1663 QLRKMQAQMKELWREVEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDR 1727
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
864-1254 |
1.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 864 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA--EQLRAEAELCAEAEETRGRLAA--RKQELEL 939
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelERLKKRLTGLTPEKLEKELEELekAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 940 VVSELEARVGEeeecsrqMQTEKKRLQQHIQELEAHLEAEEGARQKLQ-------LEKVTteAKMKKFEEDLLLLEDQNS 1012
Cdd:PRK03918 406 EISKITARIGE-------LKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkelLEEYT--AELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1013 KLSKERKLLEDRLAEFSS---------QAAEEEEKVKSLNKLRLKYEAtiadmedrlRKEEKGRQELEKLKRRLDGESSE 1083
Cdd:PRK03918 477 KLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELEKKA---------EEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1084 LqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLK--------------SLREAQAALAEAQEDLESERV 1149
Cdd:PRK03918 548 L-EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEerlkelepfyneylELKDAEKELEREEKELKKLEE 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1150 ARTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREqEVTELKKTLEE-ETRIHEAavQELRQRHGQALGELAEQ 1228
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELRE-EYLELSRELAGlRAELEEL--EKRREEIKKTLEKLKEE 702
|
410 420
....*....|....*....|....*.
gi 327478526 1229 LEQARRGKGAWEKTRLALEaEVSELR 1254
Cdd:PRK03918 703 LEEREKAKKELEKLEKALE-RVEELR 727
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
871-1229 |
1.99e-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: 49.95 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 871 LQARAQELQKVQE-LQQQsarevGELQGRVAQLEEERARLAEQlraeAELCAEAEETRGRLAARKQELELVVSELEARVG 949
Cdd:COG3096 329 YQAASDHLNLVQTaLRQQ-----EKIERYQEDLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 950 EEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERKLLEDRLAEFS 1029
Cdd:COG3096 400 DYQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVAD 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1030 SQAAEEEEKVKSLNKlrlkyeatIADMEDRLRKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQQQRAEELRAQ 1101
Cdd:COG3096 469 AARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1102 LGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELED 1174
Cdd:COG3096 541 FCQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1175 TLDSTNAQQELRSK---REQEVTELKKTLEEETRIHEAAVQELRQRHGQA---LGELAEQL 1229
Cdd:COG3096 621 ALADSQEVTAAMQQlleREREATVERDELAARKQALESQIERLSQPGGAEdprLLALAERL 681
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
903-1312 |
2.09e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 903 EEERARLAEQlraEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEEcsrqmqtekkrLQQHIQELEahleaeegA 982
Cdd:PRK04863 278 ANERRVHLEE---ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD-----------LEQDYQAAS--------D 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 983 RQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK 1062
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1063 EEKGRQELEKLKRRLDGES------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEdeggARAQLLKSLREAQAA 1136
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1137 LAEAQEDLESERVARTKaekqrRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEetrihEAAVQELRQ 1216
Cdd:PRK04863 492 SEAWDVARELLRRLREQ-----RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDELEQLQE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1217 RHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAE----------LSSLQTARQEGEQRRRRLELQLQEVQGRAG 1286
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQQLLERER 641
|
410 420
....*....|....*....|....*.
gi 327478526 1287 DGERARAEAAEKLQRAQAELENVSGA 1312
Cdd:PRK04863 642 ELTVERDELAARKQALDEEIERLSQP 667
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1047-1168 |
2.17e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1047 LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAEDEGgarAQL 1126
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 327478526 1127 LKSLReaqaalaeAQEDLESERVARTKAEKQRRDLGEELEAL 1168
Cdd:PRK00409 590 IKELR--------QLQKGGYASVKAHELIEARKRLNKANEKK 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
956-1172 |
2.21e-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: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 956 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1035
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1036 EEKVKSLNKL------------------------RLKYEATIAD-MEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVE 1090
Cdd:COG4942 103 KEELAELLRAlyrlgrqpplalllspedfldavrRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1091 QQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALaeaqedlesERVARTKAEKQRRDLGEELEALRG 1170
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---------ARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 327478526 1171 EL 1172
Cdd:COG4942 254 KL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1524-1673 |
2.57e-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: 47.61 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1524 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1602
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1603 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE 1673
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
867-1400 |
2.80e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 867 QDEVLQARAQE--LQKVQELQQQSArevgELQGRVAQLEEERARLaeqlraeaelcaeaeetrgRLAARKQELELvvseL 944
Cdd:COG4913 241 HEALEDAREQIelLEPIRELAERYA----AARERLAELEYLRAAL-------------------RLWFAQRRLEL----L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 945 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVtteakmKKFEEDLLLLEDQNSKLSKERKLLEDR 1024
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1025 LAEFSSQAAEEEEkvkSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--------- 1095
Cdd:COG4913 368 LAALGLPLPASAE---EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniparlla 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1096 --EELRAQLGRKEEELQAA--L--ARAEDE----------GGAR----------AQLLKSLREAQAALAeaqedLESERV 1149
Cdd:COG4913 445 lrDALAEALGLDEAELPFVgeLieVRPEEErwrgaiervlGGFAltllvppehyAAALRWVNRLHLRGR-----LVYERV 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1150 ARTKAEKQRRDLGEelEALRGELEdtLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHG---------- 1219
Cdd:COG4913 520 RTGLPDPERPRLDP--DSLAGKLD--FKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGngtrhekddr 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1220 --------------QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQrrrrlELQLQEVQGRA 1285
Cdd:COG4913 596 rrirsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAEREI 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1286 GDGERARAEAAE---KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEA 1362
Cdd:COG4913 671 AELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
570 580 590
....*....|....*....|....*....|....*...
gi 327478526 1363 AGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEE 1400
Cdd:COG4913 751 LEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
982-1316 |
3.30e-05 |
|
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: 48.53 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 982 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLN------KLRLK-YEATIA 1054
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEaakeelRIELRdKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1055 DMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEG------GAR-AQLL 1127
Cdd:pfam19220 122 ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaelaelTRRlAELE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1128 KSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH 1207
Cdd:pfam19220 202 TQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1208 EAAVQEL---RQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGR 1284
Cdd:pfam19220 282 ERRLKEAsieRDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKR 361
|
330 340 350
....*....|....*....|....*....|....*.
gi 327478526 1285 ----AGDGERARAEAAEKLQRAQAELENVSGALNEA 1316
Cdd:pfam19220 362 feveRAALEQANRRLKEELQRERAERALAQGALEIA 397
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1143-1363 |
3.38e-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: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1143 DLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQAL 1222
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1223 GELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRA 1302
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1303 QAELENVSGALNEAESKTIRLSKELSSTEAQLhdaQELLQEETRAKLALGSRVRAMEAEAA 1363
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1154-1929 |
3.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1154 AEKQRRDLGEELEALRGELEDTLDSTNAQQELR---SKREQEVTELKKTLEEE---TRIHEAAVQE-LRQ-----RHGQA 1221
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaASDHLNLVQTaLRQqekieRYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1222 LGELAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrLELQlqevQGRAG---DGERA 1291
Cdd:PRK04863 357 LEELEERLEEqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQA----------LDVQ----QTRAIqyqQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1292 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR-EQLE 1370
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVaRELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1371 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1450
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA-----------ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1451 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsltraleeeqeareeLERQNRALRAEL 1530
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA---------------------------------------RAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1531 EALLS-SKDDVGKSvheleracrvaeQAANDLRAQVTELEDELTAAEDaklRLEVTVQALKTQHERdLQGRDEAGEERRR 1609
Cdd:PRK04863 613 ARLREqSGEEFEDS------------QDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1610 QLAK---------------------------QLRDAEVERDEERKQRTLAvaarkKLEGELEEL------KAQMASAGQG 1656
Cdd:PRK04863 677 ALAErfggvllseiyddvsledapyfsalygPARHAIVVPDLSDAAEQLA-----GLEDCPEDLyliegdPDSFDDSVFS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1657 KEEAVKQLrkmqaQMKELWREVEETRTSREEIFSQnRESEKRLKGLEAEVLRLQEELAASDRaRRQAQQDRDEMADEVAN 1736
Cdd:PRK04863 752 VEELEKAV-----VVKIADRQWRYSRFPEVPLFGR-AAREKRIEQLRAEREELAERYATLSF-DVQKLQRLHQAFSRFIG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1737 GNLSKA------AILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELS--AERSFSAKAESGRQQLE 1808
Cdd:PRK04863 825 SHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLD 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1809 RqiqelrgrlGEEDAGARARHKMTIAALE---SKLAQAEEQLEQETRERILSGKLVRRAEKR---LKEVVlqveeERRVA 1882
Cdd:PRK04863 905 E---------AEEAKRFVQQHGNALAQLEpivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVV-----QRRAH 970
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 327478526 1883 ---DQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTE 1929
Cdd:PRK04863 971 fsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1524-1947 |
3.97e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1524 RALRAELEALLSSKDDVGKSVHELERAcrvaEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1602
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1603 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKL----EGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREV 1678
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1679 EETRTSREEIFSQNRESEKR-----------LKGLEAEVLRLQEELAA---------------SDRARRQAQQDRDEMAD 1732
Cdd:COG4717 230 EQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1733 EVANGNLSKAAILEEKRQLEgrlgqleeeleeeqSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAEsgRQQLERQIQ 1812
Cdd:COG4717 310 LPALEELEEEELEELLAALG--------------LPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1813 ELRGRLG---EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQL 1889
Cdd:COG4717 374 ALLAEAGvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1890 EKGNLRVKQLKRQLeEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG4717 452 REELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1053-1237 |
4.02e-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: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1053 IADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDeggARAQL--LKSL 1130
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1131 REAQAALAeaqeDLESERVARTKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEETRIHEAA 1210
Cdd:COG1579 89 KEYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 327478526 1211 VQELRQRHGQALGELAEQL----EQARRGKG 1237
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1592-1902 |
5.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1592 QHERDLQGRDEAGEERRRQL--AKQLRDAEVERDEE-RKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLRKMQ 1668
Cdd:PRK04863 276 RHANERRVHLEEALELRRELytSRRQLAAEQYRLVEmARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1669 AQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRA----------RRQAQQDRDEM-----ADE 1733
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERAkqlcgLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1734 VANGNLSkaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSF-----------SAKAES 1802
Cdd:PRK04863 435 LTADNAE--DWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvarellrrlrEQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1803 GR-QQLERQIQELRGRLGEEdagararhkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRV 1881
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|.
gi 327478526 1882 ADQLRDQLEKGNLRVKQLKRQ 1902
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAAR 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1085-1339 |
5.69e-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: 47.84 E-value: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1085 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEE 1164
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---------------------ALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1165 LEALRGELEDTldsTNAQQELRSKREQEVTELKKTLeeetriheAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1244
Cdd:COG4942 78 LAALEAELAEL---EKEIAELRAELEAQKEELAELL--------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1245 ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLS 1324
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 327478526 1325 KELSSTEAQLHDAQE 1339
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1524-1947 |
6.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1524 RALRAELEALLSSKDDVGKSVHELERACRVAEQAAND--------LRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER 1595
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1596 DLqgrdEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGK---EEAVKQLRKMQA--- 1669
Cdd:COG4913 378 SA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAeal 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1670 --------------QMKEL---WRE--------------------------VEET------RTSREEIFSQNRESEKRLK 1700
Cdd:COG4913 454 gldeaelpfvgeliEVRPEeerWRGaiervlggfaltllvppehyaaalrwVNRLhlrgrlVYERVRTGLPDPERPRLDP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1701 G----------------LEAEVLRL--------QEELAASDRA-----------RRQAQQDRDEMADEVANG--NLSKAA 1743
Cdd:COG4913 534 DslagkldfkphpfrawLEAELGRRfdyvcvdsPEELRRHPRAitragqvkgngTRHEKDDRRRIRSRYVLGfdNRAKLA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1744 ILEEKR-QLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAersfsakaesgrQQLERQIQELRGRLGEED 1822
Cdd:COG4913 614 ALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV------------ASAEREIAELEAELERLD 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1823 AGararhKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGnlRVKQLKRQ 1902
Cdd:COG4913 682 AS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRALLEER 754
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 327478526 1903 LEEAEEEASRAQAgRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG4913 755 FAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1107-1476 |
1.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1107 EELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDT---LDSTNA 1181
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1182 QQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ 1261
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1262 TARQEGEQRRRRLELQ-----------LQEVQGRAGDGERARAEAA-----------EKLQRAQAELENVSGALNEAESK 1319
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1320 TIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQE- 1398
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1399 --------------EEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQlVSTLE 1464
Cdd:COG4717 394 aeeyqelkeeleelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELA 472
|
410
....*....|..
gi 327478526 1465 KKQRKFDQLLAE 1476
Cdd:COG4717 473 ELLQELEELKAE 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
815-1229 |
1.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 815 RGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHwqwwRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQ------QQS 888
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 889 AREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV----VSELEARVGEEEECSRQMQTEKKR 964
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 965 LQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--------------------------LLEDQNSKLSKER 1018
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1019 KLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--- 1095
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1096 -------EELRAQLGRKEE--ELQAALARAEDEGGARAQLLKSLrEAQAALAEAQEDLESERVARTKAEKQRRDLGEELE 1166
Cdd:COG4717 378 eagvedeEELRAALEQAEEyqELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327478526 1167 ALRGELEDtLDSTNAQQELRSKREQEVTELKKTLEEETRIH------EAAVQELRQRHGQALGELAEQL 1229
Cdd:COG4717 457 ELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVLERASEY 524
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1555-1694 |
1.10e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.50 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1555 EQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALK-----TQHERD-LQGRDEAGEERRRQLAKQLRDAEVERDEERKQ 1628
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRaslsaAEAERSrLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 327478526 1629 RTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWR--------EVEETRTSREEIFSQNRE 1694
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRrlnvalaqRVQELNRYRSEFFGRLRE 205
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1522-1713 |
1.20e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1522 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRD 1601
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE-RLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1602 EAGEERRR------QLAKQLRDAEVERDEERKQRTLavaarkklEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELW 1675
Cdd:COG1340 130 LSPEEEKElvekikELEKELEKAKKALEKNEKLKEL--------RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 327478526 1676 REVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1713
Cdd:COG1340 202 KEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
818-1349 |
1.29e-04 |
|
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: 47.42 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 818 LARRAFQKRQQQ---QSALRVMQRNCAAYLKLRHWQWWRLFTKVKPLlqvtrQDEVLQARAQELQKVQELQQQ---SARE 891
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLESTVSQL-----RSELREAKRMYEDKIEELEKQlvlANSE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 892 VGELQGRVAQLEEERARLAEQLRAEAelcaeaeetrGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQE 971
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLL----------ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 972 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLrlkyea 1051
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL------ 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1052 tIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE--------------------QMVEQQQRAEELRAQL--------- 1102
Cdd:pfam15921 502 -TASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnvqtecealklQMAEKDKVIEILRQQIenmtqlvgq 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1103 -GRKEEELQAALARAEDEGGARAQLLKSLR-------EAQAALAEAQEDLESERVARTKAEKQR----RDLGEELEALRG 1170
Cdd:pfam15921 581 hGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERlravKDIKQERDQLLN 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1171 ELEDTLDSTNAQQElrskrEQEVteLKKTLEEETRIHEAAVQELRQRHGQALGELAE---QLEQARRGKGAWEKTRLALE 1247
Cdd:pfam15921 661 EVKTSRNELNSLSE-----DYEV--LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrnTLKSMEGSDGHAMKVAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1248 AEVSELRAELSSLQTarqegeqRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1327
Cdd:pfam15921 734 KQITAKRGQIDALQS-------KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570 580 590
....*....|....*....|....*....|...
gi 327478526 1328 SSTEAQLHDA-----------QELLQEETRAKL 1349
Cdd:pfam15921 807 ANMEVALDKAslqfaecqdiiQRQEQESVRLKL 839
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1697-1947 |
1.66e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1697 KRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADevangnlskaaiLEEKRQLEGRLgqleeELEEEQSNSELLNDRY 1776
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARER------------LAELEYLRAAL-----RLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1777 RKLLLQVESLTTELSAersfsakAESGRQQLERQIQELRGRLgEEDAGARarhkmtIAALESKLAQAEEQLEQETRERil 1856
Cdd:COG4913 298 EELRAELARLEAELER-------LEARLDALREELDELEAQI-RGNGGDR------LEQLEREIERLERELEERERRR-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1857 sgklvRRAEKRLKEVVLQVEEER----RVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAE 1932
Cdd:COG4913 362 -----ARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250
....*....|....*
gi 327478526 1933 SMNREVTTLRNRLRR 1947
Cdd:COG4913 437 NIPARLLALRDALAE 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
886-1351 |
1.81e-04 |
|
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: 46.76 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 886 QQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEeeecsrqmqtekkrl 965
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE--------------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 966 qqhiqeleahleaeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER----KLLEDRLAEFSSQAAEEEEKVKS 1041
Cdd:pfam12128 302 ----------------KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1042 L----NKLRLKYEATIAdmedrLRKEEKGRqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAE 1117
Cdd:pfam12128 366 LtgkhQDVTAKYNRRRS-----KIKEQNNR-DIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1118 DEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRrdlgEELEALRGELEdtlDSTNAQQELRSKREQEVTELk 1197
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVE---RLQSELRQARKRRDQASEAL- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1198 ktleeetRIHEAAVQELRQRHGQALGELAEQ----LEQARRGKGAWEKTRLALEAEVSELRAELS-SLQTARQEGEQRRR 1272
Cdd:pfam12128 509 -------RQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 327478526 1273 RLELQLQEVQgragdgeraRAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQellQEETRAKLAL 1351
Cdd:pfam12128 582 GVKLDLKRID---------VPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTAL 648
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1157-1479 |
1.81e-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: 46.87 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1157 QRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV------------QELRQRHGQALGE 1224
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlnlvqtalrqQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1225 LAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrlelqLQEVQGRAGDGERAR---AE 1294
Cdd:COG3096 359 LTERLEEqeevveeAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA--------------LDVQQTRAIQYQQAVqalEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1295 AAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAA-GLREQLEEEA 1373
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1374 AARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDL 1453
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAELEQRLRQQQNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
330 340 350
....*....|....*....|....*....|
gi 327478526 1454 ----EQQRQLVSTLEKKQRKFDQLLAEEKA 1479
Cdd:COG3096 574 aeavEQRSELRQQLEQLRARIKELAARAPA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1421-1654 |
1.95e-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: 45.91 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1421 LTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEekaavlraveereraeaegREREA 1500
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------------------LEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1501 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKD--DVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDA 1578
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1579 KLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAG 1654
Cdd:COG4942 173 RAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1690-1925 |
1.99e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1690 SQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEvangnlskaailEEKRQLEGRLGQLEEELEEEQSNS 1769
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1770 ELLNDRYRKLLLQVESLTTELSAersfsAKAESGRQQLERQIQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQ 1849
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1850 ETRerilsgklvrraeKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLkrqleeaeeeaSRAQAGRRRLQRELE 1925
Cdd:COG3206 310 EAQ-------------RILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVE 361
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
674-698 |
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 327478526 674 YKESLSRLMATLSNTNPSFVRCIVP 698
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1325-1947 |
2.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1325 KELSSTEAQLHDAQEllQEETRAKL-ALGSRVRAMEAEAAGLREQLEEEAAARERAGRELqtAQAQLSEWRRRQEEEAGA 1403
Cdd:COG4913 235 DDLERAHEALEDARE--QIELLEPIrELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1404 LEAGEEARRRAAREAEALTQRLAE-KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEkkqrkfdqLLAEEKAAVL 1482
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALG--------LPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1483 RAVEERERAEAEGREREARALSLTRALEEEQEAREELerQNRALRAELEALLSSKDDVGKSVHEL-ERACRVAEQAANDL 1561
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--ELRELEAEIASLERRKSNIPARLLALrDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1562 RA-----QVTELEDE--------------------------LTAAEDAKLRLEVTVQALKTQHERDLQGRDEAG------ 1604
Cdd:COG4913 461 PFvgeliEVRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1605 --------EERRRQLAKQLRDAEVERDEERKQRTLAV--------------------------------AARKKLEGELE 1644
Cdd:COG4913 541 dfkphpfrAWLEAELGRRFDYVCVDSPEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1645 ELKAQMASAGQGKEEAVKQLRKMQAQmKELWREVEETRtsreeifsqnrESEKRLKGLEAEVLRLQEELAASDRArrqaQ 1724
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQER-REALQRLAEYS-----------WDEIDVASAEREIAELEAELERLDAS----S 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1725 QDRDEMADEVAngnlskaAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTEL-SAERSFSAKAESG 1803
Cdd:COG4913 685 DDLAALEEQLE-------ELEAELEELEEELDE--------------LKGEIGRLEKELEQAEEELdELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1804 RQQLERQIQELRGRLGEEDAGARARHKMT--IAALESKLAQAEEQLEQETRErilsgkLVRRAEKRLKEVVLQVEEERRV 1881
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEerIDALRARLNRAEEELERAMRA------FNREWPAETADLDADLESLPEY 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1882 ADQLrDQLEKGNLRVKqlkrqleeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG4913 818 LALL-DRLEEDGLPEY--------------EERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1007-1119 |
3.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1007 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK-----------------------E 1063
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnkeyealqkeiesL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1064 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDE 1119
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1628-1898 |
3.58e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1628 QRTLA-VAARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWREVEETRTSREEIFSqNRESEKRLKGLEAEV 1706
Cdd:PRK11281 66 EQTLAlLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1707 LRLQEELA-----------ASDRARRQ---AQQDRDEMADEVANGNLSKAAILEEKRQLegrlgqleeeleeEQSNSELL 1772
Cdd:PRK11281 138 QNAQNDLAeynsqlvslqtQPERAQAAlyaNSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1773 N--DRYRKLLLQVESLTTELSAERSFSAKAESgrQQLERQIQELRGRLGEEDagararhkmtiaaLESKLAQAEEQLEQE 1850
Cdd:PRK11281 205 NaqNDLQRKSLEGNTQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINSKR-------------LTLSEKTVQEAQSQD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 327478526 1851 TRERILSGKLVRRaekrlkevvlQVEEERRVADQLRDQLEKGN------LRVKQ 1898
Cdd:PRK11281 270 EAARIQANPLVAQ----------ELEINLQLSQRLLKATEKLNtltqqnLRVKN 313
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
859-1171 |
3.63e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 859 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERA-RLAEQLRAEAELCAEAEETRGRLAARK 934
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 935 ---QELELVVSELEARVGEEEECSRQMQTEK--KRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE- 1008
Cdd:pfam02029 105 ennEEEENSSWEKEEKRDSRLGRYKEEETEIreKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKi 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1009 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE----LEKLKRRLDGESSEL 1084
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRRRRQEKESEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1085 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARaqllkslreaqaalaeaqedlESERVARTKAEKQRrdLGEE 1164
Cdd:pfam02029 265 FEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE---------------------EAERKLREEEEKRR--MKEE 321
|
....*..
gi 327478526 1165 LEALRGE 1171
Cdd:pfam02029 322 IERRRAE 328
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1608-1753 |
4.39e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1608 RRQLAKQLRDAEVERDEERKQRTLAVAARKKlEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKelwREVEETRTSREE 1687
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-EAEEAELEQEREIETARIAEAEAELAKKKAEER---REAETARAEAEA 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1688 IFSQNRESEKRLKGLEAEVLRLQE--ELAASDRARRQAQQDRDEMADEVANgnlSKAAILEEKRQLEG 1753
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAEREReiELQEKEAEREEAELEADVRKPAEAE---KQAAEAEAEAEAEA 331
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1087 |
4.71e-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: 45.40 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 862 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAAR-------- 933
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvlsrsi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 934 ---KQELELVVSELEARVGEEEECSRQmqteKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ 1010
Cdd:TIGR04523 478 nkiKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1011 N----------------SKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLK 1074
Cdd:TIGR04523 554 LkkenlekeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
250
....*....|...
gi 327478526 1075 RRLDGESSELQEQ 1087
Cdd:TIGR04523 634 KNIKSKKNKLKQE 646
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
788-1083 |
4.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 788 RAGVLAQLEEERDLKVTDIIVSFQAAargylarRAFQKRQQQQSALRVMQRNCAAYLKLRHWQWWRLFTK-VKPLLQVTR 866
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEeKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 867 QDEVLQARAQELQKVQELQQQSAREvgelqgrVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 946
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEE-------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 947 RVGEEEECSRQMQTEKKRLQQhiqeleahLEAEEGARQKLQLEKVTTEAKMKKF--EEDLLLLEDQNSKLSKERKLLEDR 1024
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKKKIAHLKKEEEKKAEEIrkEKEAVIEEELDEEDEKRRMEVDKK 1799
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 1025 LAEFSSQAAEEEEKVKS----LNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE 1083
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGKEgnlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1291-1480 |
5.97e-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: 44.37 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1291 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLE 1370
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1371 EEAAARERAGRELQT-----------AQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGR 1439
Cdd:COG4942 101 AQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 327478526 1440 RRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAA 1480
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1610-1895 |
6.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1610 QLAKQLRDAEVERDEERKQRTlAVAARKKLEGELEELKAQMASAgqgkEEAVKQLRKmqaqmkelwreveetrtsREEIF 1689
Cdd:COG3206 152 AVANALAEAYLEQNLELRREE-ARKALEFLEEQLPELRKELEEA----EAALEEFRQ------------------KNGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1690 SqnreSEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEekrqlegrlgqleeeleeeqsns 1769
Cdd:COG3206 209 D----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1770 ellNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQ 1849
Cdd:COG3206 262 ---SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 327478526 1850 eTRERILSgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR 1895
Cdd:COG3206 339 -LEARLAE---LPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1031-1238 |
6.19e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 44.93 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1031 QAAEEEEKVKSLNKLRLKY---EATIADMEDRLRKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQQQRAEELRA 1100
Cdd:PLN03188 1038 PESTDESPEKKLEQERLRWteaESKWISLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1101 QLGRKEEELQAALARAED------EGGARAQLLKSLREAQAALAEAQEDLESERvartkaEKQRRDLGEELEALRGELED 1174
Cdd:PLN03188 1118 DLEEKHIQLLARHRRIQEgiddvkKAAARAGVRGAESKFINALAAEISALKVER------EKERRYLRDENKSLQAQLRD 1191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1175 TLDSTNAQQEL--RSKREQE--VTELKKTLEEETRIHEA--AVQELRQRHGQALGELAEQLEQARRGKGA 1238
Cdd:PLN03188 1192 TAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
984-1333 |
7.08e-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: 44.63 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 984 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1063
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1064 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEElqaalaraedeggaraqlLKSLREAQAALAEAQED 1143
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE------------------IKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1144 LEServARTKAEKQRRDLGEELEALRGELEDTldstnaQQELRSKreqeVTELKKtLEEETRIHEAAVQELRQRHGQaLG 1223
Cdd:TIGR04523 459 LDN---TRESLETQLKVLSRSINKIKQNLEQK------QKELKSK----EKELKK-LNEEKKELEEKVKDLTKKISS-LK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1224 ELAEQLEQarrgkgawEKTRlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQ--LQEVQGRAGDGERARAEAAEKLQR 1301
Cdd:TIGR04523 524 EKIEKLES--------EKKE--KESKISDLEDELNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350
....*....|....*....|....*....|..
gi 327478526 1302 AQAELENVSGALNEAESKTIRLSKELSSTEAQ 1333
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
899-1301 |
7.50e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 899 VAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEE--CSRQMQTEKKRLQQHIQELEAhl 976
Cdd:pfam02029 7 AARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeaFLDRTAKREERRQKRLQEALE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 977 eaeegaRQKlQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLlEDRLAEfssqAAEEEEKVKSLNKLRLKYEATIADM 1056
Cdd:pfam02029 85 ------RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1057 EDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAA 1136
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1137 LAEAQEDLESERVARTKAEKQRRDLGE----ELEALRGEledtldstnaQQElrskREQEVTELKKTLEEETRIHEAavq 1212
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1213 ELRQRhgqalgelaEQLEQARRGKGAWEKTRLALEAEvselraelsslqtarqegeqrrrrlelqlqevqgragdgeRAR 1292
Cdd:pfam02029 296 EEQRR---------KQEEAERKLREEEEKRRMKEEIE----------------------------------------RRR 326
|
....*....
gi 327478526 1293 AEAAEKLQR 1301
Cdd:pfam02029 327 AEAAEKRQK 335
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1742-1947 |
7.95e-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: 43.98 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1742 AAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEe 1821
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1822 dagARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1901
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 327478526 1902 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
876-1217 |
8.14e-04 |
|
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: 44.58 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 876 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRgrLAARKQELELVVSELEARVGEEEECS 955
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE--LLADRVQEAQDKINEELKLLKQKIDE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 956 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLledrlaefssQAAEE 1035
Cdd:pfam02463 748 EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE----------EAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1036 EEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqmvEQQQRAEELRAQLGRKEEELQAALAR 1115
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL---LQELLLKEEELEEQKLKDELESKEEK 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1116 AEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDstnaQQELRSKREQEVTE 1195
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE----EEEERNKRLLLAKE 970
|
330 340
....*....|....*....|..
gi 327478526 1196 LKKTLEEETRIHEAAVQELRQR 1217
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNK 992
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
939-1392 |
9.55e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.33 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 939 LVVSELEARVGEEEECSRqmqTEKKRLQQHIQELEAHLEAEEgaRQKLQLEKVTTEAKMKKFE-EDLLLLEDQNSKLSKE 1017
Cdd:pfam05483 349 FVVTEFEATTCSLEELLR---TEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1018 RKLLEDRLAEFSSQAAEE----EEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVE 1090
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1091 QQQRAEELRAQLGRKEEELQAALARAEdeggaraQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDlgeELEALRG 1170
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR----EEFIQKGD---EVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1171 ELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgqalgelaeqleQARRGKGAWEKTRL-ALEAE 1249
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN------------KALKKKGSAENKQLnAYEIK 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1250 VSELRAELSSL-QTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE--KLQ-----RAQAELENVSGALNEAESKTI 1321
Cdd:pfam05483 638 VNKLELELASAkQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavKLQkeidkRCQHKIAEMVALMEKHKHQYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1322 RLSKELSStEAQLHDAQEllQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSE 1392
Cdd:pfam05483 718 KIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1051-1318 |
9.56e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1051 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQLL 1127
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1128 KSLREAQAALAEAQEDLE------------SERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTE 1195
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1196 LKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAweKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLE 1275
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA--AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 327478526 1276 LQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1318
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGA 289
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1544-1823 |
1.00e-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: 44.56 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1544 VHELERACRVAEQAANDLRAQVTELEDELTAAED----AKLRLEVTVQALKTQHERDLQ--------------------- 1598
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdsLKSQLADYQQALDVQQTRAIQyqqavqalekaralcglpdlt 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1599 ------------GRDEAGEERRRQLAKQLRDAEVERDEERKqrtlAVAARKKLEGE-------------LEELKAQMASA 1653
Cdd:COG3096 436 penaedylaafrAKEQQATEEVLELEQKLSVADAARRQFEK----AYELVCKIAGEversqawqtarelLRRYRSQQALA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1654 GQGK---------EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQ 1724
Cdd:COG3096 512 QRLQqlraqlaelEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1725 QDRDEMADEvANGNLSKAAILEekrQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVEsltTELSAERSFSAKAesgR 1804
Cdd:COG3096 592 ARIKELAAR-APAWLAAQDALE---RLREQSGEALADSQEV--------TAAMQQLLERE---REATVERDELAAR---K 653
|
330
....*....|....*....
gi 327478526 1805 QQLERQIQELRGRLGEEDA 1823
Cdd:COG3096 654 QALESQIERLSQPGGAEDP 672
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1018-1200 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1018 RKLLEdrLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqmveqqqRAEE 1097
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1098 LRAQLG--RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDT 1175
Cdd:COG1579 78 YEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*
gi 327478526 1176 LDstnaqqELRSKREQEVTELKKTL 1200
Cdd:COG1579 158 LE------ELEAEREELAAKIPPEL 176
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
894-1159 |
1.32e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 894 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELE 973
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 974 AHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERkllEDRLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1053
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1054 ADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREA 1133
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260
....*....|....*....|....*.
gi 327478526 1134 QAALAEAQEDLESERVARTKAEKQRR 1159
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEEK 268
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1423-1947 |
1.48e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1423 QRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraVEERERAEAEGREREARA 1502
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1503 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE---QAANDLRAQVTELEDELTAAEDAK 1579
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1580 LRLEVTVQALktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASagqgKEE 1659
Cdd:PRK03918 355 EELEERHELY----EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1660 AVKQLRKMQAQMKELWREVEETRtsREEIFsqnRESEKRLKGLEAEVLRLQEELaasDRARRQAQQDRDEMADEVANGNL 1739
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEH--RKELL---EEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1740 SKaaILEEKRQLEGRL-GQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFsakaESGRQQLERQIQELRGRL 1818
Cdd:PRK03918 499 KE--LAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1819 GEEDAGARARHKMTIAALESKLaqaeEQLEQETRERILsgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1898
Cdd:PRK03918 573 AELLKELEELGFESVEELEERL----KELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 327478526 1899 LKRQLEeaeeeasraQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:PRK03918 645 LRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1297-1845 |
1.72e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1297 EKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRvramEAEAAGLREQLEEEAAAR 1376
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1377 ERAGRELQtaqaQLSEWRRRQEEeagaLEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1456
Cdd:PRK03918 269 EELKKEIE----ELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1457 RQLVSTLEKKQRKFDQLlaeEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnraLRAELEALLSS 1536
Cdd:PRK03918 341 EELKKKLKELEKRLEEL---EERHELYEEAKAKKEELERLKKRLTGLTPEK------------------LEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1537 KDDVGKSVHELERACRVAEQAANDLRAQVTELEDeltaaedAKLRLEVTVQALKTQHERDLQGRDEAG-----------E 1605
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1606 ERRRQLAKQLRDAEVERDEERKQRTLAVAAR--KKLEGELEELKAQMASAGQGKEEAVKQ-LRKMQAQMKELWREVE--- 1679
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEqlKELEEKLKKYNLEELEKKAEEYEKLKEkLIKLKGEIKSLKKELEkle 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1680 ETRTSREEIFSQNRESEKRLKGLEAEVL------------RLQE---------ELAASDRARRQAQQDRDEMADEVANGN 1738
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEelgfesveeleeRLKElepfyneylELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1739 LSKAAILEEKRQLEGRLGQLEEELEEeqsnsellnDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRL 1818
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
570 580
....*....|....*....|....*..
gi 327478526 1819 GEedagaRARHKMTIAALESKLAQAEE 1845
Cdd:PRK03918 704 EE-----REKAKKELEKLEKALERVEE 725
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1034-1307 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1034 EEEEKVKSLNKLRLKYEAtiadmEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEEL-RAQLGRKEEEL 1109
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEK-----EEKAREVERRRKLEEAEKARqaeMDRQAAIYAEQERMAMERERELeRIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1110 QAALARAEDEGGARAQLLKSLREAQAALAEA-QEDLESERVARTKAEKQRRDLGE---ELEALRGELEDTldstnAQQEL 1185
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERvRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1186 RSKREQEVTELKKTLEEETRiHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRaelsslqTARQ 1265
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE-RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK-------QAMI 509
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 327478526 1266 EGEQRRRRLELQLQEVQGRAGDGERARaeAAEKLQRAQAELE 1307
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEME 549
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1348 |
1.88e-03 |
|
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: 43.17 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 894 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSE----------LEARVGEEEECSRQMQTEKK 963
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 964 RLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSL 1042
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1043 NKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE----LQEQMVEQQQRAEELRAQLGRKEEELQAALARAED 1118
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1119 EGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNaqqelrsKREQEVTELKK 1198
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN-------NKEVELEELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1199 TLEEEtrihEAAVQELRQrhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTARQEGEQRRRRLELQL 1278
Cdd:pfam05483 413 ILAED----EKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1279 QEVQGR----AGDGERARAEAAEKLQRAQ---AELENVSGALNEAESKTIRLSKE---LSSTEAQLHDAQELLQEETRAK 1348
Cdd:pfam05483 481 EKEKLKnielTAHCDKLLLENKELTQEASdmtLELKKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQK 560
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1018-1258 |
2.09e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1018 RKLLeDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEE---KGRQELEKLKRRlDGESSELQEQmVEQQQR 1094
Cdd:COG0497 144 RELL-DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDllrFQLEELEAAALQ-PGEEEELEEE-RRRLSN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1095 AEELRAQLGrkeeelQAALARAEDEGGArAQLLKSLREAQAALAEAQEDLE--SERVARTKAEKQrrDLGEELEALRGEL 1172
Cdd:COG0497 221 AEKLREALQ------EALEALSGGEGGA-LDLLGQALRALERLAEYDPSLAelAERLESALIELE--EAASELRRYLDSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1173 E---DTLDSTNA-QQELRS-KR-----EQEVTELKKTLEEE--------TRIH--EAAVQELRQrhgqALGELAEQLEQA 1232
Cdd:COG0497 292 EfdpERLEEVEErLALLRRlARkygvtVEELLAYAEELRAElaelensdERLEelEAELAEAEA----ELLEAAEKLSAA 367
|
250 260
....*....|....*....|....*.
gi 327478526 1233 RRgkgaweKTRLALEAEVSELRAELS 1258
Cdd:COG0497 368 RK------KAAKKLEKAVTAELADLG 387
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
796-1182 |
2.13e-03 |
|
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: 43.18 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 796 EEERDLKVTDIIVSfQAAARGYLARRAFQKRQQQQSALRVMQRNCAAyLKLrhwqwwrlftkvkpllQVTRQDEVLQARA 875
Cdd:pfam15921 507 EKERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL----------------QMAEKDKVIEILR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 876 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEeeecs 955
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEARVSD----- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 956 rqMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1035
Cdd:pfam15921 630 --LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1036 EEKVKSLNKlrlkyeaTIADMEDRLRKEEKGRQELEKLKR-RLDGESSELQeQMVEQQQRAEELRAQLGRKEEELQAALA 1114
Cdd:pfam15921 708 LEQTRNTLK-------SMEGSDGHAMKVAMGMQKQITAKRgQIDALQSKIQ-FLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1115 RAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQ 1182
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEValDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1013-1361 |
2.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1013 KLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME--DRLRKEEKGRQELEKLKRRLDGESSELQ--EQM 1088
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEelEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1089 VEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQllkslreaqAALAEAQEDLESERVARTKAEKQRRDLGEELEAL 1168
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1169 RGELEDTLDSTNAQQELRSKREQEVT-----------------------------------------ELKKTLEEETRIH 1207
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1208 EAAVQELRQRHGQAlgELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQ--LQEVQGRA 1285
Cdd:COG4717 306 ELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1286 GDGERARAEAAEKLQRAQAELENVSGALNEAESKTI---------RLSKELSSTEAQLHDAQELLQEETRAKLALGSRVR 1356
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELREELAELEAELE 463
|
....*
gi 327478526 1357 AMEAE 1361
Cdd:COG4717 464 QLEED 468
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1201-1755 |
2.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1201 EEETRIHEAAVQELRQRHGQA----LGELAEQLEQARRGKGAWE---------KTRLALEAEVSELRAELSSLqtARQEG 1267
Cdd:COG3899 663 EERRALHRRIARALEARGPEPleerLFELAHHLNRAGERDRAARlllraarraLARGAYAEALRYLERALELL--PPDPE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1268 EQRRRRLELQLQEVQGRAGDGERARaEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1347
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAE-ALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALAL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1348 KLALGSRV-----------------RAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEA 1410
Cdd:COG3899 820 AERLGDRRlearalfnlgfilhwlgPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1411 RRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERER 1490
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1491 AEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELED 1570
Cdd:COG3899 980 AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAA 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1571 ELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQM 1650
Cdd:COG3899 1060 AALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLA 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1651 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1730
Cdd:COG3899 1140 AALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEA 1219
|
570 580
....*....|....*....|....*
gi 327478526 1731 ADEVANGNLSKAAILEEKRQLEGRL 1755
Cdd:COG3899 1220 AALLLLLLLAALALAAALLALRLLA 1244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
958-1673 |
2.28e-03 |
|
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: 43.17 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 958 MQTEKKRLQQHIQELEAHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1037
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1038 KVKSLNKLRLKYEATIADMEDRLRKEEKGRQELeklkrRLDGESS------ELQEQMVEQQQRAEELRAQLGRKEEELQA 1111
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1112 ALARAEDeggaRAQLLKSLREAQAALAEAQEDLESERVARTKAEKQrrdLGEELEALRGELEDTLDSTnaqqelrskreQ 1191
Cdd:pfam05483 245 LLIQITE----KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE---LIEKKDHLTKELEDIKMSL-----------Q 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1192 EVTELKKTLEEETRIHEAAVQELRQrhgqalgELAEQLEQArrgkgawEKTRLALEAEVSELRAELSSlqtarqegeqrr 1271
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTE-------EKEAQMEEL-------NKAKAAHSFVVTEFEATTCS------------ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1272 rrLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQ--ELLQEETRAK- 1348
Cdd:pfam05483 361 --LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKe 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1349 LALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEK 1428
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1429 TETVDRLERGRRRLQQELDDATmdlEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARAL----- 1503
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenk 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1504 --SLTRALEEEQEAREELERQNRALR----AELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTEL----EDELT 1573
Cdd:pfam05483 596 cnNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkiseEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1574 AAEDAKLRLEvtvQALKTQHERDLQGRDEAG------EERRRQLAK--QLRDAEVERDEERKQRTlaVAARKKLEGELEE 1645
Cdd:pfam05483 676 EVEKAKAIAD---EAVKLQKEIDKRCQHKIAemvalmEKHKHQYDKiiEERDSELGLYKNKEQEQ--SSAKAALEIELSN 750
|
730 740
....*....|....*....|....*...
gi 327478526 1646 LKAQMASAGQGKEEAVKQLRKMQAQMKE 1673
Cdd:pfam05483 751 IKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
865-1123 |
2.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 865 TRQDEVLQARAQELQ----KVQELQQQSAREVGELQGR----------------VAQLEEERARLAEQLRAEAELCAEAE 924
Cdd:COG4913 609 RAKLAALEAELAELEeelaEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 925 ETRGRLAARKQELELVVSELEARVGEEEECSRQmQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDL 1004
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1005 LL-LEDQNSKLSKERKLLEDRLaefssqaaeeeekVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesse 1083
Cdd:COG4913 768 REnLEERIDALRARLNRAEEEL-------------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE-------- 826
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 327478526 1084 lqEQMVEQQQRAEELRAQL-GRKEEELQAALARAEDEGGAR 1123
Cdd:COG4913 827 --DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1525-1924 |
2.51e-03 |
|
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: 42.90 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1525 ALRAELEALLSSKDD-VGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKL--------RLEVTVQALKTQHER 1595
Cdd:pfam12128 283 ETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaaadqeQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1596 -----DLQGRDEAGEERRRQLAKQLRDAEVERDEER---------KQRTLAVAARKKLEGEL-EELKAQMASAGQGK--- 1657
Cdd:pfam12128 363 lkaltGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKlakireardRQLAVAEDDLQALESELrEQLEAGKLEFNEEEyrl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1658 EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRlkglEAEVLRLQEELAASDRARRQAQqdrDEMADEVANG 1737
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQAS---EALRQASRRL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1738 NLSKAAILEEKRQLEGRLGQLEEELEEEQSnseLLNDRYRKLLLQVESLTTELSAERSFSAKAESGR------------- 1804
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRKEAP---DWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlygvkldlkridv 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1805 ---QQLERQIQELRGRLGEEDAGARARHkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE-EERR 1880
Cdd:pfam12128 593 pewAASEEELRERLDKAEEALQSAREKQ----AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDK 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 327478526 1881 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQREL 1924
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1586-1945 |
2.80e-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: 42.80 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1586 VQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERdeeRKQRTLAVAARkklEGELEELKAQMASAGQGKEEAVKQLR 1665
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER---RRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1666 KMQAQMKElwREVEETRtsREEIFSQnresEKRLKGLEaevlRLQEElaasdrarRQAQQDRDEMADEVANgnlsKAAIL 1745
Cdd:pfam17380 352 RIRQEERK--RELERIR--QEEIAME----ISRMRELE----RLQME--------RQQKNERVRQELEAAR----KVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1746 EEKRQLEGRLGQLEEELEEEQSNsellNDRYRKLLLQVESLTTELSAERsfsakaesgRQQLERQIQELRGRLGEEDaga 1825
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVR---------LEEQERQQQVERLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1826 RARHKMTIAALESKLAQAEEQleqetRERILSGKLVRRAEKrlkevvlQVEEERRvadqlRDQLEKgnlrvKQLKRQLEE 1905
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQ-----RRKILEKELEERKQA-------MIEEERK-----RKLLEK-----EMEERQKAI 529
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 327478526 1906 AEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1945
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1044-1161 |
3.15e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1044 KLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesselqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEgGAR 1123
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAE-KEL 469
|
90 100 110
....*....|....*....|....*....|....*...
gi 327478526 1124 AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1161
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1190-1365 |
3.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1190 EQEVTELKKTLEEetriHEAAVQELRQRHGqaLGELAEQLEQarrgkgawektrlaLEAEVSELRAELSSLQTARQEGEQ 1269
Cdd:COG3206 181 EEQLPELRKELEE----AEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1270 RRRRLELQLQEVQGRAGD--GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1347
Cdd:COG3206 241 RLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170
....*....|....*....
gi 327478526 1348 KL-ALGSRVRAMEAEAAGL 1365
Cdd:COG3206 321 ELeALQAREASLQAQLAQL 339
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1093-1597 |
3.90e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1093 QRAEELRAQLGRKEEELQAALARAEDEGGAR---------AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGE 1163
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYLAGrfeeaeallERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1164 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTR 1243
Cdd:COG3899 809 AYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1244 LALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1323
Cdd:COG3899 889 AAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAA 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1324 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGA 1403
Cdd:COG3899 969 AAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAA 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1404 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLR 1483
Cdd:COG3899 1049 LAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAA 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1484 AVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRA 1563
Cdd:COG3899 1129 ARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAA 1208
|
490 500 510
....*....|....*....|....*....|....
gi 327478526 1564 QVTELEDELTAAEDAKLRLEVTVQALKTQHERDL 1597
Cdd:COG3899 1209 LLALALLALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1090-1482 |
4.29e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1090 EQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALR 1169
Cdd:COG5278 104 EQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1170 GELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAE 1249
Cdd:COG5278 184 ALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1250 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSS 1329
Cdd:COG5278 264 AAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1330 TEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEE 1409
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 1410 ARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1482
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAA 496
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1019-1341 |
4.44e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1019 KLLEDRLAEFSsqaaeeeEKVKSLnklrlkyEATIADMEDRLR-KEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEE 1097
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1098 LRAQLGRKEEELQAALARAEDEGGARaqllkslREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGEledtld 1177
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1178 stnaqqelrskREQEVTELKKTLEEETRIHE---AAVQELrqrhGQALGELAEQLE-QARRGKG---AWEKTRLA-LEAE 1249
Cdd:pfam00038 140 -----------HEEEVRELQAQVSDTQVNVEmdaARKLDL----TSALAEIRAQYEeIAAKNREeaeEWYQSKLEeLQQA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1250 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEklqRAQAELENVSGALNEAESKTIRLSKELss 1329
Cdd:pfam00038 205 AARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEM-- 279
|
330
....*....|..
gi 327478526 1330 tEAQLHDAQELL 1341
Cdd:pfam00038 280 -ARQLREYQELL 290
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1033-1365 |
4.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1033 AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAA 1112
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1113 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1192
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1193 VTELKKTLEEETRIH-EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1271
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1272 RRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLAL 1351
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 327478526 1352 GSRVRAMEAEAAGL 1365
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
995-1357 |
4.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 995 AKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS--QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEK 1072
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1073 LKRRLDGESSELQEqmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVART 1152
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1153 KAEKQRR-----------DLGEELEALRGELEDTLDS------------TNAQQELRSKREQEVTELKKT--LEEETRIH 1207
Cdd:COG4717 238 AAALEERlkearlllliaAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASLGKEAEELqaLPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1208 EAAVQELRQRHG----QALGELAEQLEQARRGKGAW-EKTRLALEAEVSELRAELSSL-------------QTARQEGEQ 1269
Cdd:COG4717 318 EEELEELLAALGlppdLSPEELLELLDRIEELQELLrEAEELEEELQLEELEQEIAALlaeagvedeeelrAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1270 RRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDA------QELLQE 1343
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELLQE 477
|
410
....*....|....
gi 327478526 1344 ETRAKLALGSRVRA 1357
Cdd:COG4717 478 LEELKAELRELAEE 491
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1792-1887 |
5.94e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1792 AERSFSAKAESGRQQLERQIQELRGR--LGEEDAGARARHKMTIAALESKLAQAEEQLEQ-------ETRERILsgKLVR 1862
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaaeTSQERKQ--KRKE 220
|
90 100
....*....|....*....|....*.
gi 327478526 1863 RAEKRLKEVVLQVEEERRVAD-QLRD 1887
Cdd:PRK11448 221 ITDQAAKRLELSEEETRILIDqQLRK 246
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
982-1198 |
6.19e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 982 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYE---------AT 1052
Cdd:PHA02562 214 NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1053 IADMEDRLRK-EEKGRQ---ELEKLKRRLDgessELQEQMVE---QQQRAEELRAQLGRKEEELQAALARAEDeggARAQ 1125
Cdd:PHA02562 294 ISEGPDRITKiKDKLKElqhSLEKLDTAID----ELEEIMDEfneQSKKLLELKNKISTNKQSLITLVDKAKK---VKAA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 327478526 1126 LlkslreaqaalaeaqedleservarTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREQEVTELKK 1198
Cdd:PHA02562 367 I-------------------------EELQAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1088-1258 |
6.55e-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: 40.29 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1088 MVEQQQRAEEL------RAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE-RVARTKAEKQRRD 1160
Cdd:COG1579 2 MPEDLRALLDLqeldseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1161 LGE-----ELEALRGELEdtldstnAQQELRSKREQEVTELKKTLEEetriHEAAVQELRQRHGQALGELAEQLEQARRG 1235
Cdd:COG1579 82 LGNvrnnkEYEALQKEIE-------SLKRRISDLEDEILELMERIEE----LEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|...
gi 327478526 1236 KGAWEKTRLALEAEVSELRAELS 1258
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIP 173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1007-1216 |
6.64e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1007 LEDQNSKLSKERKLLEDRLAEF---------SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRL 1077
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1078 --DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALaeaqedLESERVARTKAE 1155
Cdd:COG3206 260 lqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQLQQEAQRI------LASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 327478526 1156 KQRRDLGEELEALRGELEDTldstnaqqelrSKREQEVTELKKTLEEETRIHEAAVQELRQ 1216
Cdd:COG3206 327 AREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1613-1713 |
6.65e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1613 KQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLR-KMQAQMKELWREVEETRTSREeifsq 1691
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKL----- 265
|
90 100
....*....|....*....|...
gi 327478526 1692 nRESEKRLK-GLEAEVLRLQEEL 1713
Cdd:cd16269 266 -KEQEALLEeGFKEQAELLQEEI 287
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1605-1750 |
6.67e-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: 40.29 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1605 EERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQA--QMKELWREVEETR 1682
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1683 TSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANgnlsKAAILEEKRQ 1750
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA----ELEELEAERE 166
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1153-1389 |
7.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1153 KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRHGQALGELAEQLEQA 1232
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1233 RRGKGAWEKTRLALEAE-VSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEAAEKLQRAQAELENVSG 1311
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAEL-------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 327478526 1312 ALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQ 1389
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1220-1354 |
8.10e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1220 QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKL 1299
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1300 QRAQAELEnvsgALNEAESKtirLSKELSSTEAQLhDAQELLQEETRAKLA-LGSR 1354
Cdd:PRK09039 133 ARALAQVE----LLNQQIAA---LRRQLAALEAAL-DASEKRDRESQAKIAdLGRR 180
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1655-1947 |
8.10e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1655 QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEMADEV 1734
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENT--KEKIAEYTKSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1735 ANGNLSKAAILEE-KRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSfSAKAESGRQQLERQIQE 1813
Cdd:COG5185 314 LEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKS-SEELDSFKDTIESTKES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1814 LRGRLGEedagARARHKMTIAALESKLAQAEEQLEQETRErilsgklvrraekrLKEVVLQVEEERRVADQLRDQLEKGN 1893
Cdd:COG5185 393 LDEIPQN----QRGYAQEILATLEDTLKAADRQIEELQRQ--------------IEQATSSNEEVSKLLNELISELNKVM 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 327478526 1894 LRVKQL--KRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1947
Cdd:COG5185 455 READEEsqSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
1034-1108 |
8.40e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 40.90 E-value: 8.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 327478526 1034 EEEEKVKSLNKLRL--KYEATIADMEDRLRKEEKgrqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1108
Cdd:pfam12004 373 EESSGPESREELKQaeKYEQEISKLKERLRVSNR---KLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEE 446
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
857-1100 |
8.80e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.07 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 857 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREVGElQGRVAQLEEERA--RLAEQLRAEAELcaeaeetrGRLAARK 934
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEKKLE-QERLRWTEAESKwiSLAEELRTELDA--------SRALAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 935 QELELvvsELEARVGEEEECSRQMQTE--KKRLQQ-------HIQELEAHLEAEEGARQklqLEKVTTEAKMKKFEEDLL 1005
Cdd:PLN03188 1084 QKHEL---DTEKRCAEELKEAMQMAMEghARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAESKFI 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1006 -LLEDQNSKL----SKERKLLEDRLAEFSSQAAEEEEKVKSLNKL--RLK-YEATIADMEDRLRKEE----KGRQELEKL 1073
Cdd:PLN03188 1158 nALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQIDKL 1237
|
250 260
....*....|....*....|....*..
gi 327478526 1074 KRRLDGESSELQEQMVEQQQRAEELRA 1100
Cdd:PLN03188 1238 KRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1029-1154 |
9.66e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 327478526 1029 SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1108
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 327478526 1109 LQAALaRAEDEGGARAQLLKSLREAQAALAEAQEDLEsERVARTKA 1154
Cdd:COG2433 457 ERREI-RKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| |
