|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
92-770 |
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: 1266.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK-------------GTLEDQILQANPILEAFGNAKTVRNNNSSRFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDV 330
Cdd:cd01377 148 FIRIHFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGeLTIDGVDDA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd01377 228 EEFKLTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRThRQGASFIGILDIAGFEIFDINSFEQICINYTNEKL 490
Cdd:cd01377 308 GREWVTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 491 QQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKP-MGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIV 569
Cdd:cd01377 387 QQFFNHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 PDMRSKS--HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefagicaAEMNETAFGMRSRKG 647
Cdd:cd01377 467 KPKPKKSeaHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY-------EESGGGGGKKKKKGG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 648 MFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 727
Cdd:cd01377 540 SFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRY 619
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 25150354 728 EILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01377 620 SILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
92-770 |
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: 1166.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGAtrnKSLNAAAQQNIVQKPDVRnpIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS---KPKGSGAVPHPAVNPAVL--IGELEQQLLQANPILEAFGNAKTVKNDNSSRFGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14911 156 FIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14911 316 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPD 571
Cdd:cd14911 396 QLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 572 MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGICAAEMNETAFGMRSRKGMFRT 651
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRT 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 652 VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILT 731
Cdd:cd14911 556 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 635
|
650 660 670
....*....|....*....|....*....|....*....
gi 25150354 732 PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14911 636 PNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-770 |
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: 1068.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAqqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------------GELERQLLQANPILESFGNAKTVKNDNSSRFGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14920 147 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14920 227 NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14920 307 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd14920 387 QLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE----FAGICAAEMNETAFGMR 643
Cdd:cd14920 467 KPrQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTETAFGSAYK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14920 547 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 724 RHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14920 627 RQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
80-770 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1068.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 80 IEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSML 159
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 160 QEREDQSILCTGESGAGKTENTKKVIQYLAHVAGATRnkslnaaaqqnivqkpdvRNPIGELEHQLLQANPILEAFGNSK 239
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGS------------------AGNVGRLEEQILQSNPILEAFGNAK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 240 TVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVN 319
Cdd:pfam00063 143 TVRNNNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 320 RG-ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIE 398
Cdd:pfam00063 223 SGcYTIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 399 LQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSF 478
Cdd:pfam00063 303 LEKALCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 479 EQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKL 557
Cdd:pfam00063 383 EQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 558 QKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGICAAEMNE 637
Cdd:pfam00063 462 YSTFSKHPHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 638 TAFGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNR 717
Cdd:pfam00063 542 KSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNR 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 25150354 718 VPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:pfam00063 622 ITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
73-782 |
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: 1022.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 73 NPPKFDKIEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIAD 152
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 153 TAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqnivqkpdvrnpiGELEHQLLQANPIL 232
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------------GSVEDQILESNPIL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 233 EAFGNSKTVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVD 312
Cdd:smart00242 141 EAFGNAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 313 NYRFLvNRG--ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAM-LQDDRVIQKVC 389
Cdd:smart00242 221 DYRYL-NQGgcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAStVKDKEELSNAA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 390 HLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAG 469
Cdd:smart00242 300 ELLGVDPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 470 FEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKA 548
Cdd:smart00242 379 FEIFEVNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 549 NDKSFVEKLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfa 628
Cdd:smart00242 458 TDQTFLEKLNQHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV-- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 629 gicaaemnetafGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIR 708
Cdd:smart00242 536 ------------SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIR 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 709 ICRQGFPNRVPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFRTGVLAHLEEERD 782
Cdd:smart00242 604 IRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
92-770 |
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: 997.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIvqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIALSH----------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14932 151 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14932 231 LFAETMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14932 311 RDYVQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd14932 391 QLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAFG-MRS 644
Cdd:cd14932 471 KPkKLKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrIVGLdKVAGMGESLHGaFKT 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 RKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd14932 551 RKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 725 HRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14932 631 QRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
92-770 |
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: 944.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAqqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSIT--------------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14921 147 FIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14921 227 MFQETLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14921 307 RDVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd14921 387 QLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAF--GMR 643
Cdd:cd14921 467 KPkQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLdQMAKMTESSLpsASK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14921 547 TKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEF 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 724 RHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14921 627 RQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
92-770 |
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: 937.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaAQQNIVQKPdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKK----DQNSLALSH------GELEKQLLQANPILEAFGNAKTVKNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd15896 151 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd15896 231 LFTETMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd15896 311 RDYVQKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd15896 391 QLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFF 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAFGMRSR 645
Cdd:cd15896 471 KPkKLKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrIVGLdKVSGMSEMPGAFKTR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd15896 551 KGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 726 RYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd15896 631 RYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-770 |
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: 926.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ-----------------GELERQLLQANPILEAFGNAKTVKNDNSSRFGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14919 144 FIRINFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14919 224 MFQETMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14919 304 RDYVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd14919 384 QLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAF--GMR 643
Cdd:cd14919 464 KPkQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLdQVAGMSETALpgAFK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14919 544 TRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 724 RHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14919 624 RQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-770 |
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: 912.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqnivQKPDVRnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGR-----------KEPGVP---GELERQLLQANPILEAFGNAKTVKNDNSSRFGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNvDDVQ 331
Cdd:cd14930 147 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14930 226 LFQETLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14930 306 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 568
Cdd:cd14930 386 QLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP-DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfaGICAAE----MNETAFGMR 643
Cdd:cd14930 466 RPrHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVGLEqvssLGDGPPGGR 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14930 544 PRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 724 RHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14930 624 RQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
29-1133 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 897.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 29 CWVPDQNEGFLIGSI-KRETNDEVLVELVDTSRQVTISRD----DVQKANPPKFDKIEDMSELTYLNEASVLHNLKDRYY 103
Cdd:COG5022 12 CWIPDEEKGWIWAEIiKEAFNKGKVTEEGKKEDGESVSVKkkvlGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 104 SSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKK 183
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 184 VIQYLAHVAGATRNKslnaaaqqnivqkpdvrnpIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGYI 263
Cdd:COG5022 172 IMQYLASVTSSSTVE-------------------ISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 264 SGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTINSMRI 342
Cdd:COG5022 233 CGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 343 MGFADDEISSIMRVVSAVLLLGNLEFtQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQE 422
Cdd:COG5022 313 IGIDEEEQDQIFKILAAILHIGNIEF-KEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 423 QAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGaSFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILE 502
Cdd:COG5022 392 QALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 503 QEEYQREGIEWDFIDFgLDLQPTIDLIEK--PMGVLALLDEECLFPKANDKSFVEKLQKTHNKH--PKFIVPDMRSKShF 578
Cdd:COG5022 471 QEEYVKEGIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnPKFKKSRFRDNK-F 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 579 AVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemnetafgMRSRKGMFRTVSQLHKE 658
Cdd:COG5022 549 VVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE---------------NIESKGRFPTLGSRFKE 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 659 QLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDV---- 734
Cdd:COG5022 614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtg 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 735 IPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFRTGVLAHLEEERDLKLTALIMNFQAQCRGFLSRRLYTRRQQQSSA 814
Cdd:COG5022 694 EYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKK 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 815 IRIIQRNGLAYLKLRNWQWWRLFTKVKPLLQVTRTDDEIRAKDDELRaTKERLLKMEHDFRENEKkldqviVERAVIQEQ 894
Cdd:COG5022 774 IQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACII-KLQKTIKREKKLRETEE------VEFSLKAEV 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 895 LQQESENSAELDDIRGRLQTRNQELEY--IVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDK 972
Cdd:COG5022 847 LIQKFGRSLKAKKRFSLLKKETIYLQSaqRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFK 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 973 TNVDQRL-RNLEERLVELQdaydkLLKEKRLLEEKVEglttqLLDHEERAKHGVKAKGRLENQLHELEQDLNRERqykSE 1051
Cdd:COG5022 927 TELIARLkKLLNNIDLEEG-----PSIEYVKLPELNK-----LHEVESKLKETSEEYEDLLKKSTILVREGNKAN---SE 993
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1052 LEQHKRKlLAELEDSKDHLAEKMGKVEELNNQLMkRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERN 1131
Cdd:COG5022 994 LKNFKKE-LAELSKQYGALQESTKQLKELPVEVA-ELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKL 1071
|
..
gi 25150354 1132 AR 1133
Cdd:COG5022 1072 RR 1073
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
92-770 |
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: 844.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRH-EMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGatRNKSLNAAAQQNIVQkpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG--SGSSKSSSSASSIEQ-------------QILQSNPILEAFGNAKTVRNDNSSRFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-----ITLP 325
Cdd:cd00124 146 KFIELQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLnssgcDRID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 326 NVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAF 403
Cdd:cd00124 226 GVDDAEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEdeEDEDSSAEVADDESLKAAAKLLGVDAEDLEEAL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 404 LRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQ-GASFIGILDIAGFEIFDINSFEQIC 482
Cdd:cd00124 306 TTRTIKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 483 INYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTH 561
Cdd:cd00124 386 INYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAH 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 562 NKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDpfvagiwkdaefagicaaemnetafg 641
Cdd:cd00124 465 GSHPRFFSKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ-------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 642 mrsrkgmfrtvsqlHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd00124 519 --------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFD 584
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 722 EFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd00124 585 EFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
92-770 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 786.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTG--------GTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDD 329
Cdd:cd14927 153 FIRIHFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLVSMNpyDYHFCSQGVTTVDNMDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 409
Cdd:cd14927 232 GEELMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 410 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14927 312 VGNEYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKF 567
Cdd:cd14927 390 KLQQFFNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNF 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVP--DMRSK--SHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaeFAGICAAEMNETAFGMR 643
Cdd:cd14927 470 QKPrpDKKRKyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN--YVGSDSTEDPKSGVKEK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGM-FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQE 722
Cdd:cd14927 548 RKKAAsFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYAD 627
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 723 FRHRYEILTPDVIPKN-FIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14927 628 FKQRYRILNPSAIPDDkFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
92-770 |
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: 753.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRnkslnaaaqqnivqKPDVRNPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK--------------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLL-EGVDNYRFLVNRGITLPNVDDV 330
Cdd:cd14909 147 FIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd14909 227 EEFSLTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKL 490
Cdd:cd14909 307 GNEFVTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 491 QQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIV 569
Cdd:cd14909 386 QQFFNHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 PDM----RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefAGICAAEmnETAFGMRSR 645
Cdd:cd14909 466 PKPpkpgQQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH--AGQSGGG--EQAKGGRGK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGM-FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd14909 542 KGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 725 HRYEILTPDVIPKNfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14909 622 MRYKILNPAGIQGE-EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
93-770 |
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: 751.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAgatrnkslnaaAQQNIVQKPDVRNPiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIA-----------ATGDLAKKKDSKMK-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDV 330
Cdd:cd14913 150 IRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYpFISQGeILVASIDDA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd14913 229 EELLATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNEK 489
Cdd:cd14913 309 GNEYVTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 490 LQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFI 568
Cdd:cd14913 387 LQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VPDM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGICAAEmnETAFGMRSR 645
Cdd:cd14913 467 KPKVvkgRAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--ATFATADADS--GKKKVAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd14913 543 GSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 726 RYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14913 623 RYRVLNASAIPEgQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
847-1919 |
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: 742.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 847 TRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDM 926
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 927 RDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEK 1006
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1007 VEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMK 1086
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1087 RDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQD 1166
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1167 LMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR 1246
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1247 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEE 1326
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1327 TRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE--SVNQQLEELRKKNLRDVEHLQKQ 1404
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1405 LEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLS 1484
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1485 LLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEV 1564
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1565 TNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQL 1644
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1645 KKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN---DELEELRAKGGGIS 1721
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERdelADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1722 SEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESG 1801
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1802 AQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLD 1881
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 25150354 1882 EAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLR 1919
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
92-770 |
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: 733.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAaaqqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK----------------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILrgcsAKEKSEyLLEGV------DNYRFLVNRGITLP 325
Cdd:cd14934 145 FIRIHFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQIL----SNKKPE-LIESLllvpnpKEYHWVSQGVTVVD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 326 NVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLR 405
Cdd:cd14934 220 NMDDGEELQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 406 PRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINY 485
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 486 TNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKH 564
Cdd:cd14934 379 TNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 565 PKFIVPD----MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemnetAF 640
Cdd:cd14934 459 SNFLKPKggkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPA---------GS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 641 GMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPF 720
Cdd:cd14934 530 KKQKRGSSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQY 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 25150354 721 QEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14934 610 PEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
92-770 |
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: 717.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivqkpdvrnPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK-----------------KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcsAKEKSEYLL--EGVDNYRFLVNRGITLPNVDD 329
Cdd:cd14929 144 FIRMHFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSG--KKELRDLLLvsANPSDFHFCSCGAVAVESLDD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 409
Cdd:cd14929 222 AEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 410 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14929 302 VGNEYVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKF 567
Cdd:cd14929 380 KLQQFFNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDMRSKS---HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemNETAFGMRS 644
Cdd:cd14929 460 QKPKPDKKKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTD------SAIQFGEKK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 RK--GMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQE 722
Cdd:cd14929 534 RKkgASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 723 FRHRYEILTPDVIPKN-FIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14929 614 FKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
93-770 |
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: 699.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAgATRNKSlnaaaqqnivqKPDVRNPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIA-AIGDRS-----------KKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILrgcsAKEKSEYL-----LEGVDNYRFLVNRGITLPNV 327
Cdd:cd14917 150 IRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQIL----SNKKPELLdmlliTNNPYDYAFISQGETTVASI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 328 DDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPR 407
Cdd:cd14917 226 DDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 408 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTN 487
Cdd:cd14917 306 VKVGNEYVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 488 EKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPK 566
Cdd:cd14917 385 EKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 567 FIVP---DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGicAAEMNETAFGMR 643
Cdd:cd14917 465 FQKPrniKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF--ANYAG--ADAPIEKGKGKA 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14917 541 KKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 25150354 724 RHRYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14917 621 RQRYRILNPAAIPEgQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
93-770 |
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: 693.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYY-SSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivqkpdvrnpigELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET--------------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDV 330
Cdd:cd01380 142 YIEILFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGsPVIDGVDDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd01380 222 AEFEETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDIAGFEIFDINSFEQICINYTNEK 489
Cdd:cd01380 302 RSEVIVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 490 LQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPK--F 567
Cdd:cd01380 382 LQQQFNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhF 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDMrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaefagicaaemnetafgmrSRKg 647
Cdd:cd01380 461 KKPRF-SNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-----------------------------NRK- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 648 mfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 727
Cdd:cd01380 510 --KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRY 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 25150354 728 EILTPDViPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01380 588 RVLLPSK-EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
93-770 |
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: 683.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAGATRNKSlnaAAQQNIVQkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKK---EQQPGKMQ--------GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDV 330
Cdd:cd14923 151 IRIHFGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLISTNPFDFpFVSQGeVTVASIDDS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd14923 230 EELLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKL 490
Cdd:cd14923 310 GNEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 491 QQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIV 569
Cdd:cd14923 389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 PDM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaeFAGICAAEMNETAFGMRSRK 646
Cdd:cd14923 469 PKPakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN--YAGAEAGDSGGSKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 647 GMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHR 726
Cdd:cd14923 547 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 727 YEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14923 627 YRILNASAIPEgQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
93-770 |
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: 683.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVA--GATRNKSLNAAAQQnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAvtGEKKKEEATSGKMQ------------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVD 328
Cdd:cd14910 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNpyDYAFVSQGEITVPSID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd14910 229 DQEELMATDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14910 309 KVGNEYVTKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKF 567
Cdd:cd14910 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicAAEMNETAFGMRS 644
Cdd:cd14910 468 QKPKPakgKVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAA---EAEEGGGKKGGKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 RKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd14910 545 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 725 HRYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14910 625 QRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
94-770 |
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: 680.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 94 VLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGES 173
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 174 GAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFI 253
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQ------------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 254 RINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDDVQ 331
Cdd:cd14918 151 RIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNpyDYAFVSQGEITVPSIDDQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd14918 230 ELMATDSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd14918 310 NEYVTKGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVP 570
Cdd:cd14918 389 QFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 571 DM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETA-FGMRSRK 646
Cdd:cd14918 469 KVvkgKAEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASL-----FSTYASAEADSGAkKGAKKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 647 GMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHR 726
Cdd:cd14918 544 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 727 YEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14918 624 YKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
93-770 |
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: 680.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAG-ATRNKSLNAAAQQnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNANK------------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDD 329
Cdd:cd14916 150 FIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNpyDYAFVSQGEVSVASIDD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 409
Cdd:cd14916 229 SEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 410 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEK 489
Cdd:cd14916 309 VGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 490 LQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFI 568
Cdd:cd14916 388 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 569 VP---DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGICAAEMNETAfGMRSR 645
Cdd:cd14916 468 KPrnvKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF--STYASADTGDSGKGK-GGKKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd14916 545 GSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 726 RYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14916 625 RYRILNPAAIPEgQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-770 |
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: 675.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVA--GATRNKSLNAAAQQnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAvtGEKKKEEITSGKMQ------------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVD 328
Cdd:cd14912 150 KFIRIHFGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYpFVSQGeISVASID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd14912 229 DQEELMATDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14912 309 KVGNEYVTKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKF 567
Cdd:cd14912 388 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETAFGMR- 643
Cdd:cd14912 468 QKPKVvkgKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYL-----FSGAQTAEGASAGGGAKk 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 --SRKG-MFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPF 720
Cdd:cd14912 543 ggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILY 622
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 721 QEFRHRYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14912 623 ADFKQRYKVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
93-770 |
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: 675.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVA--GATRNKSLNAAAQQnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtGEKKKEEAASGKMQ------------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVD 328
Cdd:cd14915 150 KFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLITTNPYDFaFVSQGeITVPSID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd14915 229 DQEELMATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14915 309 KVGNEYVTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKF 567
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNF 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDM---RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicAAEMNETAFGMRS 644
Cdd:cd14915 468 QKPKPakgKAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTA---EAEGGGGKKGGKK 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 RKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd14915 545 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 25150354 725 HRYEILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14915 625 QRYKVLNASAIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
93-770 |
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: 665.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqnivqkpdvrnpIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESE-------------------VERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQ 331
Cdd:cd01378 143 MEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFtQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd01378 223 DFKEVLNAMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REF---VNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd01378 302 GGGrsvYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFP-KANDKSFVEKLQKTHNKHPK 566
Cdd:cd01378 382 KLQQIFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPH 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 567 FIVPDMR---SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemnetafgmr 643
Cdd:cd01378 461 FECPSGHfelRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD-------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 644 SRKgmfR--TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd01378 527 SKK---RppTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 722 EFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01378 604 KFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
93-770 |
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: 655.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVagaTRNKSlnaaaqqnivqkpdvrnpigELEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---TNNHS--------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSA-KE-KSEYLLEGVDNYRFLVNRG-ITLPNVDD 329
Cdd:cd14883 139 IEVCFDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHsKElKEKLKLGEPEDYHYLNQSGcIRIDNIND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDR-VIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd14883 219 KKDFDHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKeILKIVAKLLGVDPDKLKKALTIRQI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKsldRTH--RQGASFIGILDIAGFEIFDINSFEQICINYT 486
Cdd:cd14883 299 NVRGNVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINS---CTNpgQKNSRFIGVLDIFGFENFKVNSFEQLCINYT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 487 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEK-PMGVLALLDEECLFPKANDKSFVEKLQKTHNKHP 565
Cdd:cd14883 376 NEKLHKFFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 566 KFIVPDMR-SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWK---DAEFAGICAAEMNETAFG 641
Cdd:cd14883 455 YYEKPDRRrWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdLLALTGLSISLGGDTTSR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 642 MRSRKGmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd14883 535 GTSKGK--PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFK 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 722 EFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14883 613 EFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
92-770 |
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: 633.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGatrnkslNAAAQQNIVqkpdvrnpigelEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGG-------RAVTEGRSV------------EQQVLESNPLLEAFGNAKTVRNNNSSRFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG--ITLPNVD 328
Cdd:cd01384 142 KFVEIQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYL-NQSkcFELDGVD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKVCHLLGLPVIELQKAFLR 405
Cdd:cd01384 221 DAEEYRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 406 PRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQICINY 485
Cdd:cd01384 301 RVIVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 486 TNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKH 564
Cdd:cd01384 380 ANEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDH 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 565 PKFIVPDmRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAgicAAEMNETafgmrS 644
Cdd:cd01384 459 KRFSKPK-LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL-----FP---PLPREGT-----S 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 RKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd01384 525 SSSKFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 725 HRYEILTPDVIPKNFiDGKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd01384 605 DRFGLLAPEVLKGSD-DEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
92-770 |
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: 626.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGAtrnKSLnaaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQ---HSW--------------------IEQQILEANPILEAFGNAKTIRNDNSSRFGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDV 330
Cdd:cd01381 138 YIDIHFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKS--DQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd01381 218 AEFADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAS--FIGILDIAGFEIFDINSFEQICINYT 486
Cdd:cd01381 298 FTRGETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFA 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 487 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHP 565
Cdd:cd01381 378 NENLQQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 566 KFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFvagiwkdaeFAGICAAEMNETAfGMRSR 645
Cdd:cd01381 457 NYLKPKSDLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF---------LKQLFNEDISMGS-ETRKK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd01381 527 S---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 726 RYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01381 604 RYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
93-770 |
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: 623.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKgkKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAGATRNkslnaaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-----------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQ 331
Cdd:cd01383 137 IDIHFDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 411
Cdd:cd01383 217 KFHELKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 412 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 491
Cdd:cd01383 297 GDKIVKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 492 QLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFivp 570
Cdd:cd01383 377 QHFNRHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF--- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 571 DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNS----TDPFVAGIWKDAEfagicAAEMNETAFGMRSRK 646
Cdd:cd01383 453 KGERGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCscqlPQLFASKMLDASR-----KALPLTKASGSDSQK 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 647 gmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHR 726
Cdd:cd01383 528 ---QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARR 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 727 YEILTPDviPKNFIDGKESVRKMI-TALDIDTNLYRIGQSKVFFR 770
Cdd:cd01383 605 YGFLLPE--DVSASQDPLSTSVAIlQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
92-770 |
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: 567.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGATrnkslnaaaqqnivqkpdvrnpIGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG----------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEyLLEGvdnyrflvnrgitlPNVDDV 330
Cdd:cd01382 139 KFVEIHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREK-LLKD--------------PLLDDV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQE-----------KKSDQAmlqddrvIQKVCHLLGLPVIEL 399
Cdd:cd01382 204 GDFIRMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENgsdsgggcnvkPKSEQS-------LEYAAELLGLDQDEL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 400 QKAfLRPR-------------IKVGREFvnkaqnqEQAEFAVEAIAKASYERLFKWLVTRINKSLdrTHRQGASFIGILD 466
Cdd:cd01382 277 RVS-LTTRvmqttrggakgtvIKVPLKV-------EEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 467 IAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLF 545
Cdd:cd01382 347 IAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKL 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 546 PKANDKSFVEKLQKTHNKHPKFIVP---------DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDP 616
Cdd:cd01382 426 PKPSDQHFTSAVHQKHKNHFRLSIPrksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 617 FVAGIWkdaefagiCAAEMNETAFGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLE 696
Cdd:cd01382 506 FIRSLF--------ESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILS 577
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 697 QLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKnfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01382 578 QLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
92-770 |
1.62e-180 |
|
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: 561.70 E-value: 1.62e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNkslnaaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcsAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDV 330
Cdd:cd14872 138 WVEIHFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLAS--PDPASRGGWGSSAAYGYLSLSGcIEVEGVDDV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQE------KKSDQAmlqDDRVIQKVCHLLGLPVIELQKAFL 404
Cdd:cd14872 216 ADFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGggkslvSGSTVA---NRDVLKEVATLLGVDAATLEEALT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 405 RPRIKV-GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICI 483
Cdd:cd14872 293 SRLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCI 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 484 NYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEK-PMGVLALLDEECLFPKANDKSFVEKLQKTHN 562
Cdd:cd14872 373 NFTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 563 KHPKFI-VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFagicaaemnetafg 641
Cdd:cd14872 452 AKSTFVyAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG-------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 642 mrSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd14872 518 --DQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHE 595
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 25150354 722 EFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14872 596 RFLKRYRFLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
92-768 |
2.97e-175 |
|
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: 548.24 E-value: 2.97e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEF------KGKKRHEMPPHIFAIADTAYRSMLQERE-- 163
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 164 --DQSILCTGESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqQNIVQKPDVRNpigelehQLLQANPILEAFGNSKTV 241
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHG-------QNATERENVRD-------RVLESNPILEAFGNARTN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 242 KNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG 321
Cdd:cd14901 147 RNNNSSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL-NSS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 322 ---ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQEKKSDQAMLQDDRVIQKVCHLLGLPVI 397
Cdd:cd14901 226 qcyDRRDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 398 ELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAS-FIGILDIAGFEIFDIN 476
Cdd:cd14901 306 VLEKTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 477 SFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgldlqPTIDLI-----EKPMGVLALLDEECLFPKANDK 551
Cdd:cd14901 386 SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNNDACvamfeARPTGLFSLLDEQCLLPRGNDE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 552 SFVEKLQKTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGiwkdaefagi 630
Cdd:cd14901 461 KLANKYYDLLAKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS---------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 631 caaemnetafgmrsrkgmfrTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRIC 710
Cdd:cd14901 531 --------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKIS 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 711 RQGFPNRVPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNL-----YRIGQSKVF 768
Cdd:cd14901 591 RSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
92-770 |
1.83e-172 |
|
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: 540.90 E-value: 1.83e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQ----EREDQS 166
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 167 ILCTGESGAGKTENTKKVIQYLAHVAGAtRNKSLNAAAQQNIVQKPdvrNPIGELEHQLLQANPILEAFGNSKTVKNDNS 246
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSG-FAQGASGEGEAASEAIE---QTLGSLEDRVLSSNPLLESFGNAKTLRNDNS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 247 SRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLE-GVDNYRFLVNRGiTLP 325
Cdd:cd14890 157 SRFGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQtPVEYFYLRGECS-SIP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 326 NVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQamLQDDRVIQ---KVCHLLGLPVIELQKA 402
Cdd:cd14890 236 SCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTV--LEDATTLQslkLAAELLGVNEDALEKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 403 FLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQIC 482
Cdd:cd14890 314 LLTRQLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLC 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 483 INYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-----KPmGVLALLDEECLFPKAN-DKSFVEK 556
Cdd:cd14890 393 INYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLDDCWRFKGEEaNKKFVSQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 557 LQKTH-------------NKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwk 623
Cdd:cd14890 471 LHASFgrksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR--------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 624 daefagicaAEMNETAFGMRsrkgmFRTvsqlhkeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGV 703
Cdd:cd14890 542 ---------RSIREVSVGAQ-----FRT-------QLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGM 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150354 704 LEGIRICRQGFPNRVPFQEFRHRYEILTPDVipknfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14890 601 MEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
92-770 |
6.39e-170 |
|
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: 533.56 E-value: 6.39e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVagatrNKSLNAAAQQnivqkpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV-----NQRRNNLVTE-----------------QILEATPLLEAFGNAKTVRNDNSSRFGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDmSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGIT--LPNVDD 329
Cdd:cd01387 139 YLEVFFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKY-FYLNQGGNceIAGKSD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ---EKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRP 406
Cdd:cd01387 217 ADDFRRLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 407 RIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINkSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYT 486
Cdd:cd01387 297 VTETRRERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 487 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHP 565
Cdd:cd01387 376 NENLQYYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 566 KFIVPDMrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaefagICAAEMNETAFGMRSR 645
Cdd:cd01387 455 LYSKPRM-PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS-----HRAQTDKAPPRLGKGR 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 ----KGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd01387 529 fvtmKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQ 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 722 EF--RHRYEILTPDVIPKNFIDGKESVRKMITAldIDTNLYRIGQSKVFFR 770
Cdd:cd01387 609 VFidRYRCLVALKLPRPAPGDMCVSLLSRLCTV--TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
93-770 |
1.26e-168 |
|
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: 529.16 E-value: 1.26e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAGATrNKSLnaaaqqnivqkpdvrnpigelEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN-NRTL---------------------EEKILQVNPLMEAFGNARTVINDNSSRFGKY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSE-YLLEGVDNYRFLVNRGITLPNVDD-- 329
Cdd:cd01379 140 LEMKFTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkYKLPENKPPRYLQNDGLTVQDIVNns 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 --VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ----AMLQDDRVIQKVCHLLGLPVIELQKAF 403
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEAL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 404 LRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL--DRTHRQGASFIGILDIAGFEIFDINSFEQI 481
Cdd:cd01379 300 TSHSVVTRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 482 CINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQKt 560
Cdd:cd01379 380 CINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHN- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 561 hNKHPKFIVpdmRSKSH---FAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAgiwkdaefagicaaemne 637
Cdd:cd01379 458 -NIKSKYYW---RPKSNalsFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 638 tafgmrsrkgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNR 717
Cdd:cd01379 516 ------------QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHR 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 25150354 718 VPFQEFRHRYEIL----TPDVIPKnfidgKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd01379 584 ILFADFLKRYYFLafkwNEEVVAN-----RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
92-770 |
2.36e-167 |
|
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: 525.80 E-value: 2.36e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKK-RHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGatrnkslnaaaqqnivqkpdvrNPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSP----------------------SDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDV 330
Cdd:cd14897 139 KFIELHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QE-------FHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAF 403
Cdd:cd14897 219 EEleyyrqmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEAL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 404 LRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL----DRTHRQGASFIGILDIAGFEIFDINSFE 479
Cdd:cd14897 299 ISNVNTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 480 QICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQ 558
Cdd:cd14897 379 QLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 559 KTHNKHPKFiVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVagiwkdaefagicaaemnet 638
Cdd:cd14897 458 KYCGESPRY-VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFI-------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 639 afgmrsrKGMFrtvSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRV 718
Cdd:cd14897 517 -------SDLF---TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRI 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 25150354 719 PFQEFRHRYEILTPDViPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd14897 587 KYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
92-770 |
1.83e-166 |
|
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: 525.40 E-value: 1.83e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAgatrnkslnaaaqqnivQKPDVRNpigeLEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALS-----------------QKGYGSG----VEQTILGAGPVLEAFGNAKTAHNNNSSRFGK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFL-VNRGITLPNVDDV 330
Cdd:cd01385 140 FIQVNYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnQSDCYTLEGEDEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEK--KSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd01385 220 YEFERLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL----DRTHRQGASfIGILDIAGFEIFDINSFEQICIN 484
Cdd:cd01385 300 VTVGETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCIN 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 485 YTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNK 563
Cdd:cd01385 379 YANEHLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 564 HPKFIVPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGI----------WKDAEFAGICAA 633
Cdd:cd01385 458 NKYYEKPQVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWAVLRAFFRAMA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 634 EMNETafGMRSRKG--------MFRTVSQLHKEQ---------------LTKLMTTLRNTSPHFVRCIIPNHEKKSGKIN 690
Cdd:cd01385 537 AFREA--GRRRAQRtaghsltlHDRTTKSLLHLHkkkkppsvsaqfqtsLSKLMETLGQAEPFFIRCIKSNAEKKPLRFD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 691 SNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILtpdvIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01385 615 DELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
92-732 |
1.65e-163 |
|
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: 516.55 E-value: 1.65e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKgKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAhVAGAT--RNKSLnaaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSR 248
Cdd:cd14888 80 GESGAGKTESTKYVMKFLA-CAGSEdiKKRSL--------------------VEAQVLESNPLLEAFGNARTLRNDNSSR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 249 FGKFIRINFDM---------SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQIlrgCSAKEKS---EYLLEGVDNYRF 316
Cdd:cd14888 139 FGKFIELQFSKlkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQL---CAAAREAkntGLSYEENDEKLA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 317 ------------------LVNRGIT------LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQE 371
Cdd:cd14888 216 kgadakpisidmssfephLKFRYLTksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 372 KKSDQAMLQD--DRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINK 449
Cdd:cd14888 296 ACSEGAVVSAscTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 450 SLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI 529
Cdd:cd14888 376 SIGYSKDNSLLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 530 -EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVG 608
Cdd:cd14888 455 qEKPLGIFCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQE 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 609 LMQNSTDPFVAGIWKdAEFAGICAAEMnetafgmrsRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGK 688
Cdd:cd14888 534 VIKNSKNPFISNLFS-AYLRRGTDGNT---------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 25150354 689 INSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 732
Cdd:cd14888 604 FDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
92-770 |
2.46e-162 |
|
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: 513.17 E-value: 2.46e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqkpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTIK----------------------KIIEVNPLLESFGNAKTVRNDNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKseYLLEGVDNYRFL-VNRGITLPNVDD 329
Cdd:cd14903 139 KFTQLQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ--AMLQDDRVIQKVCHLLGLPVIELQKAFLRPR 407
Cdd:cd14903 217 RKHFARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEksAIAPGDQGAVYATKLLGLSPEALEKALCSRT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 408 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQICINYTN 487
Cdd:cd14903 297 MRAAGDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYAN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 488 EKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKF 567
Cdd:cd14903 376 EKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 568 IVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKD-AEFAGICAAEMNETAFGMRSRK 646
Cdd:cd14903 455 IEFPRTSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEkVESPAAASTSLARGARRRRGGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 647 GMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHR 726
Cdd:cd14903 535 LTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDK 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 727 YEILTPDViPKNFIDGKESVRKMITALDIDT-NLYRIGQSKVFFR 770
Cdd:cd14903 615 FWLFLPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
92-770 |
1.69e-159 |
|
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: 505.45 E-value: 1.69e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSE----DLIEEFKgKKRHEMPPHIFAIADTAYRSMLQER----E 163
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpgfDSQRKEE-ATASSPPPHVFSIAERAYRAMKGVGkgqgT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 164 DQSILCTGESGAGKTENTKKVIQYLA----HVAGATRNKSLNAAAQQnivqkpdvrnpigeLEHQLLQANPILEAFGNSK 239
Cdd:cd14892 80 PQSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHES--------------IEECVLLSNLILEAFGNAK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 240 TVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvN 319
Cdd:cd14892 146 TIRNDNSSRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFL-N 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 320 RG--ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQ--KVCHLLGLP 395
Cdd:cd14892 225 QGncVEVDGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 396 VIELQKAFLRPRIKVGR-EFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQ---------GASFIGIL 465
Cdd:cd14892 305 AAELMFKLVTQTTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGIL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 466 DIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEK-PMGVLALLDEECL 544
Cdd:cd14892 385 DIFGFEIMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQML 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 545 FP-KANDKSFVEKLQKTH-NKHPKFIVPDMRSkSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQnstdpfvagiw 622
Cdd:cd14892 464 LKrKTTDKQLLTIYHQTHlDKHPHYAKPRFEC-DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLR----------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 623 kdaefagicaaemnetafgmRSRKgmFRTvsqlhkeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNG 702
Cdd:cd14892 532 --------------------SSSK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSG 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 703 VLEGIRICRQGFPNRVPFQEFRHRYEILTPDV--IPKNFIDGKESVRKM----ITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14892 583 VLEVVRIRREGFPIRRQFEEFYEKFWPLARNKagVAASPDACDATTARKkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
92-770 |
9.24e-159 |
|
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: 503.17 E-value: 9.24e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAgatrnkslnaaaqQNIVQKPdVRNPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVIS-------------QQSLELS-LKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDD 329
Cdd:cd14873 147 KFVQLNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGcVEDKTISD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQekkSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 409
Cdd:cd14873 227 QESFREVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 410 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLdrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEK 489
Cdd:cd14873 304 LRGEEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 490 LQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIV 569
Cdd:cd14873 382 LQEYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVK 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 PDMRSkSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETAFGMRSRKGmf 649
Cdd:cd14873 461 PRVAV-NNFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDL-----FEHVSSRNNQDTLKCGSKHRR-- 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 650 RTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEI 729
Cdd:cd14873 533 PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKV 612
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 730 LTPDvipknfIDGKESVRKMITAL----DIDTNLYRIGQSKVFFR 770
Cdd:cd14873 613 LMRN------LALPEDVRGKCTSLlqlyDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
92-730 |
1.09e-158 |
|
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: 503.41 E-value: 1.09e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRH--------EMPPHIFAIADTAYRSMLQER 162
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 163 EDQSILCTGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKPDVRNPIgelEHQLLQANPILEAFGNSKTVK 242
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKSTKSI---EQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 243 NDNSSRFGKFIRINFDM-SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEG---VDNYRFL- 317
Cdd:cd14907 158 NDNSSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLk 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 318 VNRGITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQA--MLQDDRVIQKVCHLLGLP 395
Cdd:cd14907 238 KSNCYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 396 VIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL-------DRTHRQGASFIGILDIA 468
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 469 GFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDF--IDFgLDLQPTIDLIEK-PMGVLALLDEECLF 545
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 546 PKANDKSFVEKLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkda 625
Cdd:cd14907 477 ATGTDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI---- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 626 eFAGICAAEMNETAFGMRSRKGMfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLE 705
Cdd:cd14907 553 -FSGEDGSQQQNQSKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLE 630
|
650 660
....*....|....*....|....*
gi 25150354 706 GIRICRQGFPNRVPFQEFRHRYEIL 730
Cdd:cd14907 631 SIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
94-770 |
4.87e-149 |
|
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: 476.71 E-value: 4.87e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 94 VLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSML----QEREDQSILC 169
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 170 TGESGAGKTENTKKVIQYLAHVAGATrnkslnaaaqqnivqkpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRF 249
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGN-----------------------SQLEQQILQVNPLLEAFGNAQTVMNDNSSRF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 250 GKFIRINFdMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRgitLPNVDD 329
Cdd:cd14889 140 GKYIQLRF-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNG---AGCKRE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEF----HSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFL 404
Cdd:cd14889 216 VQYWkkkyDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFeMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 405 RPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQG--ASFIGILDIAGFEIFDINSFEQIC 482
Cdd:cd14889 296 CTVTFTRGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQAC 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 483 INYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDL-IEKPMGVLALLDEECLFPKANDKSFVEKLQKTH 561
Cdd:cd14889 376 INLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHF 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 562 NKHPKFIVPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDP-----FVAGIWKDAEFAGICAA-EM 635
Cdd:cd14889 455 KGNSYYGKSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPllsvlFTATRSRTGTLMPRAKLpQA 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 636 NETAFGmRSRKgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFP 715
Cdd:cd14889 534 GSDNFN-STRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFS 609
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 716 NRVPFQEFRHRYEILtpdVIPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd14889 610 WRPSFAEFAERYKIL---LCEPALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
58-768 |
6.70e-146 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 473.75 E-value: 6.70e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 58 TSRQVTISRDDVQKANPP-KFDKIEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK 136
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 137 GKKRHE-MPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAhvAGATRNKSLNaaaqqniVQKpdvr 215
Cdd:PTZ00014 155 DAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLK-------IQN---- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 216 npigelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQIL 295
Cdd:PTZ00014 222 --------AIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 296 RGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKK-- 373
Cdd:PTZ00014 294 KGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgg 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 374 -SDQAMLQDD--RVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKS 450
Cdd:PTZ00014 374 lTDAAAISDEslEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNAT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 451 LDrtHRQG-ASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLI 529
Cdd:PTZ00014 454 IE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLL 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 530 -EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVG 608
Cdd:PTZ00014 531 cGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVE 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 609 LMQNSTDPFVAGIWKDAEfagicaAEMNETAfgmrsrKGMFRTvSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGK 688
Cdd:PTZ00014 611 VVKASPNPLVRDLFEGVE------VEKGKLA------KGQLIG-SQF-LNQLDSLMSLINSTEPHFIRCIKPNENKKPLD 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 689 INSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVF 768
Cdd:PTZ00014 677 WNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVF 756
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
92-770 |
1.54e-144 |
|
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: 463.75 E-value: 1.54e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLI--YTYSGLFCVVINPYKKLPiysEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQERE---DQS 166
Cdd:cd14891 1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 167 ILCTGESGAGKTENTKKVIQYLAHvagatRNKSLNAAAQQNIVQKPDVRNPIG-ELEHQLLQANPILEAFGNSKTVKNDN 245
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTT-----RAVGGKKASGQDIEQSSKKRKLSVtSLDERLMDTNPILESFGNAKTLRNHN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 246 SSRFGKFIRINFDMSGY-ISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-IT 323
Cdd:cd14891 153 SSRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 324 LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF----TQEKKSDQAMLQDDRVIQKVCHLLGLPVIEL 399
Cdd:cd14891 233 DDNIDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 400 QKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRtHRQGASFIGILDIAGFEIFDI-NSF 478
Cdd:cd14891 313 EKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 479 EQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKL 557
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 558 QKTHNKHPKFIVPDMRSKSH-FAVVHYAGRVDYSADQWLMKNMDplnenvvglmqnstdpfvagiwkdaefagICAAEMN 636
Cdd:cd14891 471 HKTHKRHPCFPRPHPKDMREmFIVKHYAGTVSYTIGSFIDKNND-----------------------------IIPEDFE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 637 ETafgmrsrkgmFRTvSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPN 716
Cdd:cd14891 522 DL----------LAS-SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPT 590
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150354 717 RVPFQEFRHRY-EILTPDVIP------KNFIDGkesvrkMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14891 591 RVTYAELVDVYkPVLPPSVTRlfaendRTLTQA------ILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
92-770 |
1.41e-141 |
|
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: 456.68 E-value: 1.41e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK--GKKRHE-------MPPHIFAIADTAYRSMLQE- 161
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 162 REDQSILCTGESGAGKTENTKKVIQYLAHVAGAtrnkslnaaaqQNIVQKPDVRNPIGELEHQLLQANPILEAFGNSKTV 241
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNG-----------EEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 242 KNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY--------LLEGVDN 313
Cdd:cd14908 150 RNDNSSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYefhdgitgGLQLPNE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 314 YRFlVNRG--ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAML---QDDRVIQKV 388
Cdd:cd14908 230 FHY-TGQGgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 389 CHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDI 467
Cdd:cd14908 309 AKLLGVDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 468 AGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFP 546
Cdd:cd14908 389 FGFECFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 547 -KANDKSFVEKL--------QKTHNKHPKFIVPD-MRSKSHFAVVHYAGRVDYSADQWLM-KNMDPLnenvvglmqnstd 615
Cdd:cd14908 468 iRGSDANYASRLyetylpekNQTHSENTRFEATSiQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEI------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 616 PFVAGIwkdaefagicaaemnetafgmrsrkgMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVL 695
Cdd:cd14908 535 PLTADS--------------------------LFESGQQF-KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 696 EQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP----DVIPKNFID---GKESVRKMITAL-------------DI 755
Cdd:cd14908 588 EQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipeVVLSWSMERldpQKLCVKKMCKDLvkgvlspamvsmkNI 667
|
730
....*....|....*
gi 25150354 756 DTNLYRIGQSKVFFR 770
Cdd:cd14908 668 PEDTMQLGKSKVFMR 682
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
93-733 |
7.92e-140 |
|
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: 449.76 E-value: 7.92e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEF-----------KGKKRHEMPPHIFAIADTAYRSM-- 158
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 159 --LQEREDQSILCTGESGAGKTENTKKVIQYLAHvAGATRNKsLNAAAQQNIVQKPDvrnpigelehQLLQANPILEAFG 236
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNLA-ASVSMGKSTSGIAA----------KVLQTNILLESFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 237 NSKTVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEyllegvDNYRf 316
Cdd:cd14900 150 NARTLRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR------DMYR- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 317 lvnrgitlpnvddvqefhSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSD-QAMLQDDRVIQKV------C 389
Cdd:cd14900 223 ------------------RVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 390 HLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRIN---KSLDRTHRQGAS-FIGIL 465
Cdd:cd14900 285 TLLSVDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKSHGGLhFIGIL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 466 DIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECL 544
Cdd:cd14900 365 DIFGFEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 545 FPKANDKSFVEKLQKTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNStdpfvagiwk 623
Cdd:cd14900 444 MPKGSDTTLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG---------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 624 daefagicaaemnetafgmrsrkGMFrtvsqlhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGV 703
Cdd:cd14900 514 -----------------------LQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGV 563
|
650 660 670
....*....|....*....|....*....|
gi 25150354 704 LEGIRICRQGFPNRVPFQEFRHRYEILTPD 733
Cdd:cd14900 564 MEAVRVARAGFPIRLLHDEFVARYFSLARA 593
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
92-770 |
3.81e-139 |
|
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: 449.01 E-value: 3.81e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqkpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA----------------------KVIDVNPLLESFGNAKTTRNDNSSRFG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNR--GITLPNVD 328
Cdd:cd14904 139 KFTQLQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQkVCHLLGLPVIELQKAFLRPRI 408
Cdd:cd14904 219 DAKLFASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSV 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 409 KVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 488
Cdd:cd14904 298 VTRNESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 489 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHN---KHP 565
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 566 KFIVPDMRsKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagiCAAEMNETAFGmRSR 645
Cdd:cd14904 457 SIDFPKVK-RTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSG-KGT 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd14904 531 KAPKSLGSQF-KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELAT 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 25150354 726 RYEILTPDVIPKNfiDGKESVRKMITALDIDTNL-YRIGQSKVFFR 770
Cdd:cd14904 610 RYAIMFPPSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
92-723 |
1.99e-138 |
|
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: 449.34 E-value: 1.99e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFK--------GKKRHEMPPHIFAIADTAYRSMLQ-E 161
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 162 REDQSILCTGESGAGKTENTKKVIQYLAHVaGATRNKSLNAAAQQNIVQKpdvrnpigelehQLLQANPILEAFGNSKTV 241
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-GRDQSSTEQEGSDAVEIGK------------RILQTNPILESFGNAQTI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 242 KNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSaKEKSEYL-LEGVDNYRFLVNR 320
Cdd:cd14902 148 RNDNSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGAD-KTLLDLLgLQKGGKYELLNSY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 321 GIT-----LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKVCHLL 392
Cdd:cd14902 227 GPSfarkrAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASrfhLAKCAELM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 393 GLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD--------RTHRQGASFIGI 464
Cdd:cd14902 307 GVDVDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 465 LDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEEC 543
Cdd:cd14902 387 LDIFGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQEC 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 544 LFPKANDKSFVEKLQKTHNKHPKFIVPdmrskshfavvHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWK 623
Cdd:cd14902 466 LMPKGSNQALSTKFYRYHGGLGQFVVH-----------HFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 624 DAEFAGICAaemnETAFGMRSRKGMFRT--VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCN 701
Cdd:cd14902 535 DENRDSPGA----DNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSV 610
|
650 660
....*....|....*....|..
gi 25150354 702 GVLEGIRICRQGFPNRVPFQEF 723
Cdd:cd14902 611 GVLEAVRIARHGYSVRLAHASF 632
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
92-768 |
6.66e-137 |
|
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: 442.50 E-value: 6.66e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRH-EMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAhvagATRNKSLNAAAQQNIvqkpdvrnpigelehqlLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNMDLRIQTAI-----------------MAANPVLEAFGNAKTIRNNNSSRFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDV 330
Cdd:cd14876 140 RFMQLDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKK---SDQAMLQDD--RVIQKVCHLLGLPVIELQKAFLR 405
Cdd:cd14876 220 ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEqgvDDAAAISNEslEVFKEACSLLFLDPEALKRELTV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 406 PRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAsFIGILDIAGFEIFDINSFEQICINY 485
Cdd:cd14876 300 KVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 486 TNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKH 564
Cdd:cd14876 379 TNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 565 PKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGIcAAEMNETAfgmrs 644
Cdd:cd14876 458 GKFKPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKAL-----FEGV-VVEKGKIA----- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 645 rKGMFrTVSQLHKeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 724
Cdd:cd14876 527 -KGSL-IGSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFL 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 25150354 725 HRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVF 768
Cdd:cd14876 604 YQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
92-770 |
4.57e-130 |
|
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: 423.04 E-value: 4.57e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAgatrnkslnaaaqqnivQKPDvRNPIGELEHQLlqanPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLY-----------------QDQT-EDRLRQPEDVL----PILESFGHAKTILNANASRFGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFdMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGIT--LPNVDD 329
Cdd:cd14896 139 VLRLHL-QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETY-YYLNQGGAcrLQGKED 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ--AMLQDDRVIQKVCHLLGLPVIELQKAFLRPR 407
Cdd:cd14896 217 AQDFEGLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 408 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDIAGFEIFDINSFEQICINYT 486
Cdd:cd14896 297 TETPYGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 487 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDfGLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHP 565
Cdd:cd14896 377 SERLQLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHP 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 566 KFIVPDMrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefagicaaemnETAFGMRSR 645
Cdd:cd14896 456 SYAKPQL-PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA-----------EPQYGLGQG 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 646 KGmfrTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 725
Cdd:cd14896 524 KP---TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 25150354 726 RYEILTPDVIPkNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14896 601 RFGALGSERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
92-770 |
3.59e-127 |
|
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: 416.71 E-value: 3.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnIVQKpdvrnpigelehqlLQA-NPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVL--------SVEK--------------LNAaLTVLEAFGNVRTALNGNATRFS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLE--GVDNYRFLVnrgiTLPNVD 328
Cdd:cd01386 139 QLFSLDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIV----PLQKPE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQ----EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFL 404
Cdd:cd01386 215 DKQkaaaAFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIF 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 405 RPRIKVGREFVNKAQNQEQAEF------------AVEAIAKASYERLFKWLVTRINKSLDRTHRQGASfIGILDIAGFE- 471
Cdd:cd01386 295 KHHLSGGPQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQn 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 472 -----IFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEK--------------- 531
Cdd:cd01386 374 pahsgSQRGATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrded 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 532 PMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKS----HFAVVHYAGR--VDYSADQWLMK-NMDPLNE 604
Cdd:cd01386 454 RRGLLWLLDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 605 NVVGLMQNSTDPfvagiwkdaefagicaaemnetaFGMRSRKGMFrtvSQLhKEQLTKLMTTLRNTSPHFVRCIIPNH-- 682
Cdd:cd01386 534 NATQLLQESQKE-----------------------TAAVKRKSPC---LQI-KFQVDALIDTLRRTGLHFVHCLLPQHna 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 683 EKKSGK----------INSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKNF-----IDGKESVR 747
Cdd:cd01386 587 GKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVE 666
|
730 740
....*....|....*....|...
gi 25150354 748 KMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd01386 667 ELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
92-770 |
1.59e-120 |
|
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: 396.87 E-value: 1.59e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYS-SLIYTYSGLFCVVINPYKKLPIYSEDLIEEF-KGKKRHEMPPHIFAIADTAYRSM-LQEREDQSIL 168
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 169 CTGESGAGKTENTKKVIQYLahvaGATRNKSLNAAAQQNIVQKPDvrnpigeleHQLLQANPILEAFGNSKTVKNDNSSR 248
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYL----GQLSYMHSSNTSQRSIADKID---------ENLKWSNPVMESFGNARTVRNDNSSR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 249 FGKFIRINFD-MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY-LLEGVDNYRFL------VNR 320
Cdd:cd14875 148 FGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLnggntfVRR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 321 GITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKkSDQAMLQDDRVIQKVCHLLGLPVIELQ 400
Cdd:cd14875 228 GVDGKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQ-NDKAQIADETPFLTACRLLQLDPAKLR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 401 KAFLrprIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQGASFIGILDIAGFEIFDINSFE 479
Cdd:cd14875 307 ECFL---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 480 QICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKL-Q 558
Cdd:cd14875 384 QLCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLwD 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 559 KTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemnet 638
Cdd:cd14875 464 QWANKSPYFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEK------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 639 afGMRSRKgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRV 718
Cdd:cd14875 532 --GLARRK---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRR 606
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150354 719 PFQEFRHRYEILTPDVIPKNFIDGKESvRKMITALDIDTNLYR-------IGQSKVFFR 770
Cdd:cd14875 607 PIEQFCRYFYLIMPRSTASLFKQEKYS-EAAKDFLAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
92-770 |
2.25e-120 |
|
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: 395.79 E-value: 2.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRH-----EMPPHIFAIADTAYRSMLQEREDQ 165
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 166 SILCTGESGAGKTENTKKVIQYLAHvaGATRNKSlnaaaqqnivqkpDVRNPIgelehqlLQANPILEAFGNSKTVKNDN 245
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY--GHSTSST-------------DVQSLI-------LGSNPLLESFGNAKTLRNNN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 246 SSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG--IT 323
Cdd:cd14886 139 SSRFGKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFL-NASkcYD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 324 LPNVDDVQEFHSTINSMRIMgFADDEISSIMRVVSAVLLLGNLEFTQEKKS---DQAMLQDDRVIQKVCHLLGLPVIELQ 400
Cdd:cd14886 218 APGIDDQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 401 KAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINK--SLDRTHRQgasFIGILDIAGFEIFDINSF 478
Cdd:cd14886 297 QAIITKVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEiiQFDADARP---WIGILDIYGFEFFERNTY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 479 EQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEKP-MGVLALLDEECLFPKANDKSFVEKL 557
Cdd:cd14886 374 EQLLINYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 558 qKTHNKHPKFIvPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemNE 637
Cdd:cd14886 453 -KSKIKNNSFI-PGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIP---------NE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 638 TAfgmrSRKGMFrtVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNR 717
Cdd:cd14886 522 DG----NMKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYN 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 718 VPFQEFRHRYEILT--PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14886 596 DTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
92-732 |
3.40e-120 |
|
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: 395.76 E-value: 3.40e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKR-HEMPPHIFAIADTAYRSMLQERE--DQSI 167
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 168 LCTGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSS 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER--------------IEQRILNSNPVMEAFGNACTLRNNNSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 248 RFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLpnv 327
Cdd:cd14880 147 RFGKFIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 328 dDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFT---QEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFL 404
Cdd:cd14880 224 -EEDCFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFAdseDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQ 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 405 RPRIKVGREFV--NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQIC 482
Cdd:cd14880 303 IRTIRAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLC 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 483 INYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKANDKS-FVEKLQKT 560
Cdd:cd14880 383 INYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRIESA 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 561 HNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaAEMNETAF 640
Cdd:cd14880 462 LAGNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------EEKTQEEP 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 641 GMRSRKGMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPF 720
Cdd:cd14880 536 SGQSRAPVLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSH 614
|
650
....*....|..
gi 25150354 721 QEFRHRYEILTP 732
Cdd:cd14880 615 QNFVERYKLLRR 626
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
93-770 |
5.73e-120 |
|
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: 396.63 E-value: 5.73e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHeMPPHIFAIADTAYRSM---LQE----RED 164
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDLHKYREEMPGWTA-LPPHVFSIAEGAYRSLrrrLHEpgasKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 165 QSILCTGESGAGKTENTKKVIQYLAHVagatrnkSLNAAAQQNIVQKpdvRNPIGElehQLLQANPILEAFGNSKTVKND 244
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAES-------SKHTTATSSSKRR---RAISGS---ELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 245 NSSRFGKFIRINF-----DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVN 319
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 320 RG----ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSD---------------QAMLQ 380
Cdd:cd14895 228 SGgqcyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 381 DDRVIQK---VCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDR---- 453
Cdd:cd14895 308 SLTVQQHldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 454 ------THRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDlQPTID 527
Cdd:cd14895 388 lnpnkaANKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 528 LIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNEN 605
Cdd:cd14895 467 MLEqRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 606 VVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETAFG---MRSRKGMFRTV---SQLhKEQLTKLMTTLRNTSPHFVRCII 679
Cdd:cd14895 547 LFSVLGKTSDAHLREL-----FEFFKASESAELSLGqpkLRRRSSVLSSVgigSQF-KQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 680 PNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILtpdVIPKNFIDGKESvrKMITALDIDTnl 759
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL---VAAKNASDATAS--ALIETLKVDH-- 693
|
730
....*....|.
gi 25150354 760 YRIGQSKVFFR 770
Cdd:cd14895 694 AELGKTRVFLR 704
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
92-730 |
1.05e-117 |
|
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: 390.49 E-value: 1.05e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKR-HEMPPHIFAIADTAYRSMLQEREDQSILC 169
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 170 TGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRF 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEK------------DILTSNPILEAFGNSRTTKNHNSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 250 GKFIRINFDMS-GYISGANIEFYLLEKSRVL-RQAQDERSFHIFYQILRGCSAKEKSEYLLEG-VDNYRFLVNR------ 320
Cdd:cd14906 149 GKFLKIEFRSSdGKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARddviss 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 321 ---------GITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKV 388
Cdd:cd14906 229 fksqssnknSNHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVtasLESV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 389 CHLLGLPVIELQKAFLRPRIKV-GREFVNKAQNQ-EQAEFAVEAIAKASYERLFKWLVTRINKSLDR----------THR 456
Cdd:cd14906 309 SKLLGYIESVFKQALLNRNLKAgGRGSVYCRPMEvAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 457 QGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGV 535
Cdd:cd14906 389 KNNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 536 LALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTD 615
Cdd:cd14906 468 LSLLDDECIMPKGSEQSLLEKYNKQYHNTNQYYQRTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSN 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 616 PFVAGIWKdaefagicAAEMNETAFGMRSRKGMfrTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVL 695
Cdd:cd14906 547 FLKKSLFQ--------QQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670
....*....|....*....|....*....|....*
gi 25150354 696 EQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 730
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
92-727 |
2.51e-112 |
|
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: 375.20 E-value: 2.51e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIE--------EFKGKKRHEMP--PHIFAIADTAYRSMLQ 160
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRgyaydhnsQFGDRVTSTDPrePHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 161 EREDQSILCTGESGAGKTENTKKVIQYLAHVAGATrnkslNAAAQQNIVQKPDVRNPIGELEHQLLQANPILEAFGNSKT 240
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTG-----NNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNART 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 241 VKNDNSSRFGKFIRINF-DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRG---CSAKEKSEYLL--EGVDNY 314
Cdd:cd14899 156 VRNDNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnnCVSKEQKQVLAlsGGPQSF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 315 RfLVNRGITLPNVDDVQ---EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQ--- 386
Cdd:cd14899 236 R-LLNQSLCSKRRDGVKdgvQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSstt 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 387 -------KVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRT----- 454
Cdd:cd14899 315 gafdhftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 455 ---------HRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPT 525
Cdd:cd14899 395 gadesdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRAC 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 526 IDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNK---HPKF-IVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMD 600
Cdd:cd14899 474 LELFEhRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKknsHPHFrSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKD 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 601 PLNENVVGLMQNSTDPFVAGIWKDAEFAGICAAEMNETAFGMRSRKGMFRT----VSQLHKEQLTKLMTTLRNTSPHFVR 676
Cdd:cd14899 554 SFCESAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVR 633
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 677 CIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 727
Cdd:cd14899 634 CIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
92-770 |
4.32e-101 |
|
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: 340.07 E-value: 4.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYsedlIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLahvagatrnksLNAAAQQNivqkpdvrnpigELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14937 77 ESGSGKTEASKLVIKYY-----------LSGVKEDN------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQ 331
Cdd:cd14937 134 YIKIELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 332 EFHSTINSMRIMGFADDEiSSIMRVVSAVLLLGNLEFTQ-EK--KSDQAMLQDDR--VIQKVCHLLGLPVIELQKAFLRP 406
Cdd:cd14937 214 DFGNLMISFDKMNMHDMK-DDLFLTLSGLLLLGNVEYQEiEKggKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 407 RIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYT 486
Cdd:cd14937 293 EKTIANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 487 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDlQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPK 566
Cdd:cd14937 372 NEEIHSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 567 FIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicaaemneTAFGmrsRK 646
Cdd:cd14937 451 YASTKKDINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS---------ESLG---RK 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 647 GMfrtVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRIcRQGFPNRVPFQEFRHR 726
Cdd:cd14937 519 NL---ITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 25150354 727 YEILTPDVIPKNFIDGKESVrKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14937 595 FEYLDYSTSKDSSLTDKEKV-SMILQNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
89-769 |
1.01e-98 |
|
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: 333.36 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 89 LNEASVLHNLKDRYYSSLIYTY---SGLfcVVINPYKKLPIYSEDLIEEFK-------GKKRHEMPPHIFAIADTAYRSM 158
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 159 LQEREDQSILCTGESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivqkpdvrnPIGElehQLLQANPILEAFGNS 238
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT-----------------KLSS---QISAAEFVLDSFGNA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 239 KTVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLV 318
Cdd:cd14879 139 KTLTNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 319 NRG----ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQKVCHLL 392
Cdd:cd14879 219 SYGchplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 393 GLPVIELQKAfLRPRIK-VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFE 471
Cdd:cd14879 299 GVSPEDLETS-LTYKTKlVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 472 IFD---INSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEwdfidfgLDLQPTID-------LIEKPMGVLALLDE 541
Cdd:cd14879 378 NRSstgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDnsdcvrlLRGKPGGLLGILDD 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 542 ECL-FPKANDKSFVEKLQKTHNKHPKFIV----PDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLnenvvglmqnSTDp 616
Cdd:cd14879 451 QTRrMPKKTDEQMLEALRKRFGNHSSFIAvgnfATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 617 FVAgiwkdaefagicaaemnetafgmrsrkgMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLE 696
Cdd:cd14879 520 FVN----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKA 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 697 QLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPdvipknFIDGKESVRKMITALDIDTNLYRIGQSKVFF 769
Cdd:cd14879 571 QIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
92-770 |
1.61e-96 |
|
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: 327.16 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYS---EDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSIL 168
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYStmvSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 169 CTGESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSR 248
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT----------------------FDSRFKHVNCILEAFGHAKTTLNDLSSC 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 249 FGKFIRINF-DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRGI----- 322
Cdd:cd14878 139 FIKYFELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTMredvs 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 323 TLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKA 402
Cdd:cd14878 218 TAERSLNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 403 FLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL---DRTHRQGASFIGILDIAGFEIFDINSFE 479
Cdd:cd14878 298 LTTDIQYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 480 QICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQ 558
Cdd:cd14878 378 QLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQ 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 559 ---KTHNKHPKFI--------VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAef 627
Cdd:cd14878 458 sllESSNTNAVYSpmkdgngnVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK-- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 628 agicaaemnetafgmrsrkgMFRTVSQLHKeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGI 707
Cdd:cd14878 536 --------------------LVTIASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 708 RICRQGFPNRVPFQEFRHRYEILTpDVIP--KNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLA-DTLLgeKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
92-770 |
2.05e-94 |
|
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: 323.52 E-value: 2.05e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYS--------SLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQERE 163
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 164 DQSILCTGESGAGKTENTKKVIQYLAHVAgaTRNKSLNAAAqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKN 243
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS--DRRHGADSQG----------------LEARLLQSGPVLEAFGNAHTVLN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 244 DNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRgit 323
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPESTDLRR--- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 324 lpnvddvqefhsTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ------------------------------EKK 373
Cdd:cd14887 220 ------------ITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTdqepetskkrkltsvsvgceetaadrshssEVK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 374 SDQAMLQDDRVIQK----VCHLLGLP--VIELQKAFLRPRIKVGREfVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRI 447
Cdd:cd14887 288 CLSSGLKVTEASRKhlktVARLLGLPpgVEGEEMLRLALVSRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 448 NKSLDRTHR-------------QGASFIGILDIAGFEIF---DINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREG- 510
Cdd:cd14887 367 NAGLQRSAKpsesdsdedtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGv 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 511 -IEWDFIDFGLDLQPTIDLIEKPMGVLALL-------------------------DEECLFP-----KANDKSFVEKLQK 559
Cdd:cd14887 447 fQNQDCSAFPFSFPLASTLTSSPSSTSPFSptpsfrsssafatspslpsslsslsSSLSSSPpvwegRDNSDLFYEKLNK 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 560 --THNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaEFAGICAAEMN 636
Cdd:cd14887 527 niINSAKYKNITPALsRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS-----------TYTRLVGSKKN 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 637 EtafGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPN 716
Cdd:cd14887 596 S---GVRAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPC 672
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 25150354 717 RVPFQEFRHRYEILTPDVIpKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 770
Cdd:cd14887 673 RLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
93-732 |
1.47e-91 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 310.29 E-value: 1.47e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKlpIYSEDLIEEFKGKKRHeMPPHIFAIADTAYRSMLQErEDQSILCTGE 172
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHvagatRNKSLNAaaqqnivqkpdvrnpigeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----RTASTTS------------------IEKLITAANLILEAFGNAKTQLNDNSSRFGKR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDmsGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQIlrgCSAKE---KSEYLlegvdNYRFLVNRGITLpnVDD 329
Cdd:cd14898 135 IKLKFD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQF---CASKRlniKNDFI-----DTSSTAGNKESI--VQL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMGFADdeISSIMRVVSAVLLLGNLEFTQEkksDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 409
Cdd:cd14898 203 SEKYKMTCSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVND---GILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQ 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 410 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRThrqGASFIGILDIAGFEIFDINSFEQICINYTNEK 489
Cdd:cd14898 278 VKGETIEVFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEK 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 490 LQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLqKTHNKHpkFIV 569
Cdd:cd14898 355 IQNDFIKKMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKI-KKYLNG--FIN 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 PDMRSKshFAVVHYAGRVDYSADQWLMKNMDPLNENVVGlmqnstDPFVAgiwkdaefagicaaemnetafgmrsRKGMF 649
Cdd:cd14898 431 TKARDK--IKVSHYAGDVEYDLRDFLDKNREKGQLLIFK------NLLIN-------------------------DEGSK 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 650 RTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEI 729
Cdd:cd14898 478 EDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRI 557
|
...
gi 25150354 730 LTP 732
Cdd:cd14898 558 LGI 560
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
92-722 |
1.72e-80 |
|
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: 281.41 E-value: 1.72e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHE-------MPPHIFAIADTAYRSMLQERE 163
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 164 DQSILCTGESGAGKTENTKKVIQYLAHVagatrnkslNAAAQQNivqkpdvrnpigELEHQLLQANPILEAFGNSKTVKN 243
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI---------QTDSQMT------------ERIDKLIYINNILESMSNATTIKN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 244 DNSSRFGKFIRINFD---------MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY-LLEGVDN 313
Cdd:cd14884 140 NNSSRCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRnLVRNCGV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 314 YRFLVN------RGIT--------------LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNleftqekk 373
Cdd:cd14884 220 YGLLNPdeshqkRSVKgtlrlgsdsldpseEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN-------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 374 sdqamlqddRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRIN----- 448
Cdd:cd14884 292 ---------RAYKAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlk 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 449 ----KSLDRTH--RQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDL 522
Cdd:cd14884 363 ckekDESDNEDiySINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SY 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 523 QPTIDLIEKpmgVLALLDE-----ECLFPKANDKSFV-----EKLQKTHNKHPK-FIVPDMRS---------KSHFAVVH 582
Cdd:cd14884 442 SDTLIFIAK---IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHDADgtakkqnikKNIFFIRH 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 583 YAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFvagiwkdaefagicaaeMNETAFGmrSRKGMFRTVSQLHKEQLTK 662
Cdd:cd14884 519 YAGLVTYRINNWIDKNSDKIETSIETLISCSSNRF-----------------LREANNG--GNKGNFLSVSKKYIKELDN 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 663 LMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQE 722
Cdd:cd14884 580 LFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
93-732 |
2.14e-78 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 273.53 E-value: 2.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPiysEDL-IEEFKGKKRHempPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG---NPLtLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGAtrnkslnaaaqqnivqkpdvrNPIGELEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAGG---------------------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFdMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEG--VDNYRFLVNRGITLPNVDD 329
Cdd:cd14881 135 FIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGysPANLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 330 VQEFHSTINSMRIMG--FADdeissIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRvIQKVCHLLGLPVIELQKAFLRPR 407
Cdd:cd14881 214 AARFQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLTTRT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 408 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINkSLDRTHRQGAS-----FIGILDIAGFEIFDINSFEQIC 482
Cdd:cd14881 288 HNARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 483 INYTNEKLQQLFNNTMFILEQEEYQREGIEWDF-IDFgLDLQPTIDLIEK-PMGVLALLDEECLfPKANDKSFVEKLQKT 560
Cdd:cd14881 367 INLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 561 HNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaefagiCaaemnetAF 640
Cdd:cd14881 445 HRQNPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN----------------C-------NF 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 641 GmrsrkgmFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPF 720
Cdd:cd14881 502 G-------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRF 574
|
650
....*....|..
gi 25150354 721 QEFRHRYEILTP 732
Cdd:cd14881 575 KAFNARYRLLAP 586
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-770 |
3.49e-78 |
|
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: 274.28 E-value: 3.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKgkKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAhVAGATRNKSLnaaaqqnivqkpdvrnpigelEHQLLQANPILEAFGNSKTVKNDNSSRFGK 251
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL-TTDLSRSKYL---------------------RDYILESGIILESFGHASTDSNHNSSRWGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 252 FIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDV 330
Cdd:cd14905 138 YFEMFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGsISVESIDDN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQekKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 410
Cdd:cd14905 218 RVFDRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQ--KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 411 grefVNKAQNQEqaefavEAIAKASYERLFKWLVTRINKSLDRThrQGASFIGILDIAGFEIFDINSFEQICINYTNEKL 490
Cdd:cd14905 296 ----VNEAVENR------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 491 QQLFNNTMFILEQEEYQREGIEW-DFIDFGlDLQPTIDLIEKpmgVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFiv 569
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF-- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 570 pdMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGiwKDAEF-AGICAAEMNEtafgmrsrkgM 648
Cdd:cd14905 438 --GKKPNKFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS--RDGVFnINATVAELNQ----------M 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 649 FRTVSQLHKEQLT--KLMTTLRNTSP-----------------------------------------------HFVRCII 679
Cdd:cd14905 504 FDAKNTAKKSPLSivKVLLSCGSNNPnnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 680 PNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFP----NRVPFQEFRHRYEiltpdvIPKNFIDGKESVRKmiTALDI 755
Cdd:cd14905 584 PNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRFSFFFQ------NQRNFQNLFEKLKE--NDINI 655
|
730
....*....|....*...
gi 25150354 756 DTNL---YRIGQSKVFFR 770
Cdd:cd14905 656 DSILpppIQVGNTKIFLR 673
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
93-770 |
1.48e-74 |
|
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: 262.75 E-value: 1.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 173 SGAGKTENTKKVIQYLAHVAgatrnKSLNAAAQqnivqkpdvrnpigelehQLLQANPILEAFGNSKTVKNDNSSRFGKF 252
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATG------------------RVESSIKAILALVNAGTPLNADSTRCILQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 253 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEK-SEYLLEGVDNYRFL----VNRGITLPNV 327
Cdd:cd14882 139 YQLTFGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLrippEVPPSKLKYR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 328 DD-----VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSdqAMLQDDRVIQKVCHLLGLPVIELQKA 402
Cdd:cd14882 219 RDdpegnVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 403 FLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINK--SLDRTHRQGASFIGILDIAGFEIFDINSFEQ 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMkmSFPRAVFGDKYSISIHDMFGFECFHRNRLEQ 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 481 ICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTID-LIEKPMGVLALLDEEClfPKANDKSFVekLQK 559
Cdd:cd14882 377 LMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDAS--RSCQDQNYI--MDR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 560 THNKHPKFIVPDmrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKdaefagicaaemNETA 639
Cdd:cd14882 452 IKEKHSQFVKKH--SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT------------NSQV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 640 FGMRSRKGMFRTVSQlhkEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVP 719
Cdd:cd14882 518 RNMRTLAATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIP 594
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 720 FQEFRHRYEILTPDvIPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 770
Cdd:cd14882 595 FQEFLRRYQFLAFD-FDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
92-770 |
4.32e-74 |
|
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: 260.96 E-value: 4.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFkgkkrhemppHIFAIADTAYRSMLQERED-QSILCT 170
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 171 GESGAGKTENTKKVIQYLAhvagaTRNKSLNAAAQQNIVQKpdvrnpigelehqllqanpILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT-----SQPKSKVTTKHSSAIES-------------------VFKSFGCAKTLKNDEATRFG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDmSGYISGANIEFYL-LEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGITLPNV-D 328
Cdd:cd14874 127 CSIDLLYK-RNVLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKF-FYINQGNSTENIqS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 329 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKS----DQAMLQDDRVIQKVCHLLGLPVIELQkAFL 404
Cdd:cd14874 205 DVNHFKHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPnveqDVVEIGNMSEVKWVAFLLEVDFDQLV-NFL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 405 RPRIKVGREF-VNKAQNQEqaefavEAIAKASYERLFKWLVTRINKSLDRTHRQGAsfIGILDIAGFEIFDINSFEQICI 483
Cdd:cd14874 284 LPKSEDGTTIdLNAALDNR------DSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLI 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 484 NYTNEKLQQLFNNTMFILEQEEYQREGIEWDF-IDFGLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTH 561
Cdd:cd14874 356 NSVNERIENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNH 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 562 NKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFagicaaemnetafg 641
Cdd:cd14874 436 TDRSSYGKARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSS-------------- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 642 mrSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 721
Cdd:cd14874 502 --NTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 25150354 722 EFRHRYEILTPDVIPKnFIDGKESVRKMITALDID-TNLYRIGQSKVFFR 770
Cdd:cd14874 580 TFARQYRCLLPGDIAM-CQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
95-728 |
9.08e-73 |
|
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: 259.90 E-value: 9.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 95 LHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKR----------HEMPPHIFAIADTAYRSMLQERED 164
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 165 QSILCTGESGAGKTENTKKVIQYLAHVAGAT--RNKSLNAAAqqnivqkpdVRNPIGElehQLLQANPILEAFGNSKTVK 242
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETepRPDSEGASG---------VLHPIGQ---QILHAFTILEAFGNAATRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 243 NDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGC----SAKEKSEyLLEGVDNYRFLV 318
Cdd:cd14893 152 NRNSSRFAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhdpTLRDSLE-MNKCVNEFVMLK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 319 NRGITLPNVD-DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF---------------TQEKKSDQAMLQDD 382
Cdd:cd14893 231 QADPLATNFAlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 383 RVIQKVCHLLGLPVIELQKAFLRprikvgREFVNKAQNQ----------EQAEFAVEAIAKASYERLFKWLVTRINKSL- 451
Cdd:cd14893 311 AQILLAAKLLEVEPVVLDNYFRT------RQFFSKDGNKtvsslkvvtvHQARKARDTFVRSLYESLFNFLVETLNGILg 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 452 ---DRTHRQG----ASFIGILDIAGFEIFD--INSFEQICINYTNEKLQQLF-NNTMFI----LEQEEYQREGIEWD--F 515
Cdd:cd14893 385 gifDRYEKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENRLTVnsN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 516 IDFGLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKSH-------------FAVV 581
Cdd:cd14893 465 VDITSEQEKCLQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTneylapskdwrllFIVQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 582 HYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKdAEFAGICAAEMNETAFGMRSRKGMFRTVSQLHKE--- 658
Cdd:cd14893 545 HHCGKVTYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGA-AQMAAASSEKAAKQTEERGSTSSKFRKSASSAREskn 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 659 -----------QLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 727
Cdd:cd14893 624 itdsaatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
.
gi 25150354 728 E 728
Cdd:cd14893 704 K 704
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-768 |
1.56e-65 |
|
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: 237.81 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK-GKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKPDVRNPI-GELEHQLLQANPILEAFGNSKTVKNDNSSRFG 250
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNIHNEENTDYqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 251 KFIRINFDmSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDV 330
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 331 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ---------------------------EKKSDQAMLQDDR 383
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKafrkksllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 384 VIQKVCHLLGLPVIELQKAFLRPRIkVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHR--QGASF 461
Cdd:cd14938 321 NLLLACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 462 IGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTID-LIEKPMGVLALLD 540
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 541 EECLFPKANDKSFVEKL-QKTHNKHPKFIVPD--MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPF 617
Cdd:cd14938 480 ENVSTKTIFDKSNLHSSiIRKFSRNSKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEY 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 618 VAGI--WKDAEFAGICAAEMN----ETAFGMRSRKgmFRTVSQ----LHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKS- 686
Cdd:cd14938 560 MRQFcmFYNYDNSGNIVEEKRrysiQSALKLFKRR--YDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 687 GKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVipknfidgKESVRKMITALDIDTNLYRIGQSK 766
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNEDL--------KEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 25150354 767 VF 768
Cdd:cd14938 710 IF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
114-262 |
1.28e-55 |
|
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: 191.40 E-value: 1.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 114 FCVVINPYKKLPIYSEDLIEEF-KGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAHVA 192
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFyRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 193 GATRNKSLNAAAQQNIVQKpdvrnpiGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGY 262
Cdd:cd01363 81 FNGINKGETEGWVYLTEIT-------VTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
98-711 |
1.36e-28 |
|
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: 125.24 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 98 LKDRYYSSLIYTYSGLFCV-VINPYKKL------PIYSEDLIEEFKGKKRHE--MPPHIFAIAD---------------- 152
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 153 ----TAYRSMLQEReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------GATRN---KSLNAAAQQNIVQ 210
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsGSTRQpkiKLFTSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 211 KPDVRNPIGELEHQ------------------------------------------------------------------ 224
Cdd:cd14894 166 RTEEARTIALLEAKgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledeeqlrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 225 ---LLQANPILEAFGNSKTVKNDNSSRFGKF--IRINFDMSGY---ISGANIEFYLLEKSRVLRQA------QDERSFHI 290
Cdd:cd14894 246 lsiVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 291 FYQILRGCSAKE-----KSEYLLEGVD--NYRFLVNRGITLPNV--------DDVQEFHSTINSMRIMGFADDEISSIMR 355
Cdd:cd14894 326 LYAMVAGVNAFPfmrllAKELHLDGIDcsALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 356 VVSAVLLLGNLEFTQEKKSDQAMLQDDRVI---QKVCHLLGLPVIELQKAFLRPR---IKVGREFVNKAQNQEQAEFAVE 429
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTGALnapQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 430 AIAKASYERLFKWLVTRINK-------SLDRTHRQ---------GASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 493
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAR 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 494 FNNTMFILEQEEYQREGIEWDfidfgldlQPTIDLIEKPMGVLALLDEECLFPKAND----------KSFVEKLQKTHNK 563
Cdd:cd14894 566 EEQVIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNSS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 564 H----PKFI------VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENV-VGLMQNSTDPFVAGIWKDAEFAgiCA 632
Cdd:cd14894 638 RlpepPRVLsnakrhTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLlVGLKTSNSSHFCRMLNESSQLG--WS 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 633 AEMNETAFG-MRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICR 711
Cdd:cd14894 716 PNTNRSMLGsAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
864-1693 |
2.78e-26 |
|
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: 118.24 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 864 KERLLKMEHDfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLqtRNQELEYIVNDMRDRLSEEEQQNEKNNDE 943
Cdd:TIGR02168 175 KETERKLERT-RENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 944 RRKQMETVRDLeeqleqeeqarQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEkrlleekVEGLTTQLLDHEERAKH 1023
Cdd:TIGR02168 252 EEELEELTAEL-----------QELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1024 GVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESA 1103
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1104 NVTLMQKQMRDMQTTIDELREdmETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIE 1183
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1184 QIQHTMEGKIEEQKAKFSRQ--VEELHDQIEQHKKQRSQLEKQQNQ--------ADQERADMAQEIALLQASRADIDKKR 1253
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLdsLERLQENLEGFSEGVKALLKNQSGlsgilgvlSELISVDEGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1254 KIHEAHLMEIQANLAESDEHKRTLIdqlersrdELDHLNRVREEEEHAFanmqrRLATAEGQIQELNEQIQEETRLKIAN 1333
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFL--------PLDSIKGTEIQGNDRE-----ILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1334 INRARQL---EDEKNALLDEKEEAEGLR-AHLEKEIHAARqgaGEARRKAEESVNQQLEelRKKNLRDVEHLQKQLEESE 1409
Cdd:TIGR02168 619 SYLLGGVlvvDDLDNALELAKKLRPGYRiVTLDGDLVRPG---GVITGGSAKTNSSILE--RRREIEELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1410 VAKERILQSKKKIQQELEDssmELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEV 1489
Cdd:TIGR02168 694 AELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1490 DIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNlqiAEDARLRLEVTNQAL 1569
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1570 KSESDRAISNKDV---------EAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEY 1640
Cdd:TIGR02168 848 EELSEDIESLAAEieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1641 NKQLKK--------NQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREAN 1693
Cdd:TIGR02168 928 ELRLEGlevridnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1119-1696 |
1.54e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1119 IDELREDMETERNARNKAEmTRREVVAQLEKVKGDV-LDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQK 1197
Cdd:COG1196 195 LGELERQLEPLERQAEKAE-RYRELKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1198 AKFSR---QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHK 1274
Cdd:COG1196 274 LELEElelELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1275 RTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEA 1354
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1355 EGLRAHLEKEIHAARQGAGEARRKAEesvnqQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1434
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEE-----ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1435 NVRASHRDSEKRqkkfesqmaeeRVAVQKALLDRDAMSQELRDRETRVLSLLNEVdimkehlEESDRVRRSLQQELQDSI 1514
Cdd:COG1196 509 GVKAALLLAGLR-----------GLAGAVAVLIGVEAAYEAALEAALAAALQNIV-------VEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1515 SNKDDFgknvheLEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKR-RGLLK 1593
Cdd:COG1196 571 AGRATF------LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRaVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1594 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLR 1673
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580
....*....|....*....|...
gi 25150354 1674 EADRKFRAVEAEREQLREANEGL 1696
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEEL 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
977-1911 |
2.52e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.15 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 977 QRLRNLEERLVELQDaydkLLKEkrlLEEKVEGLTTQlldheerAKHGVKAKgRLENQLHELEQDL--NRERQYKSELEQ 1054
Cdd:TIGR02168 179 RKLERTRENLDRLED----ILNE---LERQLKSLERQ-------AEKAERYK-ELKAELRELELALlvLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1055 hKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVtlmQKQMRDMQTTIDELREDMETERNARN 1134
Cdd:TIGR02168 244 -LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL---ANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1135 KAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVnATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQH 1214
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1215 KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkiHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRV 1294
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1295 REEEEHAFANMQRRLATaegqIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKeihAARQGAGE 1374
Cdd:TIGR02168 477 LDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA---ALGGRLQA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1375 ARRKAEESVNQQLEELRKKNLRDVEHLqkqleesevakERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM 1454
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTFL-----------PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1455 AE--ERVAVQKALLDRDAMSQELRdRETRVLSLlnevdimkehleESDRVRRSlqqelqDSISNKDDFGKNVhELEKakr 1532
Cdd:TIGR02168 619 SYllGGVLVVDDLDNALELAKKLR-PGYRIVTL------------DGDLVRPG------GVITGGSAKTNSS-ILER--- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1533 slEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDvEAEEKRRGLLKQIRDLENELENEKRGKSGA 1612
Cdd:TIGR02168 676 --RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1613 VSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREA 1692
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1693 NEGLMQARKQlelendeleelrakgggiSSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERT 1772
Cdd:TIGR02168 833 IAATERRLED------------------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1773 LNQKTEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYLEDQLNVEGQekTAANRAARRLEKRLNDTTQQF 1852
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELRE-KLAQLELRLEGLEVRIDNLQERLSEEYS--LTLEEAEALENKIEDDEEEAR 971
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150354 1853 EDEKRANEQAKELleksnlKNRNLrrqldEAEDEMSRERTKHRNVQREADDLLDANEQL 1911
Cdd:TIGR02168 972 RRLKRLENKIKEL------GPVNL-----AAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1100-1884 |
1.46e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.46 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1100 EESANVTLMQKQMRDMQTTIDELREDM--------ETERNARN---KAEMTRR--EVVAQLEKVKGDVLdkVDEATMLQD 1166
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLdrledilnELERQLKSlerQAEKAERykELKAELRELELALL--VLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1167 LMSRKDEEVNATKRAIEQIQhtmegkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR 1246
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1247 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEE 1326
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1327 TRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAeesVNQQLEELRKknlrDVEHLQKQLE 1406
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELEELEE----ELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1407 ESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALL-----------------DRD 1469
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1470 AMSQELRDRETRVL-----SLLNEVDIMKEH-------LEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE 1537
Cdd:TIGR02168 538 AIEAALGGRLQAVVvenlnAAKKAIAFLKQNelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1538 LNDM--RVQM-EELED--NLQIAEDARLRLeVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELEnekrgksga 1612
Cdd:TIGR02168 618 LSYLlgGVLVvDDLDNalELAKKLRPGYRI-VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE--------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1613 vshrkKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI-------IKEYQIECEEARQAKEDIAALLREADRKFRAVEAE 1685
Cdd:TIGR02168 688 -----ELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1686 REQLREANEGLmqarkqlelendeleelrakgggisSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITT 1765
Cdd:TIGR02168 763 IEELEERLEEA-------------------------EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1766 DLSMERTLNQKTEAEKQSLERSNRDYKAKITELeSGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRL 1845
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
810 820 830
....*....|....*....|....*....|....*....
gi 25150354 1846 NDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAE 1884
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1702 |
1.38e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 109.39 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIrAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDirgrLQTRNQELEYIVndmrdrL 930
Cdd:TIGR02169 160 DEI-AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA----LLKEKREYEGYE------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 931 SEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvDQRLRNLEERLVELQDaydkllKEKRLLEEKVEGL 1010
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI---EQLLEELNKKIKDLGE------EEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1011 TTQLldheERAKHGVKAKGRlenqlhELEQDLNRERQYKSELEqhkrKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1090
Cdd:TIGR02169 300 EAEI----ASLERSIAEKER------ELEDAEERLAKLEAEID----KLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1091 LQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSR 1170
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1171 KDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR---- 1246
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLS-KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1247 ---ADIDKKRKIHEAHL-----MEIQANLAESDEHKRTLIDQLER---SRDELDHLNRVREEE----------------- 1298
Cdd:TIGR02169 525 gtvAQLGSVGERYATAIevaagNRLNNVVVEDDAVAKEAIELLKRrkaGRATFLPLNKMRDERrdlsilsedgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1299 --------EHAFANMQR------------------RLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKE 1352
Cdd:TIGR02169 605 lvefdpkyEPAFKYVFGdtlvvedieaarrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1353 EAEGLRAHLEKEIHAARQGAGEARRKAEESvNQQLEELRKKnlrdvehLQKQLEESEVAKERILQSKKKIQQeledSSME 1432
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSS----LEQE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1433 LENVRASHRDSEKRQKKFESQMAEERVAVQKaLLDRDAMSQ-------------ELRDRETRVLSL---LNEVDIMKEHL 1496
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaelskleeEVSRIEARLREIeqkLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1497 EESdrvRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELednlqiaedarlrlevtnqalksesdra 1576
Cdd:TIGR02169 832 EKE---IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL---------------------------- 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1577 isnkdveaEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI------ 1650
Cdd:TIGR02169 881 --------ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeels 952
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1651 ---IKEYQIECEEARQAKEDIAALlreADRKFRAVEAEREQLREANEGLMQARKQ 1702
Cdd:TIGR02169 953 ledVQAELQRVEEEIRALEPVNML---AIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
968-1642 |
2.14e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 968 LLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQ 1047
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1048 YKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME 1127
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1128 TERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQkakfsrqvEEL 1207
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--------EAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1208 HDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQAsradidkkrkiheahlMEIQANLAESDEHKRTLIDQLERSRDE 1287
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLE----------------AEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1288 LDHLNRVREEEEHAFANmqrRLATAEGQIQELNEQIQEETR--LKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEI 1365
Cdd:COG1196 526 VAVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVAAAAIeyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1366 HAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEnvrASHRDSEK 1445
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL---AALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1446 RQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrVRRSLQQELQDSISNKDDFGKNVH 1525
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA---EREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1526 ELEKAKRSLEAELNDMRVQMEELED-NLQIAEDARlrlevtnqalksesdraisnkdvEAEEKRRGLLKQIRDLENElen 1604
Cdd:COG1196 757 PEPPDLEELERELERLEREIEALGPvNLLAIEEYE-----------------------ELEERYDFLSEQREDLEEA--- 810
|
650 660 670
....*....|....*....|....*....|....*...
gi 25150354 1605 ekrgksgavshRKKIENQIGELEQqlEVANRLKEEYNK 1642
Cdd:COG1196 811 -----------RETLEEAIEEIDR--ETRERFLETFDA 835
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1205-1846 |
2.43e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.49 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1205 EELHDQIEQHKKQRSQLEKQQNQAdQERADMAQEIALLQASRAdidkkrkihEAHLMEIQANLAESDEHKRTLIDQLERS 1284
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEKA-ERYRELKEELKELEAELL---------LLKLRELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1285 RDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKE 1364
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1365 IHAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDSE 1444
Cdd:COG1196 339 LEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA----QLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1445 KRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDsisnkddfgknv 1524
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE------------ 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1525 helekAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLkQIRDLENELEN 1604
Cdd:COG1196 482 -----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL-AAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1605 EKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLkknqqiikeyqieceEARQAKEDIAALLREADRKFRAVEA 1684
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG---------------AIGAAVDLVASDLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1685 EREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQIT 1764
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1765 TDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEktaanRAARRLEKR 1844
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE-----RELERLERE 775
|
..
gi 25150354 1845 LN 1846
Cdd:COG1196 776 IE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
844-1548 |
1.60e-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: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 844 LQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIV 923
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 924 NDMRDRLSEEE---QQNEKNNDERRKQMETVRDleeqleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEK 1000
Cdd:TIGR02168 354 ESLEAELEELEaelEELESRLEELEEQLETLRS----------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1001 RLLEEKVEglTTQLLDHEERAkhgvkakGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEEL 1080
Cdd:TIGR02168 424 EELLKKLE--EAELKELQAEL-------EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1081 nnqlmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRRE--VVAQLEKVKGDV--LD 1156
Cdd:TIGR02168 495 --------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAAKKAIafLK 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1157 KVDE--ATMLQdLMSRKDEEVNATKRAIEQIQHTMEG---KIEEQKAKFSRQVEEL------HDQIEQHKKQRSQLEKQQ 1225
Cdd:TIGR02168 567 QNELgrVTFLP-LDSIKGTEIQGNDREILKNIEGFLGvakDLVKFDPKLRKALSYLlggvlvVDDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1226 N----QADQERAD--MAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEE 1299
Cdd:TIGR02168 646 RivtlDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1300 HAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhAARQGAGEARRKA 1379
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREA 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1380 EESVNQQLEELRK---KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAE 1456
Cdd:TIGR02168 805 LDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1457 ERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQE---LQDSISNK-----DDFGKNVHELE 1528
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnLQERLSEEysltlEEAEALENKIE 964
|
730 740
....*....|....*....|
gi 25150354 1529 KAKRSLEAELNDMRVQMEEL 1548
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1056-1734 |
6.08e-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: 6.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1056 KRKLLAELEDSKDHLAEKMGKVEELNNQL--MKRD-------EELQHQLTRYDeesanVTLMQKQMRDMQTTIDELREDM 1126
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLepLERQaekaeryRELKEELKELE-----AELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1127 ETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNatkRAIEQIQHTMEGKIEEQkakfsRQVEE 1206
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA---RLEQDIARLEERRRELE-----ERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1207 LHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRD 1286
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1287 ELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIH 1366
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1367 AARQGagEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKR 1446
Cdd:COG1196 481 ELLEE--LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1447 QKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHE 1526
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1527 LEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDvEAEEKRRGLLKQIRDLENELENEK 1606
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL-ELEEALLAEEEEERELAEAEEERL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1607 RGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQiecEEARQAKEDIAAL----LReADRKFRAV 1682
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---RELERLEREIEALgpvnLL-AIEEYEEL 793
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1683 EAEREQLREANEGLMQARKQlelendeleelrakgggisseekrrLEAKIAQ 1734
Cdd:COG1196 794 EERYDFLSEQREDLEEARET-------------------------LEEAIEE 820
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1000-1918 |
1.33e-20 |
|
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: 99.81 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1000 KRLLEE---KVEGLTTQLLD----HEERAKHGVKAKGRLENQLHELEQDLN-------RERQYKSELEQHKRKLLAELED 1065
Cdd:pfam15921 77 ERVLEEyshQVKDLQRRLNEsnelHEKQKFYLRQSVIDLQTKLQEMQMERDamadirrRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1066 SK----DHLAEKMGKVEELNNQLMKRD---EELQHQLTRYDEESANVTLMQKQMRDMQTtidelredmeteRNARNKAEM 1138
Cdd:pfam15921 157 AKclkeDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHF------------RSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1139 TRREVVAQLEKVKGDVLDKVDEatmlqdLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQR 1218
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQ------LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1219 SQLEKQQNQADQERADMAQEIALLQAS----RADIDKKRKIHEAHLMEIQANLAESDEhkrtlidQLERSRDELDHLNrv 1294
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTvsqlRSELREAKRMYEDKIEELEKQLVLANS-------ELTEARTERDQFS-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1295 rEEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLeKEIHAARQGAGE 1374
Cdd:pfam15921 370 -QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1375 ARRKAEESVNQQLEElrkknlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM 1454
Cdd:pfam15921 448 RQMAAIQGKNESLEK--------VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1455 AEERVAVQKALLDRdamsQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSL 1534
Cdd:pfam15921 520 TKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1535 EAELNDMRVQMEELEdNLQIAEDARLR-LEVTNQALKSEsdraiSNKDVEAEEKRRGLLKQIRDLENELENEKrgksgav 1613
Cdd:pfam15921 596 EKEINDRRLELQEFK-ILKDKKDAKIReLEARVSDLELE-----KVKLVNAGSERLRAVKDIKQERDQLLNEV------- 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1614 shrKKIENQIGELEQQLEVANR----LKEEYNKQLKKNQQIIKEYQIECEEAR-----------QAKEDIAALLREADRK 1678
Cdd:pfam15921 663 ---KTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQTRntlksmegsdgHAMKVAMGMQKQITAK 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1679 FRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKR---RLEAKIAQLEEELEEEqSNCELAIDK--- 1752
Cdd:pfam15921 740 RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKmagELEVLRSQERRLKEKV-ANMEVALDKasl 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1753 -----QRKAQVQlEQITTDLSMERTLNQKtEAEKQSLErSNRDYKAKIteLESGAQSRARAQMAALEAKVQYLEDQlnve 1827
Cdd:pfam15921 819 qfaecQDIIQRQ-EQESVRLKLQHTLDVK-ELQGPGYT-SNSSMKPRL--LQPASFTRTHSNVPSSQSTASFLSHH---- 889
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1828 gqektaaNRAARRLEKRLNDTTQQFEDEKRA--NEQAKELLEKSNLKNR--NLRRQLDEAEDEMSRERTKHRNVQREADD 1903
Cdd:pfam15921 890 -------SRKTNALKEDPTRDLKQLLQELRSviNEEPTVQLSKAEDKGRapSLGALDDRVRDCIIESSLRSDICHSSSNS 962
|
970
....*....|....*....
gi 25150354 1904 L----LDANEQLTRELMNL 1918
Cdd:pfam15921 963 LqtegSKSSETCSREPVLL 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
943-1694 |
1.71e-19 |
|
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: 95.91 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 943 ERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQ---RLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLdhee 1019
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELL---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1020 rakhgvKAKGRLENQLHELEQDLnrerqykSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYD 1099
Cdd:TIGR02169 230 ------KEKEALERQKEAIERQL-------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1100 EEsanvtlMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATK 1179
Cdd:TIGR02169 297 GE------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1180 RAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAH 1259
Cdd:TIGR02169 371 AELEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1260 LMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVRE--EEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIanINRA 1337
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSklQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1338 RQLEDEKNALLDEKEEAEGLRAH---LEKEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQ---------- 1404
Cdd:TIGR02169 528 AQLGSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDE-RRDLSILSEDgvigfavdlv 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1405 ------------------LEESEVAKERILQSKKKIQQE---LEDS-SMELENVRASHRDSEKRQKKFESQMAEERVAVQ 1462
Cdd:TIGR02169 607 efdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelFEKSgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1463 KALLDRdaMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMR 1542
Cdd:TIGR02169 687 KRELSS--LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1543 VQMEELEDNLQIAEDARLRLEvtnQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQ 1622
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1623 IGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANE 1694
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
824-1415 |
4.27e-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: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 824 AYLKLRNWQWWRLftkvkpllQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSA 903
Cdd:COG1196 227 AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 904 ELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLE 983
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 984 ERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAEL 1063
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1064 EDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYdeesanvtLMQKQMRdmqttiDELREDMETERNARNKAEMTRREV 1143
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARL--------LLLLEAE------ADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1144 VAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEqiqhtmegkiEEQKAKFSRQVEELHDQIEQHKKQrsqlek 1223
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----------YLKAAKAGRATFLPLDKIRARAAL------ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1224 qqnQADQERADMAQEIALLQASRADIDKKRKIHEAHLME---IQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEH 1300
Cdd:COG1196 589 ---AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1301 AFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKAE 1380
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL-LEELLEE 744
|
570 580 590
....*....|....*....|....*....|....*
gi 25150354 1381 ESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERI 1415
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
848-1621 |
6.57e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 94.44 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 848 RTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMR 927
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 928 DRLSEEEQqnEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKrlleekv 1007
Cdd:PTZ00121 1268 RQAAIKAE--EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA------- 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1008 eglttqlldhEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKllaelEDSKDHLAEKMGKVEELNNQlMKR 1087
Cdd:PTZ00121 1339 ----------EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-----ADAAKKKAEEKKKADEAKKK-AEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1088 DEELQHQLTRYDEESANVTLMQKQMRDMQTTiDELREDMETERNA---RNKAEMTRREVVAQL---EKVKGDVLDKVDEA 1161
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKA-DEAKKKAEEAKKAdeaKKKAEEAKKAEEAKKkaeEAKKADEAKKKAEE 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1162 TMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERAdmAQEIAL 1241
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK--AEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1242 LQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNE 1321
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1322 QIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHL 1401
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKA 1718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1402 QKQLEESEVAKERILQSKKKIQQE---LEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDR 1478
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1479 ETRVLsLLNEVDIMKEHLEESDRVRRSlqQELQDSISNKDDFGKNVhELEKAKRSLEAELNDMRVQMEELEDNLQIAEDA 1558
Cdd:PTZ00121 1799 KIKDI-FDNFANIIEGGKEGNLVINDS--KEMEDSAIKEVADSKNM-QLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1559 RLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRD-LENELENEKRGKSGAVSHRKKIEN 1621
Cdd:PTZ00121 1875 DLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDiIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
984-1795 |
1.25e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 984 ERLVELQDAyDKLLKEKRLLEEKVEGlttqllDHEERA--KHGVKAKGRLENQLHELEQDlNRERQYKSELEQHKRKLLA 1061
Cdd:PTZ00121 1030 EELTEYGNN-DDVLKEKDIIDEDIDG------NHEGKAeaKAHVGQDEGLKPSYKDFDFD-AKEDNRADEATEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1062 ELEDSKDHLAEKMGKVEELnnqlMKRDEELQH-QLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTR 1140
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEA----KKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1141 REVVAQLEKV-KGDVLDKVDEATMLQDlmSRKDEEVnatkRAIEQIQHTMEgkieEQKAKFSRQVEELHDQIEQHKKQRS 1219
Cdd:PTZ00121 1178 AEAARKAEEVrKAEELRKAEDARKAEA--ARKAEEE----RKAEEARKAED----AKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1220 QLEKQQNQADQErADMAQEIALLQASRADidKKRKIHEAHLMEiqaNLAESDEHKRTlidQLERSRDELdhlnRVREEEE 1299
Cdd:PTZ00121 1248 ERNNEEIRKFEE-ARMAHFARRQAAIKAE--EARKADELKKAE---EKKKADEAKKA---EEKKKADEA----KKKAEEA 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1300 HAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKA 1379
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA-EEKKKA 1393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1380 EEsVNQQLEELRKKnlrdVEHLQKQLEESEVAKEriLQSKKKIQQELEDSSMELENVRAShrdSEKRQKKFESQMAEErv 1459
Cdd:PTZ00121 1394 DE-AKKKAEEDKKK----ADELKKAAAAKKKADE--AKKKAEEKKKADEAKKKAEEAKKA---DEAKKKAEEAKKAEE-- 1461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1460 AVQKALLDRDAMSQELRDRETRvlsllnEVDIMKEHLEE----SDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLE 1535
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK------KADEAKKKAEEakkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1536 AElNDMRVQMEELEDNLQIAEDARLRLEV--TNQALKSESDRAISNKDVE----AEEKRRGLLKQIRDLENELENEKRGK 1609
Cdd:PTZ00121 1536 AD-EAKKAEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1610 sgAVSHRKKIEnQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYqiecEEARQAKEDIAALLREADRKFRAVEAEREQL 1689
Cdd:PTZ00121 1615 --AEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1690 REANEGLM----QARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNcELAIDKQRKAQVQLEQITT 1765
Cdd:PTZ00121 1688 KKAAEALKkeaeEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEE 1766
|
810 820 830
....*....|....*....|....*....|
gi 25150354 1766 DLSMERTLNQKTEAEKQSLERSNRDYKAKI 1795
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1280-1919 |
2.64e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1280 QLERSRDELDHLNRVREEeehafanMQRRLATAEGQ------IQELNEQIQEetRLKIANINRARQLEDEKNALLDEKEE 1353
Cdd:COG1196 180 KLEATEENLERLEDILGE-------LERQLEPLERQaekaerYRELKEELKE--LEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1354 AEGLRAHLEKEIhaarqgagEARRKAEESVNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1433
Cdd:COG1196 251 LEAELEELEAEL--------AELEAELEELRLELEELELE----LEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1434 ENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEvdimkehLEESDRVRRSLQQELQDS 1513
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-------LAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1514 ISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISnKDVEAEEKRRGLLK 1593
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1594 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynkqlkknqqiikeyqieceEARQAKEDIAALLR 1673
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------------------AGLRGLAGAVAVLI 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1674 EADRKFRAVEAEREQLREANEGL--MQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAID 1751
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1752 KQRKAQVQLEQIttdlsMERTLNQKTEAEKQSLERSnRDYKAKITELESGAQSRARAQMAALEAKvqyLEDQLNVEGQEK 1831
Cdd:COG1196 611 ADARYYVLGDTL-----LGRTLVAARLEAALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1832 TAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDAN--- 1908
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppd 761
|
650
....*....|..
gi 25150354 1909 -EQLTRELMNLR 1919
Cdd:COG1196 762 lEELERELERLE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1050-1875 |
1.84e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 89.36 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1050 SELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQL-----------TRYDEESANVTLMQKQMRDMQTT 1118
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkekreYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1119 IDELREDME------TERNAR-NKAEMTRREVVAQLEKVKGDvldkvdEATMLQDLMSRKDEEVNATKRAIEQIQHTME- 1190
Cdd:TIGR02169 246 LASLEEELEklteeiSELEKRlEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEd 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1191 -----GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEkqqnqadQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQA 1265
Cdd:TIGR02169 320 aeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1266 NLAEsdehkrtLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINR-----ARQL 1340
Cdd:TIGR02169 393 KLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-EDKALEIKKQEWkleqlAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1341 EDEKNALLDEKEEAEglraHLEKEIHAARQ--GAGEARRKA---EESVNQQLEELRKKNLRDVEHLQKQL---------- 1405
Cdd:TIGR02169 465 SKYEQELYDLKEEYD----RVEKELSKLQRelAEAEAQARAseeRVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1406 --------------EESEVAKERILQSKKKIQQELedSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALldRDAM 1471
Cdd:TIGR02169 541 ievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRA--TFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY--EPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1472 SQELRDRetrvlSLLNEVDIMKEHLEESDRVrrSLQQELQD---SISNKDDFGKNvheLEKAKRSLEAELNDMRVQMEEL 1548
Cdd:TIGR02169 617 KYVFGDT-----LVVEDIEAARRLMGKYRMV--TLEGELFEksgAMTGGSRAPRG---GILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1549 EDNLQIAEDARLRLEVTNQALKSESDRA------ISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQ 1622
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDAsrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1623 IGELEqqlEVANRLKEEYNK-QLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARK 1701
Cdd:TIGR02169 767 IEELE---EDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1702 ----QLELENDELEELRAKGGGISSEEKrRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKT 1777
Cdd:TIGR02169 844 dlkeQIKSIEKEIENLNGKKEELEEELE-ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1778 EAEKQSLERSNRDYKAKITELESgaQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKR 1857
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
890
....*....|....*...
gi 25150354 1858 ANEQAKELLEKSNLKNRN 1875
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1014-1640 |
5.25e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1014 LLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRklLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQH 1093
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1094 QLTRYDEEsanvtlmQKQMRDMQTTIDELREDM---ETERNARNKAEMTRREVVAQLEKVKGDVLDKVDeatmlqdlMSR 1170
Cdd:PRK02224 242 VLEEHEER-------REELETLEAEIEDLRETIaetEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1171 KDEEVnatkraieqiqhtmegkIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADID 1250
Cdd:PRK02224 307 ADAEA-----------------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1251 KKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLK 1330
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1331 IANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhaarqgagEARRKAEESVNQQLEELrkknlrdvehlqKQLEESEV 1410
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVETIEEDRERVEELEAEL--------EDLEEEVEEVEERLERA------------EDLVEAED 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1411 AKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLlnevd 1490
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL----- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1491 imKEHLEESDRVRRSLQ--QELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIaEDARLRLEVTNQA 1568
Cdd:PRK02224 585 --KERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI-EEAREDKERAEEY 661
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1569 LKSesdraISNKDVEAEEKRRGLLKQIRDLENELENEKRGKsgavSHRKKIENQIGELEQQLEVANRLKEEY 1640
Cdd:PRK02224 662 LEQ-----VEEKLDELREERDDLQAEIGAVENELEELEELR----ERREALENRVEALEALYDEAEELESMY 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
966-1535 |
6.28e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 966 QKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKakgrLENQLHELEQDLNRE 1045
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1046 RQYKSELEQHKRKLLAELEDskdhLAEKMGKVEELnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRED 1125
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEE----LEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1126 METERNARNKAEMTRREVVAQLEKVKGDVLdKVDEATMLQDLMSR-----KDEEVNATKRAIEQIQHTMEgKIEEQKAKF 1200
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERlkkrlTGLTPEKLEKELEELEKAKE-EIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1201 SRQVEELHDQIEQHKKQRSQLEKQQNQ--------ADQERADMAQ----EIALLQASRADIDKKRKIHEAHLMEIQANLA 1268
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEeytaELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1269 ESDE--HKRTLIDQLERSRDELDHLNRVR-EEEEHAFANMQRRLATAEGQIQELNEQiqeetrlkianINRARQLEDEKN 1345
Cdd:PRK03918 491 KESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE-----------LEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1346 ALLDEKEEAEGLRAHLEKEIhaarqgaGEARRKAEESVNQQLEELRKKNLRDVEhlqkqLEESEVAKERILQSKKKIQQE 1425
Cdd:PRK03918 560 ELEKKLDELEEELAELLKEL-------EELGFESVEELEERLKELEPFYNEYLE-----LKDAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1426 LEDSSMELENVRASHRDSEKRQKKFESQMAEErvavqkalldrdamsqELRDRETRVLSLLNEVDIMKEHLEESDRVRRS 1505
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEE----------------EYEELREEYLELSRELAGLRAELEELEKRREE 691
|
570 580 590
....*....|....*....|....*....|
gi 25150354 1506 LQQELQDSISNKDDFGKNVHELEKAKRSLE 1535
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1280-1919 |
7.40e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.42 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1280 QLERSRDELDHLNRVREEEEHAFANMQRRLATAEgQIQELNEQIqEETRLKIAnINRARQLEDEKNALLDEKEEAEGLRA 1359
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAEL-RELELALL-VLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1360 HLEKEIHAArqgagearrkaeesvNQQLEELRKKNL---RDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEnv 1436
Cdd:TIGR02168 257 ELTAELQEL---------------EEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1437 RASHRDSEKRQKKFESQMAEERVAVQKALLdrdamsqelrdrETRVLSLLNEVDIMKEHLEESDRVRRSLQQELqdsisn 1516
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESRLEELEEQL------ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1517 kDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL------------------------------QIAEDARLRLEVTN 1566
Cdd:TIGR02168 382 -ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieellkkleeaelkelqaeleeleEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1567 QALKSESDR--AISNKDVEAEEK---RRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYN 1641
Cdd:TIGR02168 461 EALEELREEleEAEQALDAAERElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1642 KQLKKNQQiikeyQIECEEARQAKEDIAALLREA-------------DRKFRAVEAER---------------------- 1686
Cdd:TIGR02168 541 AALGGRLQ-----AVVVENLNAAKKAIAFLKQNElgrvtflpldsikGTEIQGNDREIlkniegflgvakdlvkfdpklr 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1687 -------------EQLREANEglMQARKQLELENDELEELRAKGGGISS---------------------EEKRRLEAKI 1732
Cdd:TIGR02168 616 kalsyllggvlvvDDLDNALE--LAKKLRPGYRIVTLDGDLVRPGGVITggsaktnssilerrreieeleEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1733 AQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELE------------- 1799
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeieeleerleea 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1800 SGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQ 1879
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 25150354 1880 LDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLR 1919
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
888-1231 |
4.99e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 81.26 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 888 RAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIV---NDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQA 964
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 965 RQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNR 1044
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1045 ERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRE 1124
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1125 DMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRK-DEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQ 1203
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEaRRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
|
330 340
....*....|....*....|....*...
gi 25150354 1204 vEELHDQIEQHKKQRSQLEKQQNQADQE 1231
Cdd:TIGR02168 1003 -DFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1549 |
1.68e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 79.73 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQviVERAVIQEQLQQES--ENSAELDDIRGRLQTRNQELEYI 922
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE--LEREIEEERKRRDKltEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 923 VNDMRDRLSEEEQQNEKNNDERRkqmETVRDLEEQLEQEEQARQKLLldktNVDQRLRNLEERLVELQDAYDKLLKEKRL 1002
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREIN---ELKRELDRLQEELQRLSEELA----DLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1003 LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNR---ERQYKSELEQHKRKLLAELEDSKD---HLAEKMGK 1076
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeaQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGS 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1077 VEE-------------LNNQLMKRDEELQH--QLTRYDEESANVTLMQKQMRDMQTTIDELRED---------METERNA 1132
Cdd:TIGR02169 533 VGEryataievaagnrLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlVEFDPKY 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1133 RNKAEMTRRE--VVAQLEKVKgDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQkaKFSRQVEELHDQ 1210
Cdd:TIGR02169 613 EPAFKYVFGDtlVVEDIEAAR-RLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ--RLRERLEGLKRE 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1211 IEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDH 1290
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1291 LNRVREEEEHAFANMQRRLatAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAArq 1370
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-- 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1371 gagEARRKAEEsvnQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKF 1450
Cdd:TIGR02169 846 ---KEQIKSIE---KEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1451 ESQMAEERVAVQkALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKA 1530
Cdd:TIGR02169 916 RKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
730
....*....|....*....
gi 25150354 1531 KRSLEAELNDMRVQMEELE 1549
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYE 1013
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1113-1702 |
1.02e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1113 RDMQTTIDELREDMETERNARNKAEMTRR--EVVAQLEKVKGDVLDKVDEATMLQDLMSRkdeevnatkRAIEQIQhtme 1190
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAA---------LRLWFAQ---- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1191 gkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkiheahLMEIQANLAES 1270
Cdd:COG4913 288 -----------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1271 DEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRlkiANINRARQLEDEKNALLDE 1350
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEKEIHAARqgagearrkaeESVNQQLeELRKKNLRDV-EHLQKQLEES--EVAKERILQSKKK---IQQ 1424
Cdd:COG4913 428 IASLERRKSNIPARLLALR-----------DALAEAL-GLDEAELPFVgELIEVRPEEErwRGAIERVLGGFALtllVPP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1425 ELEDSSME-LENVRASHR-DSEK---RQKKFESQMAEERVAVQKALLDRDAMSQELRDRetrvlsLLNEVDIMK-EHLEE 1498
Cdd:COG4913 496 EHYAAALRwVNRLHLRGRlVYERvrtGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE------LGRRFDYVCvDSPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1499 SDRVRRSLQQELQdsISN------KDD---------FGKN----VHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDAR 1559
Cdd:COG4913 570 LRRHPRAITRAGQ--VKGngtrheKDDrrrirsryvLGFDnrakLAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1560 LRLEVTNQALKSESD-RAISNKDVEAEEKRRGLLK---QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANR 1635
Cdd:COG4913 648 EALQRLAEYSWDEIDvASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1636 LKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRA-VEAEREQLREANEGLMQARKQ 1702
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEErIDALRARLNRAEEELERAMRA 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1247-1920 |
1.16e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1247 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVRE-----------EEEHAFANMQRRLATAEGQ 1315
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAllkekreyegyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1316 IQELNEQIQEETRL---KIANINRARQLEDEKNALLDEKEEAEGLR-----AHLEKEIHAARQGAGEARRKAEESVNQ-- 1385
Cdd:TIGR02169 246 LASLEEELEKLTEEiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELEDAEERla 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1386 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1465
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1466 LDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSisnkddfGKNVHELEKAKRSLEAELNDMRVQM 1545
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-------EWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1546 EELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVeAEEKRRGLLKQIRDLenelenekrGKSGAvSHRKKIENQIGE 1625
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV-LKASIQGVHGTVAQL---------GSVGE-RYATAIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1626 LEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLR-----------EADRKFRAV------------ 1682
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdlvEFDPKYEPAfkyvfgdtlvve 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1683 --EAEREQL-----------------------REANEGLMQARKQleleNDELEELRAKGGGISSEEKrRLEAKIAQLEE 1737
Cdd:TIGR02169 628 diEAARRLMgkyrmvtlegelfeksgamtggsRAPRGGILFSRSE----PAELQRLRERLEGLKRELS-SLQSELRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1738 ELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRaRAQMAALEAKV 1817
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL-EEDLHKLEEAL 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1818 QYLEDQLNVE-----GQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERT 1892
Cdd:TIGR02169 782 NDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
730 740
....*....|....*....|....*...
gi 25150354 1893 KHRNVQREADDLLDANEQLTRELMNLRG 1920
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKK 889
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1269-1848 |
1.18e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1269 ESDEHKR--TLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELN--EQIQEETRLKIAninrarQLEDEK 1344
Cdd:PRK02224 201 EKDLHERlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtlEAEIEDLRETIA------ETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1345 NALLDEKEEAEGLRAHLEKEIHAARQGAGeARRKAEESVNQQLEEL--RKKNLRDV-----EHLQKQLEESEVAKERILQ 1417
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELedRDEELRDRleecrVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1418 SK---KKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAM---SQELRDRETRVLSLLNEVDI 1491
Cdd:PRK02224 354 LEeraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAedfLEELREERDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1492 MKEHLEESDRVRRSLQ---------QELQDSisnkdDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARlrl 1562
Cdd:PRK02224 434 TLRTARERVEEAEALLeagkcpecgQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV--- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1563 evtnqalksESDRAISNKdveaEEKRRGLLKQIRDLENELEnEKRGKsgAVSHRKKIENQIGELEQQLEVANRLKEEYNK 1642
Cdd:PRK02224 506 ---------EAEDRIERL----EERREDLEELIAERRETIE-EKRER--AEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1643 QLKKNQQIIKEYQiECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEndeleelrakgggisS 1722
Cdd:PRK02224 570 AREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK---------------R 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1723 EEKRRLEAKIaqleeeleeEQSNCELAIDKQRKAQVQLEQITTDLsmertlnQKTEAEKQSLERSNRDYKAKITELESga 1802
Cdd:PRK02224 634 ERKRELEAEF---------DEARIEEAREDKERAEEYLEQVEEKL-------DELREERDDLQAEIGAVENELEELEE-- 695
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1803 qsrARAQMAALEAKVQYLED-QLNVEGQEKTAA-------NRAARRLEKRLNDT 1848
Cdd:PRK02224 696 ---LRERREALENRVEALEAlYDEAEELESMYGdlraelrQRNVETLERMLNET 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
845-1570 |
1.40e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 76.65 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEiRAKDDELRATKERLLKME-----HDFRENEKKLDQVIVERAVIQEQLQQESEnsaELDDIRGRLQTRNQEL 919
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTE---EISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 920 EYIvNDMRDRLSEEEQ-----QNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYD 994
Cdd:TIGR02169 275 EEL-NKKIKDLGEEEQlrvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 995 KLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKM 1074
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1075 GKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREV----------- 1143
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeervrggrave 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1144 -------------VAQLEKVKGD-----------------VLDKVDEATMLQDLMSRK-----------------DEEVN 1176
Cdd:TIGR02169 514 evlkasiqgvhgtVAQLGSVGERyataievaagnrlnnvvVEDDAVAKEAIELLKRRKagratflplnkmrderrDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1177 ATKRAI----------EQIQH----------------------------TMEGKIEEQ-----------------KAKFS 1201
Cdd:TIGR02169 594 SEDGVIgfavdlvefdPKYEPafkyvfgdtlvvedieaarrlmgkyrmvTLEGELFEKsgamtggsraprggilfSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1202 RQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQL 1281
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1282 ERSRDELDHLNRVREEEEHAFANMQRRLATAEgqiQELNEQiqeetrlkianinRARQLEDEKNALLDEKEEAEGLRAHL 1361
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHS-------------RIPEIQAELSKLEEEVSRIEARLREI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1362 EKEIhaarqgagearrKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHR 1441
Cdd:TIGR02169 818 EQKL------------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1442 DSEKRQKKFESQMAEERVAVQKALLDRDamsqelrDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISnKDDFG 1521
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQ 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 25150354 1522 KNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALK 1570
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
852-1681 |
3.55e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.39 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 852 EIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLS 931
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 932 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLlldKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLT 1011
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE---EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1012 TQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEqhKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEEL 1091
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE--ESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1092 QHQLTRYDEESANVTLMQKQMRDMQttiDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRK 1171
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEE---RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1172 DEEVNATKRAIEQIQHtmegkieeqkakfSRQVEELHDQIEQHKKQRSQLEKQQNQADQERaDMAQEIALLQASRADIDK 1251
Cdd:pfam02463 550 IVEVSATADEVEERQK-------------LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-EIDPILNLAQLDKATLEA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1252 KRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEldhlnrvrEEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKI 1331
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG--------VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1332 ANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhaarqgAGEARRKAEESVNQQLEELRKKNLrdvehLQKQLEESEVA 1411
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE------LLADRVQEAQDKINEELKLLKQKI-----DEEEEEEEKSR 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1412 KERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDI 1491
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1492 MKEHLEESDRVRRSLQQELQdsISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKS 1571
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEEL--ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1572 ESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQII 1651
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
810 820 830
....*....|....*....|....*....|
gi 25150354 1652 KEYQIECEEARQAKEDIAALLREADRKFRA 1681
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1031-1873 |
4.06e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.01 E-value: 4.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1031 LENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQK 1110
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1111 QMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLdKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTme 1190
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL-TLCTPCMPDTYHERKQVLEKELKHLREALQQT-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1191 gkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIheAHLMEIQANLAES 1270
Cdd:TIGR00618 239 -----------QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--APLAAHIKAVTQI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1271 DEhkrtlidQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANinrarqleDEKNALLDE 1350
Cdd:TIGR00618 306 EQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH--------EVATSIREI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEKEihaarqgagearRKAEESVNQQLEELRKKNLRDVEHLQKQleESEVAKERILQSKK---KIQQELE 1427
Cdd:TIGR00618 371 SCQQHTLTQHIHTL------------QQQKTTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLahaKKQQELQ 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1428 DSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALL-DRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDR---VR 1503
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPA 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1504 RSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDraisnkdve 1583
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP--------- 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1584 aeeKRRGLLKQIRDLENELENEKRGKSGAV-SHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQ-QIIKEYQIECEEA 1661
Cdd:TIGR00618 588 ---NLQNITVRLQDLTEKLSEAEDMLACEQhALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAlQLTLTQERVREHA 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1662 RQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRlEAKIAQLEEELEE 1741
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL-GSDLAAREDALNQ 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1742 EQSNCELAIDKQRKAQVQL-EQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITEL---ESGAQSRARAQMAALEAKV 1817
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAhFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLktlEAEIGQEIPSDEDILNLQC 823
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 25150354 1818 QYL---EDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKN 1873
Cdd:TIGR00618 824 ETLvqeEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
968-1609 |
4.31e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 968 LLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLE--EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRE 1045
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1046 RQykSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdeeLQHQLTRydeesanvtlmqkqmrdmqttIDELRED 1125
Cdd:COG4913 296 EL--EELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDR---------------------LEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1126 METERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKakfsRQVE 1205
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR----RELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1206 ELHDQIEQHKKQRSQLEKQQNQAdqeRADMAQEIAL-------------------------------------------L 1242
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLAL---RDALAEALGLdeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1243 QASRA--DIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLE----RSRDELDHL-----NRVREEEEHAFANMQRRLaT 1311
Cdd:COG4913 500 AALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAElgrrfDYVCVDSPEELRRHPRAI-T 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1312 AEGQ-----------------------------IQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLE 1362
Cdd:COG4913 579 RAGQvkgngtrhekddrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1363 KEI-----HAARQGAGEARRKAEESvNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVR 1437
Cdd:COG4913 659 DEIdvasaEREIAELEAELERLDAS-SDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1438 ASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNE-----VDIMKEH----------------- 1495
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRaeeelERAMRAFnrewpaetadldadles 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1496 LEESDRVRRSLQQElqDSISNKDDFGKNVHELEKAKRS-----LEAELNDMRVQMEELED---NLQIAEDARLRLEVT-- 1565
Cdd:COG4913 814 LPEYLALLDRLEED--GLPEYEERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDslkRIPFGPGRYLRLEARpr 891
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1566 --------NQALKSESDRAISNKDVEAEEK---RRGLLKQIRDLENELENEKRGK 1609
Cdd:COG4913 892 pdpevrefRQELRAVTSGASLFDEELSEARfaaLKRLIERLRSEEEESDRRWRAR 946
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1296-1843 |
4.60e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1296 EEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKianiNRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEA 1375
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE----ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1376 RRKAEESVNQQLE-ELRKKNLRDVEHLQKQLEES-EVAKERILQSKKKIQ-----QELEDSSMELENVRASHRDSEKRQK 1448
Cdd:PRK03918 234 EELKEEIEELEKElESLEGSKRKLEEKIRELEERiEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1449 KFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQ----ELQDSISNKDDFGKNV 1524
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1525 HELEKAK-------RSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALkSESDRA------------ISNKDVEAE 1585
Cdd:PRK03918 394 EELEKAKeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-TEEHRKelleeytaelkrIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1586 EKRRGLLKQIRDLENELENEKRgksgaVSHRKKIENQIGELEQQLEVANrlkeeynkqLKKNQQIIKEYQIECEEARQAK 1665
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESE-----LIKLKELAEQLKELEEKLKKYN---------LEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1666 EDIAALLREADRKfravEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEaKIAQLEEELEEEQSN 1745
Cdd:PRK03918 539 GEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1746 CELAIDKQRKAQVQLEQITTDLS-----MERTLNQKTEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYL 1820
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAetekrLEELRKELEELEKKYSEEEYEELREEYLELSR-ELAGLRAELEELEKRREEI 692
|
570 580
....*....|....*....|...
gi 25150354 1821 EDQLNVEGQEKTAANRAARRLEK 1843
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEK 715
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
965-1666 |
6.04e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 965 RQKLLLDKTNVDQRlrnleERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrLENQLHELEQDLNR 1044
Cdd:TIGR00618 165 KKELLMNLFPLDQY-----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1045 ERQYKSELEQhKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDE-----ELQHQLTRYDEESANVTLMQKQMRDMQTTI 1119
Cdd:TIGR00618 238 TQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1120 DELREDMETERNARNKAEMTRREVVAQ------LEKVKGDVLDKVDEATMLQDLMSRKDEEVNATkRAIEQIQHTMEGKI 1193
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQrrllqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1194 EEQKAKFSRQVEELHDQIEQHKKQRSqLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDE- 1272
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQq 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1273 --HKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDE 1350
Cdd:TIGR00618 475 lqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEKEIHAARQGAGEARRKAE--ESVNQQLEELRKKNLRDVEHLQKQLEESevakeRILQSKKKIQQELED 1428
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEdiPNLQNITVRLQDLTEKLSEAEDMLACEQ-----HALLRKLQPEQDLQD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1429 SSMELENVRASHRDSEKRQKKFESQMAEERVAvQKALLDRDAMSQELRDRE---TRVLSLLNEVDIMKEHLEESDRVRRS 1505
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLASRQlalQKMQSEKEQLTYWKEMLAQCQTLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1506 LQQELQDSisnkddfGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAE 1585
Cdd:TIGR00618 709 LETHIEEY-------DREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1586 EKRRGLLKQIRDLENELENEKRGKSgavSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI---IKEYQIECEEAR 1662
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEA---EIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATlgeITHQLLKYEECS 858
|
....
gi 25150354 1663 QAKE 1666
Cdd:TIGR00618 859 KQLA 862
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
979-1653 |
8.69e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 73.90 E-value: 8.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 979 LRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRK 1058
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1059 LLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRedmeterNARNKAEM 1138
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-------NKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1139 TRREVVAQLEKVK---GDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHK 1215
Cdd:TIGR04523 202 LLSNLKKKIQKNKsleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1216 KQRSQLEKQQNQADQERADMAQEIA--LLQASRADIDKKRKiheaHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNR 1293
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLNNQKEqdWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1294 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETrLKIANINRARQLEDEKNALLDEK-EEAEGLRAHLEKEIHAARQGA 1372
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE-SQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1373 GEARRKAEESVNQ--QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKF 1450
Cdd:TIGR04523 436 IKNNSEIKDLTNQdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1451 ESQMAEERVAVQKALLDRDAMSQELRDRETRVlsllnevdimkehleesdrvrrslqqelqdsisNKDDFGKNVHELEKA 1530
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDEL---------------------------------NKDDFELKKENLEKE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1531 KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSEsdraISNKDVEAEEkrrgllkqirdLENELENEKRGKS 1610
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISS-----------LEKELEKAKKENE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 25150354 1611 GAVSHRKKIENQIGELEQQLEvanRLKEEYNKQLKKNQQIIKE 1653
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVK---QIKETIKEIRNKWPEIIKK 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
905-1489 |
8.98e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 905 LDDIRGRL--------QTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETvRDLEEQLEQEEQARQkllldktnvd 976
Cdd:PRK02224 182 LSDQRGSLdqlkaqieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARET-RDEADEVLEEHEERR---------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 977 QRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKG-------RLENQLHELEqdlNRERQYK 1049
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELE---DRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1050 SELEQHkRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLtrydeESANVTLmqkqmRDMQTTIDELREDMETE 1129
Cdd:PRK02224 328 DRLEEC-RVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL-----EEAREAV-----EDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1130 RNARNKAEMTRREVVAQLEkvkgDVLDKVDEATmlQDLMSRKDEEVNATKRAIEQIQHTMEGKIEE--QKAKFSRQVEEL 1207
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLE----ELREERDELR--EREAELEATLRTARERVEEAEALLEAGKCPEcgQPVEGSPHVETI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1208 HD---QIEQHKKQRSQLEKQQNQADQ--ERADMAQE----IALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLI 1278
Cdd:PRK02224 471 EEdreRVEELEAELEDLEEEVEEVEErlERAEDLVEaedrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1279 DQLERSRDEldhLNRVREEEEHAfanmQRRLATAEGQIQELNEQIQEETRL-----KIANINRARQLEDEKNALLDEKEE 1353
Cdd:PRK02224 551 AEAEEKREA---AAEAEEEAEEA----REEVAELNSKLAELKERIESLERIrtllaAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1354 aeglrahLEKEIHAARQgagEARRKAEESVNQ-QLEELRKKNLRDVEHLQK---QLEESEVAKERILQSKKKIQQELEds 1429
Cdd:PRK02224 624 -------ERRERLAEKR---ERKRELEAEFDEaRIEEAREDKERAEEYLEQveeKLDELREERDDLQAEIGAVENELE-- 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1430 smELENVRASHRDSEKRQKKFESqMAEERVAVQKALLDRDAmsqELRDRETRVLS-LLNEV 1489
Cdd:PRK02224 692 --ELEELRERREALENRVEALEA-LYDEAEELESMYGDLRA---ELRQRNVETLErMLNET 746
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
851-1755 |
1.78e-12 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 73.08 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIRAKDDELRATKERLLKMEhdfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDmrdrl 930
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 931 seEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvdQRLRNLEERLVELQDAYDKLLKEKRLLEEKvegl 1010
Cdd:pfam02463 231 --YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKS---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1011 ttQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKrKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1090
Cdd:pfam02463 301 --ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1091 LQHQLTRYDEESANVTLMQKQMRDmqttiDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKvdeatmlqdlmsR 1170
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKS-----EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI------------E 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1171 KDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADID 1250
Cdd:pfam02463 441 LKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1251 KKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFAN-MQRRLATAEGQIQELNEQIQEETRL 1329
Cdd:pfam02463 521 GGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPlGARKLRLLIPKLKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1330 KIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEElRKKNLRDVEHLQKQLEESE 1409
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE-KSEVKASLSELTKELLEIQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1410 VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAlldrdamSQELRDRETRVLSLLNEV 1489
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-------NEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1490 DIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDmrvQMEELEDNLQIAEDARLRLEVTNQAL 1569
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL---RALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1570 KSESDRAISNKDVEAEEKRRGLL--KQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQ-QLEVANRLKEEYNKQLKK 1646
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAeeELERLEEEITKEELLQELLLKEEELEEQKLKDELESkEEKEKEEKKELEEESQKL 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1647 NQQIIKEYQIECEEAR-QAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEK 1725
Cdd:pfam02463 910 NLLEEKENEIEERIKEeAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
890 900 910
....*....|....*....|....*....|
gi 25150354 1726 RRLEAKIAQLEEELEEEQSNCELAIDKQRK 1755
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1275-1886 |
2.04e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1275 RTLIDQLERSRDELDHLNRVREEEEHAFAnmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEA 1354
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1355 EGLR-AHLEKEIHAARQGAGEARRKAEEsVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1433
Cdd:COG4913 336 GGDRlEQLEREIERLERELEERERRRAR-LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1434 ENVRASHRDSEKRQKKFESQmaeeRVAVQKALLD-RDAMSQELRDRETRVLSLLNEVDIMKEHLE-----EsdRVRRSLQ 1507
Cdd:COG4913 415 RDLRRELRELEAEIASLERR----KSNIPARLLAlRDALAEALGLDEAELPFVGELIEVRPEEERwrgaiE--RVLGGFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1508 QELqdsISNKDDFgknvhelEKAKRSLEAELNDMRVQMEELEDNLQIAEDARL-------RLEVTNQALKSEsdraisnk 1580
Cdd:COG4913 489 LTL---LVPPEHY-------AAALRWVNRLHLRGRLVYERVRTGLPDPERPRLdpdslagKLDFKPHPFRAW-------- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1581 dVEAEEKRRGLLKQIRDLEnELENEKRG-------KSGAVSHRKKI--------------ENQIGELEQQLEVANRLKEE 1639
Cdd:COG4913 551 -LEAELGRRFDYVCVDSPE-ELRRHPRAitragqvKGNGTRHEKDDrrrirsryvlgfdnRAKLAALEAELAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1640 YNKQLKKNQQIIKEYQIECEEARQAKEDIAALL--READRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKG 1717
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1718 GGIsSEEKRRLEAKIAQLEeeleeeqsncelaiDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITE 1797
Cdd:COG4913 709 DEL-KGEIGRLEKELEQAE--------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1798 LESGAQSRARAQMAALEAKV-QYLEDQlNVEGQEKTAANRAARRLEKRLNDTTQqfEDEKRANEQAKELLEKSNLKNR-N 1875
Cdd:COG4913 774 RIDALRARLNRAEEELERAMrAFNREW-PAETADLDADLESLPEYLALLDRLEE--DGLPEYEERFKELLNENSIEFVaD 850
|
650
....*....|.
gi 25150354 1876 LRRQLDEAEDE 1886
Cdd:COG4913 851 LLSKLRRAIRE 861
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1174-1797 |
2.51e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1174 EVNATKRAIEQI---QHTMEGKIEEQKAKF---SRQVEELHDQIEQHKKQRSQLEKQQnqadQERADMAQEIALLQASRA 1247
Cdd:PRK03918 173 EIKRRIERLEKFikrTENIEELIKEKEKELeevLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1248 DIDKKRKIHEAHLMEIQANLAESDEHKRTL------IDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNE 1321
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELeekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1322 QIQEETRLKianiNRARQLEDEKNALLDEKEEAEGLRAHLEkeihaarqgagEARRKAEEsvnqqLEELRKK-NLRDVEH 1400
Cdd:PRK03918 329 RIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYE-----------EAKAKKEE-----LERLKKRlTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1401 LQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDSEKRQKKfesqmAEERVAVQKALLDRDamsqelrdret 1480
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELKK-----AKGKCPVCGRELTEE----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1481 rvlsllNEVDIMKEHLEESDRVRRSLQQelqdsisnkddFGKNVHELEKAKRSLEAELNDMRvqmeELEDNLQIAEdarl 1560
Cdd:PRK03918 449 ------HRKELLEEYTAELKRIEKELKE-----------IEEKERKLRKELRELEKVLKKES----ELIKLKELAE---- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1561 RLEVTNQALKSESDRAISNKDVEAE---EKRRGLLKQIRDLENELENEKRGKsgavSHRKKIENQIGELEQQL-EVANRL 1636
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELK----KKLAELEKKLDELEEELaELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1637 KE---EYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEEL 1713
Cdd:PRK03918 580 EElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1714 RAKGggiSSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQItTDLSMERTLNQKTEAEKQSLERSNRDYKA 1793
Cdd:PRK03918 660 EYEE---LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-EKAKKELEKLEKALERVEELREKVKKYKA 735
|
....
gi 25150354 1794 KITE 1797
Cdd:PRK03918 736 LLKE 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1476-1922 |
5.70e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1476 RDRETRVLSLLNEVDIMKEHLE-ESDRVRR--SLQQELQD-----SISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEE 1547
Cdd:COG1196 185 EENLERLEDILGELERQLEPLErQAEKAERyrELKEELKEleaelLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1548 LEDNLQIAEDARLRLEVTNQALKsESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELE 1627
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1628 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQAR-KQLELE 1706
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLeRLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1707 NDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLER 1786
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1787 SNRDYkakitelesGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDttqqfEDEKRANEQAKELl 1866
Cdd:COG1196 502 DYEGF---------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV-----EDDEVAAAAIEYL- 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1867 eKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1922
Cdd:COG1196 567 -KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1278-1700 |
7.41e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1278 IDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINRARQLEDEKNALLDEKEEAEGL 1357
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1358 RAHLE--KEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEN 1435
Cdd:COG4717 152 EERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1436 VRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIM---------KEHLEESDRV---- 1502
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflllarekASLGKEAEELqalp 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1503 -RRSLQQELQDSISNKDDFGKNVHELE-KAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQAlKSESDRAISNK 1580
Cdd:COG4717 312 aLEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA-GVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1581 dVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKK--IENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQI-- 1656
Cdd:COG4717 391 -LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEdg 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 25150354 1657 ECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQAR 1700
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1034-1698 |
1.39e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1034 QLHELEQDLNRERQykseleqhKRKLLAELEDSKDHLAEKMGKVEELnnqlmkrdEELQHQLTRYDEESAnVTLMQKQMR 1113
Cdd:COG4913 236 DLERAHEALEDARE--------QIELLEPIRELAERYAAARERLAEL--------EYLRAALRLWFAQRR-LELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1114 DMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKvdeatmLQDLMSRKDEEVNATKRAIEQIQHTMEG-- 1191
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLAAlg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1192 -KIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAEs 1270
Cdd:COG4913 373 lPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1271 dehkrtlidQLERSRDEL----DHLNrVREEEE----------HAFAnmqRRLATAEGQIQELN---EQIQEETRLKIAN 1333
Cdd:COG4913 452 ---------ALGLDEAELpfvgELIE-VRPEEErwrgaiervlGGFA---LTLLVPPEHYAAALrwvNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1334 INRARQLED----EKNALLDEKEEAEG-----LRAHLEKEIHAARQGAGEARRKAEESVNQ-----QLEELRKKNLRDVE 1399
Cdd:COG4913 519 VRTGLPDPErprlDPDSLAGKLDFKPHpfrawLEAELGRRFDYVCVDSPEELRRHPRAITRagqvkGNGTRHEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1400 HLQKQLEESEVAKERILQSK-KKIQQELEDSSMELENVRASHRDSEKRQkkfesqMAEERVA-VQKALLDRDAMSQELRD 1477
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEAElAELEEELAEAEERLEALEAELDALQERR------EALQRLAeYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1478 RETRvlsllnevdimKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAED 1557
Cdd:COG4913 673 LEAE-----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1558 ---ARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRgksgavSHRKKIENQIGELEQQLEVAN 1634
Cdd:COG4913 742 larLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR------AFNREWPAETADLDADLESLP 815
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1635 RLKEEYNKQ----LKKNQQIIKEYQIECEEarqakEDIAALLREADrkfRAVEAEREQLREANEGLMQ 1698
Cdd:COG4913 816 EYLALLDRLeedgLPEYEERFKELLNENSI-----EFVADLLSKLR---RAIREIKERIDPLNDSLKR 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1368-1886 |
1.97e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1368 ARQGAGEARRKAEESVNQ---QLEELRKKNLRD-VEHLQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDS 1443
Cdd:PRK02224 174 ARLGVERVLSDQRGSLDQlkaQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRD----EADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1444 EKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVD--------------IMKEHLEESDRVRRSLQQE 1509
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllaeaglddadaeAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1510 LQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDraisnkdvEAEEKRR 1589
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE--------ELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1590 GLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynKQLKKNQQIIKEYQIEC--EEARQAKED 1667
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA--GKCPECGQPVEGSPHVEtiEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1668 IAALLREADRKFRAVEAEREQLREANEglMQARKQLELENDELEELRAkgggisSEEKRRLEAKIAQLEEELEEEQSNCE 1747
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVE--AEDRIERLEERREDLEELI------AERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1748 LAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNR--DYKAKITELESGAQSRaRAQMAALeakvqyleDQLN 1825
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERL-REKREAL--------AELN 622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1826 VEGQEKTAANRAARR-LEKRLNDttQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1886
Cdd:PRK02224 623 DERRERLAEKRERKReLEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
982-1875 |
2.89e-11 |
|
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: 69.23 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 982 LEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlENQLHELEQDLNRERQYKSELEQHKRKLLA 1061
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE---KLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1062 ELEDSKDHLAEKMGKVEELNnqlmkrdeelqhqltryDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRR 1141
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKL-----------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1142 EVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQiqhtMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQL 1221
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA----EEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1222 EKQQNQADQERADMAQEIALLQaSRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHA 1301
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQ-LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1302 FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE 1381
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1382 SVNQQLEELRKKnlRDVEHLQKqleeSEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAV 1461
Cdd:pfam02463 546 STAVIVEVSATA--DEVEERQK----LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1462 QKALLDRDamsqeLRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDM 1541
Cdd:pfam02463 620 KRAKVVEG-----ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1542 RVQMEELEDNLQIAEdarLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIEN 1621
Cdd:pfam02463 695 LRRQLEIKKKEQREK---EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1622 QIGELEQQLEVANRLKEEYNKQLKKnqqiiKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARK 1701
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKL-----KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1702 QLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEK 1781
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1782 QSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQ 1861
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
890
....*....|....
gi 25150354 1862 AKELLEKSNLKNRN 1875
Cdd:pfam02463 1007 LIRAIIEETCQRLK 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
820-1428 |
3.30e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 68.84 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 820 RNGLAYLKLRNWQWWRLFTKVKPLLQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQES 899
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 900 ENSaeldDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLdktnvdQRL 979
Cdd:TIGR00618 312 IHT----ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT------QHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 980 RNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQ-------DLNRERQYKSEL 1052
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaitcTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1053 EQHKRKL------LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDM 1126
Cdd:TIGR00618 462 QESAQSLkereqqLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1127 ETERNARNKAEMTRRevvaQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEE 1206
Cdd:TIGR00618 542 TSEEDVYHQLTSERK----QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1207 LHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQ-----------ASRADIDKKRKIHEAHLMEIQANLAESDEHKR 1275
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1276 TLIDQLERSRDELDHL---NRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKI---------------ANINRA 1337
Cdd:TIGR00618 698 MLAQCQTLLRELETHIeeyDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLkarteahfnnneevtAALQTG 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1338 RQLEDEKNALLDEKEEAE---GLRAHLEKEIHAARQGAGEAR-------RKAEESVNQQLEELRKKnLRDVEHLQKQLEE 1407
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREedtHLLKTLEAEIGQEIPSDEDILnlqcetlVQEEEQFLSRLEEKSAT-LGEITHQLLKYEE 856
|
650 660
....*....|....*....|.
gi 25150354 1408 SEVAKERILQSKKKIQQELED 1428
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1222-1915 |
5.14e-11 |
|
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: 68.07 E-value: 5.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1222 EKQQNQADQERADMAQEiallqASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEldhlnrvREEEEHA 1301
Cdd:pfam02463 145 EIIAMMKPERRLEIEEE-----AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-------AKKALEY 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1302 FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE 1381
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1382 SVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASH-------RDSEKRQKKFESQm 1454
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKReaeeeeeEELEKLQEKLEQL- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1455 aeERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKD------DFGKNVHELE 1528
Cdd:pfam02463 372 --EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEeeeesiELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1529 KAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRG 1608
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1609 K---------SGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLK-KNQQIIKEYQIECEEARQAKEDIAALLREADRK 1678
Cdd:pfam02463 530 RlgdlgvaveNYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1679 FRAVEAEREQLREAN--EGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKA 1756
Cdd:pfam02463 610 KATLEADEDDKRAKVveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1757 QVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLE---DQLNVEGQEKTA 1833
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrlKKEEKEEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1834 ANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTR 1913
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
..
gi 25150354 1914 EL 1915
Cdd:pfam02463 850 KL 851
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
891-1407 |
6.54e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 6.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 891 IQEQLQQESENSAELDDIRGRLQTRNQEleyivndmRDRLSEEEQQNEKNNDERRKQMETvrDLEEQLEQEEQARQKLLL 970
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQ--------IELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 971 dktnVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLttqlldHEERAKHGVKAKGRLENQLHELEQDLNRERQ--- 1047
Cdd:COG4913 293 ----LEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRLEQLEREIERLERELEERERrra 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1048 ----------------------YKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANV 1105
Cdd:COG4913 363 rleallaalglplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1106 TLMQKQMRDM---QTTIDE-----------LREDMETERNARNKA----------------------EMTRREVVAQLEK 1149
Cdd:COG4913 439 PARLLALRDAlaeALGLDEaelpfvgelieVRPEEERWRGAIERVlggfaltllvppehyaaalrwvNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1150 VKGDVLD----KVDEATM--------------LQDLMSRK--------DEEVNATKRAIeqiqhTMEGKIeeqKAKFSRQ 1203
Cdd:COG4913 519 VRTGLPDperpRLDPDSLagkldfkphpfrawLEAELGRRfdyvcvdsPEELRRHPRAI-----TRAGQV---KGNGTRH 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1204 VEELHDQIEQH-------KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHlmeiqANLAESDEHKRT 1276
Cdd:COG4913 591 EKDDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1277 LIDQLERSRDELDHLnrvrEEEEHAFANMQRRLATAEGQIQELNEQI----QEETRLKiANINRARQLEDEKNALLDEKE 1352
Cdd:COG4913 666 AEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELdelkGEIGRLE-KELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1353 EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEE 1407
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1289-1900 |
8.69e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.45 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1289 DHLNRVREEEEHAFANMQRRLataeGQIQELNEQIQEETRLKIANIN-RARQLEDEKNALLD----EKEEAEGLRAHLEK 1363
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQSVIDLQtKLQEMQMERDAMADirrrESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1364 EIHAArQGAGEARRKAEESVNQQLEELRKKNLRDvEHLQKQLEESEVAKERilQSKKKIQQELEDSSMELENVRAS---- 1439
Cdd:pfam15921 150 TVHEL-EAAKCLKEDMLEDSNTQIEQLRKMMLSH-EGVLQEIRSILVDFEE--ASGKKIYEHDSMSTMHFRSLGSAiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1440 --HRDSEKRQKKFESQMAEERVAVQKAlLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNK 1517
Cdd:pfam15921 226 lrELDTEISYLKGRIFPVEDQLEALKS-ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1518 DDFGKN--------VHELEKAKRSLEAELNDMRV----QMEELEDNLQIAEDARLRLEVTNQALKSESdraiSNKDVEAE 1585
Cdd:pfam15921 305 QEQARNqnsmymrqLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1586 EKRRGLLKQIRDLENELENEKR------GKSGAVSH-RKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIEC 1658
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRlwdrdtGNSITIDHlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1659 EEA-------RQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKgggisSEEKRRLEAK 1731
Cdd:pfam15921 461 EKVssltaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQH 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1732 IAQLEEELEEEQSNCE-LAIDKQRKAQV------QLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESgAQS 1804
Cdd:pfam15921 536 LKNEGDHLRNVQTECEaLKLQMAEKDKVieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI-LKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1805 RARAQMAALEAKVQYLEDQ---LNVEGQEKTaanRAARRLEKrlnDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLD 1881
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEkvkLVNAGSERL---RAVKDIKQ---ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
650
....*....|....*....
gi 25150354 1882 EAEDEMSRERTKHRNVQRE 1900
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
852-1630 |
1.00e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 67.38 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 852 EIRAKDDELRATKERLLKMEHDFRENEKKLDQViveraviqeqLQQESENSAELDDIRGRlqtrnqeleyIVNDMRDRLS 931
Cdd:TIGR00606 263 KIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLNDLYHNHQR----------TVREKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 932 EEEQQNEKNNDERRkqmetVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLlkekrlleEKVEGLT 1011
Cdd:TIGR00606 323 DCQRELEKLNKERR-----LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF--------ERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1012 TQLLDHEERAKHGVKAKGRLENQL-HELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQL------ 1084
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELqqlegs 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1085 MKRDEELQHQLTRYD------EESANVTLMQKQMRDMQTT----------IDELREDMETERNARNKAEMTRREVVAQLE 1148
Cdd:TIGR00606 470 SDRILELDQELRKAErelskaEKNSLTETLKKEVKSLQNEkadldrklrkLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1149 KVKGDVLDKVDEAT----------MLQDLMSRKDEEVNATKRAIEQIQ------HTMEGKIEEQKAKFSRQVEELHDQI- 1211
Cdd:TIGR00606 550 QIRKIKSRHSDELTsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNkelaslEQNKNHINNELESKEEQLSSYEDKLf 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1212 -----EQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRD 1286
Cdd:TIGR00606 630 dvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1287 ELDHLNRVREEEEHAFANMqrrLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALldekEEAEGLRAHLEKEIH 1366
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI----EEQETLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1367 AARQgagearRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAK--ERILQSKKKIQQELEDSSMELENVRASHRDSE 1444
Cdd:TIGR00606 783 SAKV------CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1445 KRQKKFESQMAE---ERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFG 1521
Cdd:TIGR00606 857 EQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1522 KNVHE--------------------------LEKAKRSLEAELNDMRVQMEELEDNLQ-IAEDARLRLEVTNQALKSES- 1573
Cdd:TIGR00606 937 KKAQDkvndikekvknihgymkdienkiqdgKDDYLKQKETELNTVNAQLEECEKHQEkINEDMRLMRQDIDTQKIQERw 1016
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1574 ------DRAISNKDVEAEEKRRGLLKQI------------RDLENELENEKRGKSGAVSHRKKIENQIGELEQQL 1630
Cdd:TIGR00606 1017 lqdnltLRKRENELKEVEEELKQHLKEMgqmqvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
932-1667 |
1.59e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 932 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKL---LKEKRLLEEKVE 1008
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLdneIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1009 GLTTQLLDHEERAKHGVkakgrlENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRD 1088
Cdd:TIGR00606 283 KDNSELELKMEKVFQGT------DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1089 EELQHQLTRYDEEsanvtlmqKQMRDMQTTIDELREDMETERNARNKAEMTRREvvaqlekvkgdvldKVDEATMLQDLM 1168
Cdd:TIGR00606 357 DRHQEHIRARDSL--------IQSLATRLELDGFERGPFSERQIKNFHTLVIER--------------QEDEAKTAAQLC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1169 SRKDEEVNATKRAIEQIQHTMEGK---IEEQKAKFSRQVEELhdqieqhKKQRSQLEKQQNQADQ-ERADMAQEIALLQA 1244
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIRDEKKGLgrtIELKKEILEKKQEEL-------KFVIKELQQLEGSSDRiLELDQELRKAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1245 SRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLErsrdELDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQ 1324
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME----QLNHHTTTRTQME----MLTKDKMDKDEQIRKIKSRHS 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1325 EETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARrKAEESVNQQLEELRKKNLR-------- 1396
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN-NELESKEEQLSSYEDKLFDvcgsqdee 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1397 -DVEHLQKQLEESEVAK----------------------------ERILQSKKKIQQELEDSSMELENVRASHRDSEKRQ 1447
Cdd:TIGR00606 639 sDLERLKEEIEKSSKQRamlagatavysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1448 KKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrvrrslQQELQDSISNKDDFGKNVHEL 1527
Cdd:TIGR00606 719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE--------QETLLGTIMPEEESAKVCLTD 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1528 EKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQAL-KSESDRAISNKDVEAEEKRRGLLKQIRDLE---NELE 1603
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELK 870
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1604 NEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKED 1667
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1059-1498 |
2.38e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1059 LLAELEDSKDHLAEKMGKVEELNNQLMKRDE----ELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARN 1134
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEeelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1135 KAEMTRRevVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQH 1214
Cdd:COG4717 127 LLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1215 KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEL------ 1288
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1289 ------DHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLE 1362
Cdd:COG4717 285 llallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1363 KEIHAARQGAGEARRKA--EESVNQQLEELRKKN--LRDVEHLQKQLEESEVAKERILQ--SKKKIQQELEDSSMELENV 1436
Cdd:COG4717 365 LEELEQEIAALLAEAGVedEEELRAALEQAEEYQelKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1437 RASHRDSEKRQKKFESQM--AEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEE 1498
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
851-1174 |
2.55e-10 |
|
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: 65.86 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENS-AELDDIRGRLQTRNQELEYI---VNDM 926
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkSELKELEARIEELEEDLHKLeeaLNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 927 RDRLSEEEQQNEknNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDaydkllkEKRLLEEK 1006
Cdd:TIGR02169 785 EARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-------QIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1007 VEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmk 1086
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-- 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1087 rdEELQHQLTRYDEESANVTlmqkQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQD 1166
Cdd:TIGR02169 934 --SEIEDPKGEDEEIPEEEL----SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*...
gi 25150354 1167 LMSRKDEE 1174
Cdd:TIGR02169 1008 RIEEYEKK 1015
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1389-1919 |
6.36e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 6.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1389 ELRKKNLRDV----EHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESqmaeerVAVQKA 1464
Cdd:PRK03918 175 KRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE------LEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1465 LLDRDAMSQELRDRETRvlSLLNEVdimKEHLEESDRVRRSLQqELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQ 1544
Cdd:PRK03918 249 SLEGSKRKLEEKIRELE--ERIEEL---KKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1545 MEELEDNLQIAEDARLRLEVTNQALKS-ESDRAISNKDVEAEEKRRGLLKQIR------------DLENELENEKRGKSG 1611
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKAKKEELErlkkrltgltpeKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1612 AVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKK------------NQQIIKEYQIECEEARQAKEDIAALLREADRKF 1679
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1680 RAVEAEREQLREanegLMQARKqlelENDELEELRAKGGGISSEEkrrLEAKIAQLeeeleeeqsncELAIDKQRKAQVQ 1759
Cdd:PRK03918 483 RELEKVLKKESE----LIKLKE----LAEQLKELEEKLKKYNLEE---LEKKAEEY-----------EKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1760 LEQITTDLSMERTLNQKTEAekqsLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAanraar 1839
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA------ 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1840 rlEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRErtKHRNVQREADDLLDANEQLTRELMNLR 1919
Cdd:PRK03918 611 --EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELE 686
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
835-1426 |
7.73e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 835 RLFTKVKPLLQVTRTDDEIRAKDDELRATKERLlkmehdfRENEKKLDqvivERAVIQEQLQQESEnsaELDDIRGRLQT 914
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELREELEKL-------EKEVKELE----ELKEEIEELEKELE---SLEGSKRKLEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 915 RNQELEYIVNDMRDRLSEEEqqneknndERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYD 994
Cdd:PRK03918 260 KIRELEERIEELKKEIEELE--------EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 995 KL-LKEKRL--LEEKVEGLTTQLLDHEERAKHGVKAKGRLEN--QLHELEQDLNRERQYKSELEQHKRKLlaELEDSKDH 1069
Cdd:PRK03918 332 ELeEKEERLeeLKKKLKELEKRLEELEERHELYEEAKAKKEEleRLKKRLTGLTPEKLEKELEELEKAKE--EIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1070 LAEKMGKVEELNNQLMKRDEELQ----------HQLTRYDEESanvtLMQKQMRDMQTTIDELREDMETERNARNKAEMT 1139
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKE----LLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1140 RREVVAQLEKVK-GDVLDKVDEATmlQDLMSRKDEEVNATKRAIEqiqhTMEGKIEEQKAKFSRQVEELhDQIEQHKKQR 1218
Cdd:PRK03918 486 EKVLKKESELIKlKELAEQLKELE--EKLKKYNLEELEKKAEEYE----KLKEKLIKLKGEIKSLKKEL-EKLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1219 SQLEKQQNQADQERADMAQEIALLQASRADIDKKR--KIHEAHLMEIQANLAESDehkrtlidqLERSRDELDHLNRVRE 1296
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEELEERlkELEPFYNEYLELKDAEKE---------LEREEKELKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1297 EEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIAniNRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEAR 1376
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE 707
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1377 RKAEESvnqqleELRKKNLRDVEHLQKQLEESEV-AKERILQSKKKIQQEL 1426
Cdd:PRK03918 708 KAKKEL------EKLEKALERVEELREKVKKYKAlLKERALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
845-1390 |
8.20e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQqesensaELDDIRGRLQTRNqeleyivN 924
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR-------DLRERLEELEEER-------D 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 925 DMRDRLSEEEqqneknnderrkqmetvrdleeqleqeeqarqkllLDKTNVDQRLRNLEERLVELQDAydklLKEKRL-- 1002
Cdd:PRK02224 297 DLLAEAGLDD-----------------------------------ADAEAVEARREELEDRDEELRDR----LEECRVaa 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1003 --LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSkdhlAEKMGKVEEL 1080
Cdd:PRK02224 338 qaHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA----PVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1081 NNQLMKRDEELQHQLTrydEESANVTLMQKQMRDMQTTIDELR-----------EDMETERNARNKAEMTRREvVAQLEK 1149
Cdd:PRK02224 414 LEELREERDELREREA---ELEATLRTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAE-LEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1150 VKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQhTMEGKIEEQkakfSRQVEELHDQIEQHKKQRSQLEKQQNQAD 1229
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA-ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1230 QERADMAQEIALLQASRADIDKKRkiheahlmEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEehafanmQRRL 1309
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERI--------ESLERIRTLLAAIADAEDEIERLREKREALAELNDER-------RERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1310 ATAEGQIQELNEQIQEEtRLKIANINRAR------QLEDEKNALLDEKEEAEGLRAHLEKEIHA-----ARQGAGEARRK 1378
Cdd:PRK02224 630 AEKRERKRELEAEFDEA-RIEEAREDKERaeeyleQVEEKLDELREERDDLQAEIGAVENELEEleelrERREALENRVE 708
|
570
....*....|..
gi 25150354 1379 AEESVNQQLEEL 1390
Cdd:PRK02224 709 ALEALYDEAEEL 720
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1081-1452 |
8.56e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 63.99 E-value: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1081 NNQLMKRDEELqHQLTRYDEESANVTLMQKQMRDMQTTIDELREdmETERNARnkaEMTRREVVAQLEKVKGDVLDKVDE 1160
Cdd:pfam17380 261 NGQTMTENEFL-NQLLHIVQHQKAVSERQQQEKFEKMEQERLRQ--EKEEKAR---EVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1161 ATMLQDLMSRKDEevnatkRAIEQIQHtmegkiEEQKAKFSR-QVEELHDQIEQHKK-QRSQLEKQQ-NQADQERADMAQ 1237
Cdd:pfam17380 335 IYAEQERMAMERE------RELERIRQ------EERKRELERiRQEEIAMEISRMRElERLQMERQQkNERVRQELEAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1238 EIALLQASRadidkKRKIHEaHLMEIQANLAESDEHKRTLIDQLERSRDEldHLNRVREEEEHAFANMQR-RLATAEGQI 1316
Cdd:pfam17380 403 KVKILEEER-----QRKIQQ-QKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQVERlRQQEEERKR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1317 QELNEQIQEETRLKIANINRA---RQLEDEKNALLDEKEEaeglRAHLEKEIhaarqgagEARRKA--EESVNQQLEELR 1391
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERK----RKLLEKEM--------EERQKAiyEEERRREAEEER 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1392 KKnlrdvehlQKQLEESEVAKERILQSKKKiQQELEDSSMELENVRAShRDSEKRQKKFES 1452
Cdd:pfam17380 543 RK--------QQEMEERRRIQEQMRKATEE-RSRLEAMEREREMMRQI-VESEKARAEYEA 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
876-1437 |
9.80e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 876 ENEKKLDQVIVERAVIQEQL----QQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDeRRKQMETV 951
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIkndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 952 RDLEEQLEQEEQARQKLLldkTNVDQRLRNLEERLVELQdaydkllkekrLLEEKVEGLTTQLLDHEERAKHGVKAKGRL 1031
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNI---DKIKNKLLKLELLLSNLK-----------KKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1032 ENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLmqKQ 1111
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWN--KE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1112 MRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKvkgdvldkvdEATMLQDLMSRKDEEVNATKRAIEQIQHTMEG 1191
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK----------ELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1192 KIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKiheahlmeiqaNLAESD 1271
Cdd:TIGR04523 382 YKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-----------DLTNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1272 EHKRTLIDQLERSRDE----LDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETrlkianiNRARQLEDEKNAL 1347
Cdd:TIGR04523 450 SVKELIIKNLDNTRESletqLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE-------EKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1348 LDEKEEAEGLRAHLEKEIhaarqgagearRKAEESVNQQLEELRKKNLRDV-EHLQKQLEESEVAKERILQSKKKIQQEL 1426
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKI-----------SDLEDELNKDDFELKKENLEKEiDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
570
....*....|.
gi 25150354 1427 EDSSMELENVR 1437
Cdd:TIGR04523 592 DQKEKEKKDLI 602
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
977-1382 |
1.53e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 977 QRLRNLEERLVELQDAYDKLLKEKRLLEEKVE--GLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQ 1054
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1055 HKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEEsanvtlMQKQMRDMQTTIDELREDMETERNARN 1134
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE------LEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1135 KAEMTRREVVAQLEKVKGDVLDKVDE-----------ATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSR- 1202
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSLILTiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAl 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1203 ---------QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLmEIQANLAESDEH 1273
Cdd:COG4717 329 glppdlspeELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1274 KRTLIDQLERSRDELDHLNRVREEEEHafANMQRRLATAEGQIQELNEQIQeETRLKIANINRARQLEDeknaLLDEKEE 1353
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELA-ELEAELEQLEEDGELAE----LLQELEE 480
|
410 420 430
....*....|....*....|....*....|..
gi 25150354 1354 AEGLRAHLEKEIHAARQGA---GEARRKAEES 1382
Cdd:COG4717 481 LKAELRELAEEWAALKLALellEEAREEYREE 512
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
923-1692 |
1.76e-09 |
|
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: 63.32 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 923 VNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEkrl 1002
Cdd:pfam12128 211 VVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1003 LEEKVEGLTTQLLDHEERAKHGVKA-KGRLENQLHELEQDLNRERQYKSElEQHKRKLLAELEDSkdhlaekmgkveeLN 1081
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAaDAAVAKDRSELEALEDQHGAFLDA-DIETAAADQEQLPS-------------WQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1082 NQLMKRDEELQHQLTRY-DEESANVTLMQKQMRDMQTTIDELREDMETERNARNKaemtrrevvaQLEKVKGDvldkvde 1160
Cdd:pfam12128 354 SELENLEERLKALTGKHqDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDR----------QLAVAEDD------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1161 atmLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV--EELHDQIEQHKKQRSQLEKQQNQADQERADMAQE 1238
Cdd:pfam12128 417 ---LQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatPELLLQLENFDERIERAREEQEAANAEVERLQSE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1239 IALLQASRADIDKKRKIHEAHLMEIQANLAEsdehkrtLIDQLERSRDELDHLnrVREEEEHAFANMQRRLATAEGQIQE 1318
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDE-------LELQLFPQAGTLLHF--LRKEAPDWEQSIGKVISPELLHRTD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1319 LNEQIQEEtrlkianinrarQLEDEKNALldekeeaeGLRAHLEkeihaarqgageaRRKAEESV--NQQLEELR---KK 1393
Cdd:pfam12128 565 LDPEVWDG------------SVGGELNLY--------GVKLDLK-------------RIDVPEWAasEEELRERLdkaEE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1394 NLRDVEHLQKQLEESEVAkerilqskkkIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDR-DAMS 1472
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQ----------ANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkDSAN 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1473 QELRDRETRVLSLLNEVDIMKEHLeesdrvrrslqqelqdsisnKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL 1552
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQ--------------------KEQKREARTEKQAYWQVVEGALDAQLALLKAAIAAR 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1553 QIAEDARLRlevtnqALKSESDRAISNKDVEaEEKRRGLLKQIRDLENELENEKRGKSGAVS------HRKKIENQigEL 1626
Cdd:pfam12128 742 RSGAKAELK------ALETWYKRDLASLGVD-PDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqETWLQRRP--RL 812
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1627 EQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREA 1692
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED 878
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1017-1891 |
1.93e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.05 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1017 HEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLaekmgkveelnnQLMKRDEELQHQLT 1096
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL------------NLVQTALRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1097 RYDEEsanvtlmqkqmrdmqttIDELREDMETERNARNKAemtrREVVAQLEKVKGDVLDKVDE-ATMLQDLMSRKDEev 1175
Cdd:PRK04863 352 RYQAD-----------------LEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDElKSQLADYQQALDV-- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1176 nATKRAIeQIQHTMEGKieeQKAKFSRQVEELHdqIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKI 1255
Cdd:PRK04863 409 -QQTRAI-QYQQAVQAL---ERAKQLCGLPDLT--ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1256 HEAHLMEIQANLAesDEHKRTLIDQLERSRDELDHLNRvreeeehafanMQRRLATAEgqiQELNEQIQEETRLKIANIN 1335
Cdd:PRK04863 482 VRKIAGEVSRSEA--WDVARELLRRLREQRHLAEQLQQ-----------LRMRLSELE---QRLRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1336 RARQLEDEknalldekEEAEGLRAHLEKEIHAARQGAGEARRKAEEsVNQQLEELRkknlRDVEHLQKQLEESEVAKERI 1415
Cdd:PRK04863 546 LGKNLDDE--------DELEQLQEELEARLESLSESVSEARERRMA-LRQQLEQLQ----ARIQRLAARAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1416 LQSKKKIQQELEDSSMeLENVRASHRDSEKrqkkfESQMAEERVAVQKALLDR------------DAMSQELRDRETRVl 1483
Cdd:PRK04863 613 ARLREQSGEEFEDSQD-VTEYMQQLLERER-----ELTVERDELAARKQALDEeierlsqpggseDPRLNALAERFGGV- 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1484 sLLNEV--DIMkehLEES-------------------DRVRRSLQQE---------LQDSISNKDDFGKNVHELEKA--- 1530
Cdd:PRK04863 686 -LLSEIydDVS---LEDApyfsalygparhaivvpdlSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEELEKAvvv 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1531 -------------------KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNK-DVEAEEKRRG 1590
Cdd:PRK04863 762 kiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfEADPEAELRQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1591 LLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynkqlkknqQIIKEYQiECEEARQAKEDIAA 1670
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE---------TLADRVE-EIREQLDEAEEAKR 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1671 LLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAI 1750
Cdd:PRK04863 912 FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLR 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1751 DKQRKAQVQLEQITTDLSMERtlNQKTEAEK--QSLERSNRDYKAKITELE-----------SGAQSRARAQMAALEA-- 1815
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ--AQLAQYNQvlASLKSSYDAKRQMLQELKqelqdlgvpadSGAEERARARRDELHArl 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1816 -----KVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRE 1890
Cdd:PRK04863 1070 sanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLSADELRS 1149
|
.
gi 25150354 1891 R 1891
Cdd:PRK04863 1150 M 1150
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1201-1419 |
2.04e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1201 SRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQ 1280
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1281 LERSRDELDHLNRVREEEEHA-----------FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLD 1349
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1350 EKEEAEGLRAHLEKEIhAARQGAGEARRKAEESVNQQLEELrKKNLRDVEHLQKQLEESEVAKERILQSK 1419
Cdd:COG4942 179 LLAELEEERAALEALK-AERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1173-1393 |
2.33e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1173 EEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKK 1252
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1253 RKIHEAHLMEIQANLAESDEHKRTLI-------DQLERSRDELDHLNRVREEEEHAFANMQRRLATaegQIQELNEQIQE 1325
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAA---LRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1326 ETRLKianinraRQLEDEKNALLDEKEEAEGLRAHLEKEIhAARQGAGEARRKAEESVNQQLEELRKK 1393
Cdd:COG4942 176 LEALL-------AELEEERAALEALKAERQKLLARLEKEL-AELAAELAELQQEAEELEALIARLEAE 235
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1032-1706 |
3.38e-09 |
|
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: 62.05 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1032 ENQLHELEQDLNRERQYKSEL----EQHKRKLLAELEDSKDHLAEKMGKVEELN--NQLMKRDEELQHQLTRYDEESANV 1105
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELqfenEKVSLKLEEEIQENKDLIKENNATRHLCNllKETCARSAEKTKKYEYEREETRQV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1106 TL-MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEK-VKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIE 1183
Cdd:pfam05483 185 YMdLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1184 QIQHtmegKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEK-----QQNQADQERADMAQEIALL---------QASRADI 1249
Cdd:pfam05483 265 ESRD----KANQLEEKTKLQDENLKELIEKKDHLTKELEDikmslQRSMSTQKALEEDLQIATKticqlteekEAQMEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1250 DKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRL 1329
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1330 kianINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKAEESVNQQLEELRKknlrDVEHLQKQLEESE 1409
Cdd:pfam05483 421 ----LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL-TAIKTSEEHYLKEVEDLKT----ELEKEKLKNIELT 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1410 VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKfesqmaeervavqkalldrdaMSQELRDRETRVLSLLNEV 1489
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---------------------MLKQIENLEEKEMNLRDEL 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1490 DIMKEHLEESdrvRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQiaedarlRLEVTNQAL 1569
Cdd:pfam05483 551 ESVREEFIQK---GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE-------ELHQENKAL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1570 KSESdrAISNKDVEAEEKRrgllkqIRDLENELENEKRGKSGAV-SHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQ 1648
Cdd:pfam05483 621 KKKG--SAENKQLNAYEIK------VNKLELELASAKQKFEEIIdNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1649 QIIKEYQIECEEA----RQAKEDIAALLREADRK---FRAVEAEREQLREANE--------GLMQARKQLELE 1706
Cdd:pfam05483 693 EIDKRCQHKIAEMvalmEKHKHQYDKIIEERDSElglYKNKEQEQSSAKAALEielsnikaELLSLKKQLEIE 765
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
26-69 |
3.86e-09 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 53.97 E-value: 3.86e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 25150354 26 RKLCWVPDQNEGFLIGSIKRETNDEVLVELvDTSRQVTISRDDV 69
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1335-1914 |
5.71e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1335 NRARQLEDEKNALLDEKEEAEGLRAHLEKEihaarqgAGEARRKAEESvnQQLEELRK-KNLRDVEHLQKQLEESEVAKE 1413
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARK-------AEEAKKKAEDA--RKAEEARKaEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1414 RILQSKKKIQQEledssmelenvrashRDSEKRQKKFESQMAEErvaVQKALLDRDAmsQELRDRETRVLSllnevdimk 1493
Cdd:PTZ00121 1158 RKAEDARKAEEA---------------RKAEDAKKAEAARKAEE---VRKAEELRKA--EDARKAEAARKA--------- 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1494 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE----LNDMRVQMEELEDNLQIAEDARLRLEVTNQAL 1569
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEeirkFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1570 KSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIEnqigELEQQLEVANRLKEEYNKQLKKNQQ 1649
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE----EAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1650 IIKEYQIECEEARQAKEDI---AALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKR 1726
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1727 RLEAkiAQLEEELEEEQSNCELAIDKQRKAQvqleqittdlSMERTLNQKTEAEKqsLERSNRDYKAKITELESGAQSRA 1806
Cdd:PTZ00121 1445 KADE--AKKKAEEAKKAEEAKKKAEEAKKAD----------EAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1807 RAQMAALEAKVQYLEDQLNVEgqEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1886
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580
....*....|....*....|....*...
gi 25150354 1887 MSRERTKHRNVQREADDLLDAnEQLTRE 1914
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKA-EEAKKA 1615
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
845-1127 |
6.07e-09 |
|
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: 61.61 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVN 924
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 925 DMRDRLSEEEQQNEKNNDERRKQMETV-------RDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLL 997
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIeslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 998 KEKRLLEEKVEGLTTQLLDHEERakhgvkaKGRLENQLHELEQDLNRErqYKSELE---QHKRKLLAELEDSKDHLAEKM 1074
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELR-------LEGLEVRIDNLQERLSEE--YSLTLEeaeALENKIEDDEEEARRRLKRLE 978
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1075 GKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTIDELREDME 1127
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYDF-------LTAQKEDLTEAKETLEEAIE 1024
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1193-1589 |
7.61e-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: 60.91 E-value: 7.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1193 IEEQKAKFSRQVEELHDQIEQhkkQRSQLEKQQNQADQERADMAQEIAllQASRADIDKKRKIHEAHlmeiqANLAESDE 1272
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQAAIYAEQ-----ERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1273 HKRTLIDQLERSRDeldhLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEEtrlkianinrarqLEDEKNALLDEKE 1352
Cdd:pfam17380 348 RELERIRQEERKRE----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQE-------------LEAARKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1353 eaeglrahlekeihaaRQGAGEARRKAEESVNQQLEELRKKNLRDVEhlqkqlEESEVAKERILQSKKKIQQELEdssme 1432
Cdd:pfam17380 411 ----------------RQRKIQQQKVEMEQIRAEQEEARQREVRRLE------EERAREMERVRLEEQERQQQVE----- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1433 lenvRASHRDSEKRQKKFESQmAEERVAVQKALLDRDAMSQELRDRETRVLsllnevdimkehleESDRVRRSLQQELQD 1512
Cdd:pfam17380 464 ----RLRQQEEERKRKKLELE-KEKRDRKRAEEQRRKILEKELEERKQAMI--------------EEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150354 1513 SisnkddfgKNVHELEKAKRSLEAElndmRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRR 1589
Cdd:pfam17380 525 R--------QKAIYEEERRREAEEE----RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1305-1656 |
1.40e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1305 MQRRLATAEGQIQELNEQIQEEtRLKIANINRARQLEDEKNalLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVN 1384
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-RLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1385 QqleELRKKNLRDVEHLQKQLEESEVAKERILQSKKkiQQELEDSSMELENVRASHRDSEKRQKKFESQMAE-ERVAVQK 1463
Cdd:pfam17380 355 Q---EERKRELERIRQEEIAMEISRMRELERLQMER--QQKNERVRQELEAARKVKILEEERQRKIQQQKVEmEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1464 alldrdamsQELRDRETRVLSLLNEVDIMKEHLEESDRvrrslQQELQDSISNKDDFGKNVHELEKAKRS-LEAELNDMR 1542
Cdd:pfam17380 430 ---------EEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELEKEKRDrKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1543 VQMEELEDNLQ-IAEDARLRLEVTNQAlkSESDRAIsnkdveAEEKRRGLLKQIRDLENELEnekrgksgavsHRKKIEN 1621
Cdd:pfam17380 496 ILEKELEERKQaMIEEERKRKLLEKEM--EERQKAI------YEEERRREAEEERRKQQEME-----------ERRRIQE 556
|
330 340 350
....*....|....*....|....*....|....*...
gi 25150354 1622 QI---GELEQQLEVANRlKEEYNKQLKKNQQIIKEYQI 1656
Cdd:pfam17380 557 QMrkaTEERSRLEAMER-EREMMRQIVESEKARAEYEA 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1313-1917 |
1.75e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 59.98 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1313 EGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELrk 1392
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKEL-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1393 KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQ-----MAEERVAVQKALLD 1467
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1468 RDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKR--SLEAELNDMRVQM 1545
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhTLTQHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1546 EELEDNLQI--AEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEkrgksgavshrkkIENQI 1623
Cdd:TIGR00618 389 TTLTQKLQSlcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT-------------AQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1624 GELEQQLEVANRLKEEyNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQL--REANEGLMQARK 1701
Cdd:TIGR00618 456 LEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1702 QLELENDELEELrAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEK 1781
Cdd:TIGR00618 535 QTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1782 QSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYledQLNVEGQEKTAANRAARRLEKRLNDTTQQFED----EKR 1857
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQkmqsEKE 690
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1858 ANEQAKELLEKSNLknrnLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMN 1917
Cdd:TIGR00618 691 QLTYWKEMLAQCQT----LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1509-1870 |
2.06e-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: 59.70 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1509 ELQDSISNKDDFGKnvhELEKAKRSLE-AELNDMRVQ--MEELEDNLQIAEDARLRLEvTNQALKSESdraisnKDVEAE 1585
Cdd:TIGR02169 157 KIIDEIAGVAEFDR---KKEKALEELEeVEENIERLDliIDEKRQQLERLRREREKAE-RYQALLKEK------REYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1586 EkrrgLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKN--------QQIIKEYQIE 1657
Cdd:TIGR02169 227 E----LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1658 CEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLmqarkqlELENDELEELRAKGGGISSEEKRRLEAKIAQLEE 1737
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1738 ELEEEQSncelAIDKQRKAQVQLEQITTDL-SMERTLNQKTEAEKQSLERSNR------DYKAKITELESGAQSrARAQM 1810
Cdd:TIGR02169 376 VDKEFAE----TRDELKDYREKLEKLKREInELKRELDRLQEELQRLSEELADlnaaiaGIEAKINELEEEKED-KALEI 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1811 AALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLND----------TTQQFEDEKRANEQAKELLEKSN 1870
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKlqrelaeaeaQARASEERVRGGRAVEEVLKASI 520
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
844-1406 |
2.86e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.08 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 844 LQVTRTDDEIRAKDDELR----ATKERLLKMEH--DFRENEKK--LDQVIVERAVIQEQL---QQESEN-SAELDDIRGR 911
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNgelsAADAAVAKDRSelEALEDQHGafLDADIETAAADQEQLpswQSELENlEERLKALTGK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 912 LQTRNQELEY----IVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEqaRQKLLLDKTNVDQRLRNLEERLV 987
Cdd:pfam12128 370 HQDVTAKYNRrrskIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLEAGKLEFNEEEYRLKSRLG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 988 ELQDAYDKLLKEKRLLEEKV----------EGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKR 1057
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLEnfderierarEEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1058 K-------LLAELEDSKDHLAEKMGKVeeLNNQLMKR--------DEELQHQLTRYdeeSANVTLMQKQMRDMQTTIDEL 1122
Cdd:pfam12128 528 QlfpqagtLLHFLRKEAPDWEQSIGKV--ISPELLHRtdldpevwDGSVGGELNLY---GVKLDLKRIDVPEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1123 REdmetERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSR 1202
Cdd:pfam12128 603 RE----RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1203 QVEELHDQIEQHKKQ-----RSQLEKQQNQADQERADMAQEIALLQASR--------ADIDKKRKIHEAHLMEIQA---- 1265
Cdd:pfam12128 679 SANERLNSLEAQLKQldkkhQAWLEEQKEQKREARTEKQAYWQVVEGALdaqlallkAAIAARRSGAKAELKALETwykr 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1266 ----------NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFA----NMQRRLATAEGQIQELNEQ---IQEETR 1328
Cdd:pfam12128 759 dlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQlarLIADTK 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1329 LKIANINRARQLEDEKNALLDEkeEAEGLRAHLEK--EIHAArQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLE 1406
Cdd:pfam12128 839 LRRAKLEMERKASEKQQVRLSE--NLRGLRCEMSKlaTLKED-ANSEQAQGSIGER-LAQLEDLKLKRDYLSESVKKYVE 914
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1277-1799 |
3.49e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1277 LIDQLERSRDELDHLNRVREEEEhafanmqRRLATAEGQIQELNEQIQEETRLKI---ANINRARQLEDEKNALLDEKEE 1353
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDE-------KSHSITLKEIERLSIEYNNAMDDYNnlkSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1354 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRkknlrDVEHLQKQLEEsevaKERILQSKKKIQQELEDSSMEL 1433
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-----DYFKYKNDIEN----KKQILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1434 ENVRASHRDSEKRQKKFEsqmaeervavqkallDRDAMSQELRDRETRVLSLLNEVDIMKEHLEE--------SDRVRRS 1505
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYD---------------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEyskniermSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1506 LQ-QELQDSISNK--DDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAE----------------DARLRLEVTN 1566
Cdd:PRK01156 397 LKiQEIDPDAIKKelNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeekSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1567 QALKSESD-RAISNKDVEAEEKRRGLLKQIRDLE----NELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYN 1641
Cdd:PRK01156 477 KKSRLEEKiREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1642 ---------KQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEE 1712
Cdd:PRK01156 557 slkledldsKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1713 LrakgggisSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYK 1792
Cdd:PRK01156 637 E--------IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILR 708
|
....*..
gi 25150354 1793 AKITELE 1799
Cdd:PRK01156 709 TRINELS 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1576-1812 |
4.10e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1576 AISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQ 1655
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1656 iecEEARQAKEDIAALLREAdrkFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGIsSEEKRRLEAKIAQL 1735
Cdd:COG4942 97 ---AELEAQKEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150354 1736 EEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAA 1812
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
926-1220 |
4.48e-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: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 926 MRDRLSEEEQQNEKNNDERRKQ-------METVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDA------ 992
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIenrldelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvks 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 993 -YDKLLKEKRLLEEKVEGLTTQLLDHEER-AKHGVKAKG-----------RLENQLHELEQDLNRERQYKSELEQHKRKL 1059
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1060 LAELEDSKDHLAEKMGKVEELNNQLMKRDEEL-QHQLTRYDEESANVTL------MQKQMRDMQTTIDELREDMETERNA 1132
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRLGDLkkerdeLEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1133 RNKAEMTRREV---VAQLEKVKGDVLDKVDEATMLQDLMSRKD---------EEVNAtkRAIEQIQHTME--GKIEEQKA 1198
Cdd:TIGR02169 919 LSELKAKLEALeeeLSEIEDPKGEDEEIPEEELSLEDVQAELQrveeeiralEPVNM--LAIQEYEEVLKrlDELKEKRA 996
|
330 340
....*....|....*....|..
gi 25150354 1199 KFSRQVEELHDQIEQHKKQRSQ 1220
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKRE 1018
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1372-1698 |
5.51e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 5.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1372 AGEARRKAEESVNQQLEELRKKNLRDVEhlQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQK--- 1448
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERyqa 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1449 ---KFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQ-----DSISNKDDF 1520
Cdd:PRK04863 356 dleELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQaleraKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1521 gkNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDrAISNKDveAEEKRRGLLKQIRDLEN 1600
Cdd:PRK04863 436 --TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAG-EVSRSE--AWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1601 ELENEKrgksgavshrkKIENQIGELEQQLEV---ANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADR 1677
Cdd:PRK04863 511 LAEQLQ-----------QLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340
....*....|....*....|.
gi 25150354 1678 KFRAVEAEREQLREANEGLMQ 1698
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAA 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
851-1321 |
7.31e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAE-LDDIRGR---LQTRNQELEYIVNDM 926
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREdADDLEERaeeLREEAAELESELEEA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 927 RDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEerlVELQDAYDKLLKEKRLLEEK 1006
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE---ATLRTARERVEEAEALLEAG 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1007 VEGLTTQLLDHEERakhgVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKL--LAELEDSKDHLAEKMGKVEELNNQL 1084
Cdd:PRK02224 453 KCPECGQPVEGSPH----VETIEEDRERVEELEAELEDLEEEVEEVEERLERAedLVEAEDRIERLEERREDLEELIAER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1085 MKRDEELQHQLTRYDEESanvtlmqkqmrdmqttiDELREDMETERNARNKAEM---TRREVVAQLEKVKGDVLDKVDEA 1161
Cdd:PRK02224 529 RETIEEKRERAEELRERA-----------------AELEAEAEEKREAAAEAEEeaeEAREEVAELNSKLAELKERIESL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1162 TMLQDLMSRKDEevnatkrAIEQIqhtmeGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEkqqNQADQERADMAQEial 1241
Cdd:PRK02224 592 ERIRTLLAAIAD-------AEDEI-----ERLREKREALAELNDERRERLAEKRERKRELE---AEFDEARIEEARE--- 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1242 lqasradidkKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEhAFANMQRRLATAEGQIQELNE 1321
Cdd:PRK02224 654 ----------DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE-ALENRVEALEALYDEAEELES 722
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
857-1308 |
8.12e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.15 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 857 DDELRATKErlLKM----EHDFRENEKKLDQVIVER-AVIQEQLQQESENSA---------ELDDIRGRLQtrnqELEYI 922
Cdd:PRK04778 47 NDELEKVKK--LNLtgqsEEKFEEWRQKWDEIVTNSlPDIEEQLFEAEELNDkfrfrkakhEINEIESLLD----LIEED 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 923 VNDMRDRLSEEEQQNEKNnderRKQMETVRDLEEQleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYdkllkekrl 1002
Cdd:PRK04778 121 IEQILEELQELLESEEKN----REEVEQLKDLYRE------LRKSLLANRFSFGPALDELEKQLENLEEEF--------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1003 leEKVEGLTTQLlDHEERAKHGVKakgrLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNn 1082
Cdd:PRK04778 182 --SQFVELTESG-DYVEAREILDQ----LEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLD- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1083 qLMKRDEELQHQLTRYDEESANVTL--MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDE 1160
Cdd:PRK04778 254 -IEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1161 ATMLQD---LMSRKDEEVNATKRAIEQIQHTME---GKIEEQKAKFS----------RQVEELHDQIEQHKKQRSQLEKQ 1224
Cdd:PRK04778 333 IDRVKQsytLNESELESVRQLEKQLESLEKQYDeitERIAEQEIAYSelqeeleeilKQLEEIEKEQEKLSEMLQGLRKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1225 QNQADQERADMAQEIALLqasradidkKRKIHEAHL----MEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEH 1300
Cdd:PRK04778 413 ELEAREKLERYRNKLHEI---------KRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATE 483
|
....*...
gi 25150354 1301 AFANMQRR 1308
Cdd:PRK04778 484 DVETLEEE 491
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
917-1325 |
8.15e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 57.17 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 917 QELEYIVNDMRDRLSEEEQQNEKNnderRKQMETVRDLEEQleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYDKL 996
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKN----REEVEELKDKYRE------LRKTLLANRFSYGPAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 997 lkekrlleekvEGLTTQLlDHEERAKHGVKakgrLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGK 1076
Cdd:pfam06160 166 -----------EELTESG-DYLEAREVLEK----LEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYA 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1077 VEELNnqLMKRDEELQHQLTRYDEESANVTL--MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdv 1154
Cdd:pfam06160 230 LEHLN--VDKEIQQLEEQLEENLALLENLELdeAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE--- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1155 ldkvDEATMLQDLMSRKDEEVNATKRAIEQIQhtmegKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERAD 1234
Cdd:pfam06160 305 ----EQNKELKEELERVQQSYTLNENELERVR-----GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1235 MAQEIALLQASRADIDKKRKiheahlmEIQANLAESDEHKRTLIDQLERSR------DELDHLNRVREEEEHAFA----- 1303
Cdd:pfam06160 376 IEEEQEEFKESLQSLRKDEL-------EAREKLDEFKLELREIKRLVEKSNlpglpeSYLDYFFDVSDEIEDLADelnev 448
|
410 420
....*....|....*....|....*..
gi 25150354 1304 --NM---QRRLATAEGQIQELNEQIQE 1325
Cdd:pfam06160 449 plNMdevNRLLDEAQDDVDTLYEKTEE 475
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
851-1257 |
1.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVI------QEQLQQESENSAELDDIRGRLQTRNQELEYIVN 924
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqlLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 925 DMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLE 1004
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1005 EK------------------VEGLTTQLLDHEER---------------AKHGVKAKGRLENQLHELEQDLNRERQYKSE 1051
Cdd:COG4717 241 LEerlkearlllliaaallaLLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1052 LEQHKRKLLAELEDSKDHLAEKMGKVEELnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERN 1131
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1132 ARNKaemtRREVVAQLEKVKGDVLDKVDEATmlqdlmsrkDEEVNAtkrAIEQIQHTMEgKIEEQKAKFSRQVEELHDQI 1211
Cdd:COG4717 400 LKEE----LEELEEQLEELLGELEELLEALD---------EEELEE---ELEELEEELE-ELEEELEELREELAELEAEL 462
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 25150354 1212 EQHKKQR--SQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHE 1257
Cdd:COG4717 463 EQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1109-1332 |
1.67e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1109 QKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQht 1188
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1189 meGKIEEQKAKFSRQVEELHDQIEQHKKQ-------------RSQLEKQQNQADQERAD-MAQEIALLQASRADIDKKRK 1254
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1255 iheahlmEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIA 1332
Cdd:COG4942 175 -------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
777-1408 |
1.89e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 777 LEEERDlKLTALIMNFQAQCRGFLSRRLYTRRQQQS--SAIRIIQRNGlaylKLRNWQWWRLFTKVKPLLQVTRTddeir 854
Cdd:pfam15921 262 LQQHQD-RIEQLISEHEVEITGLTEKASSARSQANSiqSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRS----- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 855 akddELRATKErllKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDirgrlqtrnqELEYIVNDMRDR---LS 931
Cdd:pfam15921 332 ----ELREAKR---MYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD----------QLQKLLADLHKRekeLS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 932 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKL-LLDKTNVDQRLRNLEERLVELQDAYDKLlkekrlleEKVEGL 1010
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLeALLKAMKSECQGQMERQMAAIQGKNESL--------EKVSSL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1011 TTQLLDHEErakhgvkakgrlenQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1090
Cdd:pfam15921 467 TAQLESTKE--------------MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1091 LQHQLTRYDE---ESANVTLMQKQMRDMQTTIDELREDMETE-----RNARNKAEMTRREvvAQLEKVKGDVLDKVDEAT 1162
Cdd:pfam15921 533 LQHLKNEGDHlrnVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgQHGRTAGAMQVEK--AQLEKEINDRRLELQEFK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1163 MLQDlmsRKDEEVNATKRAIEQiqhtmegkIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALL 1242
Cdd:pfam15921 611 ILKD---KKDAKIRELEARVSD--------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1243 qasradidKKRKIHEAHLMEIQANlaESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQ 1322
Cdd:pfam15921 680 --------KRNFRNKSEEMETTTN--KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1323 IQ--EETrlkIANINRARQ-LEDEKNALLDEKEEAEGLRAHLEKEIHAARQgagEARRKAEESVNQQLeELRKKNLRDVE 1399
Cdd:pfam15921 750 IQflEEA---MTNANKEKHfLKEEKNKLSQELSTVATEKNKMAGELEVLRS---QERRLKEKVANMEV-ALDKASLQFAE 822
|
650
....*....|..
gi 25150354 1400 H---LQKQLEES 1408
Cdd:pfam15921 823 CqdiIQRQEQES 834
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1209-1466 |
2.79e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1209 DQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEhkrtlidQLERSRDEL 1288
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1289 DHLNRVREEEEHAFANMQRRLataegqiQELNEQIQEETRLKIANINRA-RQLEDEKNALLDEKEEAEGLRAHLEkEIHA 1367
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL-------YRLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLA-ELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1368 ARQGAGEARRKAEESVNQQLEELRKknlrdvehLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQ 1447
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAA--------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*....
gi 25150354 1448 KKFESQMAEERVAVQKALL 1466
Cdd:COG4942 237 AAAAERTPAAGFAALKGKL 255
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1195-1799 |
3.85e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1195 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQEradmaqeiallqasradIDKKRKIHEAHLMEIQANLAESDEHK 1274
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENK-----------------LQENRKIIEAQRKAIQELQFENEKVS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1275 RTLIDQLERSRDELDHLNRVREeeehaFANMQRRLATAEGQIQELNEQIQEETRLKIANINRarQLEDEKNALLDEKEEA 1354
Cdd:pfam05483 134 LKLEEEIQENKDLIKENNATRH-----LCNLLKETCARSAEKTKKYEYEREETRQVYMDLNN--NIEKMILAFEELRVQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1355 EGLRAHLEKEIhaarqgagearrKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERIL--------QSKKKIQQEL 1426
Cdd:pfam05483 207 ENARLEMHFKL------------KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMkdltflleESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1427 EDSSMELENVRashrDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSL 1506
Cdd:pfam05483 275 EKTKLQDENLK----ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1507 QQELQDSISNKDDFGKNVHE-LEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVE-- 1583
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEki 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1584 ------AEEKRRGLL----KQIRDLENELENEKRGKSgavSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKE 1653
Cdd:pfam05483 431 aeelkgKEQELIFLLqareKEIHDLEIQLTAIKTSEE---HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1654 YQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKgggiSSEEKRRLEAKIA 1733
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK----SEENARSIEYEVL 583
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1734 QLEEELEEEQSNCELAIDKQRKAQVQLEQITTDlsmERTLNQKTEAEKQSLERsnrdYKAKITELE 1799
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQE---NKALKKKGSAENKQLNA----YEIKVNKLE 642
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1192-1382 |
3.93e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1192 KIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQAsraDIDKKRKIHEAHLMEIQAN----- 1266
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERARALYRSggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1267 ----LAESDE-----HKRTLIDQL-ERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINR 1336
Cdd:COG3883 104 yldvLLGSESfsdflDRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 25150354 1337 ARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEES 1382
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
625-680 |
5.38e-07 |
|
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: 51.58 E-value: 5.38e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 625 AEFAGICAAEMNETAfgmrSRKG-MFRTV-----SQLHKEQLTKLMTTLRNTSPHFVRCIIP 680
Cdd:cd01363 113 LEAFGNAKTTRNENS----SRFGkFIEILldiagFEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
851-1199 |
5.66e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.74 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 851 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQvivERAVIQEQLQQESENSAELDDIRgrLQTRNQELEYIvndmrdRL 930
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDR---QAAIYAEQERMAMERERELERIR--QEERKRELERI------RQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 931 SEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvdQRLRNLEERLVELQDAydkllkekRLLEEKVEGL 1010
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQI--------RAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1011 TTQLLDhEERAKHGVKAKgrlenqLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEkmgkveELNNQLMkrDEE 1090
Cdd:pfam17380 436 EVRRLE-EERAREMERVR------LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE------EQRRKIL--EKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1091 LQHQLTRYDEESANVTLMQKQMRDMQTTIDELREdmeternaRNKAEMTRREVVaqlekvkgdvldKVDEATMLQDLMsR 1170
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--------RREAEEERRKQQ------------EMEERRRIQEQM-R 559
|
330 340
....*....|....*....|....*....
gi 25150354 1171 KDEEVNATKRAIEQIQHTMEGKIEEQKAK 1199
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1401-1918 |
5.88e-07 |
|
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: 54.64 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1401 LQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAE----------ERVAVQKALLDRDA 1470
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqknidkiknKLLKLELLLSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1471 MSQELRDRETRVLSLLNEVDIMKEHLEES-----------DRVRRSLQQELQDSISNKDDFGKNVHELEKAKR---SLEA 1536
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKqqeinektteiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1537 ELNDMRVQMEELEDNLQiaedarlrlEVTNQALKSESDRaISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHR 1616
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKE---------QDWNKELKSELKN-QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1617 KKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGL 1696
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1697 MQARKQLElendeleelrakgggissEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQK 1776
Cdd:TIGR04523 439 NSEIKDLT------------------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1777 TEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAAN--RAARRLEKRLNDTTQQFED 1854
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKE-KIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKS 579
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1855 EKRANEQAKELLEKSNLKNRNLRRQLDEAEdemsrerTKHRNVQREADDLLDANEQLTRELMNL 1918
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
975-1181 |
5.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 975 VDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSEL-- 1052
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1053 ------EQHKRKLLAELEDSKDhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDM 1126
Cdd:COG4942 112 alyrlgRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1127 ETERNARNKaemTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRA 1181
Cdd:COG4942 191 EALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1062-1288 |
7.50e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 7.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1062 ELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMEternaRNKAEMTRR 1141
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE-----ERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1142 EVVAQLEKVKGDVLDKVDEATMLQDLMSRkdeeVNATKRAIEQIQhtmegkieeqkakfsrqveelhDQIEQHKKQRSQL 1221
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADA----------------------DLLEELKADKAEL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25150354 1222 EKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEL 1288
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1039-1347 |
1.28e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1039 EQDLNRERQYKSELEQHKRKLLA----ELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTR-YDEESANVTLMQKQMR 1113
Cdd:pfam05667 196 AQPSSRASVVPSLLERNAAELAAaqewEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSaALAGTEATSGASRSAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1114 DMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKI 1193
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQ-EL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1194 EEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQadqeradMAQEIALLQASRADIDKKRKIHEAhLMEIQANLA-ESDE 1272
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELEELKEQNEELEKQYKV-------KKKTLDLLPDAEENIAKLQALVDA-SAQRLVELAgQWEK 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1273 HKRTLIDQLERSRDELDHlnrvREEEEhafanmQRRLAtaegQIQELNEQIQ---EETRLKIANInraRQLEDEKNAL 1347
Cdd:pfam05667 427 HRVPLIEEYRALKEAKSN----KEDES------QRKLE----EIKELREKIKevaEEAKQKEELY---KQLVAEYERL 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1026-1303 |
1.36e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1026 KAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdeelqhqltrydeesanv 1105
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1106 TLMQKQMRDMQTTIDELREDMEternaRNKAEMTRREVVAQlekvkgdvldKVDEATMLQDLMSRKDeeVNATKRAIEQI 1185
Cdd:COG4942 79 AALEAELAELEKEIAELRAELE-----AQKEELAELLRALY----------RLGRQPPLALLLSPED--FLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1186 QHTMEgkieeqkakfsrqveELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQA 1265
Cdd:COG4942 142 KYLAP---------------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 25150354 1266 NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFA 1303
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
870-1274 |
1.48e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 870 MEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQME 949
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 950 ----------TVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEE 1019
Cdd:pfam05483 441 lifllqarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1020 RAKHGVKAKGRLENQLHELEQdlnRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYD 1099
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1100 EESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVK---GDVLD---------KVDEATMLQDL 1167
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfEEIIDnyqkeiedkKISEEKLLEEV 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1168 MSRK---DEEVNATKRAIEQIQHT---MEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIAL 1241
Cdd:pfam05483 678 EKAKaiaDEAVKLQKEIDKRCQHKiaeMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
410 420 430
....*....|....*....|....*....|...
gi 25150354 1242 LQaSRADIDKKRKihEAHLMEIQANLAESDEHK 1274
Cdd:pfam05483 758 LK-KQLEIEKEEK--EKLKMEAKENTAILKDKK 787
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1137-1559 |
1.55e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1137 EMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKA---KFSRQVEELHDQIEQ 1213
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRdreQWERQRRELESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1214 HKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNR 1293
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1294 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEkeihAARQGAG 1373
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE----ALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1374 EARRKAEESvnQQLEELRKKNLRDVEHLQKQlEESEVAKERILQSKKKIQqeLEDSSMELENVRAshRDSEKRQKKFES- 1452
Cdd:pfam07888 241 SLQERLNAS--ERKVEGLGEELSSMAAQRDR-TQAELHQARLQAAQLTLQ--LADASLALREGRA--RWAQERETLQQSa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1453 QMAEERVAVQKA-LLDRDAMSQELR-DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhELEKA 1530
Cdd:pfam07888 314 EADKDRIEKLSAeLQRLEERLQEERmEREKLEVELGREKDCNRVQLSESRRELQELKASLR--------------VAQKE 379
|
410 420
....*....|....*....|....*....
gi 25150354 1531 KRSLEAELNDMRVQMEELEDNLQIAEDAR 1559
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
977-1415 |
1.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 977 QRLRNLEERLVELQD---AYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlenQLHELEQDLNRERQYKSELE 1053
Cdd:COG4717 71 KELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1054 QHKRKLLAELEDskdhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEEsanvtlMQKQMRDMQTTIDELREDMETERNAR 1133
Cdd:COG4717 146 ERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1134 NKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKdeeVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQ 1213
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1214 HKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAEsdehkrtlIDQLERSRDELDHLNR 1293
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE--------LQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1294 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKianiNRARQLEDEKNALLDEKEEAegLRAHLEKEIHAARQGAG 1373
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK----EELEELEEQLEELLGELEEL--LEALDEEELEEELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 25150354 1374 EARRKAEESVNQQLEELRK-----KNLRDVEHLQKQLEESEVAKERI 1415
Cdd:COG4717 439 EELEELEEELEELREELAEleaelEQLEEDGELAELLQELEELKAEL 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1354-1868 |
1.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1354 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1433
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1434 ENVRA--SHRDSEKRQKKFESQMAEERVAVQKALLDRdamsQELRDRETRVLSLLNEVDIMKEHLEES-DRVRRSLQQEL 1510
Cdd:COG4717 119 EKLEKllQLLPLYQELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELlEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1511 QDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARlRLEVTNQALKSESDRAISNKDVEAEEKRRG 1590
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1591 LLKQIRDLENELenekrgKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLkknQQIIKEYQIECEEARQAKEDIAA 1670
Cdd:COG4717 274 TIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1671 LLREADRKFRAVEAEREQLREanEGLMQARKQLELEndeleelrakgGGISSEEKRRLEAKIAQLEEELEEEQSNCELAI 1750
Cdd:COG4717 345 RIEELQELLREAEELEEELQL--EELEQEIAALLAE-----------AGVEDEEELRAALEQAEEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1751 DKQRKAQVQLEQITTDLSMERTLNQkTEAEKQSLERSNRDYKAKITELESG-AQSRARAQMAALEAKVQYLEDQLNvEGQ 1829
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREELAELEAElEQLEEDGELAELLQELEELKAELR-ELA 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 25150354 1830 EKTAANRAARRLekrLNDTTQQFEDEKRA--NEQAKELLEK 1868
Cdd:COG4717 490 EEWAALKLALEL---LEEAREEYREERLPpvLERASEYFSR 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1372-1691 |
2.36e-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: 53.03 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1372 AGEARRKAEESVNQQLEELRKKNLRDVEH-----LQKQLEESEvAKERILQskkkiqQELEDSSMELENVRASHRDSEK- 1445
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQyrlveMARELEELS-ARESDLE------QDYQAASDHLNLVQTALRQQEKi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1446 --RQKKFESqmAEERVAVQKALldRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrvrrsLQQELQDSISNKDDFGKN 1523
Cdd:COG3096 350 erYQEDLEE--LTERLEEQEEV--VEEAAEQLAEAEARLEAAEEEVDSLKSQLAD-------YQQALDVQQTRAIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1524 VHELEKAKR----------SLEAELNDMRVQME-------ELEDNLQIAEDARLRLEVTNQALKS---ESDRAisnkdvE 1583
Cdd:COG3096 419 VQALEKARAlcglpdltpeNAEDYLAAFRAKEQqateevlELEQKLSVADAARRQFEKAYELVCKiagEVERS------Q 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1584 AEEKRRGLLKQIRDLENELENEKrgksgavshrkKIENQIGELEQQLEV---ANRLKEEYNKQLKKNQQIIKEYQIECEE 1660
Cdd:COG3096 493 AWQTARELLRRYRSQQALAQRLQ-----------QLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350
....*....|....*....|....*....|.
gi 25150354 1661 ARQAKEDIAALLREADRKFRAVEAEREQLRE 1691
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
969-1512 |
3.47e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.06 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 969 LLDKTNVDQRLRnLEERLVELqdayDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRlenqlhELEQDLNRERQY 1048
Cdd:pfam07111 84 LLRETSLQQKMR-LEAQAMEL----DALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQR------ELEEIQRLHQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1049 KSELEQHKRKLLAELEDSKDHL--------AEKMGKVEELNnQLMKRDEELQHQLTRYDEE-SANVTLMQKQMRdmqtti 1119
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLekslnsleTKRAGEAKQLA-EAQKEAELLRKQLSKTQEElEAQVTLVESLRK------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1120 dELREDMETERNaRNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQ-------DLMSRKDEEVNATKRAIEQIQHTMEGK 1192
Cdd:pfam07111 226 -YVGEQVPPEVH-SQTWELERQELLDTMQHLQEDRADLQATVELLQvrvqsltHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1193 IEEQKAKFSRQVEELHDQIE----QHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLA 1268
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKaqdlEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1269 ESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETR------------LKIANIN- 1335
Cdd:pfam07111 384 RAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRkvhtikglmarkVALAQLRq 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1336 ------------------RARQLEDEKNALLDEKEeaegLRAHL-EKEIHAARQgAGEARRKAEESVNQQLEELRKKNLR 1396
Cdd:pfam07111 464 escpppppappvdadlslELEQLREERNRLDAELQ----LSAHLiQQEVGRARE-QGEAERQQLSEVAQQLEQELQRAQE 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1397 DVEHLQKQL-----------EESEVAKERILQSKKKIQQELEDSSMELEN-VRASHRDSEKRQKKFESQMAEERVAVQKa 1464
Cdd:pfam07111 539 SLASVGQQLevarqgqqestEEAASLRQELTQQQEIYGQALQEKVAEVETrLREQLSDTKRRLNEARREQAKAVVSLRQ- 617
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 25150354 1465 lLDRDAMSQELRDRETRVLSllnevdiMKEHLEESDRVRRSLQQELQD 1512
Cdd:pfam07111 618 -IQHRATQEKERNQELRRLQ-------DEARKEEGQRLARRVQELERD 657
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1238-1696 |
3.78e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1238 EIALLQASRadiDKKRKIHEaHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLataegqiq 1317
Cdd:pfam05557 8 KARLSQLQN---EKKQMELE-HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1318 elneqiqEETRLKIANINRARQLEDEKNALLdekEEAEGLRAHLEKEIHAARQGAG------EARRKAEESVNQQLEELR 1391
Cdd:pfam05557 76 -------ELNRLKKKYLEALNKKLNEKESQL---ADAREVISCLKNELSELRRQIQraelelQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1392 KK--NLRDV-EHLQKQLEESEVAKERILQSKKKIQQElEDSSMELENVR---ASHRDSEKRQKKFESQMA---------- 1455
Cdd:pfam05557 146 AKasEAEQLrQNLEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKselARIPELEKELERLREHNKhlnenienkl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1456 --EERVAVQKALLDRDAMSQE----LRDRETRVLSLLNE-VDIMKEH---LEESDRVRRSLQQELQDSISNKD---DFGK 1522
Cdd:pfam05557 225 llKEEVEDLKRKLEREEKYREeaatLELEKEKLEQELQSwVKLAQDTglnLRSPEDLSRRIEQLQQREIVLKEensSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1523 NVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESD--RAI---SNKDVEAEEKRRGLLKQIRD 1597
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyRAIlesYDKELTMSNYSPQLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1598 LENELEnekrgksgavshrkKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIK--EYQIECEEARQAKEDIAALLREA 1675
Cdd:pfam05557 385 AEDMTQ--------------KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQalRQQESLADPSYSKEEVDSLRRKL 450
|
490 500
....*....|....*....|.
gi 25150354 1676 DRkfraVEAEREQLREANEGL 1696
Cdd:pfam05557 451 ET----LELERQRLREQKNEL 467
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
979-1375 |
3.79e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 979 LRNLEERLVELQDAydkLLKEKRLLEEKvegltTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELE---QH 1055
Cdd:COG3096 274 MRHANERRELSERA---LELRRELFGAR-----RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1056 KRKL---LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTIDEL-------RED 1125
Cdd:COG3096 346 QEKIeryQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-------LKSQLADYQQALDVQqtraiqyQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1126 METERNARN----------KAEMTRREVVAQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQIQhTMEGKIEE 1195
Cdd:COG3096 419 VQALEKARAlcglpdltpeNAEDYLAAFRAKEQQATEEVLE-------LEQKLSVADAARRQFEKAYELVC-KIAGEVER 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1196 QKAkFSRQVEELHD------------QIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIdkkrkihEAHLMEI 1263
Cdd:COG3096 491 SQA-WQTARELLRRyrsqqalaqrlqQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL-------EELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1264 QANLAESDEHKRTLIDQLERSRDELDHLNRVREEeehafanmQRRLATAEGQIQELNEQIQEETRLKIANIN-----RAR 1338
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE--------LAARAPAWLAAQDALERLREQSGEALADSQevtaaMQQ 634
|
410 420 430
....*....|....*....|....*....|....*..
gi 25150354 1339 QLEDEKNALLdEKEEAEGLRAHLEKEIHAARQGAGEA 1375
Cdd:COG3096 635 LLEREREATV-ERDELAARKQALESQIERLSQPGGAE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
855-1064 |
4.01e-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: 51.30 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 855 AKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQeseNSAELDDIRGRLQTRNQELEYIVNDMRdRLSEEE 934
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQELAALEAELA-ELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 935 QQNEKNNDERRKQMETVrdLEEQLEQEEQARQKLLLDKTNVDQRLRNLE----------ERLVELQDAYDKLLKEKRLLE 1004
Cdd:COG4942 93 AELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1005 EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELE 1064
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1089-1429 |
5.35e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.59 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1089 EELQHQLTRYDEESANvtlmQKQMRDMQTTID-------ELREDMETERN--ARNKAEMTRREVVAQLEKVKGDVLDKV- 1158
Cdd:PRK10929 48 EALQSALNWLEERKGS----LERAKQYQQVIDnfpklsaELRQQLNNERDepRSVPPNMSTDALEQEILQVSSQLLEKSr 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1159 ------DEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGK-----IEEQKAKFSRQVEELhdqieQHKKQRSQLEKQQNQ 1227
Cdd:PRK10929 124 qaqqeqDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLgtpntPLAQAQLTALQAESA-----ALKALVDELELAQLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1228 AD--QERADMAQEI---------ALLQASRADIDKKRKiHEAHL-MEIQANLAE-SDEHKRTLIDQLERSRDELDHLNRv 1294
Cdd:PRK10929 199 ANnrQELARLRSELakkrsqqldAYLQALRNQLNSQRQ-REAERaLESTELLAEqSGDLPKSIVAQFKINRELSQALNQ- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1295 reeeehafaNMQRRLATAEGQIQELNEQIQeeTRLKIANINRARQLEDEKNALldekeeAEGLRAHLEkeihaarqgage 1374
Cdd:PRK10929 277 ---------QAQRMDLIASQQRQAASQTLQ--VRQALNTLREQSQWLGVSNAL------GEALRAQVA------------ 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150354 1375 arRKAEESVNQQLE----ELRKKNLRDVEHLQKQLEESEV----------AKERILQSKKKIQQELEDS 1429
Cdd:PRK10929 328 --RLPEMPKPQQLDtemaQLRVQRLRYEDLLNKQPQLRQIrqadgqpltaEQNRILDAQLRTQRELLNS 394
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
857-1284 |
8.37e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 857 DDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESEnsaELDDIRGRLQTRNQELEYIVNDmrdrLSEEEQQ 936
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK---EIPELRNKLQKVNRDIQRLKND----IEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 937 NEKNNDERRKQMETVRD--------LEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKE----KRLLE 1004
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDvtimerfqMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1005 EKVEGL------TTQLLDHEERAKHGVKAKGRLENQLHELE---QDLNRE----RQYKSELEQHKRKLLAELEDSKdHLA 1071
Cdd:TIGR00606 854 DQQEQIqhlkskTNELKSEKLQIGTNLQRRQQFEEQLVELStevQSLIREikdaKEQDSPLETFLEKDQQEKEELI-SSK 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1072 EKMGKVEELNNQLMKRDEELQH----QLTRYDEESANVTLMQK---------QMRDMQTTIDELREDMETERNARNKAEM 1138
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHgymkDIENKIQDGKDDYLKQKetelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1139 TRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQR 1218
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID-LIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1219 SqlEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQanlAESDEHKRTLIDQLERS 1284
Cdd:TIGR00606 1092 R--EPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH---SMKMEEINKIIRDLWRS 1152
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
930-1434 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 930 LSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDktnvdqRLRNLEERLVELQDAYDKLLKEKRLLEEKVEG 1009
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQK------RIRLLEKREAEAEEALREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1010 LTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDE 1089
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1090 ------ELQHQLTRYDEESANVTLMQK---QMRDMQTTIDELREDMETERNARNKAEMTRREVvAQLEKVKGDVLDKVDE 1160
Cdd:pfam05557 168 aeqrikELEFEIQSQEQDSEIVKNSKSelaRIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYREE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1161 ATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEeqkakFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIA 1240
Cdd:pfam05557 247 AATLELEKEKLEQELQSWVKLAQDTGLNLRSPED-----LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1241 LLQASRADIDKKRKIHEAHLMEIQ--------------ANLAESD------EHKRTLIDQLERSRDELDHLNRVREEEEH 1300
Cdd:pfam05557 322 QYLKKIEDLNKKLKRHKALVRRLQrrvllltkerdgyrAILESYDkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1301 AFANMQR-------RLATAEGQIQELNEQIQ-----------EETRLKIANINRARQ-LEDEKNALLDEKEEAEgLRAHL 1361
Cdd:pfam05557 402 QLSVAEEelggykqQAQTLERELQALRQQESladpsyskeevDSLRRKLETLELERQrLREQKNELEMELERRC-LQGDY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1362 EKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1434
Cdd:pfam05557 481 DPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1470-1717 |
1.27e-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: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1470 AMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELE 1549
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1550 DNLQIAEDARLRLEVTNQALKSESDRAI--SNKDVEAEEKRRGLLKQIRDLENELENEkrgksgavshrkkIENQIGELE 1627
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEE-------------LRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1628 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN 1707
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|
gi 25150354 1708 DELEELRAKG 1717
Cdd:COG4942 244 PAAGFAALKG 253
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1479-1722 |
1.48e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1479 ETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLqiaeDA 1558
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1559 RLRLEVTNQALKSESDRAISNKDVEA-----------EEKRRGLLKQIRDLENELENEKrgksgavshrKKIENQIGELE 1627
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESFSDfldrlsalskiADADADLLEELKADKAELEAKK----------AELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1628 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN 1707
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250
....*....|....*
gi 25150354 1708 DELEELRAKGGGISS 1722
Cdd:COG3883 241 AAAASAAGAGAAGAA 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1367-1592 |
1.49e-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: 49.38 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1367 AARQGAGEARRKAEESVNQQLEELRK---KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDS 1443
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKelaALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1444 EKRQKKFESQMAEERVAVQKA--------LLDRDAMSQELRDRE---TRVLSLLNEVDIMKEHLEESDRVRRSLQQELQD 1512
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1513 SISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLL 1592
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
879-1673 |
1.54e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 879 KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQ------------QNEKNNDERRK 946
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldvqqtraiqyQQAVQALERAK 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 947 QMETVRDLEEQLEQEEQARQKLLLDKtnVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLT--------TQLLDHE 1018
Cdd:PRK04863 428 QLCGLPDLTADNAEDWLEEFQAKEQE--ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvaRELLRRL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1019 ERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDhlaekmgkVEELNNQLMKRDEELQHQLTRY 1098
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE--------LEQLQEELEARLESLSESVSEA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1099 DEESanvTLMQKQMRDMQTTIDELRedmeternARNKAEMTRREVVAQLEKVKGdvlDKVDEATMLQDLMSRKDEEVNAT 1178
Cdd:PRK04863 578 RERR---MALRQQLEQLQARIQRLA--------ARAPAWLAAQDALARLREQSG---EEFEDSQDVTEYMQQLLEREREL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1179 KRAIEQiqhtmegkIEEQKAKFSRQVEELHdqieqhkkQR--SQLEKQQNQADQERADMAQEI-------------ALLQ 1243
Cdd:PRK04863 644 TVERDE--------LAARKQALDEEIERLS--------QPggSEDPRLNALAERFGGVLLSEIyddvsledapyfsALYG 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1244 ASRADI------DKKRK------------IHEAHLMEIQANLAESDEHKRTLIDQL-----------------ERSRDE- 1287
Cdd:PRK04863 708 PARHAIvvpdlsDAAEQlagledcpedlyLIEGDPDSFDDSVFSVEELEKAVVVKIadrqwrysrfpevplfgRAAREKr 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1288 LDHLNRVREEEehafanmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEknallDEKEEAEGLRAHLEKEIHA 1367
Cdd:PRK04863 788 IEQLRAEREEL-------AERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPE-----AELRQLNRRRVELERALAD 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1368 ARQGAGEARRKAEESVN--QQLEELRKK-NLRDVEHLQKQLEESEVAKERILQSKKKIQQElEDSSMELENVRASHRDSe 1444
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEglSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRFVQQH-GNALAQLEPIVSVLQSD- 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1445 krqkkfESQMAEERVAVQKALLDRDAMSQELRDretrvlslLNEVDIMKEHLEESDRVRR-SLQQELQDSISNKddfgkn 1523
Cdd:PRK04863 934 ------PEQFEQLKQDYQQAQQTQRDAKQQAFA--------LTEVVQRRAHFSYEDAAEMlAKNSDLNEKLRQR------ 993
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1524 vheLEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKsESDRAISNKDVEAEEkrrGLLKQIRDLENELE 1603
Cdd:PRK04863 994 ---LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ-ELKQELQDLGVPADS---GAEERARARRDELH 1066
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1604 NEKRgksgavSHRKKIEnqigELEQQLEVANRLKEEYNKQLKKNQqiiKEYQIECEEARQAKEDIAALLR 1673
Cdd:PRK04863 1067 ARLS------ANRSRRN----QLEKQLTFCEAEMDNLTKKLRKLE---RDYHEMREQVVNAKAGWCAVLR 1123
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1193-1437 |
1.73e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1193 IEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQER--ADMAQEIALLQASRADIDKKrkiheahLMEIQANLAES 1270
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQ-------LAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1271 DEHKRTLIDQLERSRDELDHLNrvreeEEHAFANMQRRLATAEGQIQELNEQIQEETRlkianinRARQLEDEKNALLDE 1350
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHP-------DVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 -KEEAEGLRAHLEKEIHAARQgagearrkAEESVNQQLEELRKKNLRDVEHLQKQLE---ESEVAKERILQSKKKIQQEL 1426
Cdd:COG3206 307 lQQEAQRILASLEAELEALQA--------REASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 25150354 1427 EDSSMELENVR 1437
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1351-1579 |
1.78e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEKEihAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLEES---------EVAKERILQSKKK 1421
Cdd:NF012221 1541 SQQADAVSKHAKQD--DAAQNALADKERAEAD-RQRLEQEKQQQLAAISGSQSQLESTdqnaletngQAQRDAILEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1422 IQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVA-VQKALLDRDAMSQE-LRDRETRVLSLLNEVdimKEHLEES 1499
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDrVQEQLDDAKKISGKqLADAKQRHVDNQQKV---KDAVAKS 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1500 DR-VRRS--LQQELQDSISNKddfgknvhELEKAKRSLEAELNDMRVQMEELEDNLqIAEDARLRLEVTNQALKSESDRA 1576
Cdd:NF012221 1695 EAgVAQGeqNQANAEQDIDDA--------KADAEKRKDDALAKQNEAQQAESDANA-AANDAQSRGEQDASAAENKANQA 1765
|
...
gi 25150354 1577 ISN 1579
Cdd:NF012221 1766 QAD 1768
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
892-1226 |
1.94e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 892 QEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQAR-----Q 966
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNskdgeQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 967 KLLLDKTNVDQRLRNLEE--------RLVELQDAyDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGR-------L 1031
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKnilllnqaRLQALEDL-EKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHveileeqL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1032 ENQLHELEQDLNRERQYKSELEQHKRKLLAE---LEDSKDHLAEKMGKVEELNNQLMKRDEELqhqltrydeesanvTLM 1108
Cdd:PLN02939 204 EKLRNELLIRGATEGLCVHSLSKELDVLKEEnmlLKDDIQFLKAELIEVAETEERVFKLEKER--------------SLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1109 QKQMRDMQTTIDELREDMETERNARNKAEMtrrEVVAQLEKVKGDVLDKVDEATML----QDLMSRKD------EEVNAT 1178
Cdd:PLN02939 270 DASLRELESKFIVAQEDVSKLSPLQYDCWW---EKVENLQDLLDRATNQVEKAALVldqnQDLRDKVDkleaslKEANVS 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 25150354 1179 KRAIEQIQhTMEGKIEEQKAKFSRQVEELHDQIEQHkkQRSQLEKQQN 1226
Cdd:PLN02939 347 KFSSYKVE-LLQQKLKLLEERLQASDHEIHSYIQLY--QESIKEFQDT 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
864-1289 |
2.18e-05 |
|
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: 49.63 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 864 KERLLKMEHDFRENEKKLDQVIVERAVIQEQL---QQESE-NSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEK 939
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEqNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 940 NNDERRKQMET-VRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHE 1018
Cdd:TIGR04523 318 NQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1019 ERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRY 1098
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1099 DEESANVTLMQKQMRDMQTTIDELredmeternarNKAEMTRREVVAQLEKVKGDVLDKVDEatmLQDLMSRKDEEVNAT 1178
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKL-----------NEEKKELEEKVKDLTKKISSLKEKIEK---LESEKKEKESKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1179 KRAIEQIQHTME-GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHE 1257
Cdd:TIGR04523 544 EDELNKDDFELKkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
410 420 430
....*....|....*....|....*....|..
gi 25150354 1258 AHLMEIQANLAESDEHKRTLIDQLERSRDELD 1289
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1473-1891 |
2.30e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1473 QELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL 1552
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1553 QI---AEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQ 1629
Cdd:COG4717 156 EElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1630 LEVANRlkeeyNKQLKKNQQIIK---------EYQIECEEARQAKEDIAALL----------READRKFRAVEAEREQLR 1690
Cdd:COG4717 236 LEAAAL-----EERLKEARLLLLiaaallallGLGGSLLSLILTIAGVLFLVlgllallfllLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1691 EANEGLMQAR----KQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTD 1766
Cdd:COG4717 311 PALEELEEEEleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1767 LSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEK--R 1844
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 25150354 1845 LNDTTQQFEDEKRANEQakelLEKSNLKNRNLRRQLDEAEDEMSRER 1891
Cdd:COG4717 471 LAELLQELEELKAELRE----LAEEWAALKLALELLEEAREEYREER 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1203-1394 |
2.48e-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: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1203 QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQAnlaesdehkrtlidQLE 1282
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA--------------RIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1283 RSRDELDHLNRVREEE--EHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINraRQLEDEKNALLDEKEEAEGLRAH 1360
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalQKEIESLKRRISDLEDEILELMERI-EELEEELAELE--AELAELEAELEEKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|....
gi 25150354 1361 LEKEIHAARQGAGEARRKAEESVNQQLEELRKKN 1394
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELLALYERIRKRK 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1413-1922 |
2.52e-05 |
|
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: 49.25 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1413 ERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMaEERVAVQKALLDRDAMSQELRDRETRVLSLLN-EVDI 1491
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKI-KILEQQIKDLNDKLKKNKDKINKLNSDLSKINsEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1492 MKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKS 1571
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1572 EsdRAISNKD----VEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKN 1647
Cdd:TIGR04523 195 K--LLKLELLlsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1648 QQIIkeyqieceearqakEDIAALLREADRKFRAVEAEREQLR-EANEGLMQARKQLELENDeleelrakgggissEEKR 1726
Cdd:TIGR04523 273 QKEL--------------EQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELKNQE--------------KKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1727 RLEAKIAQLEEELeeeqSNCELAIDKQRKAQVQLEqiTTDLSMERTLNQKtEAEKQSLERSNRDYKAKITELESGAQSrA 1806
Cdd:TIGR04523 325 EIQNQISQNNKII----SQLNEQISQLKKELTNSE--SENSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQIND-L 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1807 RAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1886
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 25150354 1887 MSRERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1922
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
845-1031 |
2.56e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAEL------------------- 905
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 906 DDIrGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEER 985
Cdd:COG4942 129 EDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25150354 986 LVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHG--VKAKGRL 1031
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALKGKL 255
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1060-1549 |
3.41e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 48.92 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1060 LAELEDSKDHLAEK-------MGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNA 1132
Cdd:pfam05622 2 LSEAQEEKDELAQRcheldqqVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1133 RNKAEMTrrevVAQLEKVKGDVLDKVDEATMLQdlmsrkdEEVNATKRAIEQIQHTME--GKIEEQKAKFSRQVEELHDQ 1210
Cdd:pfam05622 82 RDDYRIK----CEELEKEVLELQHRNEELTSLA-------EEAQALKDEMDILRESSDkvKKLEATVETYKKKLEDLGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1211 ieqhKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDK-KRKIHEAHLM----------------EIQANLAESDEH 1273
Cdd:pfam05622 151 ----RRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETyKRQVQELHGKlseeskkadklefeykKLEEKLEALQKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1274 KRTLI---DQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNalldE 1350
Cdd:pfam05622 227 KERLIierDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGS----Y 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEkEIHAARQGAGEARRKAeesvNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDsS 1430
Cdd:pfam05622 303 RERLTELQQLLE-DANRRKNELETQNRLA----NQRILELQQQ----VEELQKALQEQGSKAEDSSLLKQKLEEHLEK-L 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1431 MELENVRASHRDS-EKRQKKFESQMAEERVAVQKALLDRDamsQELRDRETRvlsllnevdiMKEHLEESDRVRRSLQQE 1509
Cdd:pfam05622 373 HEAQSELQKKKEQiEELEPKQDSNLAQKIDELQEALRKKD---EDMKAMEER----------YKKYVEKAKSVIKTLDPK 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 25150354 1510 LQDSISNKDDFGKN-VHELEKAKRSLEAELNDMRVQMEELE 1549
Cdd:pfam05622 440 QNPASPPEIQALKNqLLEKDKKIEHLERDFEKSKLQREQEE 480
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
879-1305 |
5.62e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 879 KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKnnDERRKQMETVRDLEEQL 958
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 959 EQEEQARQKLLLDKTNVDQRLRNLEERLVELQDaYDKLLKEKRL--LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLH 1036
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLE-QLSLATEEELqdLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1037 ELEQDLNRERQYKsELEQHKRKLLA-------------------------------------ELEDSKDHLAEKMGKVEE 1079
Cdd:COG4717 231 QLENELEAAALEE-RLKEARLLLLIaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1080 LNNQLMKRDEELQHQLTRYD-EESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvldkv 1158
Cdd:COG4717 310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE------- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1159 DEATMLQDLMsrKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV-EELHDQIEQHKKQRSQLEKQQNQADQERADMAQ 1237
Cdd:COG4717 383 DEEELRAALE--QAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1238 EIALLQASRAdIDKKRKIHEAHLMEIQaNLAESDEHKRTLIDQLERSRDEL--DHLNRVREEEEHAFANM 1305
Cdd:COG4717 461 ELEQLEEDGE-LAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYreERLPPVLERASEYFSRL 528
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1530-1699 |
5.74e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1530 AKRSLEAELNDMRVQMEelednlQIAEDARLRLEVT-----------NQALKSESDRAISNKDVEAEEKRRGLLKQIRDL 1598
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAK------RILEEAKKEAEAIkkealleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1599 ENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKeyqiecEEARQ---------AKEDIA 1669
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA------EEAKEillekveeeARHEAA 172
|
170 180 190
....*....|....*....|....*....|
gi 25150354 1670 ALLREADRkfravEAEREQLREANEGLMQA 1699
Cdd:PRK12704 173 VLIKEIEE-----EAKEEADKKAKEILAQA 197
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1244-1687 |
6.90e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 47.72 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1244 ASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEgQIQELNEQI 1323
Cdd:pfam05701 28 AHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAK-QDSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1324 QEETRLKIANINRA---RQLEDEKN---ALLDE----KEEAEGLRahleKEIHAARQGAGEARRKAEESVNQQleelrkk 1393
Cdd:pfam05701 107 VEEMEQGIADEASVaakAQLEVAKArhaAAVAElksvKEELESLR----KEYASLVSERDIAIKRAEEAVSAS------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1394 nlRDVEhlqKQLEESEVakerilqskkkiqqELEDSSMELENVRASHRDSEkrQKKFESQMAEERvavqkallDRDAMSQ 1473
Cdd:pfam05701 176 --KEIE---KTVEELTI--------------ELIATKESLESAHAAHLEAE--EHRIGAALAREQ--------DKLNWEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1474 ELRDRETRVLSLLNEVDIMKEH---LEESDRVRRSLQQELQDSISNK-DDFGKNVHELEKAKRSLEAELNDMRVQMEELE 1549
Cdd:pfam05701 227 ELKQAEEELQRLNQQLLSAKDLkskLETASALLLDLKAELAAYMESKlKEEADGEGNEKKTSTSIQAALASAKKELEEVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1550 DNLQIAEDARLRLEVTNQALKSESDRaisNKDVEAEEKRRGLLKQIR--DLENELENEKRGKSGAVSHRKKIENQIGELE 1627
Cdd:pfam05701 307 ANIEKAKDEVNCLRVAAASLRSELEK---EKAELASLRQREGMASIAvsSLEAELNRTKSEIALVQAKEKEAREKMVELP 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1628 QQLEVANRLKEEYNKQLKKNQQIIKEYQiecEEARQAKEDIAAL---LREADRKFRAVEAERE 1687
Cdd:pfam05701 384 KQLQQAAQEAEEAKSLAQAAREELRKAK---EEAEQAKAAASTVesrLEAVLKEIEAAKASEK 443
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1045-1852 |
8.26e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1045 ERQYKSELEQHKRKLLAELEDSKDHLAekMGKVEELNNQLMKRDEELQHQL---------TRYDEESANVTLMQKQMRDM 1115
Cdd:TIGR01612 961 EKSYKDKFDNTLIDKINELDKAFKDAS--LNDYEAKNNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1116 QTTIDELreDMETERNARNKAEMTRREVVAQLEKVKGDVLDKV-------------------------------DEATML 1164
Cdd:TIGR01612 1039 NKNIPNI--EIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAeinitnfneikeklkhynfddfgkeenikyaDEINKI 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1165 QDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRqVEELHDQI-------EQHKKQR---SQLEKQQNQADqERAD 1234
Cdd:TIGR01612 1117 KDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND-LEDVADKAisnddpeEIEKKIEnivTKIDKKKNIYD-EIKK 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1235 MAQEIALLQASRADIDKKRKIHEAHLMEIQANLAES-DEHKRT---LIDQLERSRDELDHLNRVREEEEhafaNMQRRLA 1310
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKiDEEKKKsehMIKAMEAYIEDLDEIKEKSPEIE----NEMGIEM 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1311 TAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLD------EKEEAEGLRAHLEKEIHAARqgagearrKAEESVN 1384
Cdd:TIGR01612 1271 DIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKiiedfsEESDINDIKKELQKNLLDAQ--------KHNSDIN 1342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1385 QQLEELRK-KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRaSHRDSEKRQKKFESQMAEErvavqk 1463
Cdd:TIGR01612 1343 LYLNEIANiYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK-DDINLEECKSKIESTLDDK------ 1415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1464 allDRDAMSQELRDRETRVLSllnevdimkehlEESDrvrrslqqeLQDSISNKDDFGKNVHELEKakrSLEAELNDMRV 1543
Cdd:TIGR01612 1416 ---DIDECIKKIKELKNHILS------------EESN---------IDTYFKNADENNENVLLLFK---NIEMADNKSQH 1468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1544 QMEELEDNLQIAEDARLRlEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENE------KRGKSGAVSHRK 1617
Cdd:TIGR01612 1469 ILKIKKDNATNDHDFNIN-ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysalaiKNKFAKTKKDSE 1547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1618 KIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLM 1697
Cdd:TIGR01612 1548 IIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETE 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1698 QARKQlelendeleelrakgggISSEEKRRLEAKIAQLEEELEEEQSNCElAIDKQRKaqvQLEQITTDLSmerTLNQKT 1777
Cdd:TIGR01612 1628 SIEKK-----------------ISSFSIDSQDTELKENGDNLNSLQEFLE-SLKDQKK---NIEDKKKELD---ELDSEI 1683
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25150354 1778 EAEKQSLERSNRDYK----AKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQF 1852
Cdd:TIGR01612 1684 EKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEF 1762
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1192-1556 |
8.27e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.41 E-value: 8.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1192 KIEEQKAKFSRqveeLHDQIEQHKKQRSQLEKQQNQADQEraDMAQEIALLQASRADIDKKRK---IHEAHLMEIQANLA 1268
Cdd:pfam03528 12 ELEKENAEFYR----LKQQLEAEFNQKRAKFKELYLAKEE--DLKRQNAVLQEAQVELDALQNqlaLARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1269 ESDEHKRTLIDQLERS-RDELDHLNRVREEE----EHAFanmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDE 1343
Cdd:pfam03528 86 VSENTKQEAIDEVKSQwQEEVASLQAIMKETvreyEVQF---HRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEENL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1344 KNALLDEKEEAEGLRA---HLEKEIHAARQGAGEARRKAEESVNQQLEELR-----KKNLRdvEHLQKQLEESEVAKERI 1415
Cdd:pfam03528 163 EDEMKKAQEDAEKLRSvvmPMEKEIAALKAKLTEAEDKIKELEASKMKELNhyleaEKSCR--TDLEMYVAVLNTQKSVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1416 LQSKKKIQQELEDSSMELENVRASHrdsekRQKKFESQMAEERVAVQKALLDRDAMSQE--LRDRETRVLSLLNEVDIMK 1493
Cdd:pfam03528 241 QEDAEKLRKELHEVCHLLEQERQQH-----NQLKHTWQKANDQFLESQRLLMRDMQRMEsvLTSEQLRQVEEIKKKDQEE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1494 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAE 1556
Cdd:pfam03528 316 HKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLGA 378
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
858-1508 |
8.45e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 858 DELRATKERL-LKMEHDFRENEKKLDQVivERAVIQEQLQQESENSAELDDIRGRlQTRNQELEYIVNDMRDRLSEEEQQ 936
Cdd:pfam05483 200 EELRVQAENArLEMHFKLKEDHEKIQHL--EEEYKKEINDKEKQVSLLLIQITEK-ENKMKDLTFLLEESRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 937 NeKNNDERRKQMETVRDleeqleqeeqarqkllldktnvdqrlrNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLD 1016
Cdd:pfam05483 277 T-KLQDENLKELIEKKD---------------------------HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1017 HEERAkhgvkakgrlENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLT 1096
Cdd:pfam05483 329 LTEEK----------EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1097 RYDEESANVTLMQKQMRDMQTTIDELRedmeternarnkaemtrrevvaQLEKVKGDVLDKVDEATMlqdLMSRKDEEVN 1176
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKK----------------------QFEKIAEELKGKEQELIF---LLQAREKEIH 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1177 ATkraieQIQHTMEGKIEEQkakFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIA----LLQASRADIDKK 1252
Cdd:pfam05483 454 DL-----EIQLTAIKTSEEH---YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDIINC 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1253 RKIHEAHLMEIQaNLAESDEHKRtliDQLERSRDEL----DHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQeETR 1328
Cdd:pfam05483 526 KKQEERMLKQIE-NLEEKEMNLR---DELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN-NLK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1329 LKIANINRARQLEDEKNALLDEKEEAEGLRAHL-EKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDvEHLQKQLEE 1407
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAyEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE-EKLLEEVEK 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1408 SEVAKERILQSKKKIQQELEDSSMELENVRASHRDS-EKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLL 1486
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQyDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
650 660
....*....|....*....|..
gi 25150354 1487 NEVDIMKehlEESDRVRRSLQQ 1508
Cdd:pfam05483 760 KQLEIEK---EEKEKLKMEAKE 778
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1616-1696 |
8.54e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1616 RKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQII--------KEYQIECEEARQAKEDIAALLRE------ADRKFRA 1681
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEdklleeaeKEAQQAIKEAKKEADEIIKELRQlqkggyASVKAHE 608
|
90
....*....|....*
gi 25150354 1682 VEAEREQLREANEGL 1696
Cdd:PRK00409 609 LIEARKRLNKANEKK 623
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
971-1666 |
8.84e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 971 DKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTtqllDHEERAKHGVKAKGRLENQ---LHEL--------- 1038
Cdd:TIGR01612 573 DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNIS----DKNEYIKKAIDLKKIIENNnayIDELakispyqvp 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1039 EQDLNRERQY---KSELEQHKR----KLLAEL-----EDSKDHLAEKmGKVEELNNQLMKRDEELQHQLTRYDEesANVT 1106
Cdd:TIGR01612 649 EHLKNKDKIYstiKSELSKIYEddidALYNELssivkENAIDNTEDK-AKLDDLKSKIDKEYDKIQNMETATVE--LHLS 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1107 LMQKQMRDMQTTIDELREDMETERNArnkaemtrrevvaQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQ 1186
Cdd:TIGR01612 726 NIENKKNELLDIIVEIKKHIHGEINK-------------DLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIK 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1187 HTMEGKIEEQKAKfSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIAllqaSRADI------DKKRKIHEAH- 1259
Cdd:TIGR01612 793 NHYNDQINIDNIK-DEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL----NKVDKfinfenNCKEKIDSEHe 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1260 -----LMEIQANLaeSDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQR---RLATAEGQIQELNEQIQEETRLK- 1330
Cdd:TIGR01612 868 qfaelTNKIKAEI--SDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKvdeYIKICENTKESIEKFHNKQNILKe 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1331 IANINrarqLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEEL---RKKNLRDVEH--LQKQL 1405
Cdd:TIGR01612 946 ILNKN----IDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYfndLKANLGKNKEnmLYHQF 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1406 EESEVAKERILQSKKKIQQELEDSSMelenvrASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1485
Cdd:TIGR01612 1022 DEKEKATNDIEQKIEDANKNIPNIEI------AIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKH 1095
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1486 LNEVDIMKE-HLEESDRVRRslqqeLQDSISNKDD-FGKNVHELEKAKRSLEAELNDMRVQMEELEDnlqiaedarlrle 1563
Cdd:TIGR01612 1096 YNFDDFGKEeNIKYADEINK-----IKDDIKNLDQkIDHHIKALEEIKKKSENYIDEIKAQINDLED------------- 1157
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1564 vtnqalksESDRAISNKDVEA-EEKRRGLLKQIRDLENELENekrgksgavshRKKIENQIGELEQ---QLEVANRLKEE 1639
Cdd:TIGR01612 1158 --------VADKAISNDDPEEiEKKIENIVTKIDKKKNIYDE-----------IKKLLNEIAEIEKdktSLEEVKGINLS 1218
|
730 740 750
....*....|....*....|....*....|....*....
gi 25150354 1640 YNKQL------------KKNQQIIKEYQIECEEARQAKE 1666
Cdd:TIGR01612 1219 YGKNLgklflekideekKKSEHMIKAMEAYIEDLDEIKE 1257
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1205-1390 |
1.00e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.38 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1205 EELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDK---------------KR-----KIHEAhLMEIQ 1264
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgeeeeleeerRRlsnaeKLREA-LQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1265 ANLAESDEhkrTLIDQLERSRDELDHLnrvrEEEEHAFANMQRRLATAEGQIQELNEQIQE---------------ETRL 1329
Cdd:COG0497 233 EALSGGEG---GALDLLGQALRALERL----AEYDPSLAELAERLESALIELEEAASELRRyldslefdperleevEERL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1330 KIAN-------------INRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAG---EARRKA----EESVNQQLEE 1389
Cdd:COG0497 306 ALLRrlarkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEklsAARKKAakklEKAVTAELAD 385
|
.
gi 25150354 1390 L 1390
Cdd:COG0497 386 L 386
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1054-1410 |
1.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1054 QHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQhQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNAR 1133
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1134 nkaemtrrevvAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQ 1213
Cdd:COG4913 692 -----------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1214 HKKQRSQLEKQQNQADQERADMAQEIALLqasradidkkRKIHEAHLMEIQANLAESDehkrtliDQLERSRDELDHLNR 1293
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEEL----------ERAMRAFNREWPAETADLD-------ADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1294 VREEEEHAF-ANMQRRLATAEGQ-IQELNEQIQEEtrlkianINRARQLEDEKNALLDEKEEAEGLRAHLE--------- 1362
Cdd:COG4913 824 LEEDGLPEYeERFKELLNENSIEfVADLLSKLRRA-------IREIKERIDPLNDSLKRIPFGPGRYLRLEarprpdpev 896
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1363 ----KEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQLEESEV 1410
Cdd:COG4913 897 refrQELRAVTSGASLFDEELSEARFAALKRLIER-LRSEEEESDRRWRARV 947
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
980-1156 |
1.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 980 RNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHeeRAKHGV----KAKGRLENQLHELEQDLNRERQYKSELEQH 1055
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLvdlsEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1056 KRKLLAELEDSKDHLAEKMGK--VEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTID-ELREDMETERNA 1132
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAE 321
|
170 180
....*....|....*....|....
gi 25150354 1133 RNKAEMTRREVVAQLEKVKGDVLD 1156
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAE 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
976-1417 |
1.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 976 DQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDH---------EERAKHGVKAKGRLENQLHELEQDlnrER 1046
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRVELERALADHESQ---EQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1047 QYKSELEQHKRKL--LAELEDSKDHLAEkmgkveelnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRE 1124
Cdd:PRK04863 862 QQRSQLEQAKEGLsaLNRLLPRLNLLAD---------ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1125 DMEternarnkaemtrrevvaQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV 1204
Cdd:PRK04863 933 DPE------------------QFEQLKQDYQQ-------AQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1205 EELHDQIEQHKKQRSQLEKQQNQADqerADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEhkrTLIDQLERS 1284
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQ---AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS---GAEERARAR 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1285 RDELDHlnrvreeeehafanmqrRLATAEGQIQELNEQIQ-EETRLKIANiNRARQLEDEknaLLDEKEEAEGLRAHLEK 1363
Cdd:PRK04863 1062 RDELHA-----------------RLSANRSRRNQLEKQLTfCEAEMDNLT-KKLRKLERD---YHEMREQVVNAKAGWCA 1120
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1364 EIHAARQGAGEARRKAEESVNQQLEELRKKN------LR----DVEHLQKQLEESEVAK--ERILQ 1417
Cdd:PRK04863 1121 VLRLVKDNGVERRLHRRELAYLSADELRSMSdkalgaLRlavaDNEHLRDVLRLSEDPKrpERKVQ 1186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1088-1270 |
1.28e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1088 DEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME--TERNARNKAEM---------TRREVVAQLEKVK----- 1151
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelQAELEALQAEIdklqaeiaeAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1152 -------GDVLDKVDEATMLQDLMSR---KDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQL 1221
Cdd:COG3883 95 lyrsggsVSYLDVLLGSESFSDFLDRlsaLSKIADADADLLEELKADKA-ELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 25150354 1222 EKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAES 1270
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1257-1919 |
1.37e-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: 47.14 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1257 EAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVrEEEEHAFANMQRRLATAEGQIQEL--------NEQIQEETR 1328
Cdd:pfam12128 199 KSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGI-MKIRPEFTKLQQEFNTLESAELRLshlhfgykSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1329 LKianinRARQLEDEKNALLDEKE-EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLE------ELRKKNLRDVEHL 1401
Cdd:pfam12128 278 QE-----ERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldadiETAAADQEQLPSW 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1402 QKQLEESEVAKERILQSKKKIQQELE--DSSMELENVRASHRDSEKRQKKFES---QMAEERVAVQkalldrdAMSQELR 1476
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKDKLAKIREArdrQLAVAEDDLQ-------ALESELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1477 DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVH----ELEKAKRSLEA---ELNDMRVQMEELE 1549
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIErareEQEAANAEVERlqsELRQARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1550 DNLQIAEDA----RLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIR-------DLENELENEKRGKS----GAVS 1614
Cdd:pfam12128 506 EALRQASRRleerQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISpellhrtDLDPEVWDGSVGGElnlyGVKL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1615 HRKKIE-NQIGELEQQLEvanrlkeeynkqlKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREAN 1693
Cdd:pfam12128 586 DLKRIDvPEWAASEEELR-------------ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1694 EGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEeeleeeqsncelaidkqRKAQVQLEQITTDLSMERTL 1773
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD-----------------KKHQAWLEEQKEQKREARTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1774 NQkteAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFE 1853
Cdd:pfam12128 716 KQ---AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQ 792
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25150354 1854 DEKRANE--QAKELLEKSNLKNR--NLRRQLDEAEDEMSRE----RTKHRNVQREADDLLDANEQLTRELMNLR 1919
Cdd:pfam12128 793 EVLRYFDwyQETWLQRRPRLATQlsNIERAISELQQQLARLiadtKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
964-1208 |
1.39e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.93 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 964 ARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEErakhgvkakgrlenQLHELEQDLN 1043
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM--------------DIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1044 RERQY----KSELEQHKRKLlaeledskdHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTI 1119
Cdd:PHA02562 259 KLNTAaakiKSKIEQFQKVI---------KMYEKGGVCPTCTQQISEGPDRITKIKDKLKE-------LQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1120 DELREDMeterNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIEEQKAK 1199
Cdd:PHA02562 323 DELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD-KIVKTKSE 397
|
....*....
gi 25150354 1200 FSRQVEELH 1208
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1399-1645 |
1.68e-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: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1399 EHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHR--DSEKRQKKFESQMAEervaVQKALLDRDAMSQELR 1476
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE----LESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1477 DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhelekakrsLEAELNDMRVQMeeLEDNLQIAE 1556
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE----------------------LEAELAELSARY--TPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1557 dARLRLEVTNQALKSESDRAIsnkdVEAEEKRRGLLKQIRDLENELENEKRgksgAVSHRKKIENQIGELEQQLEVANRL 1636
Cdd:COG3206 296 -LRAQIAALRAQLQQEAQRIL----ASLEAELEALQAREASLQAQLAQLEA----RLAELPELEAELRRLEREVEVAREL 366
|
....*....
gi 25150354 1637 KEEYNKQLK 1645
Cdd:COG3206 367 YESLLQRLE 375
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1192-1601 |
1.98e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1192 KIEEQKAKFsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALL--QASRADIDKKRKIHEAHLMEIQANLAE 1269
Cdd:COG4717 72 ELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1270 SDEHK---RTLIDQLERSRDELDHLNRVREEE--------EHAFANMQRRLATAEGQIQELNE---QIQEEtrlkianIN 1335
Cdd:COG4717 151 LEERLeelRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEeleEAQEE-------LE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1336 RARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERI 1415
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1416 LQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELR--DRETRVLSLLNEVDIMK 1493
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1494 E----HLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKA--KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQ 1567
Cdd:COG4717 384 EeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430
....*....|....*....|....*....|....
gi 25150354 1568 ALksESDRAISnkdvEAEEKRRGLLKQIRDLENE 1601
Cdd:COG4717 464 QL--EEDGELA----ELLQELEELKAELRELAEE 491
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1374-1674 |
2.03e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1374 EARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEvakerilQSKKKIQQELEDSSMELENVrashrDSEKRQKKFESQ 1453
Cdd:pfam05667 313 PAATSSPPTKVETEEELQQQREEELEELQEQLEDLE-------SSIQELEKEIKKLESSIKQV-----EEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1454 MAEERVAVQKALLDrdamsqELRDRETRVLSLLNEVDIMKEHL----EESDRVRRSLQQE---LQDSISNKDDfgknvhe 1526
Cdd:pfam05667 381 ELEKQYKVKKKTLD------LLPDAEENIAKLQALVDASAQRLvelaGQWEKHRVPLIEEyraLKEAKSNKED------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1527 leKAKRSLEaELNDMRVQMEElednlqIAEDARLRLEVTNQaLKSESDRAisNKDVEAEEKRRGLL-------KQIRDLE 1599
Cdd:pfam05667 448 --ESQRKLE-EIKELREKIKE------VAEEAKQKEELYKQ-LVAEYERL--PKDVSRSAYTRRILeivknikKQKEEIT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1600 NELENEKrgksgavSHRKKIENQIGELEQQLEVAnrlKEEYNKQLKKNQQIIKEYQI------ECEEARQAKEDIAALLR 1673
Cdd:pfam05667 516 KILSDTK-------SLQKEINSLTGKLDRTFTVT---DELVFKDAKKDESVRKAYKYlaalheNCEQLIQTVEETGTIMR 585
|
.
gi 25150354 1674 E 1674
Cdd:pfam05667 586 E 586
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1206-1903 |
2.29e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1206 ELHDQI-----EQHKKQRSQLEKQQNQadqeradmAQEIALLQasradidkkrkihEAHLMEIQANL-AESDEHKRTLID 1279
Cdd:PRK10246 180 EIYGQIsamvfEQHKSARTELEKLQAQ--------ASGVALLT-------------PEQVQSLTASLqVLTDEEKQLLTA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1280 QLERSRD-----ELDHLNRVREEEEHAFANMQRRLATAEGQIQELN------------EQIQEETrlkiANINRARQLED 1342
Cdd:PRK10246 239 QQQQQQSlnwltRLDELQQEASRRQQALQQALAAEEKAQPQLAALSlaqparqlrphwERIQEQS----AALAHTRQQIE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1343 EKNALLdekEEAEGLRAhlekeihaarqgagEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERIL---QSK 1419
Cdd:PRK10246 315 EVNTRL---QSTMALRA--------------RIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQfsqQTS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1420 KKIQ-QELEDSSMELENVRASHRDSekrqkkfESQMAEERVAVQKALLDRdamSQELRDRETRvlsllnevdimkehLEE 1498
Cdd:PRK10246 378 DREQlRQWQQQLTHAEQKLNALPAI-------TLTLTADEVAAALAQHAE---QRPLRQRLVA--------------LHG 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1499 SDRVRRSLQQELQDSISNkddfgknvHELEKAKRslEAELNDMRVQMEELEDNLQIAEdARLRLEVTNQALKSESDR--- 1575
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQN--------VTQEQTQR--NAALNEMRQRYKEKTQQLADVK-TICEQEARIKDLEAQRAQlqa 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1576 --------AISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVshrkkIENQIGELEQQLEvanRLKEEYNKQLKKN 1647
Cdd:PRK10246 503 gqpcplcgSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAA-----LRGQLDALTKQLQ---RDESEAQSLRQEE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1648 QQIIKEYQIECEEA---RQAKEDIAALLREADRKFR-------------AVEAEREQLREANEGLMQARKQLELENDE-- 1709
Cdd:PRK10246 575 QALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERqlrllsqrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTALAGya 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1710 --------------LEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTD-LSME---R 1771
Cdd:PRK10246 655 ltlpqedeeaswlaTRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQcLSLHsqlQ 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1772 TLNQKTEAEKQSLERSNRDYKAKiteLESGAQSRARAQMAA---------LEAKVQYLEDQLNvegQEKTAANRAARRLE 1842
Cdd:PRK10246 735 TLQQQDVLEAQRLQKAQAQFDTA---LQASVFDDQQAFLAAlldeetltqLEQLKQNLENQRQ---QAQTLVTQTAQALA 808
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1843 KRLNDTTQQFEDEKRANEQAKEL------LEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQ---READD 1903
Cdd:PRK10246 809 QHQQHRPDGLDLTVTVEQIQQELaqlaqqLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAqatQQVED 878
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1374-1579 |
2.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1374 EARRKAEESVNQQLEELRKknlrdvehlqkQLEESEVAKERILQSK---------KKIQQELEDSSMELENVRASHRDSE 1444
Cdd:COG3206 171 EEARKALEFLEEQLPELRK-----------ELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1445 KRQKKFESQMAEERVAV----------------QKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHL-EESDRVRRSLQ 1507
Cdd:COG3206 240 ARLAALRAQLGSGPDALpellqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1508 QELQDSISNKDdfgknvhELEKAKRSLEAELNDM---RVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISN 1579
Cdd:COG3206 320 AELEALQAREA-------SLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1332-1580 |
2.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1332 ANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQgageARRKAEESVNQQLEELRKKNlRDVEHLQKQLEESEVA 1411
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALE-QELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1412 KERILQSKKKIQQELEdssmelENVRASHRDSEKRQKKF------ESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1485
Cdd:COG4942 92 IAELRAELEAQKEELA------ELLRALYRLGRQPPLALllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1486 LNEVDIMKEHLEESDRVRRSLQQELQDSISNKDdfgKNVHELEKAKRSLEAELNDMRVQMEELEDNLqiaedARLRLEVT 1565
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALI-----ARLEAEAA 237
|
250
....*....|....*
gi 25150354 1566 NQALKSESDRAISNK 1580
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1165-1482 |
2.64e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1165 QDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSrqveelhdqIEQHKKQRSQLEKQQNQADQER---ADMAQEIAL 1241
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA---------TESLEEQLAAAEAEQELEESKReteTGIQNLTAE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1242 LQASRADIDKKRKIHEAHLMEIQA--NLAESDEHKRTLIDQLERSRDELDHLNR-VREEEEHAFANMQRRLATAEGQIQE 1318
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIENIVGevELSKSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDTLKAADRQIEE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1319 LNEQIQEETRLKIANINRARQLEDEKNAlLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE--SVNQQLEELRKKNLR 1396
Cdd:COG5185 425 LQRQIEQATSSNEEVSKLLNELISELNK-VMREADEESQSRLEEAYDEINRSVRSKKEDLNEEltQIESRVSTLKATLEK 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1397 DVEHLQKQLEESEVAKERILQSKKKIQQELEDSS-MELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQEL 1475
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHiLALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQ 583
|
....*..
gi 25150354 1476 RDRETRV 1482
Cdd:COG5185 584 QAREDPI 590
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1139-1555 |
2.80e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1139 TRREVVAQLEKVKGDVLDKVDEATMLQDLmsrkdeevnatkraiEQIQhtmegkieeqkakfsrqveELHDQIEQHKKQR 1218
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEAEDKLVQQDL---------------EQTL-------------------ALLDKIDRQKEET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1219 SQLEKQQNQADQERADMAQEIALLQASRADIDKKR-----------KIHE--AHLMEIQANLAESDEHKRTLIDQLERSR 1285
Cdd:PRK11281 83 EQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqlesRLAQtlDQLQNAQNDLAEYNSQLVSLQTQPERAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1286 DELDH-----------LNRVREEE-------------EHAFANMQ----RRLATAEGQIQELNEQIQEETRLKIANINRA 1337
Cdd:PRK11281 163 AALYAnsqrlqqirnlLKGGKVGGkalrpsqrvllqaEQALLNAQndlqRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1338 RQLEDE----KNALLDEK--EEAEglrahlekEIHAARQGAGEARRKAEESVNQQL----------------EELRKKNL 1395
Cdd:PRK11281 243 LQLLQEainsKRLTLSEKtvQEAQ--------SQDEAARIQANPLVAQELEINLQLsqrllkateklntltqQNLRVKNW 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1396 RD-VEHLQKQLEES-EVAK-----ERIL-QSKKKIQQELEDSSM--ELENVRASHRD-SEKRQKKF----------ESQM 1454
Cdd:PRK11281 315 LDrLTQSERNIKEQiSVLKgslllSRILyQQQQALPSADLIEGLadRIADLRLEQFEiNQQRDALFqpdayidkleAGHK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1455 AEERVAVQKALLDRDAMSQELRDRETRVL-SLLNEVdI-----MKEHLEESDRVRRSLQQELQDSISNKDdfgKNVHELE 1528
Cdd:PRK11281 395 SEVTDEVRDALLQLLDERRELLDQLNKQLnNQLNLA-InlqlnQQQLLSVSDSLQSTLTQQIFWVNSNKP---MDLDWLK 470
|
490 500
....*....|....*....|....*....
gi 25150354 1529 KAKRSLEAELNDMRVQM--EELEDNLQIA 1555
Cdd:PRK11281 471 AFPQALKDQFKSLKITVsfSNLWDGLFIA 499
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1194-1512 |
2.80e-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: 46.10 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1194 EEQKAKFSRQVEELHdqiEQHKKQRSQLEKQQNQADQERADMAQEIALlqASRADIDKKRKIHEAHLMEIQANLAESDEH 1273
Cdd:COG3096 784 EKRLEELRAERDELA---EQYAKASFDVQKLQRLHQAFSQFVGGHLAV--AFAPDPEAELAALRQRRSELERELAQHRAQ 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1274 KRTLIDQLERSRDELDHLNRVR------EEEEHAfanmqRRLATAEGQIQELNEQIQEETRlkiaNINRARQLEDEKNAL 1347
Cdd:COG3096 859 EQQLRQQLDQLKEQLQLLNKLLpqanllADETLA-----DRLEELREELDAAQEAQAFIQQ----HGKALAQLEPLVAVL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1348 LDEKEEAEGLRAHLEK---EIHAARQGAGE-----ARRKA---EESVnQQLEELRKKNlrdvEHLQKQLEESEVAKERIL 1416
Cdd:COG3096 930 QSDPEQFEQLQADYLQakeQQRRLKQQIFAlsevvQRRPHfsyEDAV-GLLGENSDLN----EKLRARLEQAEEARREAR 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1417 QSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERV-----AVQKALLDRDAMSQELRDRETRVLSLLNEVDI 1491
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTR 1084
|
330 340
....*....|....*....|.
gi 25150354 1492 MKEHLEESDRVRRSLQQELQD 1512
Cdd:COG3096 1085 CEAEMDSLQKRLRKAERDYKQ 1105
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
983-1601 |
2.97e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.97 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 983 EERLVELQDAYDKLLKEKRLLEEKVEGLTTQLldheERAKHGVKAKGRLENQLHELEQdlNRERQYKSELEQHKRKllAE 1062
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRI----ETQKQTLGARDESIKKLLEMLQ--SKGLPKKSGEEDWERT--RR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1063 LEDSKDHLAEKMGKVEELNNQLMKRDEELqHQLTRYDEESANVTLMQK--QMRD-----MQTTIDELREDMETERNARNK 1135
Cdd:pfam10174 187 IAEAEMQLGHLEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTviEMKDtkissLERNIRDLEDEVQMLKTNGLL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1136 AEMTRREVVAQLEKVKGD---VLDKVDEATmlQDLmSRKDEEVNA--------------TKRAIEQIQHTMEGKiEEQKA 1198
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHskfMKNKIDQLK--QEL-SKKESELLAlqtkletltnqnsdCKQHIEVLKESLTAK-EQRAA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1199 KFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQaSRADIdKKRKIheahlMEIQANLAESDEHKRTLI 1278
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-DMLDV-KERKI-----NVLQKKIENLQEQLRDKD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1279 DQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRlkianiNRARQLEDEKNALLDEKEEAEGLR 1358
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR------ERLEELESLKKENKDLKEKVSALQ 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1359 AHL-EKEI-------HAARQGAGEARRkaeESVNQQLEELRKKNLRDVEHLQKQLEESEVAKErilqsKKKIQQELEDSS 1430
Cdd:pfam10174 489 PELtEKESslidlkeHASSLASSGLKK---DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE-----AVRTNPEINDRI 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1431 MELENVRASHRD-SEKRQKKFESQMAEERvAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSlqQE 1509
Cdd:pfam10174 561 RLLEQEVARYKEeSGKAQAEVERLLGILR-EVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGA--QL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1510 LQDSISNKDDFGKNVHELEkakrsleaelndMRVQMEELEDNLQIAEDARLRLEVTNQALkSESDRAISNKDVEaeekRR 1589
Cdd:pfam10174 638 LEEARRREDNLADNSQQLQ------------LEELMGALEKTRQELDATKARLSSTQQSL-AEKDGHLTNLRAE----RR 700
|
650
....*....|..
gi 25150354 1590 GLLKQIRDLENE 1601
Cdd:pfam10174 701 KQLEEILEMKQE 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1111-1421 |
3.34e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1111 QMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvldkvdeatmlqdlmSRKDEEVNATKRAIEQIQhtme 1190
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA-----------------EKRDELNAQVKELREEAQ---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1191 gkieeqkaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQaNLAES 1270
Cdd:COG1340 61 --------ELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ-TEVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1271 DEHKRTLIDQLERSRDELDHLNRVREEEEHaFANMQRRLATAEGQIQELNEQIQEetrlkianinRARQLEDEKNALLDE 1350
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKE----------LAEEAQELHEEMIEL 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1351 KEEAEGLRAHLEkEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKK 1421
Cdd:COG1340 201 YKEADELRKEAD-ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1307-1434 |
3.37e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1307 RRLATAE-GQIQELNEQIQEETRLKIANInrarqledEKNALLDEKEEAEGLRAHLEKEIHAARQGAgearRKAEESVNQ 1385
Cdd:PRK12704 26 KKIAEAKiKEAEEEAKRILEEAKKEAEAI--------KKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLLQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 25150354 1386 QLEELRKKnLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1434
Cdd:PRK12704 94 KEENLDRK-LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1188-1470 |
3.49e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1188 TMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANL 1267
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1268 AESDEHKRTLIDQLERSRDELDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQEETRLkianINRARQLEDEKNAL 1347
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEWRQQTEVLSPEEEKEL----VEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1348 LDEKEEAEGLRAhLEKEIHAARQGAGEARRKAEESVN--QQLEELRKKNLRDVEHLQKQLEEsevAKERILQSKKKIQQE 1425
Cdd:COG1340 153 KKALEKNEKLKE-LRAELKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADEL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 25150354 1426 LEdssmELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDA 1470
Cdd:COG1340 229 HE----EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1288-1541 |
3.89e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1288 LDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEkeeaeglrahlekeiha 1367
Cdd:PLN02939 155 LEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR----------------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1368 arqgaGEARRKAEESVNQQLEELRKKNL---RDVEHLQKQLEESEVAKERILQSKKkiQQELEDSSM-ELE-NVRASHRD 1442
Cdd:PLN02939 214 -----GATEGLCVHSLSKELDVLKEENMllkDDIQFLKAELIEVAETEERVFKLEK--ERSLLDASLrELEsKFIVAQED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1443 SEK-RQKKFESQMaeERVAVQKALLDRDA-----------MSQELRDRETRVLSLLNE----------VDIM-------K 1493
Cdd:PLN02939 287 VSKlSPLQYDCWW--EKVENLQDLLDRATnqvekaalvldQNQDLRDKVDKLEASLKEanvskfssykVELLqqklkllE 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 25150354 1494 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHElEKAKRSLEAELNDM 1541
Cdd:PLN02939 365 ERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE-ESKKRSLEHPADDM 411
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1198-1903 |
4.72e-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: 45.33 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1198 AKFSRQVEELHDQIEQHKKQRSQLEKQQNQ--ADQER-ADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDehk 1274
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQlaEEQYRlVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1275 rtlidQLERSRDELDHLNRVREEEEHAFANMQRRLATAEgqiqELNEQIQEEtrlkianINRAR-QLEDEKNAL------ 1347
Cdd:COG3096 348 -----KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE----ARLEAAEEE-------VDSLKsQLADYQQALdvqqtr 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1348 -------LDEKEEAEGLRAHLEKEIHAARQGAGEARRKaEESVNQQLEELRKKnLRDVEHLQKQLEE---------SEVA 1411
Cdd:COG3096 412 aiqyqqaVQALEKARALCGLPDLTPENAEDYLAAFRAK-EQQATEEVLELEQK-LSVADAARRQFEKayelvckiaGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1412 KERILQSKKKIQQELEDSSMELENV---RASHRDSEKR---QKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1485
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQRLqqlRAQLAELEQRlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1486 LnevdimkEHLEESDRVRRSLQQELqdsisnkDDFGKNVHELEK---AKRSLEAELNDMRVQMEELEDNLQIAEDARLRL 1562
Cdd:COG3096 570 E-------EQAAEAVEQRSELRQQL-------EQLRARIKELAArapAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1563 EVTNQALKSESDraisnkdvEAEEKRRGLLKQIRDL-------ENELENEKRGKSG----------AVSHRKKIENQIGE 1625
Cdd:COG3096 636 LEREREATVERD--------ELAARKQALESQIERLsqpggaeDPRLLALAERLGGvllseiyddvTLEDAPYFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1626 LEQQLEVANrlKEEYNKQLKKNQQIIKE-YQIECEE------ARQAKE-DIAALLREADRKFR-------------AVEA 1684
Cdd:COG3096 708 ARHAIVVPD--LSAVKEQLAGLEDCPEDlYLIEGDPdsfddsVFDAEElEDAVVVKLSDRQWRysrfpevplfgraAREK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1685 EREQLREANEGLMQ-----ARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQ 1759
Cdd:COG3096 786 RLEELRAERDELAEqyakaSFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1760 LEQITTDLSM-ERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRAR--AQMAALEAKVQYL------EDQLNVEGQE 1830
Cdd:COG3096 866 LDQLKEQLQLlNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQhgKALAQLEPLVAVLqsdpeqFEQLQADYLQ 945
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1831 KTAANRAARRLEKRLNDTTQQfeDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADD 1903
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQR--RPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1311-1700 |
6.05e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 6.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1311 TAEGQIQELNEQIQEETRLKI---ANINRAR-QLEDEKNALLDEKE-EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQ 1385
Cdd:pfam09731 49 YALGEDPPLAPKPKTFRPLQPsvvSAVTGESkEPKEEKKQVKIPRQsGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1386 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIqqeLEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1465
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDS---LKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1466 LDRDAMSQELRDRETrVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFgknVHELEKAKRSLEAELNDMRVQM 1545
Cdd:pfam09731 206 EEEAAPPLLDAAPET-PPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVF---QQELVSIFPDIIPVLKEDNLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1546 EElEDNLQIAeDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENekrgksgavsHRKKIENQIgE 1625
Cdd:pfam09731 282 ND-DLNSLIA-HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEE----------VRAADEAQL-R 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1626 LEQQLEVAnRLKEEYNKQLKKnqqiikeyqieceEARQAKEDIAALLREADRKfRAVEAEREQLREANEGLMQAR 1700
Cdd:pfam09731 349 LEFERERE-EIRESYEEKLRT-------------ELERQAEAHEEHLKDVLVE-QEIELQREFLQDIKEKVEEER 408
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1045-1880 |
6.24e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1045 ERQYKSELEQHKRKllaELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRdMQTTIDELRE 1124
Cdd:COG3096 279 ERRELSERALELRR---ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1125 DMEternarnkaemtrrEVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATK-------RAIEqIQHTMEGKIEE-- 1195
Cdd:COG3096 355 DLE--------------ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqQALD-VQQTRAIQYQQav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1196 ---QKAKFSRQVEELHdqIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIheahLMEIQANLAESDE 1272
Cdd:COG3096 420 qalEKARALCGLPDLT--PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYEL----VCKIAGEVERSQA 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1273 HKrTLIDQLERSRDELDHLNRVreeeehafANMQRRLATAEgqiQELNEQIQEETRLKIANINRARQLEDEKNaLLDEKE 1352
Cdd:COG3096 494 WQ-TARELLRRYRSQQALAQRL--------QQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1353 EAEGLRAHLEKEIHAARQGAGEARRKaEESVNQQLEELRKK-----NLRDV-EHLQKQLEESevakeriLQSKKKIQQEL 1426
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQ-LEQLRARIKELAARapawlAAQDAlERLREQSGEA-------LADSQEVTAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1427 EdssMELENVRashrdsekrqkkfESQMAEERVAVQKALLDRDA--MSQELRDRETRVLS--------LLNEV--DIMKE 1494
Cdd:COG3096 633 Q---QLLERER-------------EATVERDELAARKQALESQIerLSQPGGAEDPRLLAlaerlggvLLSEIydDVTLE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1495 H----------------LEESDRVRRSLQQeLQDSIS-------NKDDFGKNVH---ELEKA------------------ 1530
Cdd:COG3096 697 DapyfsalygparhaivVPDLSAVKEQLAG-LEDCPEdlyliegDPDSFDDSVFdaeELEDAvvvklsdrqwrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1531 ----KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALkseSDRAISNKDVEAEEKRRGLLKQIRDLENELENEK 1606
Cdd:COG3096 776 plfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAF---SQFVGGHLAVAFAPDPEAELAALRQRRSELEREL 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1607 RGKSGAVSHRKKienQIGELEQQLEVANRLKEEYNkqLKKNQQIIKEYQiECEEARQAKEDIAALLREADRKFRAVEAER 1686
Cdd:COG3096 853 AQHRAQEQQLRQ---QLDQLKEQLQLLNKLLPQAN--LLADETLADRLE-ELREELDAAQEAQAFIQQHGKALAQLEPLV 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1687 EQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRL-------EAKIAQLEEELEEEQSNCELAIDKQRKAQVQ 1759
Cdd:COG3096 927 AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedaVGLLGENSDLNEKLRARLEQAEEARREAREQ 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1760 LEQIT---TDLSMERT-LNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKV-------QYLEDQLNVEG 1828
Cdd:COG3096 1007 LRQAQaqySQYNQVLAsLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELsqnrsrrSQLEKQLTRCE 1086
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1829 QEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQL 1880
Cdd:COG3096 1087 AEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLHRREL 1138
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
885-1293 |
6.30e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 885 IVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIvnDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQA 964
Cdd:PRK11281 35 LPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALL--DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 965 RQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLeekvEGLTTQLldheERAKHGVKAKgrlENQLHELEQDLNR 1044
Cdd:PRK11281 113 ETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL----VSLQTQP----ERAQAALYAN---SQRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1045 ERQYKSELEQHKRKLL-AELedskDHLAEKMgkveELNNQLMKRDEELQHQLT-RYDEESANVTLMQKQMRDMQTTIDEL 1122
Cdd:PRK11281 182 GKVGGKALRPSQRVLLqAEQ----ALLNAQN----DLQRKSLEGNTQLQDLLQkQRDYLTARIQRLEHQLQLLQEAINSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1123 RedmeternaRNKAEMTRREVVAQLEKVKGD----VLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKA 1198
Cdd:PRK11281 254 R---------LTLSEKTVQEAQSQDEAARIQanplVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1199 kfsrqveeLHDQIE--QHKKQRSQLEKQQNQA---DQERADMAQEIALLQASRADIDKKRK---IHEAHLMEIQANLAE- 1269
Cdd:PRK11281 325 --------IKEQISvlKGSLLLSRILYQQQQAlpsADLIEGLADRIADLRLEQFEINQQRDalfQPDAYIDKLEAGHKSe 396
|
410 420
....*....|....*....|....*
gi 25150354 1270 -SDEHKRTLIDQLERSRDELDHLNR 1293
Cdd:PRK11281 397 vTDEVRDALLQLLDERRELLDQLNK 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1513-1702 |
6.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1513 SISNKDDFGKNvHELEKakRSLEAELNDMRVQMEELEDNLQIAEDARLRLEV------------TNQALKSESDRAISNK 1580
Cdd:COG4913 205 PIGDLDDFVRE-YMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQIELlepirelaeryaAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1581 DVEAEEKRRGLLKQ-IRDLENELENEKRGKSGAVSHRKKIENQIGELEQQ--------LEVANRLKEEYNKQLKKNQQII 1651
Cdd:COG4913 282 RLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1652 KEYQIECEEARQA----KEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQ 1702
Cdd:COG4913 362 ARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1317-1427 |
8.14e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1317 QELNEQI----QEETRLKIANINrARQLEDEKNALLDE-KEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELR 1391
Cdd:PRK00409 516 EKLNELIasleELERELEQKAEE-AEALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 25150354 1392 KK--------NLRDVEHLQKQLEESEVAKERILQSKKKIQQELE 1427
Cdd:PRK00409 595 QLqkggyasvKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1903 |
8.74e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1639 EYNKQLKKNQQIIKEYQIECEEARQAKEDiaaLLREADRKFRAVEAEREQLREAN-EGLMQARKQLELENDELEELRakg 1717
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEE---KAREVERRRKLEEAEKARQAEMDrQAAIYAEQERMAMERERELER--- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1718 ggISSEEKRRLEAKIAQLeeeleeeqsncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITE 1797
Cdd:pfam17380 353 --IRQEERKRELERIRQE-----------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1798 LES----GAQSRARA-QMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSnlk 1872
Cdd:pfam17380 420 VEMeqirAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--- 496
|
250 260 270
....*....|....*....|....*....|.
gi 25150354 1873 nrnLRRQLDEAEDEMSRERTKHRNVQREADD 1903
Cdd:pfam17380 497 ---LEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
854-1097 |
8.77e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 854 RAKDDELRATKERLLKmehdfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVN--------- 924
Cdd:COG4913 590 HEKDDRRRIRSRYVLG-----FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidva 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 925 ---DMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLK--- 998
Cdd:COG4913 665 saeREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlar 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 999 -------EKRLLEEKVEGLTTQLLDHEERAKHGVKAK-GRLENQLHELEQDLNRErqYKSELEQHK---------RKLLA 1061
Cdd:COG4913 745 lelrallEERFAAALGDAVERELRENLEERIDALRARlNRAEEELERAMRAFNRE--WPAETADLDadleslpeyLALLD 822
|
250 260 270
....*....|....*....|....*....|....*..
gi 25150354 1062 ELEDskDHLAEKMGKVEELNNQLMKRD-EELQHQLTR 1097
Cdd:COG4913 823 RLEE--DGLPEYEERFKELLNENSIEFvADLLSKLRR 857
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1221-1889 |
8.85e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 8.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1221 LEKQQNQADQERADMAQEialLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQ--LERSRDELDHLN------ 1292
Cdd:NF041483 78 LRNAQIQADQLRADAERE---LRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLDQelAERRQTVESHVNenvawa 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1293 ---RVREEE------EHAFANMQRRLATAEGQIQELNEQIQE-------------ETRLKIANINRARQLEDEKNALLDE 1350
Cdd:NF041483 155 eqlRARTESqarrllDESRAEAEQALAAARAEAERLAEEARQrlgseaesaraeaEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1351 KEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRD-------VEHLQKQLEESEVAKE-RILQSKKKI 1422
Cdd:NF041483 235 TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAekvvaeaKEAAAKQLASAESANEqRTRTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1423 QQELEDSSMELENVRAshrdsEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEV---------DIMK 1493
Cdd:NF041483 315 ARLVGEATKEAEALKA-----EAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVltkasedakATTR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1494 EHLEESDRVRRSLQQElqdsisnKDDFGKNVHEL-EKAKRSLEAELNDMRVQMEELEDnlqiaEDARLRLEVtnQALKSE 1572
Cdd:NF041483 390 AAAEEAERIRREAEAE-------ADRLRGEAADQaEQLKGAAKDDTKEYRAKTVELQE-----EARRLRGEA--EQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1573 sdrAISNKDVEAEEKRRGLLKQIRDLENELE----------NEKRGKSGAVSHRKKIEnqigeleqQLEVANRLKEEYNK 1642
Cdd:NF041483 456 ---AVAEGERIRGEARREAVQQIEEAARTAEelltkakadaDELRSTATAESERVRTE--------AIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1643 QLKKNQQIIKEYQIECEE----ARQAKEDIAALLREADRkfRAVEAEREqlrEANEGLmqARKQLELENDELEELRAKGG 1718
Cdd:NF041483 525 TLERTRAEAERLRAEAEEqaeeVRAAAERAARELREETE--RAIAARQA---EAAEEL--TRLHTEAEERLTAAEEALAD 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1719 GISSEEKRRLEAkiAQLEEELEEEqsncelAIDKQRKAQVQLEQITTDLSMERTLN-QKTEAEKQSLE-RSNRDYKAKIT 1796
Cdd:NF041483 598 ARAEAERIRREA--AEETERLRTE------AAERIRTLQAQAEQEAERLRTEAAADaSAARAEGENVAvRLRSEAAAEAE 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1797 ELESGAQS---RARAQMAALEAKVQYLEDQLNVEGQEKtaANRAARRLEKRLNDTTQQFEDEK-RANEQAKELLEKSnlk 1872
Cdd:NF041483 670 RLKSEAQEsadRVRAEAAAAAERVGTEAAEALAAAQEE--AARRRREAEETLGSARAEADQEReRAREQSEELLASA--- 744
|
730
....*....|....*..
gi 25150354 1873 nrnlRRQLDEAEDEMSR 1889
Cdd:NF041483 745 ----RKRVEEAQAEAQR 757
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1386-1718 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1386 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1465
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1466 LDRDAMSQELRDREtrvlsllNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQM 1545
Cdd:COG4372 94 AELAQAQEELESLQ-------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1546 EELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGE 1625
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1626 LEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLEL 1705
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|...
gi 25150354 1706 ENDELEELRAKGG 1718
Cdd:COG4372 327 KLELALAILLAEL 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
845-1481 |
1.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENE-KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRN----QEL 919
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 920 EYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVE-LQDAYDKL-- 996
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELpf 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 997 ---LKEKRLLEEK----VE----GLTTQLL---DHEERAKH---GVKAKGRLenQLHELEQDLNRERQYKSeleqHKRKL 1059
Cdd:COG4913 463 vgeLIEVRPEEERwrgaIErvlgGFALTLLvppEHYAAALRwvnRLHLRGRL--VYERVRTGLPDPERPRL----DPDSL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1060 LAELeDSKDHLAEkmgkvEELNNQLMKR--------DEELQHQ---LTRYDEESANVTLMQKQMRDMQTT---------- 1118
Cdd:COG4913 537 AGKL-DFKPHPFR-----AWLEAELGRRfdyvcvdsPEELRRHpraITRAGQVKGNGTRHEKDDRRRIRSryvlgfdnra 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1119 -IDELREDMETERNARNKAEmtrrEVVAQLEKVKGDVLDKVDEATMLQDLmSRKDEEVNATKRAIEQiqhtmegkIEEQK 1197
Cdd:COG4913 611 kLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEY-SWDEIDVASAEREIAE--------LEAEL 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1198 akfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkihEAHLMEIQANLAESDEHKRTL 1277
Cdd:COG4913 678 ----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRAL 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1278 IDQLERSRDELDHLNRVREeeehafaNMQRRLATAEGQIQELNEQIqeetRLKIANINraRQLEDEKNALLDEKEEAEGL 1357
Cdd:COG4913 751 LEERFAAALGDAVERELRE-------NLEERIDALRARLNRAEEEL----ERAMRAFN--REWPAETADLDADLESLPEY 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1358 RAHLEKeihAARQGAGEARRKAEESVNQQleelrkkNLRDVEHLQKQLEES-EVAKERIlqskKKIQQEL------EDSS 1430
Cdd:COG4913 818 LALLDR---LEEDGLPEYEERFKELLNEN-------SIEFVADLLSKLRRAiREIKERI----DPLNDSLkripfgPGRY 883
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1431 MELEnVRASH-----------RDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETR 1481
Cdd:COG4913 884 LRLE-ARPRPdpevrefrqelRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWR 944
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
904-1223 |
1.09e-03 |
|
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: 43.86 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 904 ELDDIRGRLQTRNQ---ELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLR 980
Cdd:TIGR04523 322 KLEEIQNQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 981 NLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLL 1060
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1061 AELEDSKDHLAEKMGKVEELNNQ-----------------LMKRDEELQHQLTRY-------------DEESANVTLMQK 1110
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEkkeleekvkdltkkissLKEKIEKLESEKKEKeskisdledelnkDDFELKKENLEK 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1111 QMRDMQTTIDELREDMETERNARNKAEmtrrEVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEqiqhTME 1190
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQ----ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS----SII 633
|
330 340 350
....*....|....*....|....*....|...
gi 25150354 1191 GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEK 1223
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1503-1915 |
1.21e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1503 RRSLQQELQDSISNKDDfgknvHELEKAKRSLEAELNDMRVQMEELEDNLQIA----EDARLRLEVTNQALKS----ESD 1574
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQAretrDEADEVLEEHEERREEletlEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1575 RAISNKDVEAEEKRRGLLK-QIRDLENELE------NEKRGKSG-------AVS-HRKKIENQIGELEQQLEVANRLKEE 1639
Cdd:PRK02224 260 IEDLRETIAETEREREELAeEVRDLRERLEeleeerDDLLAEAGlddadaeAVEaRREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1640 YNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKggg 1719
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE--- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1720 iSSEEKRRLEAKIAQLEEELEEEQsncelaiDKQRKAQVQLEQittdlsmertlnQKTEAEKQSLERSNR-----DYKAK 1794
Cdd:PRK02224 417 -LREERDELREREAELEATLRTAR-------ERVEEAEALLEA------------GKCPECGQPVEGSPHvetieEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1795 ITELESgAQSRARAQMAALEAKVQYLEDqlnvegqektaanraARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNR 1874
Cdd:PRK02224 477 VEELEA-ELEDLEEEVEEVEERLERAED---------------LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 25150354 1875 NLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTREL 1915
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1673-1919 |
1.29e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1673 READRKFRAVEAEREQLREANEGLMQARKQlelendeleelRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDK 1752
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQ-----------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1753 QRKAQVQLEQITTDLsmertlnQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKT 1832
Cdd:COG4913 290 LELLEAELEELRAEL-------ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1833 AANRAARRLEKRLNDTTQQFEDEKRaneQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLT 1912
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
....*..
gi 25150354 1913 RELMNLR 1919
Cdd:COG4913 440 ARLLALR 446
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
850-1244 |
1.40e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 850 DDEIRAKDDELRATKERLLKMEHDFRENEKKLDqviveraVIQEQLQQESENSA----ELDDIRGRLQTRNQEL----EY 921
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNSDCKQHIE-------VLKESLTAKEQRAAilqtEVDALRLRLEEKESFLnkktKQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 922 I-------------VNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVE 988
Cdd:pfam10174 368 LqdlteekstlageIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 989 LQDAYDKLLKEK----RLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELE 1064
Cdd:pfam10174 448 KERIIERLKEQReredRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1065 DSKDHL---------AEKMGKVEELNNQLMKRDEELQHQLTRYDEESAnvtlmqKQMRDMQTTIDELREdMETERNARNK 1135
Cdd:pfam10174 528 QKKEECsklenqlkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEESG------KAQAEVERLLGILRE-VENEKNDKDK 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1136 A-----EMTRREVVAQLEKVK----GDVLDKVDEATMLQDLMSRKDEEV-NATKRAIEQIQHTMEG---KIEEQKAKFSR 1202
Cdd:pfam10174 601 KiaeleSLTLRQMKEQNKKVAnikhGQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEKtrqELDATKARLSS 680
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 25150354 1203 QVEELHDQIEQHKKQRSQLEKQQnqadQERADMAQEiALLQA 1244
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQL----EEILEMKQE-ALLAA 717
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1754-1921 |
1.45e-03 |
|
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: 43.90 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1754 RKAQVQLEQITTDLS-MERTLNQKT------EAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNV 1826
Cdd:TIGR02169 233 EALERQKEAIERQLAsLEEELEKLTeeiselEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1827 EGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLD 1906
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170
....*....|....*
gi 25150354 1907 ANEQLTRELMNLRGN 1921
Cdd:TIGR02169 393 KLEKLKREINELKRE 407
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
964-1106 |
1.52e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 964 ARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlenQLHELEQDLN 1043
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1044 RERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVT 1106
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
867-1659 |
1.70e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 867 LLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDErrK 946
Cdd:PTZ00440 648 LDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLN--Q 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 947 QMETVRDLEEQLEQEEQARQKLLLDKTNVDQRlrnLEERLVELQDAYDKLLKEKRLLEEKVEglttqlldheerakhgvk 1026
Cdd:PTZ00440 726 YTIKYNDLKSSIEEYKEEEEKLEVYKHQIINR---KNEFILHLYENDKDLPDGKNTYEEFLQ------------------ 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1027 akgrlenqlhELEQDLNRERQYKSELEQHKRkllaELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVT 1106
Cdd:PTZ00440 785 ----------YKDTILNKENKISNDINILKE----NKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLN 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1107 LMQ--KQMRDMQTTIDELREDMETER---------NARNKAEMTRREVVAQLEKVKGDVLDKVDEATML--QDLMSRKDE 1173
Cdd:PTZ00440 851 LKEleKEFNENNQIVDNIIKDIENMNkniniiktlNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIinTDNIIQKNE 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1174 EVNATKRAIEQiqhtmEGKIEEQ--KAKFSRQVEELHDQIEQHKKQRSQLE-------KQQNQADQERADMAQEIALLQA 1244
Cdd:PTZ00440 931 KLNLLNNLNKE-----KEKIEKQlsDTKINNLKMQIEKTLEYYDKSKENINgndgthlEKLDKEKDEWEHFKSEIDKLNV 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1245 SRADIDKK-----RKIHEAHLMEIQANLAESDEHKRTLIDQlersrdELDHLNRVREEEEHAFANMQRRL---ATAEGQI 1316
Cdd:PTZ00440 1006 NYNILNKKiddliKKQHDDIIELIDKLIKEKGKEIEEKVDQ------YISLLEKMKTKLSSFHFNIDIKKyknPKIKEEI 1079
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1317 QELNEQIqeETRLKiaNINrarqleDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGeARRKAEESVNQQLEELRKK--N 1394
Cdd:PTZ00440 1080 KLLEEKV--EALLK--KID------ENKNKLIEIKNKSHEHVVNADKEKNKQTEHYN-KKKKSLEKIYKQMEKTLKEleN 1148
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1395 LRDVEHLQKQLEESEVAKERIL--QSKKKIQQELEDSSMELENVRASHRDSEKRQKKfesqMAEERVAVQKAlLDRDAMS 1472
Cdd:PTZ00440 1149 MNLEDITLNEVNEIEIEYERILidHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKN----MSKERNDHLTT-FEYNAYY 1223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1473 QELRDRETRVLSLLNEVDIMKE------HLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLeaELNDMRVQME 1546
Cdd:PTZ00440 1224 DKATASYENIEELTTEAKGLKGeanrstNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFL--ISIDSEKILK 1301
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1547 ELEDNLQIAEDArlrlevtnqalksesdraisNKDVEAE-EKRRGLLKQIRDLENELENEKRGKSGAVSHrKKIENQIGE 1625
Cdd:PTZ00440 1302 EILNSTKKAEEF--------------------SNDAKKElEKTDNLIKQVEAKIEQAKEHKNKIYGSLED-KQIDDEIKK 1360
|
810 820 830
....*....|....*....|....*....|....
gi 25150354 1626 LEQQLEVANRLKEEYNKQLKKnqqiIKEYQIECE 1659
Cdd:PTZ00440 1361 IEQIKEEISNKRKEINKYLSN----IKSNKEKCD 1390
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1031-1371 |
1.79e-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: 43.40 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1031 LENQLHELEQDLNR----ERQYKSELEQHKRKL--LAELEDSKDHLAEkmgkveelnNQLMKRDEELQHQLTRYDEESAN 1104
Cdd:COG3096 841 LRQRRSELERELAQhraqEQQLRQQLDQLKEQLqlLNKLLPQANLLAD---------ETLADRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1105 VTLMQKQMRDMQTTIDELREDMEternarnkaemtrrevvaQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQ 1184
Cdd:COG3096 912 IQQHGKALAQLEPLVAVLQSDPE------------------QFEQLQADYLQ-------AKEQQRRLKQQIFALSEVVQR 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1185 IQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRadiDKKRKIHEAHLMEIQ 1264
Cdd:COG3096 967 RPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELE 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1265 A--------NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQE-----ETRLKI 1331
Cdd:COG3096 1044 ElgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQakagwCAVLRL 1123
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 25150354 1332 ANINRA-RQLEDEKNALLDekeeAEGLRAHLEKEIHAARQG 1371
Cdd:COG3096 1124 ARDNDVeRRLHRRELAYLS----ADELRSMSDKALGALRLA 1160
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1385-1552 |
1.79e-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: 42.22 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1385 QQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM-----AEERV 1459
Cdd:COG1579 17 SELDRLEHR----LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1460 AVQKALldrDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISnkddfgknvhELEKAKRSLEAELN 1539
Cdd:COG1579 93 ALQKEI---ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDEELAELEAELE 159
|
170
....*....|...
gi 25150354 1540 DMRVQMEELEDNL 1552
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
889-1289 |
2.24e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 43.25 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 889 AVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEK-----NNDERRKQMETVRDLEEQ------ 957
Cdd:PRK10246 429 VALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvkticEQEARIKDLEAQRAQLQAgqpcpl 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 958 ----LEQEEQARQKLLLDktnVDQRlrnleeRLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLEN 1033
Cdd:PRK10246 509 cgstSHPAVEAYQALEPG---VNQS------RLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1034 QLHELEQDLNRERQYKSEL-------EQHKRKL--LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRY------ 1098
Cdd:PRK10246 580 QWQAVCASLNITLQPQDDIqpwldaqEEHERQLrlLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYaltlpq 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1099 -----------DEESANVTLMQKQMRDMQTTIDELREDMETERnarnkaemTRREVVAQLEKVKGDVLDKV-DEATMLQ- 1165
Cdd:PRK10246 660 edeeaswlatrQQEAQSWQQRQNELTALQNRIQQLTPLLETLP--------QSDDLPHSEETVALDNWRQVhEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1166 DLMSRKDEEVNATKRAIEQIQH---TMEGKIEEQKAKFSR---------QVEELHDQIEQHKKQRSQLEKQQNQADQER- 1232
Cdd:PRK10246 732 QLQTLQQQDVLEAQRLQKAQAQfdtALQASVFDDQQAFLAalldeetltQLEQLKQNLENQRQQAQTLVTQTAQALAQHq 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1233 ------ADMAQEIALLQASRADIDKKRKIHEAHLMEIQANL---AESDEHKRTLIDQLERSRDELD 1289
Cdd:PRK10246 812 qhrpdgLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLkqdADNRQQQQALMQQIAQATQQVE 877
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1194-1644 |
2.42e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1194 EEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEH 1273
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1274 KRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEE 1353
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1354 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1433
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1434 ENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDS 1513
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1514 IsnkddfGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLK 1593
Cdd:COG5278 402 A------AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1594 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQL 1644
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1616-1691 |
2.45e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1616 RKKIENQIGELEQQLEVANRLKEEYNKQLK----KNQQIIKEYQIECEEAR-----QAKEDIAALLREADrkfRAVEAER 1686
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAearaEAQEIIEEARKEAEKIKeeilaEAKEEAERILEQAK---AEIEQEK 108
|
....*
gi 25150354 1687 EQLRE 1691
Cdd:cd06503 109 EKALA 113
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
1290-1386 |
2.68e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 41.42 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1290 HLNRVREEEEHAFANMQRRLATAEGQIQ-------------ELNEQIQEETRLKIAnINRARQLEDEKNALLDEKEEAEG 1356
Cdd:NF038305 98 HLNNTRRLSTQALQQINQQAGQQETQLQqqlnqlqaqtspqQLNQLLKSEQKQGQA-LASGQLPEEQKEQLQQFKSNPQA 176
|
90 100 110
....*....|....*....|....*....|
gi 25150354 1357 LRAHLEKEIHAARQGAGEARRKAEESVNQQ 1386
Cdd:NF038305 177 LDKFLAQQLTQIRTQAEEAEKQARLEALKS 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1526-1672 |
2.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1526 ELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESdraisnKDVEAEEKR-RGLLKQIRD------L 1598
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI------EEVEARIKKyEEQLGNVRNnkeyeaL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1599 ENELENEKRGKSGAVSHRKKIENQIGELEQQLEVAN----RLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALL 1672
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEaelaELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1541-1645 |
2.84e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1541 MRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIE 1620
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100
....*....|....*....|....*...
gi 25150354 1621 NQ---IGELEQQLEVANRLKEEYNKQLK 1645
Cdd:COG0542 482 QRygkIPELEKELAELEEELAELAPLLR 509
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1253-1500 |
2.90e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1253 RKIHEAHLMEIQaNLAESDEHKRT--LIDQLERSRDELDHLNRVREEEEHAFANMQR-RLATAEGQIQELNE---QIQEE 1326
Cdd:PRK05771 23 EALHELGVVHIE-DLKEELSNERLrkLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvSVKSLEELIKDVEEeleKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1327 TRLKIANINrarQLEDEKNALLDEKEEAEGLRAhLEKEIHAARQG------------AGEARRKAEESVNQQLEELRKKN 1394
Cdd:PRK05771 102 IKELEEEIS---ELENEIKELEQEIERLEPWGN-FDLDLSLLLGFkyvsvfvgtvpeDKLEELKLESDVENVEYISTDKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1395 -------------------LRDVEHLQKQLEESEVAKERILQSKKKIqQELEDssmELENVRASHRDSEKRQKKFESQMA 1455
Cdd:PRK05771 178 yvyvvvvvlkelsdeveeeLKKLGFERLELEEEGTPSELIREIKEEL-EEIEK---ERESLLEELKELAKKYLEELLALY 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 25150354 1456 EERVAV-QKA-LLDRDAMSQEL--------RDRETRVLSLLNEVDIMKEHLEESD 1500
Cdd:PRK05771 254 EYLEIElERAeALSKFLKTDKTfaiegwvpEDRVKKLKELIDKATGGSAYVEFVE 308
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1633-1816 |
3.00e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.14 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1633 ANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQlreaneglMQARKQLELENDELEE 1712
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA--------EQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1713 LRAKGggiSSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQsLERSNRDYK 1792
Cdd:TIGR02794 124 AKAKQ---AAEAKAKAEAEAERKAKEEAAKQA--EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK-AKAEEAKAK 197
|
170 180
....*....|....*....|....
gi 25150354 1793 AKITELESGAQSRARAQMAALEAK 1816
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1398-1815 |
3.08e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 42.36 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1398 VEHLQKQLEESEVAKERILQSKKKIQQELEDSSM---ELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQE 1474
Cdd:pfam19220 33 IEPIEAILRELPQAKSRLLELEALLAQERAAYGKlrrELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1475 LRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhELEKAKRSLEAELNDMRVQMEELEDnlqi 1554
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQ--------------AAEKALQRAEGELATARERLALLEQ---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1555 aEDARLRLEVTNQALKSESdraISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVShrkKIENQIGELEQQLEVAN 1634
Cdd:pfam19220 175 -ENRRLQALSEEQAAELAE---LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEA---QLEEAVEAHRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1635 RLKEEYNKQLKKNQQIIKEyqieceeARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELR 1714
Cdd:pfam19220 248 MKLEALTARAAATEQLLAE-------ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1715 AKGGGISSEEKRRLEAKIAQLeeeleeeqsncELAIDKQRKAQVQLEQittdlsmertLNQKTEAEKQSLERSNRDYKAk 1794
Cdd:pfam19220 321 AELEERAEMLTKALAAKDAAL-----------ERAEERIASLSDRIAE----------LTKRFEVERAALEQANRRLKE- 378
|
410 420
....*....|....*....|.
gi 25150354 1795 itELESGAQSRARAQmAALEA 1815
Cdd:pfam19220 379 --ELQRERAERALAQ-GALEI 396
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1063-1253 |
3.24e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1063 LEDSKDHLAEKMGKVEEL-NNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRR 1141
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNiEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1142 EVVAQLEKVKGDV--LDKVDEA-TMLQDLmSRKDEEVNATKRAIEQIQHTME---------GKIEEQKAKFSRQVEELHD 1209
Cdd:PHA02562 266 KIKSKIEQFQKVIkmYEKGGVCpTCTQQI-SEGPDRITKIKDKLKELQHSLEkldtaidelEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 25150354 1210 QIEQHK-------KQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKR 1253
Cdd:PHA02562 345 KISTNKqslitlvDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1525-1730 |
3.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1525 HELEKAKRSLEA--ELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSES-DRAISNKDVE---AEEKRRGLLKQIRDL 1598
Cdd:COG4913 242 EALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAElarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1599 ENE---LENEKRGKSGavshrkkieNQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREA 1675
Cdd:COG4913 322 REEldeLEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 25150354 1676 DRKFRAVEAE-REQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEA 1730
Cdd:COG4913 393 LEALEEELEAlEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1426-1870 |
3.40e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1426 LEDSSMELENVRASHRD-SEKRQKKFESQMAEERV--AVQKALLDRDAMSQELR-------DRETRVLSLLNEVDIMKEH 1495
Cdd:PTZ00108 906 LESETLKEKDVIVDYRDySTANTVHFTVKLNDGVLeqWEEEGIEKVFKLKSTISttnmvlfDENGKIKKYSDALDILKEF 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1496 LE---ESDRVRRS-----LQQELQdSISNKDDFGKNVHELE-----KAKRSLEAELNdmRVQMEELEDNLQIAEDARLRL 1562
Cdd:PTZ00108 986 YLvrlDLYKKRKEyllgkLERELA-RLSNKVRFIKHVINGElvitnAKKKDLVKELK--KLGYVRFKDIIKKKSEKITAE 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1563 EVTNQALKSESDRAISNKDVEAEEKRRGLLK---------QIRDLENELeNEKRGKSGAVSHR----------KKIENQI 1623
Cdd:PTZ00108 1063 EEEGAEEDDEADDEDDEEELGAAVSYDYLLSmpiwsltkeKVEKLNAEL-EKKEKELEKLKNTtpkdmwledlDKFEEAL 1141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1624 GELEQQlEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQL 1703
Cdd:PTZ00108 1142 EEQEEV-EEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1704 ELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQS 1783
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS--SDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNG 1298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1784 LERSNRDYKAKItelesgaQSRARAQMAALEAKVQylEDQLNVEGQEKTAA---------NRAARRLEKRLNDTTQQFED 1854
Cdd:PTZ00108 1299 GSKPSSPTKKKV-------KKRLEGSLAALKKKKK--SEKKTARKKKSKTRvkqasasqsSRLLRRPRKKKSDSSSEDDD 1369
|
490
....*....|....*.
gi 25150354 1855 EKRANEQAKELLEKSN 1870
Cdd:PTZ00108 1370 DSEVDDSEDEDDEDDE 1385
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1195-1463 |
3.59e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1195 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEI-------QANL 1267
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellKAKF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1268 AESDEHKRTLIDQLErsrdeLDHLNRVREEEEHAFANMQRRLataEGQIQELNEQIqEETRLKIANI-NRARQLEDEKNa 1346
Cdd:pfam15905 146 SEDGTQKKMSSLSME-----LMKLRNKLEAKMKEVMAKQEGM---EGKLQVTQKNL-EHSKGKVAQLeEKLVSTEKEKI- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1347 llDEKEEAEGLRAHLEkEIHAARQGAGEARRKAeesvnQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQEL 1426
Cdd:pfam15905 216 --EEKSETEKLLEYIT-ELSCVSEQVEKYKLDI-----AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL 287
|
250 260 270
....*....|....*....|....*....|....*..
gi 25150354 1427 EDssmELENVRASHRDSEKRQKKfESQMAEERVAVQK 1463
Cdd:pfam15905 288 ES---EKEELLREYEEKEQTLNA-ELEELKEKLTLEE 320
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
979-1370 |
3.63e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 979 LRNLEERLVELQDAYDKLLKEkrLLEEKVEGLTTQLLDHEERAKHGvkakgRLENQLHELEQDLNRERQYKSELEQHKRK 1058
Cdd:pfam19220 22 LRSLKADFSQLIEPIEAILRE--LPQAKSRLLELEALLAQERAAYG-----KLRRELAGLTRRLSAAEGELEELVARLAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1059 LLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNarnkaem 1138
Cdd:pfam19220 95 LEAALREAEAAKEELRIELRDKTAQA----EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1139 TRREVVAQLEkvkgdvldkvDEATMLQDLMSRKDEEVNATKRAIEQiqhtMEGKIEEQKAKFSRQVEELHDQIEQHKKQR 1218
Cdd:pfam19220 164 TARERLALLE----------QENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1219 SQLEKQQNQADQERADMAQEIALLQASRA--------------DIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERS 1284
Cdd:pfam19220 230 AQLEEAVEAHRAERASLRMKLEALTARAAateqllaearnqlrDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1285 RDELDHLNRVREEEEH-------AFANMQRRLATAEGQIQELNEQIQEETRlkiANINRARQLEDEKNALLDEKEEAEGL 1357
Cdd:pfam19220 310 TQQFQEMQRARAELEEraemltkALAAKDAALERAEERIASLSDRIAELTK---RFEVERAALEQANRRLKEELQRERAE 386
|
410
....*....|...
gi 25150354 1358 RAHLEKEIHAARQ 1370
Cdd:pfam19220 387 RALAQGALEIARE 399
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
979-1356 |
3.67e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 42.32 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 979 LRNLEERLVELQDAYDKLLKEKRL--------------LEEKVEGLTTQLLDHEE-----RAKHgvkakgrLENQLHELE 1039
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIaikraeeavsaskeIEKTVEELTIELIATKEslesaHAAH-------LEAEEHRIG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1040 QDLNRER---QYKSELEQHK---RKLLAELEDSKDHLAekmgKVEELNNQLMKRDEEL-QHQLTRYDEESANVTLMQKQM 1112
Cdd:pfam05701 213 AALAREQdklNWEKELKQAEeelQRLNQQLLSAKDLKS----KLETASALLLDLKAELaAYMESKLKEEADGEGNEKKTS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1113 RDMQTTIDELREDMETERNARNKA--EMTRREVVA-----QLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQI 1185
Cdd:pfam05701 289 TSIQAALASAKKELEEVKANIEKAkdEVNCLRVAAaslrsELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1186 QhTMEGKIEEQKAKFSRQVEELHDQIEQHKKQ----RSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLM 1261
Cdd:pfam05701 369 Q-AKEKEAREKMVELPKQLQQAAQEAEEAKSLaqaaREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1262 EIQAnLAESDEHKRTlIDQLERSR------DELDHLN-RVREEEEHAfanmQRRLATAEGQIQELNEqiqEETRL--KIA 1332
Cdd:pfam05701 448 AIKA-LQESESSAES-TNQEDSPRgvtlslEEYYELSkRAHEAEELA----NKRVAEAVSQIEEAKE---SELRSleKLE 518
|
410 420
....*....|....*....|....
gi 25150354 1333 NINraRQLEDEKNALLDEKEEAEG 1356
Cdd:pfam05701 519 EVN--REMEERKEALKIALEKAEK 540
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1032-1625 |
3.94e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1032 ENQLHELEQDLNRERQYKSELEQH------KRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANV 1105
Cdd:PTZ00440 549 LQSIETLIKDEKLKRSMKNDIKNKikyieeNVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYI 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1106 tLMQKQMRDMQTTIDEL------REDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEatMLQDLMSRKDEEVNATK 1179
Cdd:PTZ00440 629 -LNKFYKGDLQELLDELshflddHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDN--IIKNLKKELQNLLSLKE 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1180 RAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMaqeIALLQASRADIDKKRKIHEAH 1259
Cdd:PTZ00440 706 NIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEF---ILHLYENDKDLPDGKNTYEEF 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1260 LmeiqanlaesdEHKRTLidqLERSRDELDHLNRVREEEEhafaNMQRRLATAEGQIQELneqiQEETRLKIANINRARQ 1339
Cdd:PTZ00440 783 L-----------QYKDTI---LNKENKISNDINILKENKK----NNQDLLNSYNILIQKL----EAHTEKNDEELKQLLQ 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1340 LEDEKNALLDEKEeaeglrahLEKEIHaarqgagEARRKAEESVNQQleELRKKNLRDVEHLQKQLEESEVAK---ERIL 1416
Cdd:PTZ00440 841 KFPTEDENLNLKE--------LEKEFN-------ENNQIVDNIIKDI--ENMNKNINIIKTLNIAINRSNSNKqlvEHLL 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1417 QSKKKIQQELEDSSMELENVRAShRDSEKrqKKFESQMAEERVAVQKALLDrdamsQELRDRETRVLSLLNEVDIMKE-- 1494
Cdd:PTZ00440 904 NNKIDLKNKLEQHMKIINTDNII-QKNEK--LNLLNNLNKEKEKIEKQLSD-----TKINNLKMQIEKTLEYYDKSKEni 975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1495 ------HLEESDRVRRS---LQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQ------MEELEDNLQIAEDAR 1559
Cdd:PTZ00440 976 ngndgtHLEKLDKEKDEwehFKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKekgkeiEEKVDQYISLLEKMK 1055
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1560 LRLEV--TNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGE 1625
Cdd:PTZ00440 1056 TKLSSfhFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTE 1123
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1378-1584 |
3.98e-03 |
|
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: 41.80 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1378 KAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEE 1457
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1458 RVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE 1537
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 25150354 1538 LNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDR-AISNKDVEA 1584
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERlNASERKVEG 255
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1310-1509 |
4.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1310 ATAEGQIQELNEQIQEetrlkiaNINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARR---KAEESVNQQ 1386
Cdd:COG3883 12 AFADPQIQAKQKELSE-------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1387 LEELRK------KNLRDVEHLQkQLEESE---------VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFE 1451
Cdd:COG3883 85 REELGEraralyRSGGSVSYLD-VLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 25150354 1452 SQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQE 1509
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1500-1922 |
4.92e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1500 DRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNdmrvQMEELEDNLQIAEDARLRLEVTNQALKSESDRaisn 1579
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEK---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1580 kdVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKK----NQQIIKEYQ 1655
Cdd:COG4717 121 --LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1656 IECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQL 1735
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1736 EEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKT-----EAEKQSLERSNRDYKAKITELESGAQSRARAQM 1810
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1811 AALEAKVQYLEDQLNVEGQEKTAANRAArrLEKRLNDTtQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEA--EDEMS 1888
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEE--LRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELE 435
|
410 420 430
....*....|....*....|....*....|....
gi 25150354 1889 RERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1922
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1341-1423 |
5.14e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1341 EDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVN-----QQLEELRKKNLRDVEHLQKQ-----LEESEV 1410
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAleglaAELEEKQQELEAQLEQLQEKaaetsQERKQK 217
|
90
....*....|...
gi 25150354 1411 AKERILQSKKKIQ 1423
Cdd:PRK11448 218 RKEITDQAAKRLE 230
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1005-1254 |
6.29e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1005 EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKL---LAELEDSKDHLAEKMGKVEELN 1081
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1082 NQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNK--------AEMTRR-EVVAQLEKVKG 1152
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelvekiKELEKElEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1153 DVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQER 1232
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260
....*....|....*....|..
gi 25150354 1233 ADMAQEIALLQASRADIDKKRK 1254
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKE 261
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1381-1601 |
7.13e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1381 ESVNQQLEELRKknlrdvEHLQKQ-LEESEVAKeRILQSKKKIQQELEDSSmELENVRAS-HRDSEKRQKKFESqmAEER 1458
Cdd:pfam10168 535 QLLSRATQVFRE------EYLKKHdLAREEIQK-RVKLLKLQKEQQLQELQ-SLEEERKSlSERAEKLAEKYEE--IKDK 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1459 vavQKALLDRdamsqelrdretrvlsllnevdiMKehleesdRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAEL 1538
Cdd:pfam10168 605 ---QEKLMRR-----------------------CK-------KVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAI 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25150354 1539 NDMRVQMEELEDNLQIAEDARLRLEVTnqaLKSESDRAISNKDVEAEEKRRGLLKQIRDLENE 1601
Cdd:pfam10168 652 KQAKKKMNYQRYQIAKSQSIRKKSSLS---LSEKQRKTIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1583-1696 |
7.18e-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: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1583 EAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLK--KNQQIIKEYQIECEE 1660
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIES 100
|
90 100 110
....*....|....*....|....*....|....*.
gi 25150354 1661 ARQAKEDIAALLREADRKFRAVEAEREQLREANEGL 1696
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
845-1192 |
7.36e-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: 41.26 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 845 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKkLDQVIVERAVIQEQLQQESENSAELDDIRGR----LQTRNQELE 920
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRtagaMQVEKAQLE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 921 YIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQkllldktnvdQRLRNLEerlvELQDAYDKLLKEK 1000
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS----------ERLRAVK----DIKQERDQLLNEV 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1001 RLLEEKVEGLTTqllDHEERAKHGVKAKGRLENQLHELEQDLnreRQYKSELEQhKRKLLAELEDSKDH----------- 1069
Cdd:pfam15921 663 KTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKLKMQL---KSAQSELEQ-TRNTLKSMEGSDGHamkvamgmqkq 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1070 LAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEK 1149
Cdd:pfam15921 736 ITAKRGQIDALQSKI----QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEV 811
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 25150354 1150 vkgdVLDKVD-EATMLQDLMSRKDEEVNATKraieqIQHTMEGK 1192
Cdd:pfam15921 812 ----ALDKASlQFAECQDIIQRQEQESVRLK-----LQHTLDVK 846
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1146-1406 |
8.03e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 41.21 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1146 QLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTME------------GKIEEQKAKFSRQVEELHDQIEQ 1213
Cdd:COG4192 38 SLSNQIRYILDDSLPKLQASLKLEENSNELVAALPEFAAATNTTErsqlrnqlntqlADIEELLAELEQLTQDAGDLRAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1214 HKKQRSQLEkQQNQADQERADMAQEialLQASRADIdkkRKIHEAHLMEIQANLAESDEHKRTLIDQLErsrdeldhLNR 1293
Cdd:COG4192 118 VADLRNLLQ-QLDSLLTQRIALRRR---LQELLEQI---NWLHQDFNSELTPLLQEASWQQTRLLDSVE--------TTE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1294 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANInrARQLE------DEKNALLDEKEEAEGLRAHLEKEIHA 1367
Cdd:COG4192 183 SLRNLQNELQLLLRLLAIENQIVSLLREVAAARDQADVDNL--FDRLQylkdelDRNLQALKNYPSTITLRQLIDELLAI 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 25150354 1368 AR-QGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLE 1406
Cdd:COG4192 261 GSgEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQIS 300
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
878-1287 |
8.15e-03 |
|
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: 41.03 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 878 EKKLDQVIVERAviqEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQ 957
Cdd:pfam07888 33 QNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 958 LEQEEQARQKLLLDKTNVDQRLRNLEERLvelqdaydKLLKEKRLLEEkvegltTQLLDHEERAKhgvkakgRLENQLHE 1037
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDI--------KTLTQRVLERE------TELERMKERAK-------KAGAQRKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1038 LEQDlnrERQYKSELEQHK---RKLLAELEDSKDHLAEKMGKVEELNNQLMKrdeeLQHQLTRYDEESANVTLMQKQMRD 1114
Cdd:pfam07888 169 EEAE---RKQLQAKLQQTEeelRSLSKEFQELRNSLAQRDTQVLQLQDTITT----LTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1115 MQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIE 1194
Cdd:pfam07888 242 LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR---LQAAQLTLQLADASLALREGRARWAQERETLQQSAE-ADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1195 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQ-ADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQanlaESDEH 1273
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEVELGReKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQ----ELLEY 393
|
410
....*....|....
gi 25150354 1274 KRTLIDQLERSRDE 1287
Cdd:pfam07888 394 IRQLEQRLETVADA 407
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1169-1312 |
8.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1169 SRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQhkkqrsqLEKQQNQADQERADMAQEIALLQASRAD 1248
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN-------LDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25150354 1249 IDKKRKIHEAHLMEIQANLAE-----SDEHKRTLIDQLE-RSRDELDHLNRVREEEEHAFANMQRR--LATA 1312
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEeEARHEAAVLIKEIEEEAKEEADKKAKeiLAQA 197
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1051-1676 |
8.59e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 40.96 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1051 ELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHqltrydEESANVTLMQKQMR-------DMQTTIDELR 1123
Cdd:pfam10174 7 DLQRENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRK------EEAARISVLKEQYRvtqeenqHLQLTIQALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1124 EDMETER--NARNKAEMTRREVVAQlekvkgdvlDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHT---MEGKIEEQKA 1198
Cdd:pfam10174 81 DELRAQRdlNQLLQQDFTTSPVDGE---------DKFSTPELTEENFRRLQSEHERQAKELFLLRKTleeMELRIETQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1199 KFSRQVEELHDQIEQhkKQRSQLEKQQNQADQERadmaqeiallqasradidkKRKIHEAhlmEIQANLAESdehkrtli 1278
Cdd:pfam10174 152 TLGARDESIKKLLEM--LQSKGLPKKSGEEDWER-------------------TRRIAEA---EMQLGHLEV-------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1279 dQLERSRDELDHLnrvREEeehafanMQRRL-ATAEGQIQELNEQIQEETRLKIANINRA-RQLEDE-----KNALL--- 1348
Cdd:pfam10174 200 -LLDQKEKENIHL---REE-------LHRRNqLQPDPAKTKALQTVIEMKDTKISSLERNiRDLEDEvqmlkTNGLLhte 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1349 ---DEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQ--LEELRKKNLRDVEHLQkQLEESEVAKErilQSKKKIQ 1423
Cdd:pfam10174 269 dreEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQtkLETLTNQNSDCKQHIE-VLKESLTAKE---QRAAILQ 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1424 QELEDSSMELENvraSHRDSEKRQKKFeSQMAEERVAVQKALLDrdaMSQELRDRETRVLSLLNEVDIMKEHLEESDRVR 1503
Cdd:pfam10174 345 TEVDALRLRLEE---KESFLNKKTKQL-QDLTEEKSTLAGEIRD---LKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1504 RSLQ---QELQDSISNKDDFGKNVHE-LEKAKRSLEA----ELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDR 1575
Cdd:pfam10174 418 AGLKervKSLQTDSSNTDTALTTLEEaLSEKERIIERlkeqREREDRERLEELESLKKENKDLKEKVSALQPELTEKESS 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1576 AISNKDVEAEEKRRGLLK--QIRDLENELENEKRGKSGAVSHRKKIenqigeleQQLEVANRLKEEYNKQLKKNQQIIKE 1653
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKdsKLKSLEIAVEQKKEECSKLENQLKKA--------HNAEEAVRTNPEINDRIRLLEQEVAR 569
|
650 660
....*....|....*....|...
gi 25150354 1654 YQIECEEARQAKEDIAALLREAD 1676
Cdd:pfam10174 570 YKEESGKAQAEVERLLGILREVE 592
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1335-1433 |
9.07e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1335 NRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQleesevAKER 1414
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQ------AEAE 104
|
90
....*....|....*....
gi 25150354 1415 ILQSKKKIQQELEDSSMEL 1433
Cdd:COG0711 105 IEQERAKALAELRAEVADL 123
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
974-1146 |
9.56e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 974 NVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVK--AKGRLENQLHELEQDLNRERQYKSE 1051
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1052 LEQHKRKLLAELEDSKDHLAEKMGKV-EELNNQ---LMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME 1127
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRIlASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
170
....*....|....*....
gi 25150354 1128 TERNARNKAEMTRREVVAQ 1146
Cdd:COG3206 369 SLLQRLEEARLAEALTVGN 387
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1190-1381 |
9.59e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1190 EGKIEEQKAKFSRQVEELHDQIEQHKKQrsqlekqqnqadqeradmaqeiALLQASRADIDKKRKIHEahlmEIQANLAE 1269
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKE----------------------ALLEAKEEIHKLRNEFEK----ELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150354 1270 SDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEE-TRL-KIANINRarqlEDEKNAL 1347
Cdd:PRK12704 84 LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQlQELeRISGLTA----EEAKEIL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 25150354 1348 LDE-KEEAEGLRAHLEKEIHA-ARQgagEARRKAEE 1381
Cdd:PRK12704 160 LEKvEEEARHEAAVLIKEIEEeAKE---EADKKAKE 192
|
|
| |
