|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
76-719 |
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: 1291.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQ 314
Cdd:cd01384 161 TYLLERSRVVQVSDPERNYHCFYQLCAgAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 315 EQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSAT 394
Cdd:cd01384 241 EQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAAT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 395 VSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEY 474
Cdd:cd01384 321 LSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKMEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 475 TREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTAFTIQHYAGDV 554
Cdd:cd01384 401 TKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPKLSRTDFTIDHYAGDV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 555 IYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPP-ASEENTKSSK-SSIATRFKVQLHELMETLSSTEPHYIRCVKP 632
Cdd:cd01384 481 TYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPlPREGTSSSSKfSSIGSRFKQQLQELMETLNTTEPHYIRCIKP 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 633 NSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKVTCQKVLDKMGLQGYQIG 712
Cdd:cd01384 561 NNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEVLKGSDDEKAACKKILEKAGLKGYQIG 640
|
....*..
gi 1002232322 713 RTKVFLR 719
Cdd:cd01384 641 KTKVFLR 647
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
58-730 |
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: 1005.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 58 EAPPDGVDDMTRLSYLHEPGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGANLGDLDPHVFAIAD 137
Cdd:smart00242 2 PPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTD-EVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 138 VSYRQMMNEGRNNSILVSGESGAGKTETTKLLMRYLAYLGGRSGTGGRtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGK 217
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS-VEDQILESNPILEAFGNAKTLRNNNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 218 FVEIQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDA 296
Cdd:smart00242 160 FIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAgASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 297 EEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfHLNTAAELLMCDCKKLENALIKRE 376
Cdd:smart00242 240 EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKE--ELSNAAELLGVDPEELEKALTKRK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 377 INTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNE 456
Cdd:smart00242 318 IKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGFEIFEVNSFEQLCINYANE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 457 KLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFT 536
Cdd:smart00242 398 KLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 537 KP-KLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSK-SSIATRFKVQLHE 614
Cdd:smart00242 478 KPkKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSNAGSKKRfQTVGSQFKEQLNE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 615 LMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA-SEIVKEKNDE 693
Cdd:smart00242 558 LMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLpDTWPPWGGDA 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 1002232322 694 KVTCQKVLDKMGL--QGYQIGRTKVFLRAGQMAELDARR 730
Cdd:smart00242 638 KKACEALLQSLGLdeDEYQLGKTKVFLRPGQLAELEELR 676
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
76-719 |
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: 891.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLG-DLDPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLP-LYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLAYL----GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKIS 230
Cdd:cd00124 80 SGESGAGKTETTKLVLKYLAALsgsgSSKSSSSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 231 GAAIRTYLLERSRVCQINSPERNYHCFYFLCA-----APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNA 305
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAglsdgAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 306 MDTVGIIEQEQEAIFRVVAAVLHLGNINFAK--GSEVDSSVIKDDKsrfHLNTAAELLMCDCKKLENALIKREINTPEGV 383
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEdeEDEDSSAEVADDE---SLKAAAKLLGVDAEDLEEALTTRTIKVGGET 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 384 ITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKL--IGVLDIYGFESFKTNSFEQLCINFTNEKLQQH 461
Cdd:cd00124 317 ITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAESTsfIGILDIFGFENFEVNSFEQLCINYANEKLQQF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 462 FNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRF-TKPKL 540
Cdd:cd00124 397 FNQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFfSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 541 SRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASrcsfvsalfppaseentksskssiaTRFKVQLHELMETLS 620
Cdd:cd00124 477 AKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG-------------------------SQFRSQLDALMDTLN 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 621 STEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEK---VTC 697
Cdd:cd00124 532 STQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKkaaVLA 611
|
650 660
....*....|....*....|..
gi 1002232322 698 QKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd00124 612 LLLLLKLDSSGYQLGKTKVFLR 633
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
64-719 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 861.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 64 VDDMTRLSYLHEPGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQM 143
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLP-IYSEDMIKAYRGKRRGELPPHIFAIADEAYRSM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 144 MNEGRNNSILVSGESGAGKTETTKLLMRYLAYLG-GRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQ 222
Cdd:pfam00063 80 LQDKENQSILISGESGAGKTENTKKIMQYLASVSgSGSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 223 FDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLV 301
Cdd:pfam00063 160 FDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAgASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 302 TRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKREINTPE 381
Cdd:pfam00063 240 TDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTEN---LQKAASLLGIDSTELEKALCKRRIKTGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 382 GVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPN-SDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQ 460
Cdd:pfam00063 317 ETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIeKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 461 HFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKL 540
Cdd:pfam00063 397 FFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKPRL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 541 -SRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENT---------------KSSKSSI 604
Cdd:pfam00063 477 qGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESaaanesgkstpkrtkKKRFITV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 605 ATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA- 683
Cdd:pfam00063 557 GSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAp 636
|
650 660 670
....*....|....*....|....*....|....*...
gi 1002232322 684 SEIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:pfam00063 637 KTWPKWKGDAKKGCEAILQSLNLDKeeYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
9-1513 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 840.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 9 IGSHVWVEDKDSAWVDGEVFRID---------GKNAHVRTTKGKTVIANVSDIHPKDTeappDGVDDMTRLSYLHEPGVL 79
Cdd:COG5022 8 VGSGCWIPDEEKGWIWAEIIKEAfnkgkvteeGKKEDGESVSVKKKVLGNDRIKLPKF----DGVDDLTELSYLNEPAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 80 DNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGESG 159
Cdd:COG5022 84 HNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTD-DIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 160 AGKTETTKLLMRYLAYLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTYLL 239
Cdd:COG5022 163 AGKTENAKRIMQYLASVTSSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 240 ERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKL-GDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQEQEA 318
Cdd:COG5022 243 EKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLlQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDEEEQDQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 319 IFRVVAAVLHLGNINFAKGSEvDSSVIKDDKsrfHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVSRD 398
Cdd:COG5022 323 IFKILAAILHIGNIEFKEDRN-GAAIFSDNS---VLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 399 GLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQ 478
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 479 INWSYIEFVDNQDVLDLIEKK-PGGIIALLDEACMFPKSTHETFSQKLYEKF-KNHKR-FTKPKLSRTAFTIQHYAGDVI 555
Cdd:COG5022 479 IEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRLnKNSNPkFKKSRFRDNKFVVKHYAGDVE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 556 YQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSV 635
Cdd:COG5022 559 YDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEE 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 636 LKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASE-----IVKEKNDEKVTCQKVLDKMGL--QG 708
Cdd:COG5022 639 KSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSkswtgEYTWKEDTKNAVKSILEELVIdsSK 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 709 YQIGRTKVFLRAGQMAELDARRTEVRNNAARGVQGQFRTHVAREQFLilrnASVCLQSFVRARLACKLHECLRREA---- 784
Cdd:COG5022 719 YQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYL----QALKRIKKIQVIQHGFRLRRLVDYElkwr 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 785 AAIKIQKNIRCYfAWRTYSQLRLSAIT-LQTGLRTMAALKEFMFRKQN-KATTHIQTQWRCHRDNSNYLKLKRAALTYQC 862
Cdd:COG5022 795 LFIKLQPLLSLL-GSRKEYRSYLACIIkLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 863 AWRRRVARRELRQLRMAARDTQALKVAKEKLEERVEELTNRlgLEKKLRTDLEkSKVAEVSKLQAALNEMEqrmqdvtam 942
Cdd:COG5022 874 AQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKS--LSSDLIENLE-FKTELIARLKKLLNNID--------- 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 943 qeresakkaVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKahanaqerneeLSKEVEDADGKIKQLSDTVQRL 1022
Cdd:COG5022 942 ---------LEEGPSIEYVKLPELNKLHEVESKLKETSEEYEDLLKK-----------STILVREGNKANSELKNFKKEL 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1023 EETIQEREALLLAERQEKEEASAViaesqarneafaSKLEDAEKQIDLLQETVQRFEEaITKLQSSVTIEKQQHEETVVQ 1102
Cdd:COG5022 1002 AELSKQYGALQESTKQLKELPVEV------------AELQSASKIISSESTELSILKP-LQKLKGLLLLENNQLQARYKA 1068
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1103 LaeaqakidELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIedaDKSIAH 1182
Cdd:COG5022 1069 L--------KLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEI---SKFLSQ 1137
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1183 YHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGElQRNLEDA--DRRNNQLQDSLQRLEENVGAKESLLLTE 1260
Cdd:COG5022 1138 LVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSE-KRLYQSAlyDEKSKLSSSEVNDLKNELIALFSKIFSG 1216
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1261 REQNASTLKLLAEAHLeIDELIRKLEDSDRKSDSLQSTIKRleedgiAKEALLLTEKQAHEatrmtLTEALEKNEELL-K 1339
Cdd:COG5022 1217 WPRGDKLKKLISEGWV-PTEYSTSLKGFNNLNKKFDTPASM------SNEKLLSLLNSIDN-----LLSSYKLEEEVLpA 1284
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1340 KIHDDDKHILELQF-------TIQRLEENTAAKENLLL-----REREQNDATTKAQ--IESQERNEQLLKRFVDVDRKID 1405
Cdd:COG5022 1285 TINSLLQYINVGLFnalrtkaSSLRWKSATEVNYNSEElddwcREFEISDVDEELEelIQAVKVLQLLKDDLNKLDELLD 1364
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1406 ----LLQDTIERIGEnstiKDALLLSERQEKDAIKKElVEAGERNEELIMKIEDTDKKIEHLQnAIIKLegdiEAKDISL 1481
Cdd:COG5022 1365 acysLNPAEIQNLKS----RYDPADKENNLPKEILKK-IEALLIKQELQLSLEGKDETEVHLS-EIFSE----EKSLISL 1434
|
1530 1540 1550
....*....|....*....|....*....|..
gi 1002232322 1482 eaareENDTIRKSLAEAQEKNEELLRKISDNE 1513
Cdd:COG5022 1435 -----DRNSIYKEEVLSSLSALLTKEKIALLD 1461
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
76-719 |
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: 836.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYA-RNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd01380 1 PAVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLP-IYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLAYLGGRSGTGGRtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAI 234
Cdd:cd01380 80 SGESGAGKTVSAKYAMRYFATVGGSSSGETQ-VEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 235 RTYLLERSRVCQINSPERNYHCFYFLCAAPPEDI-KRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIE 313
Cdd:cd01380 159 RTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPElKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 314 QEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKsrfHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSA 393
Cdd:cd01380 239 EEQMEIFRILAAILHLGNVEIKATRNDSASISPDDE---HLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASIG--QDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQ 471
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALAspVKEKQHSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 472 EEYTREQINWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPKSTHETFSQKLYEKFKNHKR--FTKPKLSRTAFTIQH 549
Cdd:cd01380 396 EEYVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTAFIVKH 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 550 YAGDVIYQSDHFLDKNKDYVVAEHQELLNASrcsfvsalfppaseentKSSKSSIATRFKVQLHELMETLSSTEPHYIRC 629
Cdd:cd01380 475 FADDVEYQVEGFLEKNRDTVSEEHLNVLKAS-----------------KNRKKTVGSQFRDSLILLMETLNSTTPHYVRC 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 630 VKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKVTCQKVLDKMGL--Q 707
Cdd:cd01380 538 IKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLRDDKKKTCENILENLILdpD 617
|
650
....*....|..
gi 1002232322 708 GYQIGRTKVFLR 719
Cdd:cd01380 618 KYQFGKTKIFFR 629
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
76-719 |
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: 777.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLgdLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd01383 1 PSVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVP-LYGNEFITAYRQKLL--DSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTggrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG----IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQ 314
Cdd:cd01383 154 TYLLEKSRVVQLANGERSYHIFYQLCAgASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 315 EQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSAT 394
Cdd:cd01383 234 DQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEA---VSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 395 VSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTgRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKlsRTAFTIQHYAGD 553
Cdd:cd01383 391 YELDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 554 VIYQSDHFLDKNKDYVVAEHQELLNASRCSFV-----------SALFPPASEENTKSSKSSIATRFKVQLHELMETLSST 622
Cdd:cd01383 469 VTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPqlfaskmldasRKALPLTKASGSDSQKQSVATKFKGQLFKLMQRLENT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 623 EPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKVTCQKVLD 702
Cdd:cd01383 549 TPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLSTSVAILQ 628
|
650
....*....|....*....
gi 1002232322 703 KMGLQG--YQIGRTKVFLR 719
Cdd:cd01383 629 QFNILPemYQVGYTKLFFR 647
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
76-719 |
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: 755.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnlvdVRT---MEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSI 152
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLP----IYTeevIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 153 LVSGESGAGKTETTKLLMRYLAYL------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd01377 77 LITGESGAGKTENTKKVIQYLASVaasskkKKESGKKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNA 305
Cdd:cd01377 157 GKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSgADPELKEKLLLTGDPSYYFFLSQGELTIDGVDDAEEFKLTDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 306 MDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKREINTPEGVIT 385
Cdd:cd01377 237 FDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEE---ADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 386 TTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQN 465
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 466 VFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFT---KPKLS 541
Cdd:cd01377 394 MFVLEQEEYKKEGIEWTFIDFgLDLQPTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFkkpKPKKS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 542 RTAFTIQHYAGDVIYQSDHFLDKNKDyVVAEH-QELLNASRCSFVSALFPPASEENTKSSKSS--------IATRFKVQL 612
Cdd:cd01377 474 EAHFILKHYAGDVEYNIDGWLEKNKD-PLNENvVALLKKSSDPLVASLFKDYEESGGGGGKKKkkggsfrtVSQLHKEQL 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 613 HELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEK-N 691
Cdd:cd01377 553 NKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGfD 632
|
650 660 670
....*....|....*....|....*....|
gi 1002232322 692 DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd01377 633 DGKAACEKILKALQLdpELYRIGNTKVFFK 662
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
77-719 |
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: 750.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 77 GVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSG 156
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELP-IYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 157 ESGAGKTETTKLLMRYLAylggRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRT 236
Cdd:cd14883 81 ESGAGKTETTKLILQYLC----AVTNNHSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 237 YLLERSRVCQINSPERNYHCFYFLCA---APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIE 313
Cdd:cd14883 157 YLLEQSRITFQAPGERNYHVFYQLLAgakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 314 QEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRfhLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSA 393
Cdd:cd14883 237 EMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKEI--LKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd14883 315 RDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLEQEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKP--KLSRTAFTIQHYA 551
Cdd:cd14883 395 YEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPdrRRWKTEFGVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 552 GDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEEN----------------TKSSKSSIATRFKVQLHEL 615
Cdd:cd14883 475 GEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPDLLAltglsislggdttsrgTSKGKPTVGDTFKHQLQSL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 616 METLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILAseIVKEKNDEKV 695
Cdd:cd14883 555 VDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLD--PRARSADHKE 632
|
650 660
....*....|....*....|....*....
gi 1002232322 696 TCQKVLDKMGLQG-----YQIGRTKVFLR 719
Cdd:cd14883 633 TCGAVRALMGLGGlpedeWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
77-719 |
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: 735.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 77 GVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSG 156
Cdd:cd01381 2 GILRNLLIRYREKLIYTYTGSILVAVNPYQILP-IYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 157 ESGAGKTETTKLLMRYLAylggRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRT 236
Cdd:cd01381 81 ESGAGKTESTKLILQYLA----AISGQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 237 YLLERSRVCQINSPERNYHCFYFLCAA-PPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQE 315
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGlSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 316 QEAIFRVVAAVLHLGNINFaKGSEV---DSSVIKDdksRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSS 392
Cdd:cd01381 237 IWDIFKLLAAILHLGNIKF-EATVVdnlDASEVRD---PPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 393 ATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD---KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKM 469
Cdd:cd01381 313 ALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDssrTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 470 EQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKlSR--TAFTI 547
Cdd:cd01381 393 EQEEYDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPK-SDlnTSFGI 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 548 QHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSS--IATRFKVQLHELMETLSSTEPH 625
Cdd:cd01381 472 NHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISMGSETRKKSptLSSQFRKSLDQLMKTLSACQPF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 626 YIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVK-EKNDEKVTCQKVLDKM 704
Cdd:cd01381 552 FVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPaHKTDCRAATRKICCAV 631
|
650
....*....|....*..
gi 1002232322 705 GLQG--YQIGRTKVFLR 719
Cdd:cd01381 632 LGGDadYQLGKTKIFLK 648
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
78-719 |
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: 723.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd01378 3 INENLKKRFENDEIYTYIGHVLISVNPFKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTY 237
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVERVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQEQ 316
Cdd:cd01378 162 LLEKSRVVGQIKGERNFHIFYqLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 317 EAIFRVVAAVLHLGNINFAKGSEvDSSVIKDDKsrfHLNTAAELLMCDCKKLENALIKREINTPEG---VITTTVGPSSA 393
Cdd:cd01378 242 DSIFRILAAILHLGNIQFAEDEE-GNAAISDTS---VLDFVAYLLGVDPDQLEKALTHRTIETGGGgrsVYEVPLNVEQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASI-GQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQE 472
Cdd:cd01378 318 AYARDALAKAIYSRLFDWIVERINKSLaAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 473 EYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-KSTHETFSQKLYEKFKNHKRFTKPK----LSRTAFTI 547
Cdd:cd01378 398 EYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEFRI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 548 QHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEPHYI 627
Cdd:cd01378 478 KHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLDSKKRPPTAGTKFKNSANALVETLMKKQPSYI 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 628 RCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEI--VKEKNDEKVTCQKVLDKMG 705
Cdd:cd01378 558 RCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTwpAWDGTWQGGVESILKDLNI 637
|
650
....*....|....*
gi 1002232322 706 LQG-YQIGRTKVFLR 719
Cdd:cd01378 638 PPEeYQMGKTKIFIR 652
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
79-719 |
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: 693.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 79 LDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGES 158
Cdd:cd01382 4 LNNIRVRYSKDKIYTYVANILIAVNPYFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSGES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 159 GAGKTETTKLLMRYLAYLGGRSGTGgrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTYL 238
Cdd:cd01382 84 GAGKTESTKYILRYLTESWGSGAGP---IEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 239 LERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGDPSsfhylnqsscirvdgINDAEEYLVTRNAMDTVGIIEQEQEA 318
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPL---------------LDDVGDFIRMDKAMKKIGLSDEEKLD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 319 IFRVVAAVLHLGNINF-AKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVG-----PSS 392
Cdd:cd01382 226 IFRVVAAVLHLGNIEFeENGSDSGGGCNVKPKSEQSLEYAAELLGLDQDELRVSLTTRVMQTTRGGAKGTVIkvplkVEE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 393 ATVSRDGLAKQIYSRLFDWLVNRINASIGQDpNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQE 472
Cdd:cd01382 306 ANNARDALAKAIYSKLFDHIVNRINQCIPFE-TSSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNERILKEEQE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 473 EYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRT--------- 543
Cdd:cd01382 385 LYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPRKSKLkihrnlrdd 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 544 -AFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKS-------SIATRFKVQLHEL 615
Cdd:cd01382 465 eGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNNKDSKQKagklsfiSVGNKFKTQLNLL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 616 METLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR-ILASEIVKEknDEK 694
Cdd:cd01382 545 MDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKkYLPPKLARL--DPR 622
|
650 660
....*....|....*....|....*..
gi 1002232322 695 VTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd01382 623 LFCKALFKALGLNEndFKFGLTKVFFR 649
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
76-719 |
0e+00 |
|
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: 651.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKgANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPGLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDK---------S 226
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsgdR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAA----------PPEDIKRYKLG--------------DPSSFHYL 282
Cdd:cd14888 160 GRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareakntglsYEENDEKLAKGadakpisidmssfePHLKFRYL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 283 NQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLM 362
Cdd:cd14888 240 TKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLEKVASLLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 363 CDCKKLENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLI-GVLDIYGFESF 441
Cdd:cd14888 320 VDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFcGVLDIFGFECF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 442 KTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETF 521
Cdd:cd14888 400 QLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDEECFVPGGKDQGL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 522 SQKLYEKFKNHKRFTKPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPP----ASEENT 597
Cdd:cd14888 480 CNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFSAylrrGTDGNT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 598 KSSK-SSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFL 676
Cdd:cd14888 560 KKKKfVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFY 639
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1002232322 677 HRFRILASEivkekndekvtcqkvLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14888 640 NDYRILLNG---------------EGKKQLSIWAVGKTLCFFK 667
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
76-719 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 646.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLP-LYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTggrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCAAPPEDiKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQE 315
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPA-SRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFDDAD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 316 QEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTT-VGPSSAT 394
Cdd:cd14872 235 INNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRLMEIKGCDPTRIpLTPAQAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 395 VSRDGLAKQIYSRLFDWLVNRINASI-GQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd14872 315 DACDALAKAAYSRLFDWLVKKINESMrPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLEEAL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRF--TKPKLSRTAFTIQHYA 551
Cdd:cd14872 395 YQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFvyAEVRTSRTEFIVKHYA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 552 GDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPaSEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVK 631
Cdd:cd14872 475 GDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPP-SEGDQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 632 PNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKE-KNDEKVTCQKVLDKMG--LQG 708
Cdd:cd14872 554 PNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVKTIAKRvGPDDRQRCDLLLKSLKqdFSK 633
|
650
....*....|.
gi 1002232322 709 YQIGRTKVFLR 719
Cdd:cd14872 634 VQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
76-718 |
0e+00 |
|
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: 641.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKY------KGANLGDLDPHVFAIADVSYRQMM----N 145
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLP-LYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLfasrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 146 EGRNNSILVSGESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQ-----QVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14901 80 QKCDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERenvrdRVLESNPILEAFGNARTNRNNNSSRFGKFIR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 221 IQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLC-AAPPEDIKRYKLGDPSSFHYLNQSSC-IRVDGINDAEE 298
Cdd:cd14901 160 LGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLrGASSDELHALGLTHVEEYKYLNSSQCyDRRDGVDDSVQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 299 YLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFA-KGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKREI 377
Cdd:cd14901 240 YAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVkKDGEGGTFSMSSLAN---VRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 378 NTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD--KLIGVLDIYGFESFKTNSFEQLCINFTN 455
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGasRFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 456 EKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRF 535
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 536 TKPKLSR--TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSalfppaseentksskSSIATRFKVQLH 613
Cdd:cd14901 477 SVSKLQQgkRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLS---------------STVVAKFKVQLS 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 614 ELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEK--- 690
Cdd:cd14901 542 SLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTwkv 621
|
650 660 670
....*....|....*....|....*....|...
gi 1002232322 691 -----NDEKVTCQKVLDKMGLQGYQIGRTKVFL 718
Cdd:cd14901 622 nelaeRLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
76-719 |
0e+00 |
|
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: 631.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRtveQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTI---KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCAAPpEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQE 315
Cdd:cd14903 158 TYLLEKTRVISHERPERNYHIFYQLLASP-DVEERLFLDSANECAYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 316 QEAIFRVVAAVLHLGNINF-AKGSEVDSSVIKDDKSrfHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSAT 394
Cdd:cd14903 237 QEVLFEVLAGILHLGQLQIqSKPNDDEKSAIAPGDQ--GAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 395 VSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEY 474
Cdd:cd14903 315 DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKTVQIEY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 475 TREQINWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPKSTHETFSQKL---YEKFKNHKRFtkPKLSRTAFTIQHYA 551
Cdd:cd14903 395 EEEGIRWAHIDFADNQDVLAVIEDRL-GIISLLNDEVMRPKGNEESFVSKLssiHKDEQDVIEF--PRTSRTQFTIKHYA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 552 GDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF-PPASEENTKSSKS---------------SIATRFKVQLHEL 615
Cdd:cd14903 472 GPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFkEKVESPAAASTSLargarrrrggaltttTVGTQFKDSLNEL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 616 METLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEivKEKNDEKV 695
Cdd:cd14903 552 MTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPE--GRNTDVPV 629
|
650 660
....*....|....*....|....*....
gi 1002232322 696 T--CQKVLDKMGLQG---YQIGRTKVFLR 719
Cdd:cd14903 630 AerCEALMKKLKLESpeqYQMGLTRIYFQ 658
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
78-719 |
0e+00 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 620.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEG----RNNSIL 153
Cdd:cd14890 3 LLHTLRLRYERDEIYTYVGPILISINPYKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGvldpSNQSII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 154 VSGESGAGKTETTKLLMRYLA---------------YLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKF 218
Cdd:cd14890 83 ISGESGAGKTEATKIIMQYLAritsgfaqgasgegeAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFGKF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 219 VEIQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLnQSSCIRVDGINDAE 297
Cdd:cd14890 163 IEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALReRLKLQTPVEYFYL-RGECSSIPSCDDAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 298 EYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAkgSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREI 377
Cdd:cd14890 242 AFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE--SENDTTVLEDATTLQSLKLAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 378 NTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEK 457
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYANEK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 458 LQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIAL---LDEACMFPKSTHET-FSQKLYEKF---- 529
Cdd:cd14890 400 LQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNGKPGIfitLDDCWRFKGEEANKkFVSQLHASFgrks 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 530 ---------KNHKRFTKPKL-SRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSAlfppaseentks 599
Cdd:cd14890 480 gsggtrrgsSQHPHFVHPKFdADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRSIREV------------ 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 600 sksSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRF 679
Cdd:cd14890 548 ---SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDF 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1002232322 680 RILASEivkEKNDEKVTcqKVLDKM---GLQGYQIGRTKVFLR 719
Cdd:cd14890 625 QVLLPT---AENIEQLV--AVLSKMlglGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
79-719 |
0e+00 |
|
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: 607.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 79 LDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDV-RTMEKYKGANLGDLD-PHVFAIADVSYRQMM----NEGRNNSI 152
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVpGFDSQRKEEATASSPpPHVFSIAERAYRAMKgvgkGQGTPQSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 153 LVSGESGAGKTETTKLLMRYLA---------YLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14892 84 VVSGESGAGKTEASKYIMKYLAtasklakgaSTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQIHY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 224 DKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVT 302
Cdd:cd14892 164 NSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENaALELTPAESFLFLNQGNCVEVDGVDDATEFKQL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 303 RNAMDTVGIIEQEQEAIFRVVAAVLHLGNINF---AKGSEVDSSVIKDDKsrfhLNTAAELLMCDCKKLENALIKREINT 379
Cdd:cd14892 244 RDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFeenADDEDVFAQSADGVN----VAKAAGLLGVDAAELMFKLVTQTTST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 380 PEG-VITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQ----------DPNSDKLIGVLDIYGFESFKTNSFEQ 448
Cdd:cd14892 320 ARGsVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQqtsgvtggaaSPTFSPFIGILDIFGFEIMPTNSFEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 449 LCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-KSTHETFSQKLY- 526
Cdd:cd14892 400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKrKTTDKQLLTIYHq 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 527 EKFKNHKRFTKPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRcsfvsalfppaseentksskssiat 606
Cdd:cd14892 480 THLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSS------------------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 607 RFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEI 686
Cdd:cd14892 535 KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNK 614
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1002232322 687 VKEKNDE---------KVTCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14892 615 AGVAASPdacdattarKKCEEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
79-719 |
0e+00 |
|
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: 599.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 79 LDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGES 158
Cdd:cd01385 4 LENLRARFKHGKIYTYVGSILIAVNPFKFLP-IYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 159 GAGKTETTKLLMRYLAYLGGRSGTGGrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTYL 238
Cdd:cd01385 83 GSGKTESTNFLLHHLTALSQKGYGSG--VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 239 LERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQEQE 317
Cdd:cd01385 161 LEKSRIVSQEKNERNYHVFYYLLAgASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 318 AIFRVVAAVLHLGNINF-AKGSEVDSSVikDDKSRFHLNTAAELLMCDCKKLENALIKREINTP-EGVITTTVGPSsATV 395
Cdd:cd01385 241 QIFSVLSAVLHLGNIEYkKKAYHRDESV--TVGNPEVLDIISELLRVKEETLLEALTTKKTVTVgETLILPYKLPE-AIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 396 SRDGLAKQIYSRLFDWLVNRINASI----GQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQ 471
Cdd:cd01385 318 TRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 472 EEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTAFTIQHYA 551
Cdd:cd01385 398 EEYKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 552 GDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVS--------ALF---------------------------PPASEEN 596
Cdd:cd01385 478 GKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVReligidpvAVFrwavlrafframaafreagrrraqrtaGHSLTLH 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 597 TKSSKS-----------SIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAG 665
Cdd:cd01385 558 DRTTKSllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSG 637
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 666 YPTRKLFHDFLHRFRILASEIVKEKNDekvTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd01385 638 YSVRYTFQEFITQFQVLLPKGLISSKE---DIKDFLEKLNLDrdNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
78-719 |
0e+00 |
|
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: 596.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14873 3 IMYNLFQRYKRNQIYTYIGSILASVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGR-----SGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGA 232
Cdd:cd14873 83 SGAGKTESTKLILKFLSVISQQslelsLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 233 AIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKR-YKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGI 311
Cdd:cd14873 163 RIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREeFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVMQF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 312 IEQEQEAIFRVVAAVLHLGNINF--AKGSEVDSSVIkddksrfhLNTAAELLMCDCKKLENALIKREINTPEGVITTTVG 389
Cdd:cd14873 243 SKEEVREVSRLLAGILHLGNIEFitAGGAQVSFKTA--------LGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLN 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 390 PSSATVSRDGLAKQIYSRLFDWLVNRINASI-GQDpnSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFK 468
Cdd:cd14873 315 VQQAVDSRDSLAMALYARCFEWVIKKINSRIkGKE--DFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFS 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 469 MEQEEYTREQINWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTAFTIQ 548
Cdd:cd14873 393 LEQLEYSREGLVWEDIDWIDNGECLDLIEKKL-GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNFGVK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 549 HYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEEN--------TKSSKSSIATRFKVQLHELMETLS 620
Cdd:cd14873 472 HYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNnqdtlkcgSKHRRPTVSSQFKDSLHSLMATLS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 621 STEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKnDEKVTCQKV 700
Cdd:cd14873 552 SSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPE-DVRGKCTSL 630
|
650 660
....*....|....*....|.
gi 1002232322 701 LDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14873 631 LQLYDASNseWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
78-719 |
0e+00 |
|
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: 589.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLpNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd01379 3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNL-GIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGgrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTY 237
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNRT---LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFYFLCA--APPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDA---EEYLVTRNAMDTVGII 312
Cdd:cd01379 159 LLEKSRVVHQAIGERNFHIFYYIYAglAEDKKLAKYKLPENKPPRYLQNDGLTVQDIVNNSgnrEKFEEIEQCFKVIGFT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 313 EQEQEAIFRVVAAVLHLGNINFakgSEVDSSVIKDDKSRFH----LNTAAELLMCDCKKLENALIKREINTPEGVITTTV 388
Cdd:cd01379 239 KEEVDSVYSILAAILHIGDIEF---TEVESNHQTDKSSRISnpeaLNNVAKLLGIEADELQEALTSHSVVTRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINA--SIGQDPNSDKL-IGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQN 465
Cdd:cd01379 316 TVEEATDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPLsIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 466 VFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKnHKRFTKPKLSRTAF 545
Cdd:cd01379 396 IFAWEQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKFHNNIK-SKYYWRPKSNALSF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 546 TIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVsalfppaseentkssKSSIATRFKVQLHELMETLSSTEPH 625
Cdd:cd01379 475 GIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV---------------RQTVATYFRYSLMDLLSKMVVGQPH 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 626 YIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA---SEIVKEKNDekvTCQKVLD 702
Cdd:cd01379 540 FVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAfkwNEEVVANRE---NCRLILE 616
|
650
....*....|....*..
gi 1002232322 703 KMGLQGYQIGRTKVFLR 719
Cdd:cd01379 617 RLKLDNWALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
78-719 |
0e+00 |
|
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: 586.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFqRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd01387 3 VLWNLKTRYERNLIYTYIGSILVSVNPY-KMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGgrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdKSGKISGAAIRTY 237
Cdd:cd01387 82 SGSGKTEATKLIMQYLAAVNQRRNNL---VTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF-EGGVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQEQ 316
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRqKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 317 EAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVS 396
Cdd:cd01387 238 DSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 397 RDGLAKQIYSRLFDWLVNRINaSIGQDPNSDKL-IGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYT 475
Cdd:cd01387 318 RDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLsIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQEEYI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 476 REQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTAFTIQHYAGDVI 555
Cdd:cd01387 397 REQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAGQVW 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 556 YQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPP--ASEENTKSSKS------------SIATRFKVQLHELMETLSS 621
Cdd:cd01387 477 YQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSShrAQTDKAPPRLGkgrfvtmkprtpTVAARFQDSLLQLLEKMER 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 622 TEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASE--IVKEKNDEKVTCQK 699
Cdd:cd01387 557 CNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALklPRPAPGDMCVSLLS 636
|
650 660
....*....|....*....|.
gi 1002232322 700 VLDKMGLQG-YQIGRTKVFLR 719
Cdd:cd01387 637 RLCTVTPKDmYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
78-719 |
0e+00 |
|
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: 574.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANL-GDLDPHVFAIADVSYRQMMNEGRNNSILVSG 156
Cdd:cd14897 3 IVQTLKSRYNKDKFYTYIGDILVAVNPCKPLP-IFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 157 ESGAGKTETTKLLMRYLAYLGGRSGTGgrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRT 236
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDSD---LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 237 YLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLnQSSCIRVDGINDAEEYLVTR-------NAMDT 308
Cdd:cd14897 159 YLLEKSRVVHRGNGEKNFHIFYALFAgMSRDRLLYYFLEDPDCHRIL-RDDNRNRPVFNDSEELEYYRqmfhdltNIMKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 309 VGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDksrFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTV 388
Cdd:cd14897 238 IGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADE---YPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINASIgqDPNSDKL-------IGVLDIYGFESFKTNSFEQLCINFTNEKLQQH 461
Cdd:cd14897 315 SLRQANDSRDALAKDLYSRLFGWIVGQINRNL--WPDKDFQimtrgpsIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 462 FNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLS 541
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 542 RTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFppaseentksskssiATRFKVQLHELMETLSS 621
Cdd:cd14897 473 RVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLF---------------TSYFKRSLSDLMTKLNS 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 622 TEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKVTCQKVL 701
Cdd:cd14897 538 ADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFSNKVRSDDLGKCQKIL 617
|
650
....*....|....*...
gi 1002232322 702 DKMGLQGYQIGRTKVFLR 719
Cdd:cd14897 618 KTAGIKGYQFGKTKVFLK 635
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
76-719 |
1.56e-180 |
|
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: 563.90 E-value: 1.56e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYA-RNL-IYTYTGNILIAINPFQRLPNlvdvRTMEKYKGANLGDLDPHVFAIADVSYRQM-MNEGR--NN 150
Cdd:cd14891 1 AGILHNLEERSKlDNQrPYTFMANVLIAVNPLRRLPE----PDKSDYINTPLDPCPPHPYAIAEMAYQQMcLGSGRmqNQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 151 SILVSGESGAGKTETTKLLMRYL---------------AYLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRF 215
Cdd:cd14891 77 SIVISGESGAGKTETSKIILRFLttravggkkasgqdiEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 216 GKFVEIQFDKSG-KISGAAIRTYLLERSR-VCQINSpERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVDG 292
Cdd:cd14891 157 GKFMKLQFTKDKfKLAGAFIETYLLEKSRlVAQPPG-ERNFHIFYQLLAgASAELLKELLLLSPEDFIYLNQSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 293 INDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFakgSEVDSS----VIKDDKSRFHLNTAAELLMCDCKKL 368
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEF---DEEDTSegeaEIASESDKEALATAAELLGVDEEAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 369 ENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKT-NSFE 447
Cdd:cd14891 313 EKVITQREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 448 QLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYE 527
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 528 KFKNHKRF--TKPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVvaehqellnasrcsfvsalfpPASEENTKSSkssiA 605
Cdd:cd14891 473 THKRHPCFprPHPKDMREMFIVKHYAGTVSYTIGSFIDKNNDII---------------------PEDFEDLLAS----S 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 606 TRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASE 685
Cdd:cd14891 528 AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPP 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 1002232322 686 IVK--EKNDEKVTCQKVL--DKMGLQGYQIGRTKVFLR 719
Cdd:cd14891 608 SVTrlFAENDRTLTQAILwaFRVPSDAYRLGRTRVFFR 645
|
|
| MyosinXI_CBD |
cd15475 |
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to ... |
1706-2072 |
5.37e-175 |
|
cargo binding domain of myosin XI; Class XI myosins are a plant specific group, homologous to class V myosins. C-terminal domain of Arabidopsis myosin XI has been shown to be homologous to the cargo-binding domain of yeast myosin V myo2p, which targets myosin to vacuole- and mitochondria, as well as secretory vesicle.
Pssm-ID: 271259 Cd Length: 326 Bit Score: 535.62 E-value: 5.37e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1706 WLLTCISQYLGFFGSKPVAALLIYQCLSHWRSFEAMKTGVFDSILQAINSATEAQNDTRALAYWLSNLSTLTVLLQRSFk 1785
Cdd:cd15475 9 ALIKCVSENLGFSEGKPVAAFTIYKCLLHWKSFEAEKTSVFDRIIQTIGSAIEDQDNNDHLAYWLSNTSTLLFLLQRSL- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1786 ttrtaistpqrrrfsserifhasqtsnaglaylsgqpvvgaaglpqveakyPALLFKQQLVDLIEKVYGMISDSVKKELN 1865
Cdd:cd15475 88 ---------------------------------------------------PALLFKQQLTAYVEKIYGIIRDNLKKELS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1866 PLLELCIQDPRTSHSPAKG---HANGLGQKNQLGHWLAIVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRLL 1942
Cdd:cd15475 117 PLLSLCIQAPRTSRGSSSKsssSANSLGQQSPSSHWQSIIKSLNSLLSTLKENHVPPFLVQKIFTQVFSFINVQLFNSLL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1943 LRRECCSFSNGEYVKVGLAELKHWSDNATREFAGSAWDALKHIRQAVDFLVISLKPMRTLKEIRTDVCPALSIQQLERIV 2022
Cdd:cd15475 197 LRRECCSFSNGEYVKAGLAELELWCSQATEEYAGSSWDELKHIRQAVGFLVIHQKSRKSYDEITNDLCPVLSVQQLYRIC 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1002232322 2023 SMYWDDINGSNAISAEFTSSLKSAVREESNTVTTFSILLDDDSCIPFSLD 2072
Cdd:cd15475 277 TMYWDDKYGTQSVSPEVISSMRVLMTEDSNNAVSNSFLLDDDSSIPFSVE 326
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
76-719 |
2.01e-172 |
|
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: 543.35 E-value: 2.01e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANL---------GDLDPHVFAIADVSYRQMMNE 146
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLP-LYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 147 GR-NNSILVSGESGAGKTETTKLLMRYLAYL--------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGK 217
Cdd:cd14908 80 IRaSQSILISGESGAGKTESTKIVMLYLTTLgngeegapNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 218 FVEIQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLC-AAPPEDIKRYKLGD--------PSSFHYLNQSSCI 288
Cdd:cd14908 160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLrGGDEEEHEKYEFHDgitgglqlPNEFHYTGQGGAP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 289 RVDGINDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKL 368
Cdd:cd14908 240 DLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEEGNEKCLARVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 369 ENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD--KLIGVLDIYGFESFKTNSF 446
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDirSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 447 EQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFP-KSTHETFSQKL 525
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDECRLGiRGSDANYASRL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 526 YEKFKNHK--------RFTKPKLSRTA--FTIQHYAGDVIYQSDH-FLDKNKDYVVAEHQELLNASrcsfvsalfppase 594
Cdd:cd14908 480 YETYLPEKnqthsentRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKDEIPLTADSLFESG-------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 595 entksskssiaTRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHD 674
Cdd:cd14908 546 -----------QQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKD 614
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 675 FLHRFRILASEIVKEK-------NDEKVTCQKVLDKMGLQGY----------------QIGRTKVFLR 719
Cdd:cd14908 615 FFKRYRMLLPLIPEVVlswsmerLDPQKLCVKKMCKDLVKGVlspamvsmknipedtmQLGKSKVFMR 682
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
78-682 |
1.92e-171 |
|
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: 540.39 E-value: 1.92e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGA--------NLGDLDPHVFAIADVSYRQMMNEGRN 149
Cdd:cd14907 3 LLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDNLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENNKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 150 NSILVSGESGAGKTETTKLLMRYLAYL----------------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSS 213
Cdd:cd14907 83 QAIVISGESGAGKTENAKYAMKFLTQLsqqeqnseevltltssIRATSKSTKSIEQKILSCNPILEAFGNAKTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 214 RFGKFVEIQFD-KSGKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSS---FHYLNQSSCI 288
Cdd:cd14907 163 RFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYhLLYGADQQLLQQLGLKNQLSgdrYDYLKKSNCY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 289 RVDGINDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKgSEVDSSVIKDDKSRFHLNTAAELLMCDCKKL 368
Cdd:cd14907 243 EVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDD-STLDDNSPCCVKNKETLQIIAKLLGIDEEEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 369 ENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASI-------GQDPNSDKL-IGVLDIYGFES 440
Cdd:cd14907 322 KEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLsIGLLDIFGFEV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 441 FKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQIN--WSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTH 518
Cdd:cd14907 402 FQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKLATGTD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 519 ETFSQKLYEKFKNHKRFTKP-KLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEEN- 596
Cdd:cd14907 482 EKLLNKIKKQHKNNSKLIFPnKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGEDGSQq 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 597 ------TKSSKS--SIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPT 668
Cdd:cd14907 562 qnqskqKKSQKKdkFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPY 641
|
650
....*....|....
gi 1002232322 669 RKLFHDFLHRFRIL 682
Cdd:cd14907 642 RKSYEDFYKQYSLL 655
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
78-719 |
5.24e-168 |
|
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: 531.09 E-value: 5.24e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14911 3 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTE-KIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYL--------------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14911 82 SGAGKTENTKKVIQFLAYVaaskpkgsgavphpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 224 DKSGKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNQSScIRVDGINDAEEYLVT 302
Cdd:cd14911 162 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYqLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 303 RNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDdksrfhlNTAAE----LLMCDCKKLENALIKREIN 378
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPD-------NTVAQkiahLLGLSVTDMTRAFLTPRIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 379 TPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEK 457
Cdd:cd14911 314 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEIFELNSFEQLCINYTNEK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 458 LQQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFT 536
Cdd:cd14911 394 LQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFM 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 537 KPKLSRTA-FTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPA-----SEENTKSSKSSIATR--- 607
Cdd:cd14911 473 KTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeivgmAQQALTDTQFGARTRkgm 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 608 -------FKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR 680
Cdd:cd14911 553 frtvshlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE 632
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1002232322 681 ILASEIV-KEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14911 633 LLTPNVIpKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 674
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
76-719 |
1.84e-165 |
|
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: 523.35 E-value: 1.84e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRTveqQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA---KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNQSSC-IRVDGINDAEEYLVTRNAMDTVGIIE 313
Cdd:cd14904 158 TYLLEKSRVVSIAEGERNYHIFYqLLAGLSSEERKEFGLDPNCQYQYLGDSLAqMQIPGLDDAKLFASTQKSLSLIGLDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 314 QEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKsrfhLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSA 393
Cdd:cd14904 238 DAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQ----LSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDK-LIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQE 472
Cdd:cd14904 314 EENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKgQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVEE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 473 EYTREQINWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPKSTHETFSQK----LYEKFKN-HKRFtkPKLSRTAFTI 547
Cdd:cd14904 394 EYIREGLQWDHIEYQDNQGIVEVIDGKM-GIIALMNDHLRQPRGTEEALVNKirtnHQTKKDNeSIDF--PKVKRTQFII 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 548 QHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF----PPASEENTKSSKS-----SIATRFKVQLHELMET 618
Cdd:cd14904 471 NHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFgsseAPSETKEGKSGKGtkapkSLGSQFKTSLSQLMDN 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 619 LSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKnDEKVTCQ 698
Cdd:cd14904 551 IKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK-DVRRTCS 629
|
650 660
....*....|....*....|....
gi 1002232322 699 KVLDKMGLQG---YQIGRTKVFLR 719
Cdd:cd14904 630 VFMTAIGRKSpleYQIGKSLIYFK 653
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
61-719 |
3.82e-164 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 525.75 E-value: 3.82e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 61 PDGVDDMTRLSYLHEPGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSY 140
Cdd:PTZ00014 95 PMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDKLPPHVFTTARRAL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 141 RQMMNEGRNNSILVSGESGAGKTETTKLLMRYLAYlgGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:PTZ00014 175 ENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAS--SKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 221 IQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNqSSCIRVDGINDAEEY 299
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYqLLKGANDEMKEKYKLKSLEEYKYIN-PKCLDVPGIDDVKDF 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 300 LVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINF---AKGSEVDSSVIkDDKSRFHLNTAAELLMCDCKKLENALIKRE 376
Cdd:PTZ00014 332 EEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegkEEGGLTDAAAI-SDESLEVFNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 377 INTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIgqDPNS--DKLIGVLDIYGFESFKTNSFEQLCINFT 454
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATI--EPPGgfKVFIGMLDIFGFEVFKNNSLEQLFINIT 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 455 NEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKR 534
Cdd:PTZ00014 489 NEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPK 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPKLS-RTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSS-IATRFKVQL 612
Cdd:PTZ00014 569 YKPAKVDsNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKGKLAKGQlIGSQFLNQL 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 613 HELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKN- 691
Cdd:PTZ00014 649 DSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSl 728
|
650 660 670
....*....|....*....|....*....|
gi 1002232322 692 DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:PTZ00014 729 DPKEKAEKLLERSGLpkDSYAIGKTMVFLK 758
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
76-719 |
6.95e-164 |
|
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: 518.77 E-value: 6.95e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGA-NLGDLDPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATD-EWIRKYRDApDLTKLPPHVFYTARRALENLHGVNKSQTIIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLAYlgGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAI 234
Cdd:cd14876 80 SGESGAGKTEATKQIMRYFAS--AKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIRYGSV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 235 RTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNqSSCIRVDGINDAEEYLVTRNAMDTVGIIE 313
Cdd:cd14876 158 VAFLLEKSRIVTQDDNERSYHIFYqLLKGADSEMKSKYHLLGLKEYKFLN-PKCLDVPGIDDVADFEEVLESLKSMGLTE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 314 QEQEAIFRVVAAVLHLGNINFAKGSE---VDSSVIkDDKSRFHLNTAAELLMCDCKKLENALIkreintpegVITTTVGP 390
Cdd:cd14876 237 EQIDTVFSIVSGVLLLGNVKITGKTEqgvDDAAAI-SNESLEVFKEACSLLFLDPEALKRELT---------VKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 391 S---------SATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQH 461
Cdd:cd14876 307 QeiegrwtkdDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 462 FNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKL- 540
Cdd:cd14876 387 FIDIVFERESKLYKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVd 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 541 SRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSS-IATRFKVQLHELMETL 619
Cdd:cd14876 467 SNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSlIGSQFLKQLESLMGLI 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 620 SSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKN-DEKVTCQ 698
Cdd:cd14876 547 NSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSlDPKVAAL 626
|
650 660
....*....|....*....|...
gi 1002232322 699 KVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14876 627 KLLESSGLseDEYAIGKTMVFLK 649
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
78-691 |
6.99e-163 |
|
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: 515.24 E-value: 6.99e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKY-------------KGANlgDLDPHVFAIADVSYRQMM 144
Cdd:cd14900 3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPGLYSSDTMAKYllsfearssstrnKGSD--PMPPHIYQVAGEAYKAMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 145 N----EGRNNSILVSGESGAGKTETTKLLMRYLAY-------LGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSS 213
Cdd:cd14900 81 LglngVMSDQSILVSGESGSGKTESTKFLMEYLAQagdnnlaASVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 214 RFGKFVEIQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRyklgdpssfHYLNQsscirvdg 292
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYeMAIGASEAARKR---------DMYRR-------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 293 indaeeylVTRnAMDTVGIIEQEQEAIFRVVAAVLHLGNINF--AKGSEVDSSVIKD--DKSRFHLNTAAELLMCDCKKL 368
Cdd:cd14900 224 --------VMD-AMDIIGFTPHERAGIFDLLAALLHIGNLTFehDENSDRLGQLKSDlaPSSIWSRDAAATLLSVDATKL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 369 ENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-----KLIGVLDIYGFESFKT 443
Cdd:cd14900 295 EKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLKMDDSSKshgglHFIGILDIFGFEVFPK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 444 NSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQ 523
Cdd:cd14900 375 NSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 524 KLYEKFKNHKRFTKPKL--SRTAFTIQHYAGDVIYQSDHFLDKNKDYVvaeHQELLNAsrcsFVSALfppaseentkssk 601
Cdd:cd14900 455 KLYRACGSHPRFSASRIqrARGLFTIVHYAGHVEYSTDGFLEKNKDVL---HQEAVDL----FVYGL------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 602 ssiatRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRI 681
Cdd:cd14900 515 -----QFKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFS 589
|
650
....*....|
gi 1002232322 682 LASEIVKEKN 691
Cdd:cd14900 590 LARAKNRLLA 599
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
76-684 |
1.18e-161 |
|
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: 515.21 E-value: 1.18e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYK--------GANLGDLDPHVFAIADVSYRQMM-NE 146
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 147 GRNNSILVSGESGAGKTETTKLLMRYLAY------LGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSvgrdqsSTEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 221 IQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYkLGDPSSFHY--LNQSSC----IRVDGIN 294
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDL-LGLQKGGKYelLNSYGPsfarKRAVADK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 295 DAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINF--AKGSEVDSSVikDDKSRFHLNTAAELLMCDCKKLENAL 372
Cdd:cd14902 240 YAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFtaENGQEDATAV--TAASRFHLAKCAELMGVDVDKLETLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 373 IKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRIN---------ASIGQDPNSDKLIGVLDIYGFESFKT 443
Cdd:cd14902 318 SSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGILDIFGFESLNR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 444 NSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQ 523
Cdd:cd14902 398 NGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 524 KLYEKFknhkrftkpkLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF------PPASEENT 597
Cdd:cd14902 478 KFYRYH----------GGLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGadenrdSPGADNGA 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 598 KSSK-------SSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRK 670
Cdd:cd14902 548 AGRRrysmlraPSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRL 627
|
650
....*....|....
gi 1002232322 671 LFHDFLHRFRILAS 684
Cdd:cd14902 628 AHASFIELFSGFKC 641
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
76-719 |
3.24e-161 |
|
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: 512.08 E-value: 3.24e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYP-VYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYL-----GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKIS 230
Cdd:cd14909 80 GESGAGKTENTKKVIAYFATVgaskkTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 231 GAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKL--GDPSSFHYLNQSScIRVDGINDAEEYLVTRNAMDT 308
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLlsDNIYDYYIVSQGK-VTVPNVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 309 VGIIEQEQEAIFRVVAAVLHLGNINFA-KGSEVDSSVIKDDKSrfhlNTAAELLMCDCKKLENALIKREINTPEGVITTT 387
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKqRGREEQAEQDGEEEG----GRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 388 VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVF 467
Cdd:cd14909 315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 468 KMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYekfKNH----KRFTKPKLSR 542
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFgMDLLACIDLIE-KPMGILSILEEESMFPKATDQTFSEKLT---NTHlgksAPFQKPKPPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 TA-----FTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF--------PPASEENTKSSK----SSIA 605
Cdd:cd14909 471 PGqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFadhagqsgGGEQAKGGRGKKgggfATVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 606 TRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASE 685
Cdd:cd14909 551 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPA 630
|
650 660 670
....*....|....*....|....*....|....*.
gi 1002232322 686 IVKEKNDEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14909 631 GIQGEEDPKKAAEIILESIALdpDQYRLGHTKVFFR 666
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
78-719 |
3.95e-160 |
|
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: 508.68 E-value: 3.95e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEG----RNNSIL 153
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLH-IYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGRLargpKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 154 VSGESGAGKTETTKLLMRYLAYLGGRSGTggrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdKSGKISGAA 233
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELCRGNSQ----LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 234 IRTYLLERSRVCQINSPERNYHCFYFLCAA-PPEDIKRYKLGDPSSFHYLNQSScirvdGINDAEEYLVTR-----NAMD 307
Cdd:cd14889 157 INEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDPGKYRYLNNGA-----GCKREVQYWKKKydevcNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 308 TVGIIEQEQEAIFRVVAAVLHLGNINFaKGSEVDSSVIKDDkSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTT 387
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITF-EMDDDEALKVEND-SNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 388 VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD---KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQ 464
Cdd:cd14889 310 HTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSvelREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 465 NVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTA 544
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 545 FTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF----------------PPASEENTKSS-KSSIATR 607
Cdd:cd14889 470 FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrsrtgtlmpraklPQAGSDNFNSTrKQSVGAQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 608 FKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEiv 687
Cdd:cd14889 550 FKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCE-- 627
|
650 660 670
....*....|....*....|....*....|..
gi 1002232322 688 KEKNDEKVTCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14889 628 PALPGTKQSCLRILKATKLVGWKCGKTRLFFK 659
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
76-719 |
3.93e-159 |
|
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: 505.47 E-value: 3.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLP-LFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGrtvEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFdKSGKISGAAIR 235
Cdd:cd14896 80 GHSGSGKTEAAKKIVQFLSSLYQDQTEDR---LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCAA-PPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQ 314
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGlDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 315 EQEAIFRVVAAVLHLGNINFAKgSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSAT 394
Cdd:cd14896 236 ELTAIWAVLAAILQLGNICFSS-SERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 395 VSRDGLAKQIYSRLFDWLVNRINASIG--QDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQE 472
Cdd:cd14896 315 DARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 473 EYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRTAFTIQHYAG 552
Cdd:cd14896 395 ECQRELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 553 DVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEE-NTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVK 631
Cdd:cd14896 475 TVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQyGLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHCLN 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 632 PNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKvTCQKVLDKM-GLQG-- 708
Cdd:cd14896 555 PNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGSERQEALSDRE-RCGAILSQVlGAESpl 633
|
650
....*....|.
gi 1002232322 709 YQIGRTKVFLR 719
Cdd:cd14896 634 YHLGATKVLLK 644
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
76-719 |
3.01e-157 |
|
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: 502.56 E-value: 3.01e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVrtmEKYKGA--NLGDLDPHVFAIADVSYRQMM-------NE 146
Cdd:cd14895 1 PAFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDL---HKYREEmpGWTALPPHVFSIAEGAYRSLRrrlhepgAS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 147 GRNNSILVSGESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQ------QVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14895 78 KKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRraisgsELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 221 IQF-----DKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKR---YKLGDPSSFHYLNQSSC-IRVD 291
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLelqLELLSAQEFQYISGGQCyQRND 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 292 GINDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSE---------------VDSSVIKDDKSRFHLNT 356
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEdegeedngaasapcrLASASPSSLTVQQHLDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 357 AAELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQ-----DPN------ 425
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalNPNkaankd 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 426 SDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIA 505
Cdd:cd14895 398 TTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 506 LLDEACMFPKSTHETFSQKLYEKFKNHKRFTKpklSRT-----AFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNAS 580
Cdd:cd14895 478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSA---SRTdqadvAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 581 RCSFVSALFPP--ASEENT-----------KSSKSS--IATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTN 645
Cdd:cd14895 555 SDAHLRELFEFfkASESAElslgqpklrrrSSVLSSvgIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAK 634
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 646 VLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASeivkEKNDEKVTCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14895 635 VSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA----AKNASDATASALIETLKVDHAELGKTRVFLR 704
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
78-719 |
1.45e-154 |
|
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: 493.76 E-value: 1.45e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14920 3 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSE-NIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGR-----TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGA 232
Cdd:cd14920 82 SGAGKTENTKKVIQYLAHVASSHKGRKDhnipgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 233 AIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKR-YKLGDPSSFHYLNQSScIRVDGINDAEEYLVTRNAMDTVGI 311
Cdd:cd14920 162 NIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSdLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 312 IEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDdksrfhlNTAAE----LLMCDCKKLENALIKREINTPEGVITTT 387
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE-------NTVAQklchLLGMNVMEFTRAILTPRIKVGRDYVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 388 VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNV 466
Cdd:cd14920 314 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 467 FKMEQEEYTREQINWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSR- 542
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKd 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 -TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP------PASEENT----------KSSKS--- 602
Cdd:cd14920 474 kADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdvdrivGLDQVTGmtetafgsayKTKKGmfr 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 603 SIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRIL 682
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1002232322 683 A-SEIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14920 634 TpNAIPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
76-719 |
8.63e-154 |
|
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: 491.41 E-value: 8.63e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLP-VYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGR--TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAA 233
Cdd:cd14929 80 GESGAGKTVNTKHIIQYFATIAAMIESKKKlgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 234 IRTYLLERSRVCQINSPERNYHCFYFLCAAPPEdIKRYKL--GDPSSFHYlnqSSC--IRVDGINDAEEYLVTRNAMDTV 309
Cdd:cd14929 160 IDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE-LRDLLLvsANPSDFHF---CSCgaVAVESLDDAEELLATEQAMDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 310 GIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSsvIKDDKSRfHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVG 389
Cdd:cd14929 236 GFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQ--LEADGTE-NADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 390 PSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKM 469
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 470 EQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKRFTKPKLSRTAFTI 547
Cdd:cd14929 393 EQEEYRKEGIDWVSIDFgLDLQACIDLIE-KPMGIFSILEEECMFPKATDLTFKTKLFDNhFGKSVHFQKPKPDKKKFEA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 548 Q----HYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP---------PASEENTKSSKS--SIATRFKVQL 612
Cdd:cd14929 472 HfelvHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEnyistdsaiQFGEKKRKKGASfqTVASLHKENL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 613 HELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKN- 691
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSKf 631
|
650 660 670
....*....|....*....|....*....|.
gi 1002232322 692 -DEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14929 632 vSSRKAAEELLGSLEIDHtqYRFGITKVFFK 662
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
78-719 |
3.79e-152 |
|
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: 487.15 E-value: 3.79e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14927 3 VLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLP-VYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYL-----------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd14927 82 SGAGKTVNTKRVIQYFAIVaalgdgpgkkaQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGPT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKL--GDPSSFHYLNQSScIRVDGINDAEEYLVTRN 304
Cdd:cd14927 162 GKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLvsMNPYDYHFCSQGV-TTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 305 AMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKREINTPEGVI 384
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTES---ADKAAYLMGVSSADLLKGLLHPRVKVGNEYV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 385 TTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQ 464
Cdd:cd14927 318 TKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 465 NVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEkfkNH----KRFTKPK 539
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFgLDLQACIDLIE-KPLGILSILEEECMFPKASDASFKAKLYD---NHlgksPNFQKPR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 540 LSR-----TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF----------PPASEENTKSSKS-- 602
Cdd:cd14927 474 PDKkrkyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYenyvgsdsteDPKSGVKEKRKKAas 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 603 --SIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR 680
Cdd:cd14927 554 fqTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYR 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1002232322 681 ILASEIVKEKN--DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14927 634 ILNPSAIPDDKfvDSRKATEKLLGSLDIdhTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
76-719 |
4.35e-151 |
|
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: 484.17 E-value: 4.35e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14913 1 PAVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLP-VYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYL-------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGK 228
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIaatgdlaKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLG-DPSSFHYLNQSScIRVDGINDAEEYLVTRNAM 306
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYqILSNKKPELIELLLITtNPYDYPFISQGE-ILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 307 DTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDC---KKLENALIKRein 378
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKqreeqAEPDGTEVADKTAYLMGLNSSDLLKALCfprVKVGNEYVTK--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 379 tpegviTTTVGPSSATVsrDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKL 458
Cdd:cd14913 316 ------GQTVDQVHHAV--NALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 459 QQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKRFT 536
Cdd:cd14913 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNFQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 537 KPKLSR----TAFTIQHYAGDVIYQSDHFLDKNKD----YVVAEHQE----LLNASRCSFVSALFPPASEENTKSSKSSI 604
Cdd:cd14913 467 KPKVVKgraeAHFSLIHYAGTVDYSVSGWLEKNKDplneTVVGLYQKssnrLLAHLYATFATADADSGKKKVAKKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 605 AT---RFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRI 681
Cdd:cd14913 547 QTvsaLFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1002232322 682 LASEIVKEKN--DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14913 627 LNASAIPEGQfiDSKKACEKLLASIDIDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
78-718 |
1.83e-150 |
|
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: 482.04 E-value: 1.83e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGA-NLGDLDPHVFAIADVSYR--QMMNEGRNNSILV 154
Cdd:cd14880 3 VLRCLQARYTADTFYTNAGCTLVALNPFKPVPQLYSPELMREYHAApQPQKLKPHIFTVGEQTYRnvKSLIEPVNQSIVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLAYLGG-----RSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKI 229
Cdd:cd14880 83 SGESGAGKTWTSRCLMKFYAVVAAsptswESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQQM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 230 SGAAIRTYLLERSRVCQINSPERNYHCFYFLC-AAPPEDIKRYKLGDPSSFHYLNQSScirvdgiNDAEE--YLVTRNAM 306
Cdd:cd14880 163 TGAAVQTYLLEKTRVACQAPSERNFHIFYQICkGASADERLQWHLPEGAAFSWLPNPE-------RNLEEdcFEVTREAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 307 DTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEG--VI 384
Cdd:cd14880 236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQqqVF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 385 TTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNS-DKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFN 463
Cdd:cd14880 316 KKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSwTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 464 QNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMF--PKSTHEtFSQKLYEKFKNHKRFTKPKLS 541
Cdd:cd14880 396 AHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLnrPSSAAQ-LQTRIESALAGNPCLGHNKLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 542 RT-AFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKS--------SIATRFKVQL 612
Cdd:cd14880 475 REpSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSgqsrapvlTVVSKFKASL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 613 HELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKND 692
Cdd:cd14880 555 EQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLLRRLRPHTSSG 634
|
650 660
....*....|....*....|....*.
gi 1002232322 693 EKVTCQkvlDKMGLQGYQIGRTKVFL 718
Cdd:cd14880 635 PHSPYP---AKGLSEPVHCGRTKVFM 657
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
78-718 |
3.29e-149 |
|
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: 480.63 E-value: 3.29e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGAN-LGDLDPHVFAIADVSYRQMMNEGRNNSILVSG 156
Cdd:cd14906 3 ILNNLGKRYKSDSIYTYIGNVLISINPYKDISSIYSNLILNEYKDINqNKSPIPHIYAVALRAYQSMVSEKKNQSIIISG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 157 ESGAGKTETTKLLMRYLAYLGGRSGTGGR-------TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS-GK 228
Cdd:cd14906 83 ESGSGKTEASKTILQYLINTSSSNQQQNNnnnnnnnSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdGK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCqiNSPER---NYHCFYFLC-AAPPEDIKRYKL-GDPSSFHYLN-----------QSSCIRVDG 292
Cdd:cd14906 163 IDGASIETYLLEKSRIS--HRPDNinlSYHIFYYLVyGASKDERSKWGLnNDPSKYRYLDarddvissfksQSSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 293 INDA---EEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRFHLNTAAELLMCDCKKLE 369
Cdd:cd14906 241 NNKTesiESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 370 NALIKREINTPE--GVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNS-----------DKLIGVLDIY 436
Cdd:cd14906 321 QALLNRNLKAGGrgSVYCRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQNTQSndlaggsnkknNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 437 GFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKS 516
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMPKG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 517 THETFSQKLYEKFKNHKRFTKPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPAS--- 593
Cdd:cd14906 481 SEQSLLEKYNKQYHNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQQQItst 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 594 --EENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKL 671
Cdd:cd14906 561 tnTTKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRD 640
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 672 FHDFLHRFRILASEIVKEKND--------EKVTCQKVLDKMGLQG-------------------YQIGRTKVFL 718
Cdd:cd14906 641 FNQFFSRYKCIVDMYNRKNNNnpklasqlILQNIQSKLKTMGISNnkkknnsnsnsnttndkplFQIGKTKIFI 714
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
78-719 |
1.60e-148 |
|
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: 477.21 E-value: 1.60e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14932 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKYLP-IYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGRT---------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGK 228
Cdd:cd14932 82 SGAGKTENTKKVIQYLAYVASSFKTKKDQssialshgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLNQSScIRVDGINDAEEYLVTRNAMD 307
Cdd:cd14932 162 IVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRsELCLEDYSKYRFLSNGN-VTIPGQQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 308 TVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRfhlNTAAELLMCDCKKLENALIKREINTPEGVITTT 387
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAA---QKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 388 VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNV 466
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 467 FKMEQEEYTREQINWSYIEF-VDNQDVLDLIEKK--PGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSR- 542
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKd 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 -TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF---------------PPASEENTKSSKS---S 603
Cdd:cd14932 478 dADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWkdvdrivgldkvagmGESLHGAFKTRKGmfrT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 604 IATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA 683
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 1002232322 684 -SEIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14932 638 pNAIPKGFMDGKQACVLMVKALELDPnlYRIGQSKVFFR 676
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
78-719 |
3.30e-146 |
|
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: 470.28 E-value: 3.30e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14934 3 VLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLP-IYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGR---TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAI 234
Cdd:cd14934 82 SGAGKTENTKKVIQYFANIGGTGKQSSDgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGADI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 235 RTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKL-GDPSSFHYLNQSsCIRVDGINDAEEYLVTRNAMDTVGII 312
Cdd:cd14934 162 ESYLLEKSRVISQQAAERGYHIFYqILSNKKPELIESLLLvPNPKEYHWVSQG-VTVVDNMDDGEELQITDVAFDVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 313 EQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDdksrfhlnTAAELLMCDCKKLENALIKREINTPEGVITTT 387
Cdd:cd14934 241 AEEKIGVYKLTGGIMHFGNMKFKQKpreeqAEVDTTEVAD--------KVAHLMGLNSGELQKGITRPRVKVGNEFVQKG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 388 VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVF 467
Cdd:cd14934 313 QNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 468 KMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEkfkNH----KRFTKPKLSR 542
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFgLDLQACIDLLE-KPMGIFSILEEQCVFPKATDATFKAALYD---NHlgksSNFLKPKGGK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 -----TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF----PPASEENTK--SSKSSIATRFKVQ 611
Cdd:cd14934 469 gkgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFkeeeAPAGSKKQKrgSSFMTVSNFYREQ 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 612 LHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEK- 690
Cdd:cd14934 549 LNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGf 628
|
650 660 670
....*....|....*....|....*....|.
gi 1002232322 691 NDEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14934 629 VDNKKASELLLGSIDLDvnEYKIGHTKVFFR 659
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
78-719 |
1.14e-144 |
|
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: 466.11 E-value: 1.14e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14919 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGRT--VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd14919 82 SGAGKTENTKKVIQYLAHVASSHKSKKDQgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIEQE 315
Cdd:cd14919 162 TYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAMRIMGIPEEE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 316 QEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDdksrfhlNTAAE----LLMCDCKKLENALIKREINTPEGVITTTVGPS 391
Cdd:cd14919 242 QMGLLRVISGVLQLGNIVFKKERNTDQASMPD-------NTAAQkvshLLGINVTDFTRGILTPRIKVGRDYVQKAQTKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 392 SATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKME 470
Cdd:cd14919 315 QADFAIEALAKATYERMFRWLVLRINKALDKTKRQGaSFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 471 QEEYTREQINWSYIEF-VDNQDVLDLIEKK--PGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKL--SRTAF 545
Cdd:cd14919 395 QEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQlkDKADF 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 546 TIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP-------------------PASEENTKSSKSSIAT 606
Cdd:cd14919 475 CIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKdvdriigldqvagmsetalPGAFKTRKGMFRTVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 607 RFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA-SE 685
Cdd:cd14919 555 LYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTpNS 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 1002232322 686 IVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14919 635 IPKGFMDGKQACVLMIKALELDSnlYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
78-719 |
9.94e-144 |
|
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: 463.72 E-value: 9.94e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14921 3 VLHNLRERYFSGLIYTYSGLFCVVVNPYKHLP-IYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGRT-----VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGA 232
Cdd:cd14921 82 SGAGKTENTKKVIQYLAVVASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 233 AIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGII 312
Cdd:cd14921 162 NIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 313 EQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDdksrfhlNTAAE----LLMCDCKKLENALIKREINTPEGVITTTV 388
Cdd:cd14921 242 EEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPD-------NTAAQkvchLMGINVTDFTRSILTPRIKVGRDVVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVF 467
Cdd:cd14921 315 TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGaSFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 468 KMEQEEYTREQINWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKL--SR 542
Cdd:cd14921 395 ILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQlkDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP-------------------PASEENTKSSKSS 603
Cdd:cd14921 475 TEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKdvdrivgldqmakmtesslPSASKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 604 IATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRIL- 682
Cdd:cd14921 555 VGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILa 634
|
650 660 670
....*....|....*....|....*....|....*....
gi 1002232322 683 ASEIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14921 635 ANAIPKGFMDGKQACILMIKALELDPnlYRIGQSKIFFR 673
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
78-719 |
2.99e-140 |
|
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: 453.19 E-value: 2.99e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLG-----DLDPHVFAIADVSYRQMMNEGRNNSI 152
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPFKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 153 LVSGESGAGKTETTKLLMRYLAYlggRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGA 232
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAY---GHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 233 AIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVgI 311
Cdd:cd14886 160 KITSYMLELSRIEFQSTNERNYHIFYqCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 312 IEQEQEAIFRVVAAVLHLGNINFAKGSE--VDSSVIKDDKSRFhlNTAAELLMCDCKKLENALIKREINTPEGVITTTVG 389
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDF--GKMCELLGIESSKAAQAIITKVVVINNETIISPVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 390 PSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKM 469
Cdd:cd14886 317 QAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKS 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 470 EQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKrFTKPKLSRTAFTIQH 549
Cdd:cd14886 397 EIQEYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNS-FIPGKGSQCNFTIVH 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 550 YAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRC 629
Cdd:cd14886 476 TAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMKGKFLGSTFQLSIDQLMKTLSATKSHFIRC 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 630 VKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRIL---ASEIVKEKNDEKVTCQKVLDKMGL 706
Cdd:cd14886 556 IKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILishNSSSQNAGEDLVEAVKSILENLGI 635
|
650
....*....|....*
gi 1002232322 707 --QGYQIGRTKVFLR 719
Cdd:cd14886 636 pcSDYRIGKTKVFLR 650
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
76-719 |
3.42e-140 |
|
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: 453.41 E-value: 3.42e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14917 1 PAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGR-------TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGK 228
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDRSKKdqtpgkgTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKL-GDPSSFHYLNQSSCIrVDGINDAEEYLVTRNAM 306
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYqILSNKKPELLDMLLItNNPYDYAFISQGETT-VASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 307 DTVGIIEQEQEAIFRVVAAVLHLGNINFA-----KGSEVDSSVIKDDKSRFHLNTAAELLMCDCK---KLENALIKREIN 378
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKqkqreEQAEPDGTEEADKSAYLMGLNSADLLKGLCHprvKVGNEYVTKGQN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 379 TPEGVITTtvgpssatvsrDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKL 458
Cdd:cd14917 319 VQQVIYAT-----------GALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 459 QQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLyekFKNH----K 533
Cdd:cd14917 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKATDMTFKAKL---FDNHlgksN 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 534 RFTKPK----LSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF-------PPASEENTKSSKS 602
Cdd:cd14917 464 NFQKPRnikgKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFanyagadAPIEKGKGKAKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 603 S----IATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHR 678
Cdd:cd14917 544 SsfqtVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1002232322 679 FRILASEIVKEKN--DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14917 624 YRILNPAAIPEGQfiDSRKGAEKLLSSLDIdhNQYKFGHTKVFFK 668
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
78-719 |
3.12e-139 |
|
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: 451.06 E-value: 3.12e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd15896 3 VLHNLKERYYSGLIYTYSGLFCVVINPYKNLP-IYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYL---------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGK 228
Cdd:cd15896 82 SGAGKTENTKKVIQYLAHVasshktkkdQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDT 308
Cdd:cd15896 162 IVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAFRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 309 VGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRfhlNTAAELLMCDCKKLENALIKREINTPEGVITTTV 388
Cdd:cd15896 242 MGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAA---QKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVF 467
Cdd:cd15896 319 TQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 468 KMEQEEYTREQINWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSR-- 542
Cdd:cd15896 399 ILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKde 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP-----------------PASEENTKSSKSSIA 605
Cdd:cd15896 479 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKdvdrivgldkvsgmsemPGAFKTRKGMFRTVG 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 606 TRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA-S 684
Cdd:cd15896 559 QLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTpN 638
|
650 660 670
....*....|....*....|....*....|....*..
gi 1002232322 685 EIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd15896 639 AIPKGFMDGKQACVLMIKSLELDPnlYRIGQSKVFFR 675
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
76-719 |
5.75e-138 |
|
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: 447.26 E-value: 5.75e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14918 1 PGVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRT-------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGK 228
Cdd:cd14918 80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEsgkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 229 ISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKL--GDPSSFHYLNQSScIRVDGINDAEEYLVTRNAM 306
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLitTNPYDYAFVSQGE-ITVPSIDDQEELMATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 307 DTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDCK---KLENALIKREIN 378
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKqreeqAEPDGTEVADKAAYLQSLNSADLLKALCYprvKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 379 TPEgvITTTVGpssatvsrdGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKL 458
Cdd:cd14918 319 VQQ--VYNAVG---------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 459 QQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKRFT 536
Cdd:cd14918 388 QQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPLGIFSILEEECMFPKATDTSFKNKLYDQhLGKSANFQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 537 KPKL----SRTAFTIQHYAGDVIYQSDHFLDKNK----DYVVAEHQELLNASRCSFVSALFPPASEENTK-------SSK 601
Cdd:cd14918 467 KPKVvkgkAEAHFSLIHYAGTVDYNITGWLDKNKdplnDTVVGLYQKSAMKTLASLFSTYASAEADSGAKkgakkkgSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 602 SSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRI 681
Cdd:cd14918 547 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKV 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1002232322 682 LASEIVKEKN--DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14918 627 LNASAIPEGQfiDSKKASEKLLASIDIDhtQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
76-719 |
1.23e-137 |
|
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: 446.48 E-value: 1.23e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14910 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRTV---------EQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd14910 80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEAtsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKL--GDPSSFHYLNQSScIRVDGINDAEEYLVTRN 304
Cdd:cd14910 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLitTNPYDYAFVSQGE-ITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 305 AMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDCK---KLENALIKRE 376
Cdd:cd14910 239 AIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKqreeqAEPDGTEVADKAAYLQNLNSADLLKALCYprvKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 377 INTPEgvITTTVGpssatvsrdGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNE 456
Cdd:cd14910 319 QTVQQ--VYNAVG---------ALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 457 KLQQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKR 534
Cdd:cd14910 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPKLSR----TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTK------------ 598
Cdd:cd14910 467 FQKPKPAKgkveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAAEAEegggkkggkkkg 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 599 SSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHR 678
Cdd:cd14910 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1002232322 679 FRILASEIVKEKN--DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14910 627 YKVLNASAIPEGQfiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
76-719 |
1.26e-137 |
|
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: 446.44 E-value: 1.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14923 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRT--------VEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSG 227
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAVTGDKKKEQqpgkmqgtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 228 KISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLG-DPSSFHYLNQSScIRVDGINDAEEYLVTRNA 305
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYqIMSNKKPELIDLLLIStNPFDFPFVSQGE-VTVASIDDSEELLATDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 306 MDTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDC---KKLENALIKREI 377
Cdd:cd14923 239 IDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKqreeqAEPDGTEVADKAGYLMGLNSAEMLKGLCcprVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 378 NTPEgvITTTVGpssatvsrdGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEK 457
Cdd:cd14923 319 NVQQ--VTNSVG---------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 458 LQQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKRF 535
Cdd:cd14923 388 LQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYDQhLGKSNNF 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 536 TKPKLSR----TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP--PASE-----------ENTK 598
Cdd:cd14923 467 QKPKPAKgkaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSnyAGAEagdsggskkggKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 599 SSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHR 678
Cdd:cd14923 547 SSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1002232322 679 FRILASEIVKEKN--DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14923 627 YRILNASAIPEGQfiDSKNASEKLLNSIDVdrEQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
76-719 |
2.26e-136 |
|
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: 443.02 E-value: 2.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14915 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGR---------TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEeaasgkmqgTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLG-DPSSFHYLNQSScIRVDGINDAEEYLVTRN 304
Cdd:cd14915 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYqIMSNKKPELIEMLLITtNPYDFAFVSQGE-ITVPSIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 305 AMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDCK---KLENALIKRE 376
Cdd:cd14915 239 AVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKqreeqAEPDGTEVADKAAYLTSLNSADLLKALCYprvKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 377 INTPEgvITTTVGpssatvsrdGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNE 456
Cdd:cd14915 319 QTVQQ--VYNSVG---------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 457 KLQQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKR 534
Cdd:cd14915 388 KLQQFFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSNN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPKLSR----TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFP--PASE----------ENTK 598
Cdd:cd14915 467 FQKPKPAKgkaeAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSggQTAEaeggggkkggKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 599 SSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHR 678
Cdd:cd14915 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1002232322 679 FRILASEIVKEKN--DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14915 627 YKVLNASAIPEGQfiDSKKASEKLLGSIDIDhtQYKFGHTKVFFK 671
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
78-680 |
5.26e-136 |
|
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: 443.38 E-value: 5.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKYK---GANLGD-------LDPHVFAIADVSYRQMMNEG 147
Cdd:cd14899 3 ILNALRLRYERHAIYTHIGDILISINPFQDLPQLYGDEILRGYAydhNSQFGDrvtstdpREPHLFAVARAAYIDIVQNG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 148 RNNSILVSGESGAGKTETTKLLMRYLA--------------YLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSS 213
Cdd:cd14899 83 RSQSILISGESGAGKTEATKIIMTYFAvhcgtgnnnltnseSISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDNSS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 214 RFGKFVEIQF-DKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYK------LGDPSSFHYLNQSS 286
Cdd:cd14899 163 RFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQkqvlalSGGPQSFRLLNQSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 287 CI-RVDGINDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSRF---------HLNT 356
Cdd:cd14899 243 CSkRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVmssttgafdHFTK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 357 AAELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASI---GQDP--------- 424
Cdd:cd14899 323 AAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqASAPwgadesdvd 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 425 ---NSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPG 501
Cdd:cd14899 403 deeDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHRPI 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 502 GIIALLDEACMFPKSTHETFSQKLY---EKFKNHKRF-TKPKLSR-TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQEL 576
Cdd:cd14899 483 GIFSLTDQECVFPQGTDRALVAKYYlefEKKNSHPHFrSAPLIQRtTQFVVAHYAGCVTYTIDGFLAKNKDSFCESAAQL 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 577 LNASRCSFVSALFPPASEEN-------------------TKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLK 637
Cdd:cd14899 563 LAGSSNPLIQALAAGSNDEDangdseldgfggrtrrrakSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKPNDSHV 642
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1002232322 638 PAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR 680
Cdd:cd14899 643 GSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRYR 685
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
78-719 |
2.28e-135 |
|
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: 439.92 E-value: 2.28e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVrTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14930 3 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEA-IVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTGGR-----TVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGA 232
Cdd:cd14930 82 SGAGKTENTKKVIQYLAHVASSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 233 AIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGDPSSfHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGII 312
Cdd:cd14930 162 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS-HYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 313 EQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDdksrfhlNTAAE----LLMCDCKKLENALIKREINTPEGVITTTV 388
Cdd:cd14930 241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPD-------NTAAQklcrLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSD-KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVF 467
Cdd:cd14930 314 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 468 KMEQEEYTREQINWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSR-- 542
Cdd:cd14930 394 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRdq 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 543 TAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALF------------------PPASEENtKSSKSSI 604
Cdd:cd14930 474 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivgleqvsslgdgPPGGRPR-RGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 605 ATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA- 683
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTp 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 1002232322 684 SEIVKEKNDEKVTCQKVLDKMGLQG--YQIGRTKVFLR 719
Cdd:cd14930 633 NAIPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 670
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
92-719 |
2.51e-135 |
|
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: 439.63 E-value: 2.51e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 92 YTYTGNILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNN-SILVSGESGAGKTETTKLLM 170
Cdd:cd14875 18 YSLMGEMVLSVNPFRLMPFNSEEERKKYLALPDPRLLPPHIWQVAHKAFNAIFVQGLGNqSVVISGESGSGKTENAKMLI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 171 RYLAYLG--GRSGTGGRTVEQQVLE----SNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDK-SGKISGAAIRTYLLERSR 243
Cdd:cd14875 98 AYLGQLSymHSSNTSQRSIADKIDEnlkwSNPVMESFGNARTVRNDNSSRFGKYIKLYFDPtSGVMVGGQTVTYLLEKSR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 244 VCQINSPERNYHCFYFLCA--APPEDIKRYKLGDPSSFHYLNQ-SSCIR--VDG--INDAEEYLVTRNAMDTVGIIEQEQ 316
Cdd:cd14875 178 IIMQSPGERNYHIFYEMLAglSPEEKKELGGLKTAQDYKCLNGgNTFVRrgVDGktLDDAHEFQNVRHALSMIGVELETQ 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 317 EAIFRVVAAVLHLGNINFaKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKL-ENALIKREINtpegVITTTVGPSSATV 395
Cdd:cd14875 258 NSIFRVLASILHLMEVEF-ESDQNDKAQIADETP---FLTACRLLQLDPAKLrECFLVKSKTS----LVTILANKTEAEG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 396 SRDGLAKQIYSRLFDWLVNRINASIG--QDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd14875 330 FRNAFCKAIYVGLFDRLVEFVNASITpqGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANESLQNHYNKYTFINDEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKN-HKRFTKPKLS-RTAFTIQHYA 551
Cdd:cd14875 410 CRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkSPYFVLPKSTiPNQFGVNHYA 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 552 GDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPpaSEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVK 631
Cdd:cd14875 490 AFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLS--TEKGLARRKQTVAIRFQRQLTDLRTELESTETQFIRCIK 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 632 PNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRIL----ASEIVKEKNDEKVTC------QKvL 701
Cdd:cd14875 568 PNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLImprsTASLFKQEKYSEAAKdflayyQR-L 646
|
650
....*....|....*...
gi 1002232322 702 DKMGLQGYQIGRTKVFLR 719
Cdd:cd14875 647 YGWAKPNYAVGKTKVFLR 664
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
76-719 |
3.11e-135 |
|
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: 439.49 E-value: 3.11e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14916 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGG--------RSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSG 227
Cdd:cd14916 80 GESGAGKTVNTKRVIQYFASIAAigdrskkeNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 228 KISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKL-GDPSSFHYLNQSScIRVDGINDAEEYLVTRNA 305
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYqILSNKKPELLDMLLVtNNPYDYAFVSQGE-VSVASIDDSEELLATDSA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 306 MDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSvikDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVIT 385
Cdd:cd14916 239 FDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQA---EPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 386 TTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQN 465
Cdd:cd14916 316 KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 466 VFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKRFTKPK---- 539
Cdd:cd14916 396 MFVLEQEEYKKEGIEWEFIDFgMDLQACIDLIE-KPMGIMSILEEECMFPKASDMTFKAKLYDNhLGKSNNFQKPRnvkg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 540 LSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENT------------KSSKSSIATR 607
Cdd:cd14916 475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTgdsgkgkggkkkGSSFQTVSAL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 608 FKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIV 687
Cdd:cd14916 555 HRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 1002232322 688 KEKN--DEKVTCQKVLDKMGL--QGYQIGRTKVFLR 719
Cdd:cd14916 635 PEGQfiDSRKGAEKLLGSLDIdhNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
76-719 |
1.54e-134 |
|
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: 437.63 E-value: 1.54e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPnLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVS 155
Cdd:cd14912 1 PAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLP-VYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETTKLLMRYLAYLGGRSGTGGRTV---------EQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAVTGEKKKEEItsgkmqgtlEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLG-DPSSFHYLNQSScIRVDGINDAEEYLVTRN 304
Cdd:cd14912 160 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSnKKPELIEMLLITtNPYDYPFVSQGE-ISVASIDDQEELMATDS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 305 AMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKG-----SEVDSSVIKDDKSRFHLNTAAELLMCDCK---KLENALIKRE 376
Cdd:cd14912 239 AIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKqreeqAEPDGTEVADKAAYLQSLNSADLLKALCYprvKVGNEYVTKG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 377 INTPEgvITTTVGpssatvsrdGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNE 456
Cdd:cd14912 319 QTVEQ--VTNAVG---------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 457 KLQQHFNQNVFKMEQEEYTREQINWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLYEK-FKNHKR 534
Cdd:cd14912 388 KLQQFFNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELIE-KPMGIFSILEEECMFPKATDTSFKNKLYEQhLGKSAN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPKL----SRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASE--------------EN 596
Cdd:cd14912 467 FQKPKVvkgkAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTaegasagggakkggKK 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 597 TKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFL 676
Cdd:cd14912 547 KGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFK 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1002232322 677 HRFRILASEIVKEKN--DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14912 627 QRYKVLNASAIPEGQfiDSKKASEKLLASIDIDhtQYKFGHTKVFFK 673
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
82-718 |
6.06e-120 |
|
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: 394.99 E-value: 6.06e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 82 LAVRYARNLIYTYTG-NILIAINPFQRLPNLVDVrTMEKYK-------GANLGDLDPHVFAIADVSYRQMMNEGRNNSIL 153
Cdd:cd14879 10 LASRFRSDLPYTRLGsSALVAVNPYKYLSSNSDA-SLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRRRSEDQAVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 154 VSGESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQqVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAA 233
Cdd:cd14879 89 FLGETGSGKSESRRLLLRQLLRLSSHSKKGTKLSSQ-ISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNERGRLIGAK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 234 IRTYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKLGDPSSFHYLNQSSCIRVD---GINDAEEYLVTRNAMDTV 309
Cdd:cd14879 168 VLDYRLERSRVASVPTGERNFHVFYYLLAgASPEERQHLGLDDPSDYALLASYGCHPLPlgpGSDDAEGFQELKTALKTL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 310 GIIEQEQEAIFRVVAAVLHLGNINFAKGSEV--DSSVIKDDKSrfhLNTAAELLMCDCKKLENAL------IKREintpe 381
Cdd:cd14879 248 GFKRKHVAQICQLLAAILHLGNLEFTYDHEGgeESAVVKNTDV---LDIVAAFLGVSPEDLETSLtyktklVRKE----- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 382 gVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRIN---ASIGQDPNSdkLIGVLDIYGFESFKT---NSFEQLCINFTN 455
Cdd:cd14879 320 -LCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINqklCAPEDDFAT--FISLLDFPGFQNRSStggNSLDQFCVNFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 456 EKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEAC-MFPKSTHETFSQKLYEKFKNHKR 534
Cdd:cd14879 397 ERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQTrRMPKKTDEQMLEALRKRFGNHSS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPKL-----SRTAFTIQHYAGDVIYQSDHFLDKNkdyvvaehQELLNAsrcSFVSaLFPPASEENTKsskssiatrfk 609
Cdd:cd14879 477 FIAVGNfatrsGSASFTVNHYAGEVTYSVEGFLERN--------GDVLSP---DFVN-LLRGATQLNAA----------- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 610 vqLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFrilASEIVKE 689
Cdd:cd14879 534 --LSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERY---KSTLRGS 608
|
650 660
....*....|....*....|....*....
gi 1002232322 690 KNDEKVTCQKVLDKMGLQGYQIGRTKVFL 718
Cdd:cd14879 609 AAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
85-719 |
1.05e-108 |
|
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: 362.98 E-value: 1.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 85 RYARNLIYTYTGNILIAINPFQRLP---NLVDvRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGESGAG 161
Cdd:cd14878 10 RFGNNQIYTFIGDILLLVNPYKELPiysTMVS-QLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFILSGERGSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 162 KTETTKLLMRYLAYlggRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF-DKSGKISGAAIRTYLLE 240
Cdd:cd14878 89 KTEASKQIMKHLTC---RASSSRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGARIYTYMLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 241 RSRVCQINSPERNYHCFYFLC-AAPPEDIKRYKLGDPSSFHYLNQSscIRVDGINDA-----EEYLVTRNAMDTVGIIEQ 314
Cdd:cd14878 166 KSRLVSQPPGQSNFLIFYLLMdGLSAEEKYGLHLNNLCAHRYLNQT--MREDVSTAErslnrEKLAVLKQALNVVGFSSL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 315 EQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKSrfhLNTAAELLMCDCKKLENALIKrEINTPEG-VITTTVGPSSA 393
Cdd:cd14878 244 EVENLFVILSAILHLGDIRFTALTEADSAFVSDLQL---LEQVAGMLQVSTDELASALTT-DIQYFKGdMIIRRHTIQIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASI-GQD-PNSDKL--IGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKM 469
Cdd:cd14878 320 EFYRDLLAKSLYSRLFSFLVNTVNCCLqSQDeQKSMQTldIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYINEVLFLQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 470 EQEEYTREQINWSYIEFVDNQD-VLDLIEKKPGGIIALLDEACMFPKSTHETFSQKL------------YEKFKNHKRFT 536
Cdd:cd14878 400 EQTECVQEGVTMETAYSPGNQTgVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqsllessntnavYSPMKDGNGNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 537 KPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFppaseentKSSKSSIATRFKVQLHELM 616
Cdd:cd14878 480 ALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLF--------QSKLVTIASQLRKSLADII 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 617 ETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKN----D 692
Cdd:cd14878 552 GKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGEKKkqsaE 631
|
650 660
....*....|....*....|....*..
gi 1002232322 693 EKvtCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14878 632 ER--CRLVLQQCKLQGWQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
76-719 |
1.29e-107 |
|
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: 362.04 E-value: 1.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYA--------RNLIYTYTGNILIAINPFqRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEG 147
Cdd:cd14887 1 PNLLENLYQRYNkayinkenRNCIYTYTGTLLIAVNPY-RFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 148 RNNSILVSGESGAGKTETTKLLMRYLAYLGGRSG-TGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKS 226
Cdd:cd14887 80 RSQSILISGESGAGKTETSKHVLTYLAAVSDRRHgADSQGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 227 GKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPpediKRYKLGDPSSFHYLNQSSCIRvdgindaeeyLVTRnAM 306
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAA----VAAATQKSSAGEGDPESTDLR----------RITA-AM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 307 DTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSE------------------------------VDSSVIK-DDKSRFHLN 355
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEpetskkrkltsvsvgceetaadrshssevkCLSSGLKvTEASRKHLK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 356 TAAELL-----MCDCKKLENALIKREINTPEGVITTtvgpSSATVSRDGLAKQIYSRLFDWLVNRINASIGQ-------- 422
Cdd:cd14887 305 TVARLLglppgVEGEEMLRLALVSRSVRETRSFFDL----DGAAAARDAACKNLYSRAFDAVVARINAGLQRsakpsesd 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 423 -DPNSD-----KLIGVLDIYGFESFKT---NSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDN---- 489
Cdd:cd14887 381 sDEDTPsttgtQTIGILDLFGFEDLRNhskNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPfsfp 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 490 ---------QDVLDLI--------------EKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLS----- 541
Cdd:cd14887 461 lastltsspSSTSPFSptpsfrsssafatsPSLPSSLSSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKnitpa 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 542 ----RTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNAsrCSFVSALFppASEENT-----KSSKSSIATRFKVQL 612
Cdd:cd14887 541 lsreNLEFTVSHFACDVTYDARDFCRANREATSDELERLFLA--CSTYTRLV--GSKKNSgvraiSSRRSTLSAQFASQL 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 613 HELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKND 692
Cdd:cd14887 617 QQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREALT 696
|
730 740
....*....|....*....|....*....
gi 1002232322 693 EKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd14887 697 PKMFCKIVLMFLEINsnSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
78-694 |
2.63e-104 |
|
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: 347.27 E-value: 2.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKykgaNLGDLDPHVFAIADVSYRQMMNEGrNNSILVSGE 157
Cdd:cd14898 3 TLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMKAYLK----NYSHVEPHVYDVAEASVQDLLVHG-NQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYlggrSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDksGKISGAAIRTY 237
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE----RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFYFLCAAPPEDIKRYKLGdpSSFHYLNQSSCIRVdgindAEEYLVTRNAMDTVGIIEQEqe 317
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFID--TSSTAGNKESIVQL-----SEKYKMTCSAMKSLGIANFK-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 318 AIFRVVAAVLHLGNINFakgseVDSSVIKDDKSRFhLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVSR 397
Cdd:cd14898 223 SIEDCLLGILYLGSIQF-----VNDGILKLQRNES-FTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 398 DGLAKQIYSRLFDWLVNRINASIGQdpNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTRE 477
Cdd:cd14898 297 NSMARLLYSNVFNYITASINNCLEG--SGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMYKEE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 478 QINWSYIEFVDNQDVLDLIEkKPGGIIALLDEACMFPKSTHETFSQKLyEKFKNHKRFTKpklSRTAFTIQHYAGDVIYQ 557
Cdd:cd14898 375 GIEWPDVEFFDNNQCIRDFE-KPCGLMDLISEESFNAWGNVKNLLVKI-KKYLNGFINTK---ARDKIKVSHYAGDVEYD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 558 SDHFLDKNKDyvvaehqellNASRCSFVSALFppaseeNTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLK 637
Cdd:cd14898 450 LRDFLDKNRE----------KGQLLIFKNLLI------NDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECR 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 638 PAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEK 694
Cdd:cd14898 514 PWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITLFEVVDYRK 570
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
78-719 |
9.69e-96 |
|
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: 324.66 E-value: 9.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQrlpnLVDVrTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14937 3 VLNMLALRYKKNYIYTIAEPMLISINPYQ----VIDV-DINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYlaYLGGRSGTGGrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTY 237
Cdd:cd14937 78 SGSGKTEASKLVIKY--YLSGVKEDNE--ISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLNQSScIRVDGINDAEEYLVTRNAMDTVGIIEQEQ 316
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKnKYKIRSENEYKYIVNKN-VVIPEIDDAKDFGNLMISFDKMNMHDMKD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 317 EaIFRVVAAVLHLGNINF---AKGSEVDSSVIkDDKSRFHLNTAAELLMCDCKKLENALIKREINTPEGVITTTVGPSSA 393
Cdd:cd14937 233 D-LFLTLSGLLLLGNVEYqeiEKGGKTNCSEL-DKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIEIPLSVEES 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd14937 311 VSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYIVYEKETEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINWSYIEFVDNQDVLDLIEKKPgGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLSRT-AFTIQHYAG 552
Cdd:cd14937 391 YKAEDILIESVKYTTNESIIDLLRGKT-SIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDINkNFVIKHTVS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 553 DVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKP 632
Cdd:cd14937 470 DVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKP 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 633 NSVLKPAIFENTNVLQQLRCSGVLEAIRISCAgYPTRKLFHDFLHRFRILASEIVKEK---NDEKVT--CQKVLDKmglQ 707
Cdd:cd14937 550 NENKEKNNFNQKKVFPQLFSLSIIETLNISFF-FQYKYTFDVFLSYFEYLDYSTSKDSsltDKEKVSmiLQNTVDP---D 625
|
650
....*....|..
gi 1002232322 708 GYQIGRTKVFLR 719
Cdd:cd14937 626 LYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
76-719 |
3.46e-95 |
|
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: 324.55 E-value: 3.46e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMEKY-------KGANLGDLDPHVFAIADVSYRQMMNEGR 148
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 149 NNSILVSGESGAGKTETTKLLMRYLAYLGGRSGTGGRTveQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDK--- 225
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERI--DKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEven 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 226 ------SGKISGAAIRTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKR---------YKLGDPSSFHYLNQSS-CI 288
Cdd:cd14884 159 tqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYqVLRGLSDEDLARrnlvrncgvYGLLNPDESHQKRSVKgTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 289 RVDGIN----------DAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNinfakgsevdssvikddksrFHLNTAA 358
Cdd:cd14884 239 RLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------------RAYKAAA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 359 ELLMCDCKKLENALIKREINTPEGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDK---------- 428
Cdd:cd14884 299 ECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdnediysin 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 429 --LIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKkpggIIAL 506
Cdd:cd14884 379 eaIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 507 LDEACMFPKSTHE-----------TFSQKLYEKFKNHKRFTKP----------KLSRTAFTIQHYAGDVIYQSDHFLDKN 565
Cdd:cd14884 455 LDDITKLKNQGQKktddhffryllNNERQQQLEGKVSYGFVLNhdadgtakkqNIKKNIFFIRHYAGLVTYRINNWIDKN 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 566 KDYVVAEHQELLNASRCSFVsalfppaSEENTKSSK---SSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFE 642
Cdd:cd14884 535 SDKIETSIETLISCSSNRFL-------REANNGGNKgnfLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFK 607
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 643 NTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR-ILASEIVKEKNDEKVTCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14884 608 RLLVYRQLKQCGSNEMIKILNRGLSHKIPKKETAAALKeQIAKELEKCNSNTDIEYQRRLAALDVQFIPDGRLYAFMK 685
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
78-719 |
2.53e-91 |
|
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: 311.67 E-value: 2.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDVRTMeKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSGE 157
Cdd:cd14882 3 ILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHA-KYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 158 SGAGKTETTKLLMRYLAYLGGRSGTggrtVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIRTY 237
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG----ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 238 LLERSRVCQINSPERNYHCFYFLCAA--PPEDIKRYKLGDPSSFHYLNQSSCI--------RVDGINDAEEYLVTRNAMD 307
Cdd:cd14882 158 QLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLKEYNLKAGRNYRYLRIPPEVppsklkyrRDDPEGNVERYKEFEEILK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 308 TVGIIEQEQEAIFRVVAAVLHLGNINFAKG---SEVDSSVIkddksrfhLNTAAELLMCDCKKLENALIKREINTPEGVI 384
Cdd:cd14882 238 DLDFNEEQLETVRKVLAAILNLGEIRFRQNggyAELENTEI--------ASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 385 TTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINA------SIGQDPNSdklIGVLDIYGFESFKTNSFEQLCINFTNEKL 458
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMkmsfprAVFGDKYS---ISIHDMFGFECFHRNRLEQLMVNTLNEQM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 459 QQHFNQNVFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEAcmfPKSTHEtfSQKLYEKFKNHKR-FTK 537
Cdd:cd14882 387 QYHYNQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDA---SRSCQD--QNYIMDRIKEKHSqFVK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 538 PkLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASEENTKssksSIATRFKVQLHELME 617
Cdd:cd14882 462 K-HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNMR----TLAATFRATSLELLK 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 618 TLS----STEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILA---SEIVKEK 690
Cdd:cd14882 537 MLSiganSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLAfdfDETVEMT 616
|
650 660
....*....|....*....|....*....
gi 1002232322 691 NDekvTCQKVLDKMGLQGYQIGRTKVFLR 719
Cdd:cd14882 617 KD---NCRLLLIRLKMEGWAIGKTKVFLK 642
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
78-701 |
2.28e-88 |
|
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: 302.80 E-value: 2.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPN---LVDVRTMEKYkganlgdldPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd14881 3 VMKCLQARFYAKEFFTNVGPILLSVNPYRDVGNpltLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYL-----------AYlggrsgtggrtveQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF 223
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLfdvagggpetdAF-------------KHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 224 dKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCA--APPEDIKRYKLG-DPSSFHYLNQSScIRVDGINDAEEYL 300
Cdd:cd14881 141 -TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAglSQEERVKLHLDGySPANLRYLSHGD-TRQNEAEDAARFQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 301 VTRNAMDTVGIIEQEqeaIFRVVAAVLHLGNINFAKGSEVDSSVIKDDKsrfhLNTAAELLMCDCKKLENALIKREINTP 380
Cdd:cd14881 219 AWKACLGILGIPFLD---VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE----LKSVAALLGVSGAALFRGLTTRTHNAR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 381 EGVITTTVGPSSATVSRDGLAKQIYSRLFDWLVNRINA-----SIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTN 455
Cdd:cd14881 292 GQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 456 EKLQQHFNQNVFKMEQEEYTREQINWSY-IEFVDNQDVLDLIEKKPGGIIALLDEACMfPKSTHETFSQKLYEKFKNHKR 534
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 535 FTKPK-LSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSAlfppaseenTKSSKssiatrFKVQLH 613
Cdd:cd14881 451 LFEAKpQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQNCNFGFA---------THTQD------FHTRLD 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 614 ELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDE 693
Cdd:cd14881 516 NLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEE 595
|
....*....
gi 1002232322 694 KVT-CQKVL 701
Cdd:cd14881 596 KALeDCALI 604
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
77-719 |
2.79e-87 |
|
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: 301.54 E-value: 2.79e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 77 GVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVDvRTMEKYKGANLGDLDPHVFAIADVSYRQMMNEGRNNSILVSG 156
Cdd:cd01386 2 SVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSE-KVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 157 ESGAGKTETTKLLMRYLAyLGGRSGTGGRTVEqqVLES-NPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAIR 235
Cdd:cd01386 81 RSGSGKTTNCRHILEYLV-TAAGSVGGVLSVE--KLNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 TYLLERSRVCQINSPERNYHCFYFLCA-APPEDIKRYKL---GDPSSFhYLNQSSCIRvDGINDAEEYLVTRNAMDTVGI 311
Cdd:cd01386 158 TLLLERSRVARRPEGESNFNVFYYLLAgADAALRTELHLnqlAESNSF-GIVPLQKPE-DKQKAAAAFSKLQAAMKTLGI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 312 IEQEQEAIFRVVAAVLHLGNINFAKGSEVdssvikdDKSRF----HLNTAAELLMCDCKKLENALIKreiNTPEGVIT-T 386
Cdd:cd01386 236 SEEEQRAIWSILAAIYHLGAAGATKAASA-------GRKQFarpeWAQRAAYLLGCTLEELSSAIFK---HHLSGGPQqS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 387 TVGPSSATVSR--------------DGLAKQIYSRLFDWLVNRINASIGQDPNSDKLIGVLDIYGFE------SFKTNSF 446
Cdd:cd01386 306 TTSSGQESPARsssggpkltgvealEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQnpahsgSQRGATF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 447 EQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSYIEFVDN-QDVLDLIEKKP--------------GGIIALLDEAC 511
Cdd:cd01386 386 EDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSpGALVALIDQAPqqalvrsdlrdedrRGLLWLLDEEA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 512 MFPKSTHETFSQKLY------EKFKNHKRFTKPKLSRTaFTIQHYAG--DVIYQSDHFLDKNKDYVVAehqelLNASRcs 583
Cdd:cd01386 466 LYPGSSDDTFLERLFshygdkEGGKGHSLLRRSEGPLQ-FVLGHLLGtnPVEYDVSGWLKAAKENPSA-----QNATQ-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 584 fvsaLFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNS-----VLKPAIFENTNVL-------QQLR 651
Cdd:cd01386 538 ----LLQESQKETAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHnagkdERSTSSPAAGDELldvpllrSQLR 613
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 652 CSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKN------DEKVTCQKVLDKMGLQ--GYQIGRTKVFLR 719
Cdd:cd01386 614 GSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevaDERKAVEELLEELDLEksSYRIGLSQVFFR 689
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
77-719 |
3.33e-83 |
|
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: 287.54 E-value: 3.33e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 77 GVLDNLAVRYARNLIYTYTGNILIAINPFQRLPNlVDVRTMEKYkganlgdldpHVFAIADVSYRQM-MNEGRNNSILVS 155
Cdd:cd14874 2 GIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSI-QDQLVIKKC----------HISGVAENALDRIkSMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 156 GESGAGKTETtklLMRYLAYLGGRSGTGGRTVEQQVLESnpVLEAFGNAKTVRNNNSSRFGKFVEIQFdKSGKISGAAIR 235
Cdd:cd14874 71 GESGSGKSYN---AFQVFKYLTSQPKSKVTTKHSSAIES--VFKSFGCAKTLKNDEATRFGCSIDLLY-KRNVLTGLNLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 236 -TYLLERSRVCQINSPERNYHCFYFLCAAPPEDIK-RYKLGDPSSFHYLNQSSCirVDGIN-DAEEYLVTRNAMDTVGII 312
Cdd:cd14874 145 yTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKaKFGIKGLQKFFYINQGNS--TENIQsDVNHFKHLEDALHVLGFS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 313 EQEQEAIFRVVAAVLHLGNINFA----KGSEVDSSVIKDDKsrfHLNTAAELLMCDCKKLENALikreinTPEGVITTTV 388
Cdd:cd14874 223 DDHCISIYKIISTILHIGNIYFRtkrnPNVEQDVVEIGNMS---EVKWVAFLLEVDFDQLVNFL------LPKSEDGTTI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 389 GPSSATVSRDGLAKQIYSRLFDWLVNRINASIgQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFK 468
Cdd:cd14874 294 DLNAALDNRDSFAMLIYEELFKWVLNRIGLHL-KCPLHTGVISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFH 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 469 MEQEEYTREQINWSYI--EFVDNQDVLDLIEKKPGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKL-SRTAF 545
Cdd:cd14874 373 DQLVDYAKDGISVDYKvpNSIENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNkERLEF 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 546 TIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASeENTKSSKSSIATRFKVQLHELMETLSSTEPH 625
Cdd:cd14874 453 GVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYS-SNTSDMIVSQAQFILRGAQEIADKINGSHAH 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 626 YIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILASEIVKEKNDEKVTCQKVLDKMG 705
Cdd:cd14874 532 FVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCQNEKEIIQDILQGQG 611
|
650
....*....|....*..
gi 1002232322 706 LQ---GYQIGRTKVFLR 719
Cdd:cd14874 612 VKyenDFKIGTEYVFLR 628
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
78-719 |
5.38e-83 |
|
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: 288.53 E-value: 5.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 78 VLDNLAVRYARNLIYTYTGNILIAINPFQRLPNLVD---VRTMEKYKGanlgdLDPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd14905 3 LINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSqelVRNYNQRRG-----LPPHLFALAAKAISDMQDFRRDQLIFI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLaylGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGKISGAAI 234
Cdd:cd14905 78 GGESGSGKSENTKIIIQYL---LTTDLSRSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 235 RTYLLERSRVCQINSPERNYHCFY-FLCAAPPEDIKRYKLGDPSSFHYLNQSSCIRVDGINDAEEYLVTRNAMDTVGIIE 313
Cdd:cd14905 155 YSYFLDENRVTYQNKGERNFHIFYqFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 314 QEQEAIFRVVAAVLHLGNINFAKGSevDSSVIKDdksRFHLNTAAELLMCDCKKLENALIKREintpegvittTVGPSSA 393
Cdd:cd14905 235 EKIDLIFKTLSFIIILGNVTFFQKN--GKTEVKD---RTLIESLSHNITFDSTKLENILISDR----------SMPVNEA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 394 TVSRDGLAKQIYSRLFDWLVNRINASIGQDPNSDKLiGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEE 473
Cdd:cd14905 300 VENRDSLARSLYSALFHWIIDFLNSKLKPTQYSHTL-GILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQRE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 474 YTREQINW-SYIEFVDNQDVLDLIEKkpggIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKlsrTAFTIQHYAG 552
Cdd:cd14905 379 YQTERIPWmTPISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYFG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 553 DVIYQSDHFLDKNKDYVVAEHQELLNASRCSF------VSALFPPASEENTKSSKSSIATRFKVQLHELMETLSSTEP-- 624
Cdd:cd14905 452 QFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgVFNINATVAELNQMFDAKNTAKKSPLSIVKVLLSCGSNNPnn 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 625 ---------------------------------------------HYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAI 659
Cdd:cd14905 532 vnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTHLTFDVKSVNEQIKSLCLLETT 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 660 RISCAGYPTRKLFHDFLHRFRILASEIVKEKN-DEKVTCQKV-LDKMGLQGYQIGRTKVFLR 719
Cdd:cd14905 612 RIQRFGYTIHYNNKIFFDRFSFFFQNQRNFQNlFEKLKENDInIDSILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
79-680 |
1.68e-64 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 235.64 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 79 LDNLAVRYARNLIYTYTGNILIAINPFQRLP-----NLVDVRTMEK----YKGANLGDLDPHVFAIADVSYRQMMNEGRN 149
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPiytpdHMQAYNKSREqtplYEKDTVNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 150 NSILVSGESGAGKTETTKLLMRYLAYL---------GGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVE 220
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIgdeteprpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 221 IQFDKSGKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPED------IKRYKLGDpsSFHYLNQSSCIRVDGIN 294
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptlrdsLEMNKCVN--EFVMLKQADPLATNFAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 295 DAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSV-------IKDDKS-----RFHLNTAAELLM 362
Cdd:cd14893 242 DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVggansttVSDAQScalkdPAQILLAAKLLE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 363 CDCKKLENALIKREINTPEGVITTT----VGPSSATVSRDGLAKQIYSRLFDWLVNRINASIG----QDPNSDKLIG--- 431
Cdd:cd14893 322 VEPVVLDNYFRTRQFFSKDGNKTVSslkvVTVHQARKARDTFVRSLYESLFNFLVETLNGILGgifdRYEKSNIVINsqg 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 432 --VLDIYGFESFKT--NSFEQLCINFTNEKLQQHFNQNVFKM-------EQEEYTREQINWSYIEFVDNQD-VLDLIEKK 499
Cdd:cd14893 402 vhVLDMVGFENLTPsqNSFDQLCFNYWSEKVHHFYVQNTLAInfsfledESQQVENRLTVNSNVDITSEQEkCLQLFEDK 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 500 PGGIIALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPKLS--------------RTAFTIQHYAGDVIYQSDHFLDKN 565
Cdd:cd14893 482 PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGadttneylapskdwRLLFIVQHHCGKVTYNGKGLSSKN 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 566 KDYVVAEHQELLNASRCSFVSAL-------------FPPASEENTKSSKS---------------SIATRFKVQLHELME 617
Cdd:cd14893 562 MLSISSTCAAIMQSSKNAVLHAVgaaqmaaassekaAKQTEERGSTSSKFrksassaresknitdSAATDVYNQADALLH 641
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 618 TLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFR 680
Cdd:cd14893 642 ALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Myo5-like_CBD |
cd14945 |
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied ... |
1707-2043 |
1.24e-53 |
|
Cargo binding domain of myosin 5 and similar proteins; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5 a,b,c) in vertebrates and two (myo2 and myo4) in fungi and related to plant class XI myosins. Their C-terminal cargo binding domains is important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. MyoV-CBDs interact with several adaptor proteins that in turn interact with the cargo.
Pssm-ID: 271253 [Multi-domain] Cd Length: 288 Bit Score: 190.30 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1707 LLTCISQYLGFFGS--KPVAALLIYQCLSHWRSF--EAMKTGVFDSILQAINSATEAQNDT-RALAYWLSNLSTLTVLLQ 1781
Cdd:cd14945 6 LLRGIVTDFEPSSGdhKLTPAYILYLCIRHAASNglTGQSTSLLNKVLKTIQQVVQQHNDDmQLLAFWLSNASELLYFLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1782 RSFKTTRTAISTPQRRrfsserifhasqtsnaglaylsgqpvvgaagLPQVEAKYPALLFKQQLVDLIEKVYGMISDSVK 1861
Cdd:cd14945 86 QDSKLYGAAGEAPQKE-------------------------------EEQKLTVSDLNELKQDLEAVSIKIYQQALKYLN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1862 KELNPllelciqdprtshspakghanglgqknqlgHWLAIVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRL 1941
Cdd:cd14945 135 KNLQP------------------------------KIRDIVKFLNSFLDLLKSFHVHPEIRSQVFTQLFSFINARLFNQL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1942 LLRRECCSFSNGEYVKVGLAELKHWSDNATREfaGSAWDALKHIRQAVDFLVISLKPMRTLKEIRtDVCPALSIQQLERI 2021
Cdd:cd14945 185 ITKKDALSWSRGMQIRANISRLEEWCEGRGLE--HLAVDFLSKLIQAVQLLQLKKYTQEDIEILC-ELCPSLNPAQLQAI 261
|
330 340
....*....|....*....|..
gi 1002232322 2022 VSMYWDDINGSNAISAEFTSSL 2043
Cdd:cd14945 262 LTQYQPANYGESPVPKEILRTL 283
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
76-718 |
1.28e-50 |
|
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: 193.13 E-value: 1.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 76 PGVLDNLAVRYARNLIYTYTGNILIAINPFQRLpNLVDVRTMEKYKGAN-LGDLDPHVFAIADVSYRQMMNEGRNNSILV 154
Cdd:cd14938 1 PSVLYHLKERFKNNKFYTKMGPLLIFINPKINN-NINNEETIEKYKCIDcIEDLSLNEYHVVHNALKNLNELKRNQSIII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 155 SGESGAGKTETTKLLMRYLAYLGGRSGTGGRTVEQQVLES--------------------NPVLEAFGNAKTVRNNNSSR 214
Cdd:cd14938 80 SGESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDNihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 215 FGKFVEIQFDKSgKISGAAIRTYLLERSRVCQINSPERNYHCFYFLCAAPPEDIKR-YKLGDPSSFHYLNQSSCIRVDGi 293
Cdd:cd14938 160 FSKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKmYFLKNIENYSMLNNEKGFEKFS- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 294 NDAEEYLVTRNAMDTVGIIEQEQEAIFRVVAAVLHLGNINFAKGSEVDSSVIKddKSRFHLNTAAELLMCDCKKLENA-- 371
Cdd:cd14938 238 DYSGKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKAFRKKSLLMG--KNQCGQNINYETILSELENSEDIgl 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 372 ------------LIKREINTPEGVITTTV---------GPSSATVSR--DGLAKQIYSRLFDWLVNRINASIGQDPNSD- 427
Cdd:cd14938 316 denvknlllackLLSFDIETFVKYFTTNYifndsilikVHNETKIQKklENFIKTCYEELFNWIIYKINEKCTQLQNINi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 428 --KLIGVLDIYGFESFKTNSFEQLCINFTNEKLQQHFNQNVFKMEQEEYTREQINWSY-IEFVDNQDVLD-LIEKKPGGI 503
Cdd:cd14938 396 ntNYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYnSENIDNEPLYNlLVGPTEGSL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 504 IALLDEACMFPKSTHETFSQKLYEKFKNHKRFTKPK---LSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNAS 580
Cdd:cd14938 476 FSLLENVSTKTIFDKSNLHSSIIRKFSRNSKYIKKDditGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 581 RCSFVSALFPPASEENT-----KSSKSSIATRFKV------------------QLHELMETLSSTEPHYIRCVKPN-SVL 636
Cdd:cd14938 556 ENEYMRQFCMFYNYDNSgniveEKRRYSIQSALKLfkrrydtknqmavsllrnNLTELEKLQETTFCHFIVCMKPNeSKR 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 637 KPAIFENTNVLQQLRCSGVLEAIRISCAGYPTRKLFHDFLHRFRILaseivkeKNDEKVTCQKVLDKMGLQGYQ--IGRT 714
Cdd:cd14938 636 ELCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIK-------NEDLKEKVEALIKSYQISNYEwmIGNN 708
|
....
gi 1002232322 715 KVFL 718
Cdd:cd14938 709 MIFL 712
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
98-227 |
7.42e-38 |
|
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: 140.56 E-value: 7.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 98 ILIAINPFQRLPNLVDVRTMEKYKGANLGDLDPHVFAIADVSYRQMMnEGRNN-SILVSGESGAGKTETTKLLMRYLA-- 174
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSML-DGYNNqSIFAYGESGAGKTETMKGVIPYLAsv 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 175 ----------YLGGRSGTGGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSG 227
Cdd:cd01363 80 afnginkgetEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
999-1592 |
2.92e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.92 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 999 EELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRF 1078
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1079 EEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKL 1158
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1159 LSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQ 1238
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1239 LQDSLQRLEENVGAKESLLLTEREQNAST------------LKLLAEAHLEIDELIR---KLEDSDRKSDSLQSTIKRLE 1303
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYegflegvkaallLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1304 EDGIAKEA-LLLTEKQAHEATRMTLT--EALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATT 1380
Cdd:COG1196 555 DDEVAAAAiEYLKAAKAGRATFLPLDkiRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1381 KAqiesqERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKI 1460
Cdd:COG1196 635 AL-----RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1461 EHLQNAIIKLEGDIEAKDISLEAAREEndtIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvDAISRLSSFVMe 1540
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREE---LLEELLEEEELLEEEALEELPEPPDLEELERELERLE-REIEALGPVNL- 784
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1541 kqesdAAKRALTEARERNEDLLKRNEDLLK-RND--DLIKKIEEssKTITQLQET 1592
Cdd:COG1196 785 -----LAIEEYEELEERYDFLSEQREDLEEaRETleEAIEEIDR--ETRERFLET 832
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
191-661 |
8.62e-34 |
|
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: 142.19 E-value: 8.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 191 VLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQF-----DKSGKISGAAIRTYLLERSRVCQI------NSPERNYHCFYF 259
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSErgresgDQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 260 LCAA----PPEDIKRYKLG----DPSSFHYLNQSSCiRVDGI--------NDAEEYLVTRNAMDTVGIIEQEQEAIFRVV 323
Cdd:cd14894 329 MVAGvnafPFMRLLAKELHldgiDCSALTYLGRSDH-KLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 324 AAVLHLGNINFAKgSEVDSSVIKDDKSRFHL-NTAAELL-MCDCKKLENALIKREINTPEGVITTTVGPSSATVS--RDG 399
Cdd:cd14894 408 SAVLWLGNIELDY-REVSGKLVMSSTGALNApQKVVELLeLGSVEKLERMLMTKSVSLQSTSETFEVTLEKGQVNhvRDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 400 LAKQIYSRLFDWLVNRINA-----------------SIGQDPNSDKLIGVLDIYGFESFKTNSFEQLCINFTNEKLqqhf 462
Cdd:cd14894 487 LARLLYQLAFNYVVFVMNEatkmsalstdgnkhqmdSNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL---- 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 463 nqnvFKMEQEEYTREQINWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPKST----------HETFSQKLYEK---- 528
Cdd:cd14894 563 ----YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRnssr 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 529 -------FKNHKRFTKPKLSRTAFTIQHYAGDVIYQSDHFLDKNKDYVVAEHQELLNASRCSFVSALFPPASE------- 594
Cdd:cd14894 639 lpepprvLSNAKRHTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQlgwspnt 718
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 595 --------ENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPAIFENTNVLQQLRCSGVLEAIRI 661
Cdd:cd14894 719 nrsmlgsaESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEI 793
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1020-1607 |
8.02e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 8.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1020 QRLEETIQEREALLLA-----ERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSsvtiekq 1094
Cdd:COG1196 216 RELKEELKELEAELLLlklreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1095 qheetvvQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIE 1174
Cdd:COG1196 289 -------EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1175 DADKSIahyhdttQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKE 1254
Cdd:COG1196 362 EAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1255 SLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKn 1334
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA- 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1335 eELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLRER-EQNDATTKAQIESQERNEQLLKRFVDVD----RKIDLLQD 1409
Cdd:COG1196 514 -LLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIvVEDDEVAAAAIEYLKAAKAGRATFLPLDkiraRAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1410 TIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREEND 1489
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1490 TIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAISRLSsfvmEKQESDAAKRALTEARERNEDLLKRNEDLL 1569
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE----EELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590
....*....|....*....|....*....|....*...
gi 1002232322 1570 KRNDDLIKKIEESsktITQLQETLQRLEGKSTNLEAEN 1607
Cdd:COG1196 749 EEEALEELPEPPD---LEELERELERLEREIEALGPVN 783
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
875-1471 |
2.49e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.66 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKklrtdlekskvAEVSKLQAALNEMEQRmqdVTAMQERESakkAVEE 954
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELE-----------AELEELRLELEELELE---LEEAQAEEY---ELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLL 1034
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1035 AERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELL 1114
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1115 REAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEE--LLKKIEDADKSIAHYHDTTQRLEE 1192
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1193 NVTAVENSLKAERQHNgaIMKQLADAQVEIGELQRNLE--------DADRRNNQLQDSLQRLEENVGAK----------- 1253
Cdd:COG1196 536 YEAALEAALAAALQNI--VVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDlvasdlreada 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1254 ------ESLLLTEREQNASTLKLLAEAHLEIDELIRKLED---SDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATR 1324
Cdd:COG1196 614 ryyvlgDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGeggSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1325 MTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLlkrfVDVDRKI 1404
Cdd:COG1196 694 ELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL----EELEREL 769
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1405 DLLQDTIERIGE-NstikdalLLSERqekdaikkELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLE 1471
Cdd:COG1196 770 ERLEREIEALGPvN-------LLAIE--------EYEELEERYDFLSEQREDLEEARETLEEAIEEID 822
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
895-1637 |
4.86e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.01 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 895 ERVEELTNRLglEKKLRTDLEKSKVAEvsKLQAALNEMEQRMQDVTAMQeresaKKAVEEALEQEREKISSLTSEIEGLK 974
Cdd:TIGR02168 189 DRLEDILNEL--ERQLKSLERQAEKAE--RYKELKAELRELELALLVLR-----LEELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 975 ALLVAEQEENDLTKKAHAnaqerneELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARN 1054
Cdd:TIGR02168 260 AELQELEEKLEELRLEVS-------ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRL 1134
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1135 EESLTEKDAllTTERQETEATKKLLSEAQYKNEELLKKIEDADKSiahyHDTTQRLEENVTAVENSLKAERQHNGAIMKQ 1214
Cdd:TIGR02168 413 EDRRERLQQ--EIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1215 LADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEI----DELIRKLEDSDR 1290
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAVvvenLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1291 KSDSLQSTIkrLEEDGIAKEALLLTEKQAHEATRMTLTEA--LEKNEELLKK----------IHDD------DKHILELQ 1352
Cdd:TIGR02168 567 QNELGRVTF--LPLDSIKGTEIQGNDREILKNIEGFLGVAkdLVKFDPKLRKalsyllggvlVVDDldnaleLAKKLRPG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1353 FTI-----------------------------QRLEENTAAKENLLLREREQNDATTKAQIESQERN---EQLLKRFVDV 1400
Cdd:TIGR02168 645 YRIvtldgdlvrpggvitggsaktnssilerrREIEELEEKIEELEEKIAELEKALAELRKELEELEeelEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1401 DRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDIS 1480
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1481 LEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAIS--------RLSSFVMEKQ------ESDA 1546
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESlaaeieelEELIEELESEleallnERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1547 AKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNL-----EAENQVLRQQATATPPST 1621
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLqerlsEEYSLTLEEAEALENKIE 964
|
810
....*....|....*.
gi 1002232322 1622 AKSSASRSKITRIHRS 1637
Cdd:TIGR02168 965 DDEEEARRRLKRLENK 980
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
888-1604 |
1.18e-27 |
|
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: 122.87 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 888 VAKEKLEERVEELTNRLGLEKKLR--TDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQ--------ERESAKKAVEEALE 957
Cdd:TIGR02169 268 EEIEQLLEELNKKIKDLGEEEQLRvkEKIGELE-AEIASLERSIAEKERELEDAEERLakleaeidKLLAEIEELEREIE 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 958 QEREKISSLTSEIEGLKA---LLVAEQEE----NDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQERE 1030
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKEeleDLRAELEEvdkeFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLAERQ-------EKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTI---EKQQHEETV 1100
Cdd:TIGR02169 427 AAIAGIEAkineleeEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeaQARASEERV 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQLAEAQAKIDE-------LLREAGDTDEK-STQLETTI-QRLEESLTEKDAL------LTTERQETEATKKLLSEAQYK 1165
Cdd:TIGR02169 507 RGGRAVEEVLKAsiqgvhgTVAQLGSVGERyATAIEVAAgNRLNNVVVEDDAVakeaieLLKRRKAGRATFLPLNKMRDE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1166 NEELLKKIEDADKSIA-HYHDTTQRLEENV------TAVENSLKAERQHNGAI-MKQLADAQVEIGEL----QRNLEDAD 1233
Cdd:TIGR02169 587 RRDLSILSEDGVIGFAvDLVEFDPKYEPAFkyvfgdTLVVEDIEAARRLMGKYrMVTLEGELFEKSGAmtggSRAPRGGI 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1234 RRNNQLQDSLQRLEENVGAKESLLltereqnASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDgIAKEALL 1313
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKREL-------SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE-EEKLKER 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1314 LTEKQAHEATrmtLTEALEKNEELLKKIhddDKHILELQFTIQRLEENTAAKENLLLREREQNdattkAQIESQERNEQL 1393
Cdd:TIGR02169 739 LEELEEDLSS---LEQEIENVKSELKEL---EARIEELEEDLHKLEEALNDLEARLSHSRIPE-----IQAELSKLEEEV 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1394 lkrfvdvdRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKEL----VEAGERNEELIMKIEDTDKKIEHLQNAIIK 1469
Cdd:TIGR02169 808 --------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqiKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1470 LEGdieakdiSLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvDAISRLSSFVMEKQESDAAKR 1549
Cdd:TIGR02169 880 LES-------RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALE-EELSEIEDPKGEDEEIPEEEL 951
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1550 ALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLE 1604
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DIL |
pfam01843 |
DIL domain; The DIL domain has no known function. |
1924-2028 |
1.29e-27 |
|
DIL domain; The DIL domain has no known function.
Pssm-ID: 460359 [Multi-domain] Cd Length: 103 Bit Score: 108.45 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1924 KLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHWSdnATREFAGSAWDALKHIRQAVDFLVISLKPMRTLK 2003
Cdd:pfam01843 1 QLFSQLFYFINAELFNRLLLRKKYCSWSKGMQIRYNLSRLEEWA--RSNGLESEARDHLAPLIQAAQLLQLRKSTLEDLD 78
|
90 100
....*....|....*....|....*
gi 1002232322 2004 EIRtDVCPALSIQQLERIVSMYWDD 2028
Cdd:pfam01843 79 SIL-QVCPALNPLQLHRLLTLYQPD 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
891-1654 |
2.66e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.09 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEKSKVAEV-SKLQAALNEMEQ-----------RMQDVTAMQERESAKKAVEEA--- 955
Cdd:PTZ00121 1027 EKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGkAEAKAHVGQDEGlkpsykdfdfdAKEDNRADEATEEAFGKAEEAkkt 1106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 ----LEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDA-DGKIKQLSDTVQRLEETIQERE 1030
Cdd:PTZ00121 1107 etgkAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAEAARKAEE 1186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLlqETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKI 1110
Cdd:PTZ00121 1187 VRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA--EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1111 DELLREAGDTDEKSTQLEttIQRLEESLTEKDALLTTERQETEATKKLLSEAQyKNEELLKKIEDADKSI---------A 1181
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADE--LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKAdaakkkaeeA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEENVTAVEnsLKAERQHNGAIMKQLADAQVEIGELQRNLEDAdRRNNQLQDSLQrlEENVGAKESLLLTER 1261
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADE--AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK-KKADEAKKKAE--EDKKKADELKKAAAA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQNASTLKLLAEAHLEIDELIRKLEDSdRKSDSLQstiKRLEEDGIAKEALLLTE--KQAHEATRMtlTEALEKNEELLK 1339
Cdd:PTZ00121 1417 KKKADEAKKKAEEKKKADEAKKKAEEA-KKADEAK---KKAEEAKKAEEAKKKAEeaKKADEAKKK--AEEAKKADEAKK 1490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1340 KIHDDDKHILELQftiQRLEENTAAKENLLLREREQNDATTKAqiESQERNEQLLKrfVDVDRKIDLLQ--DTIERIGEN 1417
Cdd:PTZ00121 1491 KAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKA--EEAKKADEAKK--AEEKKKADELKkaEELKKAEEK 1563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1418 STIKDALLLSERQEKDAIKKE-LVEAGERNEELIMKIEDTDKKIEHLQnAIIKLEGDIEAKDI-SLEAAREENDTIRKSL 1495
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEeAKKAEEARIEEVMKLYEEEKKMKAEE-AKKAEEAKIKAEELkKAEEEKKKVEQLKKKE 1642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1496 AEAQEKNEELLRKISDNEYRIHLLQDTAQKlqvdaisrlssfvmEKQESDAAKRALTEARERNEDlLKRNEDLLKRNDDL 1575
Cdd:PTZ00121 1643 AEEKKKAEELKKAEEENKIKAAEEAKKAEE--------------DKKKAEEAKKAEEDEKKAAEA-LKKEAEEAKKAEEL 1707
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1576 IKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATatppSTAKSSASRSKITRIHRSPENGHILNGDTRQAEIK 1654
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE----EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
891-1613 |
2.70e-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: 118.62 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNrlgLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQdvtamqERESAKKAVEEALEQEREKISSLTSEI 970
Cdd:TIGR02168 213 ERYKELKAELRE---LELALLVLRLEELREELEELQEELKEAEEELE------ELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 971 EGL-KALLVAEQEENDLTK-KAHANAQERN-----EELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEA 1043
Cdd:TIGR02168 284 EELqKELYALANEISRLEQqKQILRERLANlerqlEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1044 SAVIAESQARN-------EAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKidELLRE 1116
Cdd:TIGR02168 364 EAELEELESRLeeleeqlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1117 AGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKN---EELLKKIEDADKSIAH-------YHDT 1186
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLdslERLQENLEGFSEGVKAllknqsgLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1187 TQRLEENV-------TAVENSLKAERQHngAIMKQLADAQVEIGELQRN-------LEDADRRNNQLQ----DSLQRLEE 1248
Cdd:TIGR02168 522 LGVLSELIsvdegyeAAIEAALGGRLQA--VVVENLNAAKKAIAFLKQNelgrvtfLPLDSIKGTEIQgndrEILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1249 NVGAKESL------------------LLTEREQNASTLKLLAEAHLEI----DELIRK----LEDSDRKSDSLQST---I 1299
Cdd:TIGR02168 600 FLGVAKDLvkfdpklrkalsyllggvLVVDDLDNALELAKKLRPGYRIvtldGDLVRPggviTGGSAKTNSSILERrreI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1300 KRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLE---ENTAAKENLLLREREQN 1376
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEaevEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1377 DATTKAQIESQERNEQLLKRfvdVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDT 1456
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1457 DKKIEHLQNAIIKLEGDIEakdiSLEAAREEndtIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDaISRLSs 1536
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIE----SLAAEIEE---LEELIEELESELEALLNERASLEEALALLRSELEELSEE-LRELE- 907
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1537 fvmekQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEEssktitQLQETLQRLEGKSTNLEAENQVLRQQ 1613
Cdd:TIGR02168 908 -----SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE------EYSLTLEEAEALENKIEDDEEEARRR 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
886-1612 |
5.74e-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: 107.46 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEE---RVEELTNRLgleKKLRTdlEKSKVAEVSKLQAALNEMEQrmqdvtamQERESAKKAVEEALEQEREK 962
Cdd:TIGR02169 179 LEEVEENIERldlIIDEKRQQL---ERLRR--EREKAERYQALLKEKREYEG--------YELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 963 ISSLTSEIEGLKALL--------VAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEreallL 1034
Cdd:TIGR02169 246 LASLEEELEKLTEEIselekrleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED-----A 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1035 AERQEKEEASavIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELL 1114
Cdd:TIGR02169 321 EERLAKLEAE--IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1115 REAGDtdekstqLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDAdksiahyhdtTQRLEENV 1194
Cdd:TIGR02169 399 REINE-------LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ----------EWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1195 tavenslkaerqhngaimKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKEslllTEREQNASTLKLLAEA 1274
Cdd:TIGR02169 462 ------------------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASE----ERVRGGRAVEEVLKAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1275 HLEIDELIRKLEDSDRK---------SDSLQSTIkrLEEDGIAKEAL-LLTEKQAHEATRMTLTEaLEKNEELLKKIHD- 1343
Cdd:TIGR02169 520 IQGVHGTVAQLGSVGERyataievaaGNRLNNVV--VEDDAVAKEAIeLLKRRKAGRATFLPLNK-MRDERRDLSILSEd 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1344 ------------DDKHILELQFTIQR--LEENTAAKENLLLRER---------EQNDATTKA----------QIESQERN 1390
Cdd:TIGR02169 597 gvigfavdlvefDPKYEPAFKYVFGDtlVVEDIEAARRLMGKYRmvtlegelfEKSGAMTGGsraprggilfSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1391 EQLLKRFVDVDRKIDLLQDTIERI-GENSTIKDALLLSERQ------EKDAIKKELVEAGERNEELIMKIEDTDKKIEHL 1463
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIeNRLDELSQELSDASRKigeiekEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1464 QNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQ-EKNEELLRKISDNEYRIHL-LQDTAQKLQvdaiSRLSSFVMEK 1541
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEArLREIEQKLN----RLTLEKEYLE 832
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1542 QESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQ 1612
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER 903
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
882-1337 |
8.45e-23 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 106.66 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 882 DTQALKVAKEKLEERVEEltnrlglekkLRTDLEKSKVAevskLQAALNEMEQRMQDVTAMQEResAKKAVEEA------ 955
Cdd:PRK02224 308 DAEAVEARREELEDRDEE----------LRDRLEECRVA----AQAHNEEAESLREDADDLEER--AEELREEAaelese 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLA 1035
Cdd:PRK02224 372 LEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1036 ER-----QEKEEASAV--IAESQARNEAFASKLEDAEKQIDLLQETVQRFEEaitklqssvtiekqqheetvvqLAEAQA 1108
Cdd:PRK02224 452 GKcpecgQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAED----------------------LVEAED 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1109 KIDELLREAGDTDEKSTQLETTIQRLEESLTEKDalltterqetEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQ 1188
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELR----------ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1189 RLEENVTAVENSLKAErqhngAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTL 1268
Cdd:PRK02224 580 KLAELKERIESLERIR-----TLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARED 654
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1269 KLLAEAHLE-IDELIRKLEDsdrKSDSLQSTIKRLEEDgIAKEALLLTEKQAHEATRMTLTEALEKNEEL 1337
Cdd:PRK02224 655 KERAEEYLEqVEEKLDELRE---ERDDLQAEIGAVENE-LEELEELRERREALENRVEALEALYDEAEEL 720
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
889-1607 |
2.05e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 105.99 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 889 AKEKLEE--RVEELTNRLGLEKklrtdLEKSKVAEVSKLQAALNEMEQRMQDvtAMQERESAKKAVEEALEQEREKISSL 966
Cdd:PTZ00121 1235 AKKDAEEakKAEEERNNEEIRK-----FEEARMAHFARRQAAIKAEEARKAD--ELKKAEEKKKADEAKKAEEKKKADEA 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 967 TSEIEGLKALLVAEQEENDLTKKAHAnAQERNEELSKEVEDADGKIKQLSDTVQRLEETiQEREALLLAERQEKEEASAV 1046
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKKAEEAKKKADA-AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1047 IAESQARNEAFASKLEDAEKQIDLLQ---ETVQRFEEAITKLQssvtiEKQQHEEtVVQLAEAQAKIDELLREAgdtdEK 1123
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKkaaAAKKKADEAKKKAE-----EKKKADE-AKKKAEEAKKADEAKKKA----EE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1124 STQLETTIQRLEESltekdalltteRQETEATKKllSEAQYKNEELLKKIEDADKSIahyhDTTQRLEENVTAVENSLKA 1203
Cdd:PTZ00121 1456 AKKAEEAKKKAEEA-----------KKADEAKKK--AEEAKKADEAKKKAEEAKKKA----DEAKKAAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1204 ERQHNGAIMKQLADA----------------------QVEIGELQRNLEDADRRNNQLQDSLQRLEEnvgakesLLLTER 1261
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAkkadeakkaeekkkadelkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEE-------AKKAEE 1591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQST--IKRLEEDGIAKEAlllTEKQAHEATRMTLTEALEKNEELLK 1339
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAeeEKKKVEQLKKKEA---EEKKKAEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1340 KIHDDDKHILELqftiQRLEENTAAKENLLLREREQndattkaqiesQERNEQLLKRFVDVDRKIDLLQDTIErigENST 1419
Cdd:PTZ00121 1669 KAEEDKKKAEEA----KKAEEDEKKAAEALKKEAEE-----------AKKAEELKKKEAEEKKKAEELKKAEE---ENKI 1730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1420 IKDALLLSERQEKDAIKKELVEAGERN--EELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSlAE 1497
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF-AN 1809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1498 AQEKNEELLRKISDNEYrihlLQDTAQKLQVDAISrlssfvMEKQESDAAKRALTEARERNEDLLKRNEDLLKRND---D 1574
Cdd:PTZ00121 1810 IIEGGKEGNLVINDSKE----MEDSAIKEVADSKN------MQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDlkeD 1879
|
730 740 750
....*....|....*....|....*....|...
gi 1002232322 1575 LIKKIEEsSKTITQLQETLQRLEGKSTNLEAEN 1607
Cdd:PTZ00121 1880 DEEEIEE-ADEIEKIDKDDIEREIPNNNMAGKN 1911
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
890-1617 |
3.23e-22 |
|
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: 105.05 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEELTNRLGLE-------------KKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQEREsaKKAVEEAL 956
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDqytqlalmefakkKSLHGKAELLT-LRSQLLTLCTPCMPDTYHERKQVLEKE--LKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 957 EQEREKISSLTSEIEGLKAL---------LVAEQEENDLTKKAHANAQERNE---------ELSKEVEDADGKIKQLSDT 1018
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQlkkqqllkqLRARIEELRAQEAVLEETQERINrarkaaplaAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1019 VQ---RLEETIQEREALLLAERQEKEEASAVIAESQARNEAFAsklEDAEKQIDLLQETVQR--FEEAITKLQSSVTIEK 1093
Cdd:TIGR00618 316 LQskmRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR---DAHEVATSIREISCQQhtLTQHIHTLQQQKTTLT 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1094 QQHE---ETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELL 1170
Cdd:TIGR00618 393 QKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1171 KKIEDADKsiahYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNledaDRRNNQLQDSLQRLEENV 1250
Cdd:TIGR00618 473 QQLQTKEQ----IHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPL----TRRMQRGEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1251 GAKESLLLTEREQNAStlkLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEdgiakeALLLTEKQAhEATRMTLTEA 1330
Cdd:TIGR00618 545 EDVYHQLTSERKQRAS---LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR------LQDLTEKLS-EAEDMLACEQ 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1331 LEKNEELLKKIHDDDKhILELQFTIQRLEENTAAKENLLL-----REREQNDATTKAQIESQERNEQLLKRfvdvdrkid 1405
Cdd:TIGR00618 615 HALLRKLQPEQDLQDV-RLHLQQCSQELALKLTALHALQLtltqeRVREHALSIRVLPKELLASRQLALQK--------- 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1406 llqdtierigenstikdalLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDI----SL 1481
Cdd:TIGR00618 685 -------------------MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDalnqSL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1482 EAAREENDTIRKSLAEAQEKNEEllrKISDNEYRIHLLQDTAQKLQvdaisrlssFVMEKQESDAAKRALTEARERNEdl 1561
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNE---EVTAALQTGAELSHLAAEIQ---------FFNRLREEDTHLLKTLEAEIGQE-- 811
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1562 lkRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATAT 1617
Cdd:TIGR00618 812 --IPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
892-1409 |
4.27e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 104.35 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 892 KLEERVEELTN-RLGLEKKLR------TDLEKSKVAEVSK-LQAALNEMEQRMQDVTAM-----QERESAKKAVEEA--- 955
Cdd:PRK02224 163 KLEEYRERASDaRLGVERVLSdqrgslDQLKAQIEEKEEKdLHERLNGLESELAELDEEieryeEQREQARETRDEAdev 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 ---LEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDA-------DGKIKQLSDTVQRLE-- 1023
Cdd:PRK02224 243 leeHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeagldDADAEAVEARREELEdr 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1024 -----ETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEE 1098
Cdd:PRK02224 323 deelrDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGD 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1099 TVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLtterqetEATKKLLSEAQYKNEELLKKIEDADK 1178
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL-------EAGKCPECGQPVEGSPHVETIEEDRE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1179 SIAHYHDTTQRLEENVTAVENSLkaERqhngaiMKQLADAQVEIGELQRNLED-----ADRRN--NQLQDSLQRLEENVG 1251
Cdd:PRK02224 476 RVEELEAELEDLEEEVEEVEERL--ER------AEDLVEAEDRIERLEERREDleeliAERREtiEEKRERAEELRERAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1252 AKESLLLTEREQnASTLKLLAEAHLE-IDELIRKLEDSDRKSDSLQSTIKRLEE-DGIAKEALLLTEKQAHEAT-----R 1324
Cdd:PRK02224 548 ELEAEAEEKREA-AAEAEEEAEEAREeVAELNSKLAELKERIESLERIRTLLAAiADAEDEIERLREKREALAElnderR 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1325 MTLTEALEKNEELLKKIhdDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKA--QIESQ-ERNEQLLKRFVDVD 1401
Cdd:PRK02224 627 ERLAEKRERKRELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigAVENElEELEELRERREALE 704
|
....*...
gi 1002232322 1402 RKIDLLQD 1409
Cdd:PRK02224 705 NRVEALEA 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
885-1495 |
7.65e-22 |
|
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: 103.76 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 885 ALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVS-KLQAALNEMEQRMQDVTAMQERESA-KKAVEEALEQEREK 962
Cdd:pfam12128 269 SDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 963 ISSLTSEIEGLKALLVA-EQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETiqEREALLLAERQEKE 1041
Cdd:pfam12128 349 LPSWQSELENLEERLKAlTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAV--AEDDLQALESELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1042 EASAVIAESQARNEAFASKLEDAEKQIDLLQET------VQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLR 1115
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQATATpelllqLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASE 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1116 EAGDTDEKSTQLETTIQRLEESLTEKD----ALLTTERQE-TEATKKLLSEAQYKNEELLKKIEDADKS----------- 1179
Cdd:pfam12128 507 ALRQASRRLEERQSALDELELQLFPQAgtllHFLRKEAPDwEQSIGKVISPELLHRTDLDPEVWDGSVGgelnlygvkld 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1180 -----IAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRL-------- 1246
Cdd:pfam12128 587 lkridVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLfdekqsek 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1247 ---EENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRklEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEAT 1323
Cdd:pfam12128 667 dkkNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1324 RMTLTEALEK-NEELLKKIHDDDKHILELQFTIQRLE---ENTAAKENLLLR----------EREQNDATTKAQIE-SQE 1388
Cdd:pfam12128 745 AKAELKALETwYKRDLASLGVDPDVIAKLKREIRTLErkiERIAVRRQEVLRyfdwyqetwlQRRPRLATQLSNIErAIS 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1389 RNEQLLKRFV-DVDRKI-------DLLQDTIERIGENSTIKDALL-----LSERQEKDAIKKELVEAGERNEELIMK--- 1452
Cdd:pfam12128 825 ELQQQLARLIaDTKLRRaklemerKASEKQQVRLSENLRGLRCEMsklatLKEDANSEQAQGSIGERLAQLEDLKLKrdy 904
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1002232322 1453 -IEDTDKKIEHLQNAIIKLEGdiEAKDISLEAAREENDTIRKSL 1495
Cdd:pfam12128 905 lSESVKKYVEHFKNVIADHSG--SGLAETWESLREEDHYQNDKG 946
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
955-1505 |
1.63e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 99.34 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLL 1034
Cdd:PRK02224 210 GLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1035 AERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQrfeeaitklQSSVTIekQQHEETVVQLAEAQAKIDEL- 1113
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLE---------ECRVAA--QAHNEEAESLREDADDLEERa 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 --LREAGDTDEKSTQ-LETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRL 1190
Cdd:PRK02224 359 eeLREEAAELESELEeAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1191 EENVTAVENSLKA-------ERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAkESLLLTEREQ 1263
Cdd:PRK02224 439 RERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1264 NASTLKLLAEAHLEIDElirkledsdrKSDSLQSTIKRLEEdgiakealLLTEKQAHEATRMTLTEALEKNEELLKKIHd 1343
Cdd:PRK02224 518 REDLEELIAERRETIEE----------KRERAEELRERAAE--------LEAEAEEKREAAAEAEEEAEEAREEVAELN- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1344 ddkhilelqftiQRLEENTAAKENlLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDA 1423
Cdd:PRK02224 579 ------------SKLAELKERIES-LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1424 LLLSERQEKdaiKKELVEAGERNEElimKIEDTDKKIEHLQNAIIKLEGDIEakdiSLEAAREEndtiRKSLAEAQEKNE 1503
Cdd:PRK02224 646 ARIEEARED---KERAEEYLEQVEE---KLDELREERDDLQAEIGAVENELE----ELEELRER----REALENRVEALE 711
|
..
gi 1002232322 1504 EL 1505
Cdd:PRK02224 712 AL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1010-1616 |
1.95e-20 |
|
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: 99.36 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1010 GKIKQLsdtvqrLEETIQEREALLlaerqekEEASAVIAESQARNEAFaSKLEDA--------------EKQIDLLQETV 1075
Cdd:TIGR02168 144 GKISEI------IEAKPEERRAIF-------EEAAGISKYKERRKETE-RKLERTrenldrledilnelERQLKSLERQA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1076 QRFEEAITKlqsSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDAllttERQETEat 1155
Cdd:TIGR02168 210 EKAERYKEL---KAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL----EVSELE-- 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1156 kKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRR 1235
Cdd:TIGR02168 281 -EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1236 NNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEED---------- 1305
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKleeaelkelq 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1306 -GIAKEALLLTEKQAHEATRM----TLTEALEKNEELLKKIHDDDKHILELQFTIQRLEEN-----TAAKENLL------ 1369
Cdd:TIGR02168 440 aELEELEEELEELQEELERLEealeELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfsEGVKALLKnqsgls 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1370 -----------------------LREREQ-----NDATTKAQIESQERNE------------------------------ 1391
Cdd:TIGR02168 520 gilgvlselisvdegyeaaieaaLGGRLQavvveNLNAAKKAIAFLKQNElgrvtflpldsikgteiqgndreilknieg 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1392 --QLLKRFVDVDRKI--------------DLLQDTIERIGEN-----------------------STIKDALLLSERQEK 1432
Cdd:TIGR02168 600 flGVAKDLVKFDPKLrkalsyllggvlvvDDLDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1433 DAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAR--------------EENDTIRKSLAEA 1498
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRkdlarleaeveqleERIAQLSKELTEL 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1499 QEKNEELLRKISDNEYRIHLLQDTAQKLQVDAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKK 1578
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
730 740 750
....*....|....*....|....*....|....*...
gi 1002232322 1579 IEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATA 1616
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
921-1596 |
4.49e-20 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.80 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 921 EVSKLQAALNEMEQRMQD-------VTAMQERES-AKKAVEEALEQEREKISSLTSEIEglkallvaEQEENDLTKKAHA 992
Cdd:PRK02224 139 EVNKLINATPSDRQDMIDdllqlgkLEEYRERASdARLGVERVLSDQRGSLDQLKAQIE--------EKEEKDLHERLNG 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 993 NAQERNEeLSKEVEDADGKIKQLSDTVQRLEETIQEREAlllaERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQ 1072
Cdd:PRK02224 211 LESELAE-LDEEIERYEEQREQARETRDEADEVLEEHEE----RREELETLEAEIEDLRETIAETEREREELAEEVRDLR 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1073 ETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESltekdalltTERQET 1152
Cdd:PRK02224 286 ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED---------ADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1153 EATkkllsEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVEnslkaerqhngaimKQLADAQVEIGELQRNLEDa 1232
Cdd:PRK02224 357 RAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELR--------------ERFGDAPVDLGNAEDFLEE- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1233 drrnnqLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAhlEIDELIRKLEDSDRksdslqstIKRLEEDGIAKEAL 1312
Cdd:PRK02224 417 ------LREERDELREREAELEATLRTARERVEEAEALLEAG--KCPECGQPVEGSPH--------VETIEEDRERVEEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1313 LlTEKQAHEATRMTLTEALEKNEELLkkihdddkhilELQFTIQRLEENTAAKENLLLREREQNDattkaqiESQERNEQ 1392
Cdd:PRK02224 481 E-AELEDLEEEVEEVEERLERAEDLV-----------EAEDRIERLEERREDLEELIAERRETIE-------EKRERAEE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1393 LLKRFVDVDRKIDLLQDTIERIGENSTikdalllSERQEKDAIKKELVEAGERNEELimkiedtdKKIEHLQNAIIKLEG 1472
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAE-------EAREEVAELNSKLAELKERIESL--------ERIRTLLAAIADAED 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1473 DIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNeyRIHLLQ---DTAQKLQVDAISRLSSFVMEKQESDAAKR 1549
Cdd:PRK02224 607 EIERLREKREALAELNDERRERLAEKRERKRELEAEFDEA--RIEEARedkERAEEYLEQVEEKLDELREERDDLQAEIG 684
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1002232322 1550 ALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSktitQLQETLQRL 1596
Cdd:PRK02224 685 AVENELEELEELRERREALENRVEALEALYDEAE----ELESMYGDL 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
894-1511 |
3.25e-19 |
|
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: 94.70 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 894 EERVEELTNRLgleKKLRTDLeKSKVAEVSKLQAALNEMEQRMQDV-TAMQERESAKKAVEEALEQEREKISSLTSEIEG 972
Cdd:TIGR04523 32 DTEEKQLEKKL---KTIKNEL-KNKEKELKNLDKNLNKDEEKINNSnNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 973 LKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRL----EETIQEREAL------LLAERQEKEE 1042
Cdd:TIGR04523 108 INSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLnnkyNDLKKQKEELenelnlLEKEKLNIQK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1043 ASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDT-- 1120
Cdd:TIGR04523 188 NIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIkk 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1121 --DEKSTQLETT---IQRLEESLTE-KDALLTTERQETEATKKLLSEaQYKNEEllKKIEDADKSIAHYHDTTQRLEENV 1194
Cdd:TIGR04523 268 qlSEKQKELEQNnkkIKELEKQLNQlKSEISDLNNQKEQDWNKELKS-ELKNQE--KKLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1195 TAVENSLKAERQHNGAIMKQLAdaqveigELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEA 1274
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQRELE-------EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1275 HLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALL--LTEKQAHEATRMTLTEALEKN-----EELLKKIHDDDKH 1347
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIknLDNTRESLETQLKVLSRSINKikqnlEQKQKELKSKEKE 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1348 ILELQFTIQRLEENTA--AKENLLLREREQNDATTKAQIESQ-------------ERNEQLLKRFVD-VDRKIDLLQDTI 1411
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKdlTKKISSLKEKIEKLESEKKEKESKisdledelnkddfELKKENLEKEIDeKNKEIEELKQTQ 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1412 ERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTI 1491
Cdd:TIGR04523 578 KSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEI 657
|
650 660
....*....|....*....|
gi 1002232322 1492 RKSLAEAQEKNEELLRKISD 1511
Cdd:TIGR04523 658 RNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
989-1414 |
9.79e-19 |
|
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: 93.58 E-value: 9.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 989 KAHANAQERN---EELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAE 1065
Cdd:TIGR02168 667 KTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1066 KQIDLLQETVQRFEEAITKLQSsvtiekqqheetvvQLAEAQAKIDELlreagdtDEKSTQLETTIQRLEESLTEKDALL 1145
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEE--------------RLEEAEEELAEA-------EAEIEELEAQIEQLKEELKALREAL 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1146 TTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGEL 1225
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1226 QRNLEDADRRNNQLQDSLQRLEENVGAKESLLltereqnastlkllaeahleiDELIRKLEDSDRKSDSLQSTIKRLEEd 1305
Cdd:TIGR02168 886 EEALALLRSELEELSEELRELESKRSELRREL---------------------EELREKLAQLELRLEGLEVRIDNLQE- 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1306 giakeallltekQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEE-NTAAKENLllreREQNdattkaqi 1384
Cdd:TIGR02168 944 ------------RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvNLAAIEEY----EELK-------- 999
|
410 420 430
....*....|....*....|....*....|
gi 1002232322 1385 esqERNEQLLKRFVDVDRKIDLLQDTIERI 1414
Cdd:TIGR02168 1000 ---ERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
955-1281 |
1.13e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 93.58 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREkISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLL 1034
Cdd:TIGR02168 672 ILERRRE-IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1035 AERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELL 1114
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1115 REAGDTdekstqlETTIQRLEESLTEKdalltteRQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENV 1194
Cdd:TIGR02168 831 RRIAAT-------ERRLEDLEEQIEEL-------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1195 TAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSL----QRLEENVGAKESLLLTEREQNASTLKL 1270
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKR 976
|
330
....*....|.
gi 1002232322 1271 LAEahlEIDEL 1281
Cdd:TIGR02168 977 LEN---KIKEL 984
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
891-1631 |
2.74e-18 |
|
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: 92.10 E-value: 2.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRtdlEKSKV---AEVSKLQAALNEMEQRMQDVTAMQERES------------------AK 949
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELH---EKQKFylrQSVIDLQTKLQEMQMERDAMADIRRRESqsqedlrnqlqntvheleAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 950 KAVEE--------ALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQE---RN---------EELSKEVEDAD 1009
Cdd:pfam15921 158 KCLKEdmledsntQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTmhfRSlgsaiskilRELDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1010 GKIKQLSDTVQRLEETIQEREALLLAERQEKEEasAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSV 1089
Cdd:pfam15921 238 GRIFPVEDQLEALKSESQNKIELLLQQHQDRIE--QLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1090 TIEKQQHEETVVQLAEAqakidelLREAGDTdekstqLETTIQRLEESLTEKDALLTTERQETEatkkllseaQYKNEEl 1169
Cdd:pfam15921 316 MRQLSDLESTVSQLRSE-------LREAKRM------YEDKIEELEKQLVLANSELTEARTERD---------QFSQES- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1170 lkkiedadksiAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDadrRNNQlqdsLQRLEEN 1249
Cdd:pfam15921 373 -----------GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD---RNME----VQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1250 VGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEdsdrksdSLQSTIKRLEEDGIAKEALLltekQAHEATRMTLTE 1329
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-------STKEMLRKVVEELTAKKMTL----ESSERTVSDLTA 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1330 ALEKNEELLKKIHDDdkhilelqftIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRfvdvDRKIDLLQD 1409
Cdd:pfam15921 504 SLQEKERAIEATNAE----------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEK----DKVIEILRQ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1410 TIER----IGENSTIKDALLLserqEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIikleGDIEAKDISLEAAR 1485
Cdd:pfam15921 570 QIENmtqlVGQHGRTAGAMQV----EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARV----SDLELEKVKLVNAG 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1486 EENdtiRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAisRLSSFVME------KQESDAAKRALTEARERNE 1559
Cdd:pfam15921 642 SER---LRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNF--RNKSEEMEtttnklKMQLKSAQSELEQTRNTLK 716
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1560 DLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATATPPSTAKSSASRSKI 1631
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKM 788
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
996-1606 |
2.83e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.05 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 996 ERNEELSKEVEDADGKIKQLSdtvQRLEETIQEREALLLAERQEKEEASAVIAESQaRNEAFASKLEDAEKQIDLLQETV 1075
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKE---KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1076 QRFEEAITKLQSSVTiEKQQH----EETVVQLAEAQAKIDE---LLREAGDTDEKSTQLETTIQRLEESLTEKDALLtte 1148
Cdd:PRK03918 255 RKLEEKIRELEERIE-ELKKEieelEEKVKELKELKEKAEEyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERI--- 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1149 rQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEEnvtavENSLKAERqhngaimkqladAQVEIGELQRN 1228
Cdd:PRK03918 331 -KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE-----LERLKKRL------------TGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1229 LEDADRRNNQLQDSLQRLEENVGAKESLLlTEREQNASTLK--------------------LLAEAHLEIDELIRKLEDS 1288
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEI-KELKKAIEELKkakgkcpvcgrelteehrkeLLEEYTAELKRIEKELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1289 DRKSDSLQSTIKRLEEDgIAKEALLLTEKqaheatrmTLTEALEKNEELLKKihdddkhilelqFTIQRLEENTAAKENL 1368
Cdd:PRK03918 472 EEKERKLRKELRELEKV-LKKESELIKLK--------ELAEQLKELEEKLKK------------YNLEELEKKAEEYEKL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1369 LLREREqndatTKAQI----ESQERNEQLLKRFVDVDRKIDLLQdtiERIGENSTIKDALLLSERQEKDAIKKELVEAGE 1444
Cdd:PRK03918 531 KEKLIK-----LKGEIkslkKELEKLEELKKKLAELEKKLDELE---EELAELLKELEELGFESVEELEERLKELEPFYN 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1445 RNEELimkiEDTDKKIEHLQNAIIKLEGDieakdisLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRihllqdtaq 1524
Cdd:PRK03918 603 EYLEL----KDAEKELEREEKELKKLEEE-------LDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--------- 662
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1525 klqvdaisRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLE 1604
Cdd:PRK03918 663 --------ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
|
..
gi 1002232322 1605 AE 1606
Cdd:PRK03918 735 AL 736
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
882-1606 |
4.07e-18 |
|
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: 91.78 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 882 DTQALKVAKEK--LEERVEELTNRLGLEKKLRTDLEKSKvaevSKLQAALNEMEQRMQ-DVTAMQERESAKKAVEEALEQ 958
Cdd:pfam01576 144 EDQNSKLSKERklLEERISEFTSNLAEEEEKAKSLSKLK----NKHEAMISDLEERLKkEEKGRQELEKAKRKLEGESTD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 959 EREKISSLTSEIEGLKALLVAEQEEndltkkaHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETI-QEREALLLAER 1037
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEE-------LQAALARLEEETAQKNNALKKIRELEAQISELQEDLeSERAARNKAEK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1038 QEKEEASAViaesqarnEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAK-IDELLRE 1116
Cdd:pfam01576 293 QRRDLGEEL--------EALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaLEELTEQ 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1117 AGDTDEKSTQLETTIQRLEESLTEKDA---LLTTERQETEATKKLLsEAQYknEELLKKIEDADKSIAHYHDTTQRLEEN 1193
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAelrTLQQAKQDSEHKRKKL-EGQL--QELQARLSESERQRAELAEKLSKLQSE 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1194 VTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAE 1273
Cdd:pfam01576 442 LESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLST 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1274 AHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQF 1353
Cdd:pfam01576 522 LQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1354 TIQRLEENTAAKENLLLREREQNDattKAQIESQERNeqllKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKD 1433
Cdd:pfam01576 602 KQKKFDQMLAEEKAISARYAEERD---RAEAEAREKE----TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKD 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1434 AIKKELVEAGERNEELIMKIEDTDKKIEHLQNaiiKLEGDIEAK---DISLEAAREENDtirKSLAEAQEKNEELLRKIS 1510
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELED---ELQATEDAKlrlEVNMQALKAQFE---RDLQARDEQGEEKRRQLV 748
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1511 DN--EYRIHLLQDTAQKLQvdAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKrndDLIKKIEESSKTITQ 1588
Cdd:pfam01576 749 KQvrELEAELEDERKQRAQ--AVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMK---DLQRELEEARASRDE 823
|
730
....*....|....*...
gi 1002232322 1589 LQETLQRLEGKSTNLEAE 1606
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAE 841
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
884-1536 |
1.93e-17 |
|
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: 89.26 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLeervEELTNRLGLEKKLRTDLEKS-KVAEVSKLQAALNEMEQRMQDVTA-----MQERESAKKAVEEALE 957
Cdd:TIGR00618 260 QLLKQLRARI----EELRAQEAVLEETQERINRArKAAPLAAHIKAVTQIEQQAQRIHTelqskMRSRAKLLMKRAAHVK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 958 QErekissltSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADgKIKQLSDTVQRLEETIQEREALLLaer 1037
Cdd:TIGR00618 336 QQ--------SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCKELD--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1038 QEKEEASAVIAESQARNeAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEK-------QQHEETVVQLAEAQaKI 1110
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKihlqesaQSLKEREQQLQTKE-QI 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1111 DELLREAGDTDEKSTQLETTIQR-LEESLTEKDALLtTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQR 1189
Cdd:TIGR00618 482 HLQETRKKAVVLARLLELQEEPCpLCGSCIHPNPAR-QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1190 LEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLL-LTEREQNASTL 1268
Cdd:TIGR00618 561 LKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQdVRLHLQQCSQE 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1269 KLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHI 1348
Cdd:TIGR00618 641 LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREF 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1349 LELQFT----IQRLEENTAAKENLLLREREQNDATTKAQIESQER-NEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDA 1423
Cdd:TIGR00618 721 NEIENAssslGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNnNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1424 LLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQnaiiKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNE 1503
Cdd:TIGR00618 801 LKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS----ATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
650 660 670
....*....|....*....|....*....|....*
gi 1002232322 1504 EL--LRKISdNEYRIHLLQDTAQKLQVDAISRLSS 1536
Cdd:TIGR00618 877 KLngINQIK-IQFDGDALIKFLHEITLYANVRLAN 910
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
999-1616 |
6.14e-17 |
|
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: 87.72 E-value: 6.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 999 EELSKEVEDADGKIKQLSDTV----QRLEETIQEREALLLAERQEKEEASAVI-------AESQARNEAFASKLEDAEKQ 1067
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEelklQELKLKEQAKKALEYYQLKEKLELEEEYllyldylKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1068 IDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTT 1147
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1148 ERQETEATKKLLSEAQYKNEELLKKIEDADKSiahyhdtTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQR 1227
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKL-------QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1228 NLEDADRRNNQLQDSLQRlEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGI 1307
Cdd:pfam02463 406 EAQLLLELARQLEDLLKE-EKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1308 AKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQF---------------TIQRLEENTAAK------E 1366
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRlgdlgvavenykvaiSTAVIVEVSATAdeveerQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1367 NLLLREREQNDATTKAQIESQERNEQLLK-RFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGER 1445
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSiAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1446 NEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQK 1525
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1526 LQVDAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRnEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEA 1605
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE-EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650
....*....|.
gi 1002232322 1606 ENQVLRQQATA 1616
Cdd:pfam02463 804 RALEEELKEEA 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
886-1507 |
6.73e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.43 E-value: 6.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEK--SKVAEVSKLQAALNEMEQRmqdvtaMQERESAKKAVEEALEQEREKI 963
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKleKEVKELEELKEEIEELEKE------LESLEGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 964 SSLTSEIEGLKAlLVAEQEEndLTKKAhanaqERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAlLLAERQEKEEa 1043
Cdd:PRK03918 269 EELKKEIEELEE-KVKELKE--LKEKA-----EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-RIKELEEKEE- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1044 saviaesqaRNEAFASKLEDAEKQIDLLQETVQRFEEAITKLqssVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEK 1123
Cdd:PRK03918 339 ---------RLEELKKKLKELEKRLEELEERHELYEEAKAKK---EELERLKKRLTGLTPEKLEKELEELEKAKEEIEEE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1124 STQLETTIQRLEESLTE-KDAL--LTTERQETEATKKLLSEAQYKN--EELLKKIEDADKSIAHYHDTTQRLEENVTAVE 1198
Cdd:PRK03918 407 ISKITARIGELKKEIKElKKAIeeLKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELE 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1199 NSLKAERQHngaimkqladaqveigelqrnledadRRNNQLQDSLQRLEENVgakESLLLTEREQNAstlkllaeahlei 1278
Cdd:PRK03918 487 KVLKKESEL--------------------------IKLKELAEQLKELEEKL---KKYNLEELEKKA------------- 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1279 deliRKLEDSDRKSDSLQSTIKRLEEDgiakeallLTEKQAHEATRMTLTEALEKNEELLKKIHDD-----DKHILELQF 1353
Cdd:PRK03918 525 ----EEYEKLKEKLIKLKGEIKSLKKE--------LEKLEELKKKLAELEKKLDELEEELAELLKEleelgFESVEELEE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1354 TIQRLEEntAAKENLLLREREQndattkaQIESQERNEQLLKRfvDVDRKIDLLQDTIERIGE-NSTIKDALLLSERQEK 1432
Cdd:PRK03918 593 RLKELEP--FYNEYLELKDAEK-------ELEREEKELKKLEE--ELDKAFEELAETEKRLEElRKELEELEKKYSEEEY 661
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1433 DAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAkdisLEAAREENDTIRKSLAEAQEKNEELLR 1507
Cdd:PRK03918 662 EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEKALERVEELREKVKK 732
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1527 |
1.71e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKsKVAEVSKLQAALNEMEQRMQDVtaMQERESAKKAVEE 954
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE-KLEELKEELESLEAELEELEAE--LEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREKISSLTSEIEGLKA-LLVAEQEENDLtKKAHANAQERNEELSKEVEDADGK--IKQLSDTVQRLEETIQEREA 1031
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNeIERLEARLERL-EDRRERLQQEIEELLKKLEEAELKelQAELEELEEELEELQEELER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1032 LllaeRQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFE-------------------------------- 1079
Cdd:TIGR02168 459 L----EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdeg 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1080 -------------------------EAI---------------------TKLQSSVTIEKQQHEET-------------- 1099
Cdd:TIGR02168 535 yeaaieaalggrlqavvvenlnaakKAIaflkqnelgrvtflpldsikgTEIQGNDREILKNIEGFlgvakdlvkfdpkl 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1100 ------------VVQ-LAEAQAKIDELLREA------------------GDTDEKSTQLETT--IQRLEESLTEkdallt 1146
Cdd:TIGR02168 615 rkalsyllggvlVVDdLDNALELAKKLRPGYrivtldgdlvrpggvitgGSAKTNSSILERRreIEELEEKIEE------ 688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1147 TERQETEATKKLlSEAQYKNEELLKKIEDADKSIahyhdttQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQ 1226
Cdd:TIGR02168 689 LEEKIAELEKAL-AELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1227 RNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELirkledsDRKSDSLQSTIKRLEEDG 1306
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-------NEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1307 IAKEALLLTEKQAHEATRMT---LTEALEKNEELLKKIHDDDKHILELQFTIQR-LEENTAAKENLLLREREQNDATTKA 1382
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDiesLAAEIEELEELIEELESELEALLNERASLEEaLALLRSELEELSEELRELESKRSEL 913
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1383 QIESQERNEQLlkrfVDVDRKIDLLQDTIERIGENstikdallLSERQEkdaikKELVEAGERNEELIMKIEDTDKKIEH 1462
Cdd:TIGR02168 914 RRELEELREKL----AQLELRLEGLEVRIDNLQER--------LSEEYS-----LTLEEAEALENKIEDDEEEARRRLKR 976
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1463 LQNAIIKLeGDIEAKdiSLEAAREEN------DTIRKSLAEAQEKNEELLRKIsDNEYRIhLLQDTAQKLQ 1527
Cdd:TIGR02168 977 LENKIKEL-GPVNLA--AIEEYEELKerydflTAQKEDLTEAKETLEEAIEEI-DREARE-RFKDTFDQVN 1042
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
877-1613 |
2.09e-16 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 86.18 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 877 RMAARDTQALKVAKEKLEERVEELTNRLGLEK-KLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEA 955
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQER-------NEELSKEVEDADGKIKQLSDTVQRLEETIQE 1028
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEElkllakeEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1029 REALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIdllqetvQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQA 1108
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ-------EKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1109 KIDELLREAGDTDEKSTQLETTIQRLEESLTEKDalltterqeteatkkllseaqyknEELLKKIEDADKsiahyHDTTQ 1188
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL------------------------EEEEESIELKQG-----KLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1189 RLEENV-TAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEEN------------------ 1249
Cdd:pfam02463 450 KEELEKqELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVllalikdgvggriisahg 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1250 ------------------------------VGAKESLLLTEREQNASTLKLLAE-----------AHLEIDELIRKLEDS 1288
Cdd:pfam02463 530 rlgdlgvavenykvaistavivevsatadeVEERQKLVRALTELPLGARKLRLLipklklplksiAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1289 DRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKhILELQFTIQRLEENTAAKENL 1368
Cdd:pfam02463 610 KATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKAS-LSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1369 LLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEE 1448
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1449 LIMKIEDTDKKIEHlqnaIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQV 1528
Cdd:pfam02463 769 LSLKEKELAEEREK----TEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1529 DAISRLSSFvmEKQESDAAKRALTEarERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQ 1608
Cdd:pfam02463 845 EQKLEKLAE--EELERLEEEITKEE--LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIE 920
|
....*
gi 1002232322 1609 VLRQQ 1613
Cdd:pfam02463 921 ERIKE 925
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
878-1609 |
2.35e-16 |
|
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: 86.00 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 878 MAARDTQaLKVAKEKLEERVEELTNrlgLEKKlRTDLEKSKVAEVSKLQAA---LNEMEQ-RMQDVTAMQERESAKKAVE 953
Cdd:pfam01576 7 MQAKEEE-LQKVKERQQKAESELKE---LEKK-HQQLCEEKNALQEQLQAEtelCAEAEEmRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EALEQEREKISSLTSEieglkallvaeqeendlTKKAHANAQERNEELSKEvEDA-----------DGKIKQLSDTVQRL 1022
Cdd:pfam01576 82 SRLEEEEERSQQLQNE-----------------KKKMQQHIQDLEEQLDEE-EAArqklqlekvttEAKIKKLEEDILLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1023 EETIQE--REALLLAER--------QEKEEASAVIAESQARNEAFASKLED----AEKQIDLLQETVQRFEEAITKLQSS 1088
Cdd:pfam01576 144 EDQNSKlsKERKLLEERiseftsnlAEEEEKAKSLSKLKNKHEAMISDLEErlkkEEKGRQELEKAKRKLEGESTDLQEQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1089 VTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQ---ETEATKKLLSEaqyK 1165
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnKAEKQRRDLGE---E 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1166 NEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAE-RQHNGAI--MKQLADAQVEigELQRNLEDADRRNNQLQDS 1242
Cdd:pfam01576 301 LEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEEtRSHEAQLqeMRQKHTQALE--ELTEQLEQAKRNKANLEKA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1243 LQRLEENVG--AKESLLLTEREQNASTLKLLAEAHLEidELIRKLEDSDRKSDSLQSTIKRLEEDgiakeallltekqaH 1320
Cdd:pfam01576 379 KQALESENAelQAELRTLQQAKQDSEHKRKKLEGQLQ--ELQARLSESERQRAELAEKLSKLQSE--------------L 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1321 EATRMTLTEALEKNEELLKKIHDDDKHileLQFTIQRLEENTAAKENL--LLREREQNDATTKAQIESQERNEQLLKRFV 1398
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQ---LQDTQELLQEETRQKLNLstRLRQLEDERNSLQEQLEEEEEAKRNVERQL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1399 DVDRKidLLQDTIERIGENSTIKDALllseRQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQnaiikleGDIEAKD 1478
Cdd:pfam01576 520 STLQA--QLSDMKKKLEEDAGTLEAL----EEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQ-------QELDDLL 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1479 ISLEAAREendtIRKSLAEAQEKNEELLRkisdnEYRIHLLQDTAQKLQVDAISRlssfvmEKQ-ESDAAKRALTEARER 1557
Cdd:pfam01576 587 VDLDHQRQ----LVSNLEKKQKKFDQMLA-----EEKAISARYAEERDRAEAEAR------EKEtRALSLARALEEALEA 651
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1558 NEDLLKRN-------EDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQV 1609
Cdd:pfam01576 652 KEELERTNkqlraemEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQA 710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
945-1614 |
2.76e-16 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 85.07 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 945 RESAKKAVEEALEQEREKISSLTSEIEGLkallvaEQEENDLTKKAHANAQ---ERNEELSKEVEDADGKIKQLS---DT 1018
Cdd:TIGR04523 52 KEKELKNLDKNLNKDEEKINNSNNKIKIL------EQQIKDLNDKLKKNKDkinKLNSDLSKINSEIKNDKEQKNkleVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1019 VQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSsvtiEKQQHEE 1098
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN----KLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1099 TVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADK 1178
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1179 SIAHYHDTTQRLEENVTAVENslKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLL 1258
Cdd:TIGR04523 282 KIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1259 TEREQnastlklLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEdgiakeallltekqaheatrmTLTEALEKNEELL 1338
Cdd:TIGR04523 360 EKQRE-------LEEKQNEIEKLKKENQSYKQEIKNLESQINDLES---------------------KIQNQEKLNQQKD 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1339 KKIHDDDKHILELQFTIQRLEEnTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDV-DRKIDLLQDTIERIGEN 1417
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKE-TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVlSRSINKIKQNLEQKQKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1418 STIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEaareeNDTIRKSLAE 1497
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK-----KENLEKEIDE 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1498 AQEKNEELlrkisdneyrihllqdtaqklqvdaisrlssfvmeKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIK 1577
Cdd:TIGR04523 566 KNKEIEEL-----------------------------------KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 1002232322 1578 KIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQA 1614
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1295-1628 |
6.07e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 84.22 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1295 LQSTIKRLEED-GIAKEALLLTEkqahEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLRER 1373
Cdd:COG1196 198 LERQLEPLERQaEKAERYRELKE----ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1374 EQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKI 1453
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1454 EDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAISr 1533
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1534 lssfvmEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQ 1613
Cdd:COG1196 433 ------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330
....*....|....*
gi 1002232322 1614 ATATPPSTAKSSASR 1628
Cdd:COG1196 507 LEGVKAALLLAGLRG 521
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
920-1525 |
7.41e-16 |
|
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: 83.72 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 920 AEVSKLQAALNEMEQRMQDVTAMQER------ESAK-KAVEEALEQEREKISSLTSEIEGLkallvaEQEENDLTKKAHA 992
Cdd:pfam10174 192 MQLGHLEVLLDQKEKENIHLREELHRrnqlqpDPAKtKALQTVIEMKDTKISSLERNIRDL------EDEVQMLKTNGLL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 993 NAQERNEELsKEVEDADGKIKQLSDTVQRLEETIQEREALLLAerqekeeasaviaeSQARNEAFASKLEDAEKQIDLLQ 1072
Cdd:pfam10174 266 HTEDREEEI-KQMEVYKSHSKFMKNKIDQLKQELSKKESELLA--------------LQTKLETLTNQNSDCKQHIEVLK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1073 ETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELlreagdTDEKSTqLETTIQRLeeslteKDALLTTERQET 1152
Cdd:pfam10174 331 ESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDL------TEEKST-LAGEIRDL------KDMLDVKERKIN 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1153 EATKKLlseaqyknEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLkaerqhnGAIMKQLADAQVEIGEL--QRNLE 1230
Cdd:pfam10174 398 VLQKKI--------ENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL-------TTLEEALSEKERIIERLkeQRERE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1231 DADRRN--NQLQDSLQRLEENVGAKESlLLTEREQNASTLKLLAEAhleideLIRKLEDSDRKSDSLQSTIKRLEEDGIA 1308
Cdd:pfam10174 463 DRERLEelESLKKENKDLKEKVSALQP-ELTEKESSLIDLKEHASS------LASSGLKKDSKLKSLEIAVEQKKEECSK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1309 KEALLLTEKQAHEATRMtltealekNEELLKKIhdddkHILELQFTIQRLEENTAAKE--NLL--LREREqndattkaqi 1384
Cdd:pfam10174 536 LENQLKKAHNAEEAVRT--------NPEINDRI-----RLLEQEVARYKEESGKAQAEveRLLgiLREVE---------- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1385 esqerNEQLLKrfvdvDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERN-------------EELIM 1451
Cdd:pfam10174 593 -----NEKNDK-----DKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRRednladnsqqlqlEELMG 662
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1452 KIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENdtiRKSLAEAQE-KNEELLRKISDNEYRIHLLQDTAQK 1525
Cdd:pfam10174 663 ALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAER---RKQLEEILEmKQEALLAAISEKDANIALLELSSSK 734
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
884-1608 |
4.08e-15 |
|
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: 82.02 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEELTNRLGLEKKLRtDLEKSKVAEVSKLQAALNEMEQRM-------QDVTAMQERESAKKAVEEAL 956
Cdd:TIGR00606 210 KYLKQYKEKACEIRDQITSKEAQLESSR-EIVKSYENELDPLKNRLKEIEHNLskimkldNEIKALKSRKKQMEKDNSEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 957 EQEREKISSLTSE----IEGLKALLVAEQEEN--DLTKKAHANAQERnEELSKEVEDADGKIKQLSDTVQRLEETIQERE 1030
Cdd:TIGR00606 289 ELKMEKVFQGTDEqlndLYHNHQRTVREKERElvDCQRELEKLNKER-RLLNQEKTELLVEQGRLQLQADRHQEHIRARD 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLA----------------ERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQ 1094
Cdd:TIGR00606 368 SLIQSlatrleldgfergpfsERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1095 QHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLeeSLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIE 1174
Cdd:TIGR00606 448 ILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL--SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1175 DADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEiGELQRNLEDADRRNNQLQDSLQRLEENVGAKE 1254
Cdd:TIGR00606 526 QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1255 slllTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDgiAKEALLLTEKQAheATRMTLTEALEKN 1334
Cdd:TIGR00606 605 ----QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKS--SKQRAMLAGATA--VYSQFITQLTDEN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1335 EELLKKIHDDDKHILELQFTIQRLEENT--------AAKENLLLREREQNDATTKAQIESQERnEQLLKRFVDVDRKIDL 1406
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEFISDLQSKLrlapdklkSTESELKKKEKRRDEMLGLAPGRQSII-DLKEKEIPELRNKLQK 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1407 LQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERnEELIMKIEDTDKKIEHLQNAIIKLEGD---------IEAK 1477
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDVERKIAQQAAKLQGSDLDrtvqqvnqeKQEK 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1478 DISLEAAREENDTIRKSLAEAQEKNEELLRKIsdNEYRIHLLQDTAQKLQVDAISRLSsfVMEKQESDAAKRALTEARER 1557
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKT--NELKSEKLQIGTNLQRRQQFEEQL--VELSTEVQSLIREIKDAKEQ 910
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1558 NEDLLKRNEDLLKRNDDLIKKIEESSKT----ITQLQETLQRLEGKSTNLEAENQ 1608
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKETSNKKaqdkVNDIKEKVKNIHGYMKDIENKIQ 965
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
894-1512 |
1.57e-14 |
|
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: 79.77 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 894 EERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLtseiegl 973
Cdd:pfam05483 201 ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL------- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 974 kallvaeQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEeasaviaesqar 1053
Cdd:pfam05483 274 -------EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE------------ 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1054 neafaSKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLA----EAQAKIDELLREAGDTDEKSTQLEt 1129
Cdd:pfam05483 335 -----AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiitmELQKKSSELEEMTKFKNNKEVELE- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1130 tiqRLEESLTEKDALLTTERQeteaTKKLLSEAQYKNEELLKKIEDADKSIahyHDttqrLEENVTAVENSLKAERQHNG 1209
Cdd:pfam05483 409 ---ELKKILAEDEKLLDEKKQ----FEKIAEELKGKEQELIFLLQAREKEI---HD----LEIQLTAIKTSEEHYLKEVE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1210 AIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLK---LLAEAHLEI-DELIRKL 1285
Cdd:pfam05483 475 DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKqieNLEEKEMNLrDELESVR 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1286 EDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRmtltealEKNEELLKKIHDDDKHILELQftiqrlEENTAAK 1365
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE-------NKCNNLKKQIENKNKNIEELH------QENKALK 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1366 ENLLLREREQNDATTKAQiesqerneQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELV----E 1441
Cdd:pfam05483 622 KKGSAENKQLNAYEIKVN--------KLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVklqkE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1442 AGERNEELIMKIEDTDKKIEHLQNAIIKlEGDIE----------------AKDISLEAAREENDTIRKSLAEAQEKNEEL 1505
Cdd:pfam05483 694 IDKRCQHKIAEMVALMEKHKHQYDKIIE-ERDSElglyknkeqeqssakaALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
....*..
gi 1002232322 1506 LRKISDN 1512
Cdd:pfam05483 773 KMEAKEN 779
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
897-1510 |
1.74e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.83 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 897 VEELTNRLGLEKKLRTDLEKSKVA---EVSKLQAALNEMEQRMQDV--------TAMQERESAKKAVEEALEQEREKISS 965
Cdd:pfam01576 358 LEELTEQLEQAKRNKANLEKAKQAlesENAELQAELRTLQQAKQDSehkrkkleGQLQELQARLSESERQRAELAEKLSK 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 966 LTSEIEGLKALL-VAEQEENDLTKKAHA------NAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQERE-------- 1030
Cdd:pfam01576 438 LQSELESVSSLLnEAEGKNIKLSKDVSSlesqlqDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEeakrnver 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 -------ALLLAERQEKEEASAVIAESQARNEaFASKLEDAEKQIDLLQETVQRFEEAITKLQSS---VTIEKQQHEETV 1100
Cdd:pfam01576 518 qlstlqaQLSDMKKKLEEDAGTLEALEEGKKR-LQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddLLVDLDHQRQLV 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQLAEAQAKIDELL---------------REAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQ--------------- 1150
Cdd:pfam01576 597 SNLEKKQKKFDQMLaeekaisaryaeerdRAEAEAREKETRALSLARALEEALEAKEELERTNKQlraemedlvsskddv 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1151 -----ETEATKKLLsEAQYknEELLKKIEDADKSIAHYHDTTQRLEENVTAV----ENSLKAERQHNGAIMKQLADaqvE 1221
Cdd:pfam01576 677 gknvhELERSKRAL-EQQV--EEMKTQLEELEDELQATEDAKLRLEVNMQALkaqfERDLQARDEQGEEKRRQLVK---Q 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1222 IGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLED-------------- 1287
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqske 830
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1288 SDRKSDSLQSTIKRLEEDGIAKEALlltEKQAhEATRMTLTEALeKNEELLKKIHDDDKHILELQFTiQRLEENTAAKEN 1367
Cdd:pfam01576 831 SEKKLKNLEAELLQLQEDLAASERA---RRQA-QQERDELADEI-ASGASGKSALQDEKRRLEARIA-QLEEELEEEQSN 904
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1368 L-LLRER--------EQNDATTKAQIESQERNE----QLLKRFVDVDRKIDLLQDTIeRIGENSTIKdAL---------- 1424
Cdd:pfam01576 905 TeLLNDRlrkstlqvEQLTTELAAERSTSQKSEsarqQLERQNKELKAKLQEMEGTV-KSKFKSSIA-ALeakiaqleeq 982
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1425 LLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREEND-------TIRKSLAE 1497
Cdd:pfam01576 983 LEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASranaarrKLQRELDD 1062
|
730
....*....|...
gi 1002232322 1498 AQEKNEELLRKIS 1510
Cdd:pfam01576 1063 ATESNESMNREVS 1075
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1395 |
1.98e-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: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1036 ERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQssvtIEKQQHEETVVQLAEAQ-AKIDELL 1114
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR----REREKAERYQALLKEKReYEGYELL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1115 REAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAqykNEELLKKIEDADKSI-AHYHDTTQRLEEN 1193
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVkEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1194 VTAVEnsLKAERQHNGAimKQLADAQVEIGELQRNLEDADR-------RNNQLQDSLQRLEENVGAKESLLLTEREQNAS 1266
Cdd:TIGR02169 307 ERSIA--EKERELEDAE--ERLAKLEAEIDKLLAEIEELEReieeerkRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1267 TLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGI---AKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHD 1343
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAdlnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1344 D----DKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQeRNEQLLK 1395
Cdd:TIGR02169 463 DlskyEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR-AVEEVLK 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
945-1341 |
5.85e-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: 78.19 E-value: 5.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 945 RESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEE 1024
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1025 TIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKqiDLLQETVQRFEEAITKLqssvtieKQQHEETVVQLA 1104
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKL-------EEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1105 EAQAKIDELLREagdtdekSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLseaqyknEELLKKIEDADKSIAHYH 1184
Cdd:TIGR02169 816 EIEQKLNRLTLE-------KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK-------EELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1185 DTTQRLEENVTAVEnslkaerqhngaimKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQN 1264
Cdd:TIGR02169 882 SRLGDLKKERDELE--------------AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1265 ASTLKL--LAEAHLEIDELIRKLEDSDRKS-DSLQSTIKRLEEdgiakeallLTEKQAH-EATRMTLTEALEKNEELLKK 1340
Cdd:TIGR02169 948 EEELSLedVQAELQRVEEEIRALEPVNMLAiQEYEEVLKRLDE---------LKEKRAKlEEERKAILERIEEYEKKKRE 1018
|
.
gi 1002232322 1341 I 1341
Cdd:TIGR02169 1019 V 1019
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
888-1208 |
1.25e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 888 VAKEKLEERVEELTNRL----GLEKKLRTDLE--KSKVAEVSKLQAALN--EMEQRMQD---VTAMQERESAKKAVEEAL 956
Cdd:PRK02224 405 VDLGNAEDFLEELREERdelrEREAELEATLRtaRERVEEAEALLEAGKcpECGQPVEGsphVETIEEDRERVEELEAEL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 957 EQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHaNAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAE 1036
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIERLEERRE-DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEA 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1037 RQEKEEASAVIAESQARNEAFASK---LEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEetvvQLAEAQAKIDEl 1113
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKREALAELNDERRE----RLAEKRERKRE- 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 LREAGDTD------EKSTQLETTIQRLEESLTEKdalltterqeTEATKKLLSEAQYKNEEL--LKKIEDADKSIAHYHD 1185
Cdd:PRK02224 639 LEAEFDEArieearEDKERAEEYLEQVEEKLDEL----------REERDDLQAEIGAVENELeeLEELRERREALENRVE 708
|
330 340
....*....|....*....|....*..
gi 1002232322 1186 TTQRLEENVTAVENS---LKAE-RQHN 1208
Cdd:PRK02224 709 ALEALYDEAEELESMygdLRAElRQRN 735
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1217-1616 |
1.63e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1217 DAQVEIGELQRnledaDRRNnqlqdSLQRLEENVGAKESLLLTEREQNASTLklLAEAHLEIDELIRKLEDSDRKSDSLQ 1296
Cdd:PRK02224 173 DARLGVERVLS-----DQRG-----SLDQLKAQIEEKEEKDLHERLNGLESE--LAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1297 STIKRLEEdgiaKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELqftiqrLEENTAAKENLLLREREQn 1376
Cdd:PRK02224 241 EVLEEHEE----RREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL------EEERDDLLAEAGLDDADA- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1377 DATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDT 1456
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1457 DKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEyriHLL---------QDTAQKLQ 1527
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE---ALLeagkcpecgQPVEGSPH 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1528 VDAIS----RLSSFVMEKQESDAAKRALTEARERNEDLLK---RNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKS 1600
Cdd:PRK02224 467 VETIEedreRVEELEAELEDLEEEVEEVEERLERAEDLVEaedRIERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
410
....*....|....*.
gi 1002232322 1601 TNLEAENQVLRQQATA 1616
Cdd:PRK02224 547 AELEAEAEEKREAAAE 562
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1277-1628 |
3.04e-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: 75.49 E-value: 3.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1277 EIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEAL--LLTEKQAHEATRMTLT-EALEKN-EELLKKIHDDDKHILELQ 1352
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqaLLKEKREYEGYELLKEkEALERQkEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1353 FTIQRLEENTAAKENLLlrereqNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIErigenstikdallLSERQEK 1432
Cdd:TIGR02169 258 EEISELEKRLEEIEQLL------EELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA-------------EKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1433 DAiKKELVEAGERNEELIMKIEDTDKKIEH-------LQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEEL 1505
Cdd:TIGR02169 319 DA-EERLAKLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1506 LRKISDNEYRIHLLQDTAQKLQVDaISRLssfvmeKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKT 1585
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEE-LADL------NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1002232322 1586 ITQLQETLQRLEGKSTNLEAENQVLRQQATATPPSTAKSSASR 1628
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVE 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1055-1683 |
3.25e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.54 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKLEDAEKQIDLLQETVQRFEEAITKL-----QSSVTIEKQQHEetvVQLaEAQAKIDELLREAGDTDEKSTQLET 1129
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQkfylrQSVIDLQTKLQE---MQM-ERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1130 TIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEEL---LKKIEDADKSIAHYHDTTQR----------------- 1189
Cdd:pfam15921 150 TVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIrsiLVDFEEASGKKIYEHDSMSTmhfrslgsaiskilrel 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1190 ------LEENVTAVEN---SLKAE---------RQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVg 1251
Cdd:pfam15921 230 dteisyLKGRIFPVEDqleALKSEsqnkielllQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1252 akeslllteREQNASTLKLLAEAHLEIDELIRKLEDSDRksdSLQSTIKRLEEDGIAKEALLL---TEKQAHEATRMTLT 1328
Cdd:pfam15921 309 ---------RNQNSMYMRQLSDLESTVSQLRSELREAKR---MYEDKIEELEKQLVLANSELTearTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1329 EALEKneeLLKKIHDDDKHI-LELQFTIQRLEENTAAKENLLLREREQNDATTKAQiesqeRNEQLLKRFVD-----VDR 1402
Cdd:pfam15921 377 DQLQK---LLADLHKREKELsLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ-----RLEALLKAMKSecqgqMER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1403 KIDLLQDTIERIGENSTIKDAL-----LLSERQEKDAIKKELVEAGERN-EELIMKIEDTDKKIEHLQNAIIKLEGDIEA 1476
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLTAQLestkeMLRKVVEELTAKKMTLESSERTvSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1477 KDISLEAAREENDTIRKSLAEAQ-------EKNE--ELLRKISDNEYRI---HllQDTAQKLQV----------DAISRL 1534
Cdd:pfam15921 529 KLQELQHLKNEGDHLRNVQTECEalklqmaEKDKviEILRQQIENMTQLvgqH--GRTAGAMQVekaqlekeinDRRLEL 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1535 SSFVMEKQESDAAKRALtEARERNEDL------------LKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLE----G 1598
Cdd:pfam15921 607 QEFKILKDKKDAKIREL-EARVSDLELekvklvnagserLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKrnfrN 685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1599 KSTNLEAENQVLRQQAtatppSTAKSSASRSKITRIHRSPENGHILN-GDTRQAEIKPSTGTSETIPSI-----GNPPDL 1672
Cdd:pfam15921 686 KSEEMETTTNKLKMQL-----KSAQSELEQTRNTLKSMEGSDGHAMKvAMGMQKQITAKRGQIDALQSKiqfleEAMTNA 760
|
730
....*....|.
gi 1002232322 1673 NNEKHVEQGEK 1683
Cdd:pfam15921 761 NKEKHFLKEEK 771
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
891-1343 |
3.46e-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: 75.06 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEKS---KVAEVSKLQAALNEMEQRMQDVTamQERESAKKAVEEA---LEQEREKIS 964
Cdd:TIGR04523 207 KKKIQKNKSLESQISELKKQNNQLKDNiekKQQEINEKTTEISNTQTQLNQLK--DEQNKIKKQLSEKqkeLEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 965 SLTSEIEGLKALLVA--EQEENDLTKKAH---ANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQE 1039
Cdd:TIGR04523 285 ELEKQLNQLKSEISDlnNQKEQDWNKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1040 KEEASAVIAESQARNEAFASKLEDAEKQIDLL-------QETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDE 1112
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1113 LLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKK-------LLSEAQYKNEELLKKIEDADKSIAHYHD 1185
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKelkskekELKKLNEEKKELEEKVKDLTKKISSLKE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1186 TTQRLEENVTAVENSLKA---------ERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENvgakesl 1256
Cdd:TIGR04523 525 KIEKLESEKKEKESKISDledelnkddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKE------- 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1257 lltereqNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEdgiAKEALLLTEKQAHEA---TRMTLTEALEK 1333
Cdd:TIGR04523 598 -------KKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS---KKNKLKQEVKQIKETikeIRNKWPEIIKK 667
|
490
....*....|
gi 1002232322 1334 NEELLKKIHD 1343
Cdd:TIGR04523 668 IKESKTKIDD 677
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
890-1690 |
7.71e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.38 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEELTNRLGLEKKLRTDLEKSkvaeVSKLQAALNEMEQRMQDVTAMQERES--AKKAVEEAlEQEREKIS--- 964
Cdd:pfam15921 298 QSQLEIIQEQARNQNSMYMRQLSDLEST----VSQLRSELREAKRMYEDKIEELEKQLvlANSELTEA-RTERDQFSqes 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 965 -SLTSEIEGLKALLVAEQEENDLTKKAHANAQERN-------EELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAE 1036
Cdd:pfam15921 373 gNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDtgnsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1037 RQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLRE 1116
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1117 AGDTDEKSTQL---ETTIQRLEESLTEKDALLTTERQETEATKKLLSE-------AQYKNEELLKKIEDadksiahyhdt 1186
Cdd:pfam15921 533 LQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEIND----------- 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1187 tQRLEenvtavensLKAERqhngaIMKQLADAQVEigELQRNLEDADRRNNQLQDS-LQRLE--ENVGAKESLLLTEREQ 1263
Cdd:pfam15921 602 -RRLE---------LQEFK-----ILKDKKDAKIR--ELEARVSDLELEKVKLVNAgSERLRavKDIKQERDQLLNEVKT 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1264 NASTLKLLAEahlEIDELIRKLEDsdrKSDSLQSTIKRLEEDgiakealLLTEKQAHEATRMTLT-------EALEKNEE 1336
Cdd:pfam15921 665 SRNELNSLSE---DYEVLKRNFRN---KSEEMETTTNKLKMQ-------LKSAQSELEQTRNTLKsmegsdgHAMKVAMG 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1337 LLKKIHDDDKHILELQFTIQRLEE--NTAAKENLLLRErEQNDATTKAQIESQERNEQL--LKRFVDVDRKIDllqdtiE 1412
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEamTNANKEKHFLKE-EKNKLSQELSTVATEKNKMAgeLEVLRSQERRLK------E 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1413 RIGENSTIKDALLLSERQEKDAIKKelveagERNEELIMKIEDTdKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIR 1492
Cdd:pfam15921 805 KVANMEVALDKASLQFAECQDIIQR------QEQESVRLKLQHT-LDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVP 877
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1493 KSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvDAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRNE---DLL 1569
Cdd:pfam15921 878 SSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELR-SVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSlrsDIC 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1570 KRNDDLIK-KIEESSKTITQLQETLQRLEgkstnLEAENQVLRQQATATPpsTAKSSASRSKITRIHRSPENGHILNGDT 1648
Cdd:pfam15921 957 HSSSNSLQtEGSKSSETCSREPVLLHAGE-----LEDPSSCFTFPSTASP--SVKNSASRSFHSSPKKSPVHSLLTSSAE 1029
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 1002232322 1649 RQAEIKPSTGTSETIPSIGNPPDLNNEKHVEQGEKLQKVLNQ 1690
Cdd:pfam15921 1030 GSIGSSSQYRSAKTIHSPDSVKDSQSLPIETTGKTCRKLQNR 1071
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1012-1595 |
9.62e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1012 IKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTI 1091
Cdd:COG4913 234 FDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1092 EKQQHEETVVQLAEAQAKIdellREAGDTDEKstQLETTIQRLEESLTEKDALLttERQEtEATKKLLSEAQYKNEELLK 1171
Cdd:COG4913 314 LEARLDALREELDELEAQI----RGNGGDRLE--QLEREIERLERELEERERRR--ARLE-ALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1172 KIEDADKSIAHYHDTTQRLEENVTAVENSLKAERqhngaimKQLADAQVEIGELQRnledadRRNN---QLQDSLQRLEE 1248
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLR-------RELRELEAEIASLER------RKSNipaRLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1249 NVGAKES-------LL-LTEREQ------------NASTL----KLLAEA-----------HLEIDELIRKLEDSDRKSD 1293
Cdd:COG4913 452 ALGLDEAelpfvgeLIeVRPEEErwrgaiervlggFALTLlvppEHYAAAlrwvnrlhlrgRLVYERVRTGLPDPERPRL 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1294 SLQSTIKRLE-EDGIAKEAL--LLTEKQAH-----------EATRMTLTEALEKNEELLKKihDDDKHILE---LQFT-- 1354
Cdd:COG4913 532 DPDSLAGKLDfKPHPFRAWLeaELGRRFDYvcvdspeelrrHPRAITRAGQVKGNGTRHEK--DDRRRIRSryvLGFDnr 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1355 --IQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLK----RFVDVD-----RKIDLLQDTIERIGENSTIKDA 1423
Cdd:COG4913 610 akLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeySWDEIDvasaeREIAELEAELERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1424 LllseRQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAkdisleAAREENDTIRKSLAE--AQEK 1501
Cdd:COG4913 690 L----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEErfAAAL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1502 NEELLRKISDN-EYRIHLLQDTAQKLQVDAISRLSSFV----MEKQESDAAKRALTEARERNEDLlkRNEDLLKRNDDLI 1576
Cdd:COG4913 760 GDAVERELRENlEERIDALRARLNRAEEELERAMRAFNrewpAETADLDADLESLPEYLALLDRL--EEDGLPEYEERFK 837
|
650 660
....*....|....*....|
gi 1002232322 1577 KKIEESSKT-ITQLQETLQR 1595
Cdd:COG4913 838 ELLNENSIEfVADLLSKLRR 857
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1103-1571 |
9.90e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 9.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1103 LAEAQAKIDELLREAGDTDEK-STQLETTIQRLEEsLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIA 1181
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELnLKELKELEEELKE-AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEenvtavensLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTER 1261
Cdd:COG4717 127 LLPLYQELEA---------LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQNASTL-KLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKK 1340
Cdd:COG4717 198 AEELEELqQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1341 IHdddkhILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGE---- 1416
Cdd:COG4717 278 VL-----FLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEElqel 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1417 ----NSTIKDALLLSERQEKDAI--------KKELVEAGERNEELimkiEDTDKKIEHLQNAIIKLEGDIEA--KDISLE 1482
Cdd:COG4717 353 lreaEELEEELQLEELEQEIAALlaeagvedEEELRAALEQAEEY----QELKEELEELEEQLEELLGELEEllEALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1483 AAREENDTIRKSLAEAQEKNEELLRKISDNEYRIH------LLQDTAQKLQvDAISRLSSFVMEKQESDAAKRALTEARE 1556
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEqleedgELAELLQELE-ELKAELRELAEEWAALKLALELLEEARE 507
|
490 500
....*....|....*....|
gi 1002232322 1557 RNED-----LLKRNEDLLKR 1571
Cdd:COG4717 508 EYREerlppVLERASEYFSR 527
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
886-1515 |
1.28e-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: 73.47 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQrmqdvtAMQERESAKKAVEEALEQEREKISS 965
Cdd:pfam02463 347 LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE------ELELKSEEEKEAQLLLELARQLEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 966 LTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEAS- 1044
Cdd:pfam02463 421 LKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSq 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1045 ------------------------------------AVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSS 1088
Cdd:pfam02463 501 keskarsglkvllalikdgvggriisahgrlgdlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKL 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1089 VTIEKQ--------QHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLS 1160
Cdd:pfam02463 581 RLLIPKlklplksiAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1161 EAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIgeLQRNLEDADRRNNQLQ 1240
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL--LADRVQEAQDKINEEL 738
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1241 DSLQRLEENVGAKESLLLTEREQNASTLKLLaeahleidELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAH 1320
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSEL--------SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1321 EAtrmtltEALEKNEELLKKIHDDDKHILELQFTIQRL-EENTAAKENLLLREREQNDATTKAQIESQERNEQLLKrfvd 1399
Cdd:pfam02463 811 KE------EAELLEEEQLLIEQEEKIKEEELEELALELkEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELE---- 880
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1400 vdrKIDLLQDTIERIGENSTIKDALLLSERQEkdaikkELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDI 1479
Cdd:pfam02463 881 ---EQKLKDELESKEEKEKEEKKELEEESQKL------NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
650 660 670
....*....|....*....|....*....|....*...
gi 1002232322 1480 --SLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYR 1515
Cdd:pfam02463 952 enNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1104-1505 |
1.49e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.56 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1104 AEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEkdalLTTERQETEATKKLLSEAQ-YKNEELLKKIEDADKSIAh 1182
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLER----LRREREKAERYQALLKEKReYEGYELLKEKEALERQKE- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1183 yhdttqrleenvtavenslkaerqhngAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAkesllLTERE 1262
Cdd:TIGR02169 241 ---------------------------AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----LGEEE 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1263 QNASTLKlLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDgiakeallltekqaheatrmtLTEALEKNEELLKKIH 1342
Cdd:TIGR02169 289 QLRVKEK-IGELEAEIASLERSIAEKERELEDAEERLAKLEAE---------------------IDKLLAEIEELEREIE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1343 DDDKHILELQFTIQRLEEntaaKENLLLREREQNDATTKaqiESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKD 1422
Cdd:TIGR02169 347 EERKRRDKLTEEYAELKE----ELEDLRAELEEVDKEFA---ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1423 ALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKdisleaaREENDTIRKSLAEAQEKN 1502
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQREL 492
|
...
gi 1002232322 1503 EEL 1505
Cdd:TIGR02169 493 AEA 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
875-1305 |
2.10e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLgleKKLRTDLEksKVAEVSKLQAALNEMEQRMQDVTAMQER-ESAKKAVE 953
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAEL---EELREELE--KLEKLLQLLPLYQELEALEAELAELPERlEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EaLEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHAN-AQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAL 1032
Cdd:COG4717 157 E-LRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1033 LLAERQEKE--------EASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLA 1104
Cdd:COG4717 236 LEAAALEERlkearlllLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1105 EAQAKIDELLREAG----DTDEKSTQLETTIQRLEESLTEKDAL---LTTERQETEAtKKLLSEAQYKNEE-LLKKIEDA 1176
Cdd:COG4717 316 LEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELeeeLQLEELEQEI-AALLAEAGVEDEEeLRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1177 DKsiahYHDTTQRLEENVTAVENSLKAERQHNGAImkQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEenvgAKESL 1256
Cdd:COG4717 395 EE----YQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELEEELEELREELAELE----AELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1257 LLTEREqnastlklLAEAHLEIDELIRKLEDSDRK-------SDSLQSTIKRLEED 1305
Cdd:COG4717 465 LEEDGE--------LAELLQELEELKAELRELAEEwaalklaLELLEEAREEYREE 512
|
|
| Myo5_CBD |
cd15470 |
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, ... |
1891-2062 |
2.50e-12 |
|
Cargo binding domain of myosin 5; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. The MyoV-CBDs directly interact with several adaptor proteins, in case of Myo5a, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin, and in case of Myo5b, Rab11-family interacting protein 2.
Pssm-ID: 271254 [Multi-domain] Cd Length: 332 Bit Score: 70.32 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1891 QKNQLGHWLAIVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHWSdNA 1970
Cdd:cd15470 136 EEILQPTLDSLLQQLNSFHTTLTQHGLDPELIKQVFRQLFYLICASTLNNLLLRKDLCSWSKGMQIRYNVSQLEEWL-RD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1971 TREFAGSAWDALKHIRQAVDFLVISLKPMRTLKEIrTDVCPALSIQQLERIVSMYWDDINGSNAISAEFTSSLKSAVREE 2050
Cdd:cd15470 215 KGLQDSGARETLEPLIQAAQLLQVKKTTEEDAQSI-CEMCTKLTTAQIVKILNLYTPVDDFEERVTPSFIRKVQARLNER 293
|
170
....*....|..
gi 1002232322 2051 SNTvTTFSILLD 2062
Cdd:cd15470 294 ADS-NQLQLLMD 304
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1032-1515 |
6.50e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1032 LLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQssvtiEKQQHEETVVQLAEAQAKID 1111
Cdd:COG4717 68 LNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1112 EL---LREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQET-EATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTT 1187
Cdd:COG4717 143 ELperLEELEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1188 QRLEENVTAVENSL----KAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQ 1263
Cdd:COG4717 223 EELEEELEQLENELeaaaLEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1264 NASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEAtRMTLTEALEKNEELLKKIHD 1343
Cdd:COG4717 303 EAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-ELQLEELEQEIAALLAEAGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1344 DDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERnEQLLKRFVDVDRKIDLLQDTIERigenstikda 1423
Cdd:COG4717 382 EDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEE---------- 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1424 lLLSERQEKDAIKKELvEAGERNEELIMKIEDTDKKIEHL--QNAIIKLEGDIeakdisLEAAREEndTIRKSLAEAQEK 1501
Cdd:COG4717 451 -LREELAELEAELEQL-EEDGELAELLQELEELKAELRELaeEWAALKLALEL------LEEAREE--YREERLPPVLER 520
|
490
....*....|....
gi 1002232322 1502 NEELLRKISDNEYR 1515
Cdd:COG4717 521 ASEYFSRLTDGRYR 534
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
875-1129 |
7.53e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEK---SKVAEVSKLQAALNEMEQR------------MQDV 939
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEArieELEEDLHKLEEALNDLEARlshsripeiqaeLSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 940 -TAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDT 1018
Cdd:TIGR02169 804 eEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1019 VQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQ--------------------IDLLQETVQRF 1078
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEElseiedpkgedeeipeeelsLEDVQAELQRV 963
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1079 EEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLET 1129
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1102-1606 |
1.19e-11 |
|
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: 70.05 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1102 QLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEatkKLLSEAQYKNEELLKKIEDADKsia 1181
Cdd:TIGR04523 48 ELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKIN---KLNSDLSKINSEIKNDKEQKNK--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 hyhdttqrLEENVtaveNSLKAERQHNGaimKQLADAQVEIGELQRNLEDADRRNN-------QLQDSLQRLEENVGAKE 1254
Cdd:TIGR04523 122 --------LEVEL----NKLEKQKKENK---KNIDKFLTEIKKKEKELEKLNNKYNdlkkqkeELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1255 SLLLTEREQNA------STLKLLAEAHleiDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLT 1328
Cdd:TIGR04523 187 KNIDKIKNKLLklelllSNLKKKIQKN---KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1329 EALEKNEELLKKIHDDDKHILELQFTIQRLEentaAKENLLLREREQN-DATTKAQIESQERN-EQLLKRFVDVDRKIDL 1406
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQKEQDwNKELKSELKNQEKKlEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1407 LQDTIERI--------GENSTIKDALLLSERQEKDaIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKD 1478
Cdd:TIGR04523 340 LNEQISQLkkeltnseSENSEKQRELEEKQNEIEK-LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1479 ISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDT--AQKLQVDAISRlsSFVMEKQESDAAKRALTEARE 1556
Cdd:TIGR04523 419 QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTreSLETQLKVLSR--SINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1557 RNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAE 1606
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDE 546
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
891-1344 |
1.29e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQERESA---KKAVEEALEQEREKISSLT 967
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELE-EELEELEAELEELREELEKLEKLLQLLPLyqeLEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 968 SEIEGLKALlvaEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVI 1047
Cdd:COG4717 153 ERLEELREL---EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1048 AESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQL 1127
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1128 ETTIQRLEES-----LTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADksIAHYHDTTQRLEENVTAVEnslK 1202
Cdd:COG4717 310 LPALEELEEEeleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAALLAEAGVED---E 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1203 AERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQrlEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELI 1282
Cdd:COG4717 385 EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD--EEELEEELEELEEELEELEEELEELREELAELEAEL 462
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1283 RKLEDSDRKSD------SLQSTIKRLEEDGIAKEALLLTEKQAHEATRMT-LTEALEKNEELLKKIHDD 1344
Cdd:COG4717 463 EQLEEDGELAEllqeleELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLERASEYFSRLTDG 531
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
879-1202 |
2.58e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEELTNRLG-LEKK---LRTDLEKSKVAE------------------VSKLQAALNEMEQRM 936
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGeLKKEikeLKKAIEELKKAKgkcpvcgrelteehrkelLEEYTAELKRIEKEL 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 937 QDVTamqERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLS 1016
Cdd:PRK03918 469 KEIE---EKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1017 DTVQRLEETIQEREALLLAERQEKEEASAVIAEsqARNEAFASkLEDAEKQIDLLQETVQRF-------------EEAIT 1083
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKE--LEELGFES-VEELEERLKELEPFYNEYlelkdaekelereEKELK 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1084 KLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTD-----EKSTQLETTIQRLEESLTEkdalLTTERQETEATKKL 1158
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyeelrEEYLELSRELAGLRAELEE----LEKRREEIKKTLEK 698
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1002232322 1159 LSEAQYKNEELLKKIEDADKSIAHyhdtTQRLEENVTAVENSLK 1202
Cdd:PRK03918 699 LKEELEEREKAKKELEKLEKALER----VEELREKVKKYKALLK 738
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
881-1337 |
3.49e-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: 3.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 881 RDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQER 960
Cdd:TIGR00618 420 RDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLEL 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 961 ekissltseieglkallvaEQEENDLTKKAHANAQERneELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEK 1040
Cdd:TIGR00618 500 -------------------QEEPCPLCGSCIHPNPAR--QDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1041 EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSvtiEKQQHEETVVQLAEAQAKID--ELLREAG 1118
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA---EDMLACEQHALLRKLQPEQDlqDVRLHLQ 635
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1119 DTDEKSTQLETTIQRLEESLTEKD----ALLTTERQE--TEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEE 1192
Cdd:TIGR00618 636 QCSQELALKLTALHALQLTLTQERvrehALSIRVLPKelLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEE 715
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1193 NVTAVENSLKAERQHNGAIMKQLADAQVEIGELQR-------NLEDADRRNN-------QLQDSLQRLEENVGAKESlLL 1258
Cdd:TIGR00618 716 YDREFNEIENASSSLGSDLAAREDALNQSLKELMHqartvlkARTEAHFNNNeevtaalQTGAELSHLAAEIQFFNR-LR 794
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1259 TEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDsLQSTIKRLEEDGiAKEALLLTEKQAHEATRMTLTEALEKNEEL 1337
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQE-EEQFLSRLEEKS-ATLGEITHQLLKYEECSKQLAQLTQEQAKI 871
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
884-1497 |
8.85e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLE--ERVEELTNRLgleKKLRTDLekskvaevsklqAALNEMEQRMQDVTAMQERESAkkavEEALEQERE 961
Cdd:COG4913 242 EALEDAREQIEllEPIRELAERY---AAARERL------------AELEYLRAALRLWFAQRRLELL----EAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 962 KISSLTSEIEGLKALLVAEQEENDLTKKAHANAQ-ERNEELSKEVEDADGKIKQLSDTVQRLEETIQereALLLAERQEK 1040
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA---ALGLPLPASA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1041 EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQ------QHEETVVQLAEAQAKIDEL- 1113
Cdd:COG4913 380 EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERrksnipARLLALRDALAEALGLDEAe 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 LREAGD-----TDEKSTQ---------LETTI----QRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEE---LLKK 1172
Cdd:COG4913 460 LPFVGElievrPEEERWRgaiervlggFALTLlvppEHYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDpdsLAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1173 IEDADKSIAHYHDTTQRLEENVTAVEnSLKAERQHNGAIM-------------------------------KQLADAQVE 1221
Cdd:COG4913 540 LDFKPHPFRAWLEAELGRRFDYVCVD-SPEELRRHPRAITragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1222 IGELQRNLEDADRRNNQLQDSLQRLEEnvgakESLLLTEREQNASTLKLLAEAHLEIDEL---IRKLEDSDRKSDSLQST 1298
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAELeaeLERLDASSDDLAALEEQ 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1299 IKRLEE--DGIAKE-ALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLRE-RE 1374
Cdd:COG4913 694 LEELEAelEELEEElDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENlEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1375 QNDATTKAQIESQERNEQLLKRFVDVDR-KIDLLQDTIERIGEnstiKDALLlsERQEKDaikkELVEAGERNEELIMki 1453
Cdd:COG4913 774 RIDALRARLNRAEEELERAMRAFNREWPaETADLDADLESLPE----YLALL--DRLEED----GLPEYEERFKELLN-- 841
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1002232322 1454 EDTDKKIEHLQNAIiklegdieakDISLEAAREENDTIRKSLAE 1497
Cdd:COG4913 842 ENSIEFVADLLSKL----------RRAIREIKERIDPLNDSLKR 875
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1069-1683 |
8.93e-11 |
|
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: 67.15 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1069 DLLQETVQRFEEA----ITKLQSSVTIEKQQHEETVVQLAE----AQAKIDELLREAGDTDEKSTQLETTIQRLEESLTE 1140
Cdd:pfam10174 40 ELKKERALRKEEAarisVLKEQYRVTQEENQHLQLTIQALQdelrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1141 KdallttERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGaIMKQLADAQV 1220
Cdd:pfam10174 120 R------LQSEHERQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWE-RTRRIAEAEM 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1221 EIGELQRNLEDADRRNNQLQDSLQR-------------LEENVGAKESLLLT-ER-----EQNASTLKLLAEAHLEI-DE 1280
Cdd:pfam10174 193 QLGHLEVLLDQKEKENIHLREELHRrnqlqpdpaktkaLQTVIEMKDTKISSlERnirdlEDEVQMLKTNGLLHTEDrEE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1281 LIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLtekqaheatrmtlteALEKNEELLKKIHDDDKHILELqftiqrLEE 1360
Cdd:pfam10174 273 EIKQMEVYKSHSKFMKNKIDQLKQELSKKESELL---------------ALQTKLETLTNQNSDCKQHIEV------LKE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1361 NTAAKEnlllrereQNDATTKAQIES----QERNEQLLkrfvdvDRKIDLLQDTIER----IGENSTIKDALLLSERQEK 1432
Cdd:pfam10174 332 SLTAKE--------QRAAILQTEVDAlrlrLEEKESFL------NKKTKQLQDLTEEkstlAGEIRDLKDMLDVKERKIN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1433 DAIKKElveagernEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISL---EAAREENDTIRKSLAEAQEKNE-ELLRK 1508
Cdd:pfam10174 398 VLQKKI--------ENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALttlEEALSEKERIIERLKEQREREDrERLEE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1509 ISDNEYRIHLLQDTAQKLQVDAISRLSSFvmekqeSDAAKRALTEArernEDLLKRNEDLLKRNDDLIKKIEESSKTITQ 1588
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTEKESSL------IDLKEHASSLA----SSGLKKDSKLKSLEIAVEQKKEECSKLENQ 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1589 LQETLQRLEGKSTNLEAENQV--LRQQATATPPSTAKSSASRSKITRIHRSPENGHiLNGDTRQAEIKPSTGTSETIPSI 1666
Cdd:pfam10174 540 LKKAHNAEEAVRTNPEINDRIrlLEQEVARYKEESGKAQAEVERLLGILREVENEK-NDKDKKIAELESLTLRQMKEQNK 618
|
650
....*....|....*..
gi 1002232322 1667 GNPpdlnNEKHVEQGEK 1683
Cdd:pfam10174 619 KVA----NIKHGQQEMK 631
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
907-1606 |
1.40e-10 |
|
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: 66.77 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 907 EKKLRTDlEKSKVAEVSKLQAALNEMEQRMQ-DVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALlvaeQEEND 985
Cdd:pfam10174 44 ERALRKE-EAARISVLKEQYRVTQEENQHLQlTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPEL----TEENF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 986 LTKKAHANAQER-NEELSKEVEDADGKI---KQL----SDTVQRLEETIQEReALLLAERQEKEEASAVIAESQARNEAF 1057
Cdd:pfam10174 119 RRLQSEHERQAKeLFLLRKTLEEMELRIetqKQTlgarDESIKKLLEMLQSK-GLPKKSGEEDWERTRRIAEAEMQLGHL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1058 ASKLEDAEKQIDLLQETVQRfeeaitKLQSSVTIEKQQHEETVVQLAEAqaKIDELLREAGDtdekstqLETTIQRLEES 1137
Cdd:pfam10174 198 EVLLDQKEKENIHLREELHR------RNQLQPDPAKTKALQTVIEMKDT--KISSLERNIRD-------LEDEVQMLKTN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1138 ltekdALLTTERQETEAtKKLlsEAQYKNEELLK-KIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQL- 1215
Cdd:pfam10174 263 -----GLLHTEDREEEI-KQM--EVYKSHSKFMKnKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLt 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1216 ------ADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGA--------KESLLLTEREQNAstlkllaeAHLEIDEL 1281
Cdd:pfam10174 335 akeqraAILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTlageirdlKDMLDVKERKINV--------LQKKIENL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1282 IRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLltekqaheatrMTLTEALEKNE---ELLKKIHDDDKHilelqftiQRL 1358
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL-----------TTLEEALSEKEriiERLKEQREREDR--------ERL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1359 EE-NTAAKENLLLRER---EQNDATTKAQ--IESQERNEQLLKRFVDVDRKIDLLQDTIErigensTIKDALLLSERQEK 1432
Cdd:pfam10174 468 EElESLKKENKDLKEKvsaLQPELTEKESslIDLKEHASSLASSGLKKDSKLKSLEIAVE------QKKEECSKLENQLK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1433 DAikKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKdisLEAARE-ENDtirKSLAEaqekneellRKISD 1511
Cdd:pfam10174 542 KA--HNAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERL---LGILREvENE---KNDKD---------KKIAE 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1512 NEYRIhLLQDTAQKLQVDAIsRLSSFVMEKQESDAAKRALTEARERNEDLLKRN-EDLLKRNDDLIKKIEESSKTITQLQ 1590
Cdd:pfam10174 605 LESLT-LRQMKEQNKKVANI-KHGQQEMKKKGAQLLEEARRREDNLADNSQQLQlEELMGALEKTRQELDATKARLSSTQ 682
|
730
....*....|....*.
gi 1002232322 1591 ETLQRLEGKSTNLEAE 1606
Cdd:pfam10174 683 QSLAEKDGHLTNLRAE 698
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
885-1360 |
1.40e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 885 ALKVAKEKLEERVEELTNRL-GLEKKLRtdlekskvaevsKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKI 963
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIrELEERIE------------ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 964 -------SSLTSEIEGLKALLV-AEQEENDL--TKKAHANAQERNEELSKEVEDADgKIKQLSDTVQRLE-----ETIQE 1028
Cdd:PRK03918 310 reiekrlSRLEEEINGIEERIKeLEEKEERLeeLKKKLKELEKRLEELEERHELYE-EAKAKKEELERLKkrltgLTPEK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1029 REALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRF--------EEAITKLQSSVTIEKQQHEETv 1100
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKELLEEYTAELKRIEKE- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 vqLAEAQAKIDELLREAgdtdeksTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEEL------LKKIE 1174
Cdd:PRK03918 468 --LKEIEEKERKLRKEL-------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYeklkekLIKLK 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1175 DADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVE-IGELQ---RNLEDADRRNNQLQDSLQRLEEnv 1250
Cdd:PRK03918 539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEerlKELEPFYNEYLELKDAEKELER-- 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1251 gaKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDslQSTIKRLEEDGIAKE---ALLLTEKQAHEATRMTL 1327
Cdd:PRK03918 617 --EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSrelAGLRAELEELEKRREEI 692
|
490 500 510
....*....|....*....|....*....|...
gi 1002232322 1328 TEALEKNEELLKKIHDDDKHILELQFTIQRLEE 1360
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEKLEKALERVEE 725
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
921-1606 |
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 1002232322 921 EVSKLQAALNEMEQRMQDV-TAMQERESAKKAveeaLEQEREKISSLTSEIEGLKALLVAEQEendlTKKAHANAQERNE 999
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQgQKVQEHQMELKY----LKQYKEKACEIRDQITSKEAQLESSRE----IVKSYENELDPLK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1000 ELSKEVEDADGKIKQLSDTVQRLEETIQEREALllaerqeKEEASaviaesQARNEAFASKLEDAEKQIDLLQETVQRFE 1079
Cdd:TIGR00606 252 NRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKD-------NSELE------LKMEKVFQGTDEQLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1080 EaitklqssvtiekqqheetvvQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEesltekdalLTTERQETEATKK-- 1157
Cdd:TIGR00606 319 R---------------------ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ---------LQADRHQEHIRARds 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1158 -LLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAI-MKQLADAQVEIGELQRNLEDA--- 1232
Cdd:TIGR00606 369 lIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLkQEQADEIRDEKKGLGRTIELKkei 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1233 -DRRNNQLQDSLQRLEENVGAKESLL------------LTEREQNASTLKLLAE------AHLEIDELIRKLEDSDRKSD 1293
Cdd:TIGR00606 449 lEKKQEELKFVIKELQQLEGSSDRILeldqelrkaereLSKAEKNSLTETLKKEvkslqnEKADLDRKLRKLDQEMEQLN 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1294 SLQSTIKRLE---EDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHIlelqftiqRLEENTAAKENLLL 1370
Cdd:TIGR00606 529 HHTTTRTQMEmltKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEI--------NQTRDRLAKLNKEL 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1371 REREQNDATTKAQIESQERNEQLLKRFV-------DVDRKIDLLQDTIER-------IGENSTIKDALLLSERQEK---- 1432
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsqDEESDLERLKEEIEKsskqramLAGATAVYSQFITQLTDENqscc 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1433 ---DAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRK- 1508
Cdd:TIGR00606 681 pvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDi 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1509 ------ISDNEYRIHLL---QDTAQKLQVDaISRLSSFVMEKQESD------AAKRALTEARERNEDLLKRNEDLLKRND 1573
Cdd:TIGR00606 761 qrlkndIEEQETLLGTImpeEESAKVCLTD-VTIMERFQMELKDVErkiaqqAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
730 740 750
....*....|....*....|....*....|...
gi 1002232322 1574 DLIKKIEESSKTITQLQETLQRLEGKSTNLEAE 1606
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1201-1613 |
1.76e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1201 LKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKEslLLTEREQNASTLKLLAEAHLEIDE 1280
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1281 LIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLtekqahEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEE 1360
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLS------LATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1361 NTAAKENLLLREREQNdattkaQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELV 1440
Cdd:COG4717 228 ELEQLENELEAAALEE------RLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1441 EAGERNEELIMKIEDTDKKIEHLqnaIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRkisdnEYRIHLLQ 1520
Cdd:COG4717 302 KEAEELQALPALEELEEEELEEL---LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL-----EELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1521 DTAQKLQVDAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRND---------DLIKKIEESSKTITQLQE 1591
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeeleeeleELEEELEELEEELEELRE 453
|
410 420
....*....|....*....|....
gi 1002232322 1592 TLQRLEGKSTNLEAENQV--LRQQ 1613
Cdd:COG4717 454 ELAELEAELEQLEEDGELaeLLQE 477
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
863-1427 |
2.56e-10 |
|
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: 65.93 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 863 AWRRRVARRELRQLRMAARDTQALKvakeKLEERVEELtNRLGLEKKLRTDL-----------EKSKVAEVSKLQAALN- 930
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELR----RLEEEVRLL-RETSLQQKMRLEAqameldalavaEKAGQAEAEGLRAALAg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 931 -EMEQRMQDVTAMQERESAKKAVEEAL----EQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNE----EL 1001
Cdd:pfam07111 127 aEMVRKNLEEGSQRELEEIQRLHQEQLssltQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAEllrkQL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1002 SKEVEDADGKIKQLSDTVQRLEETIQ----------EREALLLAE---RQEKEEASAVIAESQARNEAFASKLEDAEKQI 1068
Cdd:pfam07111 207 SKTQEELEAQVTLVESLRKYVGEQVPpevhsqtwelERQELLDTMqhlQEDRADLQATVELLQVRVQSLTHMLALQEEEL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1069 -------DLL--------QETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLreagdtdeKSTQLETTIqr 1133
Cdd:pfam07111 287 trkiqpsDSLepefpkkcRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQV--------TSQSQEQAI-- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1134 LEESLTEKDALLTTERQETEATKKLLSEAQYKN----------EELLKKIEDADKSI-AHYHDTTQRLEENVTAVEN--- 1199
Cdd:pfam07111 357 LQRALQDKAAEVEVERMSAKGLQMELSRAQEARrrqqqqtasaEEQLKFVVNAMSSTqIWLETTMTRVEQAVARIPSlsn 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1200 --SLKAERQHN--GAIMKQLADAQVEIG-----------------ELQRNLEDADRRNNQLQDSLQRLEENVGakeslll 1258
Cdd:pfam07111 437 rlSYAVRKVHTikGLMARKVALAQLRQEscpppppappvdadlslELEQLREERNRLDAELQLSAHLIQQEVG------- 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1259 TEREQNASTLKLLAEAHLEIDELIRKLEDSdRKSDSLQSTIKRLEEDGIAKEALLLTEK--QAHEATRMTLTEALEKNEE 1336
Cdd:pfam07111 510 RAREQGEAERQQLSEVAQQLEQELQRAQES-LASVGQQLEVARQGQQESTEEAASLRQEltQQQEIYGQALQEKVAEVET 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1337 LLKKihdddkhilELQFTIQRLEE--NTAAKENLLLR--------EREQNDATTKAQIES-QERNEQLLKRFVDVDRKID 1405
Cdd:pfam07111 589 RLRE---------QLSDTKRRLNEarREQAKAVVSLRqiqhratqEKERNQELRRLQDEArKEEGQRLARRVQELERDKN 659
|
650 660
....*....|....*....|..
gi 1002232322 1406 LLQDTIERIGENSTIKDALLLS 1427
Cdd:pfam07111 660 LMLATLQQEGLLSRYKQQRLLA 681
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
875-1344 |
2.68e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.13 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQ-ALKVAKEKLEERVEELTNRLGLEKKLRTDlekskvaevskLQAAlNEMEQRMQdvTAMQEResakkave 953
Cdd:COG3096 289 ELRRELFGARrQLAEEQYRLVEMARELEELSARESDLEQD-----------YQAA-SDHLNLVQ--TALRQQ-------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EALEQEREKISSLTSEIEgLKALLVAEQEENdltkkaHANAQERNEELSKEVEDADGkikQLSDTVQRLEE----TIQER 1029
Cdd:COG3096 347 EKIERYQEDLEELTERLE-EQEEVVEEAAEQ------LAEAEARLEAAEEEVDSLKS---QLADYQQALDVqqtrAIQYQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1030 EALLLAERQEK---------EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVtiekqqhEETV 1100
Cdd:COG3096 417 QAVQALEKARAlcglpdltpENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA-------GEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQLAEAQAKidELLREAGDtdekstqLETTIQRLEesltekdallTTERQETEATKKLlsEAQYKNEELLkkiEDADKSI 1180
Cdd:COG3096 490 RSQAWQTAR--ELLRRYRS-------QQALAQRLQ----------QLRAQLAELEQRL--RQQQNAERLL---EEFCQRI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1181 AHYHDTtqrlEENVTAVENSLKAERQHNGAimkQLADAQVEIGELQRNLEDADRRNNQL----------QDSLQRLEENV 1250
Cdd:COG3096 546 GQQLDA----AEELEELLAELEAQLEELEE---QAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQS 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1251 GA--KESLLLTEREQNasTLKLLAEAHLEIDELIRKLEdsdrksdSLQSTIKRLEEDGIAkeallltekqahEATRM-TL 1327
Cdd:COG3096 619 GEalADSQEVTAAMQQ--LLEREREATVERDELAARKQ-------ALESQIERLSQPGGA------------EDPRLlAL 677
|
490
....*....|....*..
gi 1002232322 1328 TEALekNEELLKKIHDD 1344
Cdd:COG3096 678 AERL--GGVLLSEIYDD 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1429-1630 |
3.58e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.40 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1429 RQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRK 1508
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1509 I------------------SDNEYRIHLLQDTAQKLQvdaiSRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLK 1570
Cdd:COG4942 113 LyrlgrqpplalllspedfLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1571 RNDDLIKK----IEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATATPPSTAKSSASRSK 1630
Cdd:COG4942 189 ALEALKAErqklLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
909-1305 |
4.32e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 909 KLRTDLEKSKVaEVSKLQAALNEMEQRMQDVTAM-----QERESAK---KAVEEALEQeREKISSLTSEIEGLKALLvAE 980
Cdd:PRK04863 290 ELRRELYTSRR-QLAAEQYRLVEMARELAELNEAesdleQDYQAASdhlNLVQTALRQ-QEKIERYQADLEELEERL-EE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 981 QEEndltkkAHANAQERNEELSKEVEDADGKIK----QLSDTVQRLEE----TIQEREALLLAERQEK---------EEA 1043
Cdd:PRK04863 367 QNE------VVEEADEQQEENEARAEAAEEEVDelksQLADYQQALDVqqtrAIQYQQAVQALERAKQlcglpdltaDNA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1044 SAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEA---ITKLQSSVTIEkqqheetvvqlaEAQAKIDELLREAGD- 1119
Cdd:PRK04863 441 EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlVRKIAGEVSRS------------EAWDVARELLRRLREq 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1120 --TDEKSTQLETTIQRLEESLTEKDALlttERQETEATKKLlsEAQYKNEELLKkiedadksiahyhDTTQRLEENVTAV 1197
Cdd:PRK04863 509 rhLAEQLQQLRMRLSELEQRLRQQQRA---ERLLAEFCKRL--GKNLDDEDELE-------------QLQEELEARLESL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1198 ENSLKAERQHNGAIMKQLADAQVEIGELQRnLEDADRrnnQLQDSLQRLEENVGAK-------ESLLLT--EREQNASTL 1268
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAA-RAPAWL---AAQDALARLREQSGEEfedsqdvTEYMQQllERERELTVE 646
|
410 420 430
....*....|....*....|....*....|....*...
gi 1002232322 1269 K-LLAEAHLEIDELIRKLEDSDRKSDslqSTIKRLEED 1305
Cdd:PRK04863 647 RdELAARKQALDEEIERLSQPGGSED---PRLNALAER 681
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
947-1181 |
5.47e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 947 SAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETI 1026
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1027 QEREALLlaerqekeeaSAVIAESQARNEAFASKLEdaekqidLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEA 1106
Cdd:COG4942 100 EAQKEEL----------AELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1107 QAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIA 1181
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1061-1609 |
5.92e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 5.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1061 LEDAEKQIDLLQETVQRFEEAITKLQssvTIEKQQHEETVVQLAEAQAKIDELlreagdtDEKSTQLETTIQRLEESLTE 1140
Cdd:COG4913 244 LEDAREQIELLEPIRELAERYAAARE---RLAELEYLRAALRLWFAQRRLELL-------EAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1141 KDALLTTERQETEATKKLLSEAQYKNEELLKK-IEDADKSIAHYHDTTQRLEENVTAVENSLKAERQhngaimkqladaq 1219
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGDRLEQLEReIERLERELEERERRRARLEALLAALGLPLPASAE------------- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1220 veigELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQnastlklLAEAHLEIDELIRkledsdRKSD---SLQ 1296
Cdd:COG4913 381 ----EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE-------LRELEAEIASLER------RKSNipaRLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1297 STIKRLEED-GIAKEAL-----LLTEKQAHEATRMTLTEAL----------EKNEELLKKIHDDDKhiLELQFTIQRLEE 1360
Cdd:COG4913 444 ALRDALAEAlGLDEAELpfvgeLIEVRPEEERWRGAIERVLggfaltllvpPEHYAAALRWVNRLH--LRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1361 NTAAKENlllREREQNDATTKAQIES---QERNEQLLKRFVD---VDRkIDLLQDTIERIGENSTIKDALLLSERQEKDA 1434
Cdd:COG4913 522 GLPDPER---PRLDPDSLAGKLDFKPhpfRAWLEAELGRRFDyvcVDS-PEELRRHPRAITRAGQVKGNGTRHEKDDRRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1435 IKKELVeAGERNEElimKIEDTDKKIEHLQNAIIKLEGDIEAkdisLEAAREENDTIRKSLAEAQEKNEELLrkisdney 1514
Cdd:COG4913 598 IRSRYV-LGFDNRA---KLAALEAELAELEEELAEAEERLEA----LEAELDALQERREALQRLAEYSWDEI-------- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1515 rihllqDTAQklQVDAISRLSSfvmEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQ 1594
Cdd:COG4913 662 ------DVAS--AEREIAELEA---ELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570
....*....|....*
gi 1002232322 1595 RLEGKSTNLEAENQV 1609
Cdd:COG4913 731 ELQDRLEAAEDLARL 745
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1079-1595 |
9.58e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1079 EEAITKLQSSVtiekQQHEETVVQLAEAQAKIdELLREAGDTDEKSTQLETTIQRLEESLtekdALLTTERQETEAtkKL 1158
Cdd:COG4913 224 FEAADALVEHF----DDLERAHEALEDAREQI-ELLEPIRELAERYAAARERLAELEYLR----AALRLWFAQRRL--EL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1159 LSEAQYKNEELLKKIEDAdksiahyHDTTQRLEENVTAVENSLKAERQHNGAimKQLADAQVEIGELQRNLEDADRRNNQ 1238
Cdd:COG4913 293 LEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGG--DRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1239 LQDSLQRLEENVGAKESLLLTEREQNASTLK----LLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLE----------- 1303
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEaleeELEALEEALAEAEAALRDLRRELRELEAEIASLErrksniparll 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1304 --------EDGIAKEAL-----LLTEKQAHEATRMTLTEAL----------EKNEELLKKIHDDDKhiLELQFTIQRLEE 1360
Cdd:COG4913 444 alrdalaeALGLDEAELpfvgeLIEVRPEEERWRGAIERVLggfaltllvpPEHYAAALRWVNRLH--LRGRLVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1361 NTAAKENlllREREQNDATTKAQIES---QERNEQLLKRFVDV-------------------------------DRKIDL 1406
Cdd:COG4913 522 GLPDPER---PRLDPDSLAGKLDFKPhpfRAWLEAELGRRFDYvcvdspeelrrhpraitragqvkgngtrhekDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1407 LQDTIerIGENSTIKDALLLSERQEkdaIKKELVEAGERNEELIMKIEDTDKKIEHLQN------AIIKLEG-------- 1472
Cdd:COG4913 599 RSRYV--LGFDNRAKLAALEAELAE---LEEELAEAEERLEALEAELDALQERREALQRlaeyswDEIDVASaereiael 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1473 -----DIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvDAISRLSSFVMEKQESDAA 1547
Cdd:COG4913 674 eaeleRLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-DRLEAAEDLARLELRALLE 752
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1002232322 1548 KRALTEARERNEDLLKRNedLLKRNDDLIKKIEESSKTITQLQETLQR 1595
Cdd:COG4913 753 ERFAAALGDAVERELREN--LEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
879-1157 |
1.28e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.82 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKvaevsKLQAALNEMEQRMQ--DVTAMQER-ESAKKAVEEA 955
Cdd:PRK04863 832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAK-----EGLSALNRLLPRLNllADETLADRvEEIREQLDEA 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQER--EKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERneelskeVEDADGKIKQLSDTVQRleetiqeREALl 1033
Cdd:PRK04863 907 EEAKRfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQT-------QRDAKQQAFALTEVVQR-------RAHF- 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1034 laerqEKEEASAVIAESQARNEAFASKLEDAEKQID----LLQETVQRFEEAI---TKLQSSVTIEKQQHEETVVQL--- 1103
Cdd:PRK04863 972 -----SYEDAAEMLAKNSDLNEKLRQRLEQAEQERTrareQLRQAQAQLAQYNqvlASLKSSYDAKRQMLQELKQELqdl 1046
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1104 -------AEAQAKI--DELLREAGDTDEKSTQLETTIQRLEESLT---------EKDalLTTERQETEATKK 1157
Cdd:PRK04863 1047 gvpadsgAEERARArrDELHARLSANRSRRNQLEKQLTFCEAEMDnltkklrklERD--YHEMREQVVNAKA 1116
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1332-1617 |
1.72e-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: 63.54 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1332 EKNEELLKKIHDDDKHILELQFTIQRLEENTaakeNLLLREREQndATTKAQIESQERNEQL---LKRFVDVDRKIDLLQ 1408
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQL----KSLERQAEK--AERYKELKAELRELELallVLRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1409 DTIERigenstikdalllsERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREEN 1488
Cdd:TIGR02168 246 EELKE--------------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1489 DTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAIS---RLSSFVMEKQESDAAKRALTEARERnedlLKRN 1565
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESleaELEELEAELEELESRLEELEEQLET----LRSK 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1566 EDLLKRNDDLI-KKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATAT 1617
Cdd:TIGR02168 388 VAQLELQIASLnNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1238-1615 |
2.65e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1238 QLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLltEK 1317
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL--QL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1318 QAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIES-QERNEQLLKR 1396
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1397 FVDVDRKIDLLQDTIERIGEN-STIKDALLLSERQEKDAIKKELVEAG-------------------------------- 1443
Cdd:COG4717 208 LAELEEELEEAQEELEELEEElEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlglla 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1444 -------ERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKisDNEYRI 1516
Cdd:COG4717 288 llflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL--EEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1517 HLLQDTAQKL----QVDAISRLSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRND--DLIKKIEESSKTITQLQ 1590
Cdd:COG4717 366 EELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELE 445
|
410 420
....*....|....*....|....*
gi 1002232322 1591 ETLQRLEGKSTNLEAENQVLRQQAT 1615
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGE 470
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
884-1157 |
2.76e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.66 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSK--VAEVSKLQAALNEMEqrmqDVTAMQERESAKKAVEEALEQERE 961
Cdd:COG3096 836 AELAALRQRRSELERELAQHRAQEQQLRQQLDQLKeqLQLLNKLLPQANLLA----DETLADRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 962 kISSLTSEIEGLKALLVAEQEEndltkkahanaQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALllaerqEKE 1041
Cdd:COG3096 912 -IQQHGKALAQLEPLVAVLQSD-----------PEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHF------SYE 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1042 EASAVIAESQARNEAFASKLEDAEKQI----DLLQETVQRFEEAI---TKLQSSVTIEKQQHEE----------TVVQLA 1104
Cdd:COG3096 974 DAVGLLGENSDLNEKLRARLEQAEEARrearEQLRQAQAQYSQYNqvlASLKSSRDAKQQTLQEleqeleelgvQADAEA 1053
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1105 EAQAKI--DELLREAGDTDEKSTQLETTIQRLE---ESL------TEKDalLTTERQETEATKK 1157
Cdd:COG3096 1054 EERARIrrDELHEELSQNRSRRSQLEKQLTRCEaemDSLqkrlrkAERD--YKQEREQVVQAKA 1115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
942-1396 |
2.93e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 942 MQERESAKKAVEEALEQEREKISSltseieglkallvaeqeendltKKAHANAQERNEELSKEVEDADGkikQLSDTVQR 1021
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTS----------------------RRQLAAEQYRLVEMARELAELNE---AESDLEQD 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1022 LeETIQEREALLL-AER-QEKEE-ASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSsvtiekqqhee 1098
Cdd:PRK04863 330 Y-QAASDHLNLVQtALRqQEKIErYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKS----------- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1099 tvvQLAEAQAKIDELLREAGdtdekstQLETTIQRLEE--------SLTEKDA---LLTTERQETEATKKLLSEAQYKN- 1166
Cdd:PRK04863 398 ---QLADYQQALDVQQTRAI-------QYQQAVQALERakqlcglpDLTADNAedwLEEFQAKEQEATEELLSLEQKLSv 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1167 -EELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAimKQLADAQVEIGELQRNLEDADRRNNQLQDSLQR 1245
Cdd:PRK04863 468 aQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLA--EQLQQLRMRLSELEQRLRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1246 LEENVGAKESLllterEQnastlkLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDgiakeallLTEKQAHEATRM 1325
Cdd:PRK04863 546 LGKNLDDEDEL-----EQ------LQEELEARLESLSESVSEARERRMALRQQLEQLQAR--------IQRLAARAPAWL 606
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1326 TLTEALEKNEEllkkihdddkHILELQFTIQRLEEntaAKENLLLREREqndaTTKAQIESQERNEQLLKR 1396
Cdd:PRK04863 607 AAQDALARLRE----------QSGEEFEDSQDVTE---YMQQLLERERE----LTVERDELAARKQALDEE 660
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1024-1266 |
3.03e-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: 61.32 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1024 ETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQL 1103
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1104 AEAQAKIDELLREAgdtdekstqlettiQRLEESLTEKDALLTTERQETEATKKLLseaQYKNEELLKKIEDADKSIAHY 1183
Cdd:COG4942 100 EAQKEELAELLRAL--------------YRLGRQPPLALLLSPEDFLDAVRRLQYL---KYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1184 HDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQ 1263
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
...
gi 1002232322 1264 NAS 1266
Cdd:COG4942 243 TPA 245
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
593-1461 |
3.07e-09 |
|
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: 62.76 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 593 SEENTKSSKSSIATRFKVQLHELMETLSSTEPHYIRCVKPNSVLKPaiFENTNvLQQLRCSGVLEAIRIScAGYPTRKLF 672
Cdd:TIGR00606 228 SKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA--LKSRK-KQMEKDNSELELKMEK-VFQGTDEQL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 673 HDFLHrFRilaSEIVKEKNDEKVTCQKVLDKMGLQGYQIGRTKvflragqmAELDARRTEVRNNAARgvqgqFRTHVARE 752
Cdd:TIGR00606 304 NDLYH-NH---QRTVREKERELVDCQRELEKLNKERRLLNQEK--------TELLVEQGRLQLQADR-----HQEHIRAR 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 753 QFLILRNASVC-LQSFVRA----RLACKLHECLRR--EAAAIKIQKNIRCYFAWRTYSQLRLSAITLQ-TGL-RTMAALK 823
Cdd:TIGR00606 367 DSLIQSLATRLeLDGFERGpfseRQIKNFHTLVIErqEDEAKTAAQLCADLQSKERLKQEQADEIRDEkKGLgRTIELKK 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 824 EFMFRKQNKATTHIQTQWRCHRDNSNYLKLKRAALTYQCAWRRRVARRELRQLRMAARDTQALKVAKEKLEERVEELTNR 903
Cdd:TIGR00606 447 EILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQ 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 904 LGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGL-KALLVAEQE 982
Cdd:TIGR00606 527 LNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLnKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 983 ENDLTKKAHaNAQERNEELSKEVEDADGKIKQLSDtVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEA------ 1056
Cdd:TIGR00606 607 KNHINNELE-SKEEQLSSYEDKLFDVCGSQDEESD-LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcq 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1057 --FASKLEDAEKQIDlLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRL 1134
Cdd:TIGR00606 685 rvFQTEAELQEFISD-LQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRL 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1135 EESLTEKDALLTTERQETEATKKLLSEAQYKnEELLKKIEDADKSIAHYHDTTQRLEENVTAVE-NSLKAERQHngaimk 1213
Cdd:TIGR00606 764 KNDIEEQETLLGTIMPEEESAKVCLTDVTIM-ERFQMELKDVERKIAQQAAKLQGSDLDRTVQQvNQEKQEKQH------ 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1214 QLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEenvgaKESLLLTEREQNASTL-KLLAEAHLEIDELIRKLEDSDRKS 1292
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELK-----SEKLQIGTNLQRRQQFeEQLVELSTEVQSLIREIKDAKEQD 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1293 DSLQSTIKRLEEDgiaKEALLLTEKQAHEATRMTLTEALEKneelLKKIHdddkhilelqFTIQRLEENTAAKENLLLRE 1372
Cdd:TIGR00606 912 SPLETFLEKDQQE---KEELISSKETSNKKAQDKVNDIKEK----VKNIH----------GYMKDIENKIQDGKDDYLKQ 974
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1373 REQNDATTKAQI-ESQERNEQLLKRFVDVDRKIDlLQDTIERIgenstIKDALLLSERQEK-DAIKKELVE-AGERNEEL 1449
Cdd:TIGR00606 975 KETELNTVNAQLeECEKHQEKINEDMRLMRQDID-TQKIQERW-----LQDNLTLRKRENElKEVEEELKQhLKEMGQMQ 1048
|
890
....*....|..
gi 1002232322 1450 IMKIEDTDKKIE 1461
Cdd:TIGR00606 1049 VLQMKQEHQKLE 1060
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
925-1286 |
3.47e-09 |
|
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: 61.83 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 925 LQAALNEMEQRMQDVtaMQERESAKKAVE-EALEQEREK------ISSLTSEIEGLKALLVAEQEENDLTKKAHANAQER 997
Cdd:pfam07888 32 LQNRLEECLQERAEL--LQAQEAANRQREkEKERYKRDReqwerqRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 998 NEELSKEV-------EDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDL 1070
Cdd:pfam07888 110 SEELSEEKdallaqrAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1071 LQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELlrEAGDTDEKSTQ-LETTIQRLEESLTEKDALLTTER 1149
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEN--EALLEELRSLQeRLNASERKVEGLGEELSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1150 QETEATkklLSEAQYKNEELLKKIEDAD------------------KSIAHYHDTTQRLEENVTAVENSLKAERQhngai 1211
Cdd:pfam07888 268 DRTQAE---LHQARLQAAQLTLQLADASlalregrarwaqeretlqQSAEADKDRIEKLSAELQRLEERLQEERM----- 339
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1212 mkQLADAQVEIGelqrnlEDADRRNNQLQDSLQRLEEnvgAKESLLLTEREQNastlKLLAEAHlEIDELIRKLE 1286
Cdd:pfam07888 340 --EREKLEVELG------REKDCNRVQLSESRRELQE---LKASLRVAQKEKE----QLQAEKQ-ELLEYIRQLE 398
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
993-1596 |
3.53e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.23 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 993 NAQERNEELSKEV-----------EDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIaeSQARNEAfaSKL 1061
Cdd:PRK01156 162 NSLERNYDKLKDVidmlraeisniDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY--NNAMDDY--NNL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1062 EDAEKQIDLLQETVQRFEEAITKLQSsvtiEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEK 1141
Cdd:PRK01156 238 KSALNELSSLEDMKNRYESEIKTAES----DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1142 DALLTTERQETEATKKLLSEAQYKNEELLKK---IEDADK---SIAHYHDTTQRLEENVTA----VENSLKAERQHNGAI 1211
Cdd:PRK01156 314 LSNIDAEINKYHAIIKKLSVLQKDYNDYIKKksrYDDLNNqilELEGYEMDYNSYLKSIESlkkkIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1212 MKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLtEREQNASTLK-----LLAEAHLEIDELIRKLE 1286
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD-ELSRNMEMLNgqsvcPVCGTTLGEEKSNHIIN 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1287 DSDRKSDSLQSTIKRLEedgiaKEALLLTEKQAHeatrmtlteaLEKNEELLKKihdddKHILELQFTIQRLEENTAAKE 1366
Cdd:PRK01156 473 HYNEKKSRLEEKIREIE-----IEVKDIDEKIVD----------LKKRKEYLES-----EEINKSINEYNKIESARADLE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1367 NLLLREREQNDATTKAqiesqernEQLLKRFVDVDRKiDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERN 1446
Cdd:PRK01156 533 DIKIKINELKDKHDKY--------EEIKNRYKSLKLE-DLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1447 EELIMKIED----TDKKIEHLQNAIIKLE---GDIEAKDISLEAAREENDTIRKSLAEA---QEKNEELLRKISDNEYRI 1516
Cdd:PRK01156 604 QEIEIGFPDdksyIDKSIREIENEANNLNnkyNEIQENKILIEKLRGKIDNYKKQIAEIdsiIPDLKEITSRINDIEDNL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1517 HLLQdtaqklqvdaiSRLssfvmekqesDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIeESSKTITQLQETLQRL 1596
Cdd:PRK01156 684 KKSR-----------KAL----------DDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKRL 741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1043-1311 |
4.28e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1043 ASAVIAESQARNEAfASKLEDAEKQIDLLQETVQRFEEAITKLQSsvtiekqqheetvvQLAEAQAKIDELLREAGDTDE 1122
Cdd:COG4942 12 ALAAAAQADAAAEA-EAELEQLQQEIAELEKELAALKKEEKALLK--------------QLAALERRIAALARRIRALEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1123 KSTQLETTIQRLEESLTEKdalltteRQETEATKKLLSE---AQYKNEEllkkiEDADKSIAHyhdttqrlEENVTAVEN 1199
Cdd:COG4942 77 ELAALEAELAELEKEIAEL-------RAELEAQKEELAEllrALYRLGR-----QPPLALLLS--------PEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1200 SLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEEnvgAKESLLLTEREQNastlKLLAEAHLEID 1279
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE---ERAALEALKAERQ----KLLARLEKELA 209
|
250 260 270
....*....|....*....|....*....|..
gi 1002232322 1280 ELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEA 1311
Cdd:COG4942 210 ELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
10-52 |
5.04e-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: 53.59 E-value: 5.04e-09
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1002232322 10 GSHVWVEDKDSAWVDGEVFRIDGKNAHVRTTKGKTVIANVSDI 52
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVETEDGKTVTVKKDDV 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
891-1344 |
5.43e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEI 970
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 971 EGLKALLVAEQEENDLtkkahanaQERNEELSKEVEDadgkIKQLSDTVQRLEETIQE-REALLLAERQEKEEASAVIAE 1049
Cdd:COG4717 129 PLYQELEALEAELAEL--------PERLEELEERLEE----LRELEEELEELEAELAElQEELEELLEQLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1050 SQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTI----EKQQHEETVVQLAEAQAKIDELLREAGDTDEKST 1125
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAaaleERLKEARLLLLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1126 QLETTIQRL---------------EESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRL 1190
Cdd:COG4717 277 GVLFLVLGLlallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1191 EEnvtaVENSLKAERQHNgAIMKQLADAQVE-IGELQRNLEDADRRnNQLQDSLQRLEENVGAKESLLLTEREQ-NASTL 1268
Cdd:COG4717 357 EE----LEEELQLEELEQ-EIAALLAEAGVEdEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEAlDEEEL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1269 KL-LAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDG-----IAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIH 1342
Cdd:COG4717 431 EEeLEELEEELEELEEELEELREELAELEAELEQLEEDGelaelLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
..
gi 1002232322 1343 DD 1344
Cdd:COG4717 511 EE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
934-1298 |
6.56e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 934 QRMQDVTAMQERESAKKAVEEALEQEREKissLTSEIEGLKALLVAEQ-EENDLTKKAHANAQErnEELSKEVEDADGKI 1012
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEE---KAREVERRRKLEEAEKaRQAEMDRQAAIYAEQ--ERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1013 KQlSDTVQRLEETIQEREALLLAERQEKEEASAviaESQARNEAFASKLEDAEKQiDLLQETVQRfeeaitklqssvTIE 1092
Cdd:pfam17380 354 RQ-EERKRELERIRQEEIAMEISRMRELERLQM---ERQQKNERVRQELEAARKV-KILEEERQR------------KIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1093 KQQHEETVVQLAEAQAKIDELLREAgdtDEKSTQLETTiqRLEESLTEKDALLTTERQETEATKKLLSEaqyKNEELLKK 1172
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLE---EERAREMERV--RLEEQERQQQVERLRQQEEERKRKKLELE---KEKRDRKR 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1173 IEDADKSIahyhdttqrLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQlqdslQRLEENVGA 1252
Cdd:pfam17380 489 AEEQRRKI---------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQ-----QEMEERRRI 554
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1002232322 1253 KESLLLTEREQNAstlkllAEAHLEIDELIRKLEDSDRKSDSLQST 1298
Cdd:pfam17380 555 QEQMRKATEERSR------LEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
906-1610 |
8.26e-09 |
|
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: 61.22 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 906 LEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTA------MQERESAKKAVEEALEQEREKISSLTSEIegLKALLVA 979
Cdd:TIGR01612 1005 LKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKnipnieIAIHTSIYNIIDEIEKEIGKNIELLNKEI--LEEAEIN 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 980 EQEENDLTKK-AHAN----AQERNEELSKEVEDADGKIKQLSdtvQRLEETIQEREALLLAERQEKEEASAVIA--ESQA 1052
Cdd:TIGR01612 1083 ITNFNEIKEKlKHYNfddfGKEENIKYADEINKIKDDIKNLD---QKIDHHIKALEEIKKKSENYIDEIKAQINdlEDVA 1159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1053 RNEAFASKLEDAEKQIDLLQETVQR---FEEAITKLQSSVT-IEKQQ---HEETVVQLAEAQAkIDELLREAGDTDEKST 1125
Cdd:TIGR01612 1160 DKAISNDDPEEIEKKIENIVTKIDKkknIYDEIKKLLNEIAeIEKDKtslEEVKGINLSYGKN-LGKLFLEKIDEEKKKS 1238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1126 qlETTIQRLEESLTEKDALlttERQETEATKKLLSEAQYKNE-ELLKKIEDADKSiahYHDTTQRLEENVTAVEN-SLKA 1203
Cdd:TIGR01612 1239 --EHMIKAMEAYIEDLDEI---KEKSPEIENEMGIEMDIKAEmETFNISHDDDKD---HHIISKKHDENISDIREkSLKI 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1204 ----ERQHNGAIMKQladaqveigELQRNLEDADRRNNQLQdslQRLEENVGAKESLLLTEREQNASTLKllaEAHLEID 1279
Cdd:TIGR01612 1311 iedfSEESDINDIKK---------ELQKNLLDAQKHNSDIN---LYLNEIANIYNILKLNKIKKIIDEVK---EYTKEIE 1375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1280 ELIRKLEDSDRKSDSLqstIKRLEEDgiakeallltekqaheatrMTLTEALEKNEELLkkihdDDKHILElqfTIQRLE 1359
Cdd:TIGR01612 1376 ENNKNIKDELDKSEKL---IKKIKDD-------------------INLEECKSKIESTL-----DDKDIDE---CIKKIK 1425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1360 ENtaakENLLLREREQNDATTKaqiESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQE-KDAIKKE 1438
Cdd:TIGR01612 1426 EL----KNHILSEESNIDTYFK---NADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEhIDKSKGC 1498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1439 LVEAG------ERNEELImkiEDTDKKIEHLQNAI--IKLEGDI-EAKDISLEAAREENDTIRKSLAEAqEKNEELLRKI 1509
Cdd:TIGR01612 1499 KDEADknakaiEKNKELF---EQYKKDVTELLNKYsaLAIKNKFaKTKKDSEIIIKEIKDAHKKFILEA-EKSEQKIKEI 1574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1510 SDNEYRIH---LLQDTAQKLQVDAISRLSSFvmekqESDAAKraLTEARERNEDLLKRNEDLLKRNDDLI-----KKIEE 1581
Cdd:TIGR01612 1575 KKEKFRIEddaAKNDKSNKAAIDIQLSLENF-----ENKFLK--ISDIKKKINDCLKETESIEKKISSFSidsqdTELKE 1647
|
730 740
....*....|....*....|....*....
gi 1002232322 1582 SSKTITQLQETLQRLEGKSTNLEAENQVL 1610
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKNIEDKKKEL 1676
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
890-1311 |
8.32e-09 |
|
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: 60.47 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERvEELTNR-LGLEKKLRTDLE--KSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSL 966
Cdd:pfam05622 3 SEAQEEK-DELAQRcHELDQQVSLLQEekNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 967 TSEIEglkalLVAEQEENDLtkkahANAQERNEELSKEVEDAdgkiKQLSDTVQRLEETiqerealllAERQEKEEASAv 1046
Cdd:pfam05622 82 RDDYR-----IKCEELEKEV-----LELQHRNEELTSLAEEA----QALKDEMDILRES---------SDKVKKLEATV- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1047 iaesqarnEAFASKLED-----------AEKQIDLLQETVQRFEEA--ITKLQSSVTIEKQQHEETVVQLAEAQAKIDEL 1113
Cdd:pfam05622 138 --------ETYKKKLEDlgdlrrqvkllEERNAEYMQRTLQLEEELkkANALRGQLETYKRQVQELHGKLSEESKKADKL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 LREAGDTDEKSTQLETTIQRLeesLTEKDALLTT--ERQETEATKKLLSEAQYKNEELLKKIEDADKSI--AHYHDTTQR 1189
Cdd:pfam05622 210 EFEYKKLEEKLEALQKEKERL---IIERDTLRETneELRCAQLQQAELSQADALLSPSSDPGDNLAAEImpAEIREKLIR 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1190 LEEnvtavENslKAERqhngaiMKQLADAQVEIGELQRNLEDADRRNNQLQD----SLQRLEENVGAKESLLLTEREQNA 1265
Cdd:pfam05622 287 LQH-----EN--KMLR------LGQEGSYRERLTELQQLLEDANRRKNELETqnrlANQRILELQQQVEELQKALQEQGS 353
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1266 ST-------------LKLLAEAHLEIDELIRKLED--------SDRKSDSLQSTIKRLEEDGIAKEA 1311
Cdd:pfam05622 354 KAedssllkqkleehLEKLHEAQSELQKKKEQIEElepkqdsnLAQKIDELQEALRKKDEDMKAMEE 420
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
940-1168 |
1.04e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 940 TAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTV 1019
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1020 QRLEETIQEREALLLAErqekeEASAVIAESQARN---EAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQH 1096
Cdd:COG3883 96 YRSGGSVSYLDVLLGSE-----SFSDFLDRLSALSkiaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1097 EETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEE 1168
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1431-1629 |
1.19e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1431 EKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKIS 1510
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1511 DNEYRIHLL------QDTAQKL-QVDAISRLSSF---VMEKQESD--AAKRALTEARERNEDLLKRNEDLLKRNDDLIKK 1578
Cdd:COG3883 97 RSGGSVSYLdvllgsESFSDFLdRLSALSKIADAdadLLEELKADkaELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1579 IEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATATPPSTAKSSASRS 1629
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1105-1612 |
1.71e-08 |
|
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: 59.99 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1105 EAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQ-------------------------ETEATKKLL 1159
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkeqakkaleyyqlkekleleeEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1160 SEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQL 1239
Cdd:pfam02463 233 KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDD 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1240 QDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSdrksdSLQSTIKRLEEDGIAKEALLLTEKQA 1319
Cdd:pfam02463 313 EEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL-----EKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1320 HEATRMTLTEALEKNEEllkKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDaTTKAQIESQERNEQLLKRFVD 1399
Cdd:pfam02463 388 SAAKLKEEELELKSEEE---KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELK-QGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1400 --VDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAK 1477
Cdd:pfam02463 464 elELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKV 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1478 DISLEAAREENDTIRKSLAEAQEKNEELLRKISDNeYRIHLLQDTAQKLQVDAISRLSSFVMEKQESDAAKRALTEARER 1557
Cdd:pfam02463 544 AISTAVIVEVSATADEVEERQKLVRALTELPLGAR-KLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1558 NEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQ 1612
Cdd:pfam02463 623 KVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1188-1623 |
1.84e-08 |
|
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: 59.75 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1188 QRLEENVTAVENSLK-AERQHNGAimkqLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNAS 1266
Cdd:pfam05557 5 IESKARLSQLQNEKKqMELEHKRA----RIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1267 TLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLeedgiakealllteKQAHEATRMTLTEALEKNEELLKKIHDDDK 1346
Cdd:pfam05557 81 KKKYLEALNKKLNEKESQLADAREVISCLKNELSEL--------------RRQIQRAELELQSTNSELEELQERLDLLKA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1347 HILELQFTIQRLEentaaKENLLLREREQNDATTKAQIESQERNEQLLK-------RFVDVDRKIDLLQDTIERIgeNST 1419
Cdd:pfam05557 147 KASEAEQLRQNLE-----KQQSSLAEAEQRIKELEFEIQSQEQDSEIVKnskselaRIPELEKELERLREHNKHL--NEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1420 IKDALLLSErqEKDAIKKELveagERNEELIMKIEDTDKKIEHLQ---NAIIKLEGDIEAKDISLEAAREENDTI----- 1491
Cdd:pfam05557 220 IENKLLLKE--EVEDLKRKL----EREEKYREEAATLELEKEKLEqelQSWVKLAQDTGLNLRSPEDLSRRIEQLqqrei 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1492 ----RKSLAEAQEKNEELLRKISDNEYRIHL--LQDTAQKLQvdaisRLSSFVMEKQesdaaKRALTEARERN------- 1558
Cdd:pfam05557 294 vlkeENSSLTSSARQLEKARRELEQELAQYLkkIEDLNKKLK-----RHKALVRRLQ-----RRVLLLTKERDgyraile 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1559 ------------EDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATATPPSTAK 1623
Cdd:pfam05557 364 sydkeltmsnysPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK 440
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1278-1611 |
2.13e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1278 IDELIR--KLEDSDRKSDSLQSTIKRLEEDgiAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDdkhilelqftI 1355
Cdd:PRK02224 155 IDDLLQlgKLEEYRERASDARLGVERVLSD--QRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEE----------I 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1356 QRLEENtaakenlllreREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTI-ERIGENSTIKDALllSERQEkda 1434
Cdd:PRK02224 223 ERYEEQ-----------REQARETRDEADEVLEEHEERREELETLEAEIEDLRETIaETEREREELAEEV--RDLRE--- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1435 ikkELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAkdisleaAREENDTIRKSLAEAQEKNEELLRKISDNEY 1514
Cdd:PRK02224 287 ---RLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE-------LRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1515 RIHLLQDTAQKLQVDAisrlssfvmekqesDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQ 1594
Cdd:PRK02224 357 RAEELREEAAELESEL--------------EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
330
....*....|....*..
gi 1002232322 1595 RLEGKSTNLEAENQVLR 1611
Cdd:PRK02224 423 ELREREAELEATLRTAR 439
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1134-1610 |
2.31e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 59.35 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1134 LEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDA----------DKSIAHY----HDTTQRLEENVTAVEN 1199
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEiqenkdlikeNNATRHLcnllKETCARSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1200 SLKAERQ----HNGAIMKQL-------ADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLL---TEREQNA 1265
Cdd:pfam05483 177 EREETRQvymdLNNNIEKMIlafeelrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLiqiTEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1266 STLK-LLAEAHLEIDELIRK-------LEDSDRKSDSLQstiKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEEL 1337
Cdd:pfam05483 257 KDLTfLLEESRDKANQLEEKtklqdenLKELIEKKDHLT---KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1338 LKKIHDDDKHILELQFTIQRLEENTAAKENLLLRER---EQNDATTK-AQIESQERNEQL----------------LKRF 1397
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQqrlEKNEDQLKiITMELQKKSSELeemtkfknnkeveleeLKKI 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1398 VDVDRKIDLLQDTIERIGE--NSTIKDALLLSERQEKDAIKKEL-VEAGERNEELIMK-IED--TDKKIEHLQNAIIKLE 1471
Cdd:pfam05483 414 LAEDEKLLDEKKQFEKIAEelKGKEQELIFLLQAREKEIHDLEIqLTAIKTSEEHYLKeVEDlkTELEKEKLKNIELTAH 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1472 GDI----------EAKDISLEAAREENDTIrkslaEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAISRLSSFVMEK 1541
Cdd:pfam05483 494 CDKlllenkeltqEASDMTLELKKHQEDII-----NCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKL 568
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1542 QESDAAKRALTEARERNEDLLKRNEDllkRNDDLIKKIEESSKTITQLQETLQRLEGKSTnleAENQVL 1610
Cdd:pfam05483 569 DKSEENARSIEYEVLKKEKQMKILEN---KCNNLKKQIENKNKNIEELHQENKALKKKGS---AENKQL 631
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
992-1138 |
3.55e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.47 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 992 ANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQ-----ARN----EAFASKLE 1062
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlgnVRNnkeyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1063 DAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDEllrEAGDTDEKSTQLETTIQRLEESL 1138
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
942-1390 |
4.19e-08 |
|
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: 58.81 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 942 MQERESAKKAVEEALEQEREKISSltseieglkallvaeqeendltKKAHANAQERNEELSKEVEDADGKIKQLSDTVQR 1021
Cdd:COG3096 274 MRHANERRELSERALELRRELFGA----------------------RRQLAEEQYRLVEMARELEELSARESDLEQDYQA 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1022 LEETIQE-REALLLAERqekeeasavIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQssvtiekQQHEETV 1100
Cdd:COG3096 332 ASDHLNLvQTALRQQEK---------IERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAE-------EEVDSLK 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQLAEAQAKIDELLREAGdtdekstQLETTIQRLEES--------LTEKDA---LLTTERQETEATKKLLSEAQykneel 1169
Cdd:COG3096 396 SQLADYQQALDVQQTRAI-------QYQQAVQALEKAralcglpdLTPENAedyLAAFRAKEQQATEEVLELEQ------ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1170 lkKIEDADKSIAHYHDTTQRLEENVTAVENS---------LKAERQHNgAIMKQLADAQVEIGELQRNLEDADRRNNQLQ 1240
Cdd:COG3096 463 --KLSVADAARRQFEKAYELVCKIAGEVERSqawqtarelLRRYRSQQ-ALAQRLQQLRAQLAELEQRLRQQQNAERLLE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1241 DSLQRLEENVGAKESLLLTEREQNASTLKLLAEAhleiDELIRKLEDSDRKSDSLQSTIKRLEedgiAKEALLLTEKQAH 1320
Cdd:COG3096 540 EFCQRIGQQLDAAEELEELLAELEAQLEELEEQA----AEAVEQRSELRQQLEQLRARIKELA----ARAPAWLAAQDAL 611
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1321 EATRMTLTEALEKNEELlkkihdddkhilelqftiqrleenTAAKENLLLRERE-----QNDATTKAQIESQERN 1390
Cdd:COG3096 612 ERLREQSGEALADSQEV------------------------TAAMQQLLEREREatverDELAARKQALESQIER 662
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1211-1615 |
4.86e-08 |
|
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: 58.49 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1211 IMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQ----NASTLKLLAEAHLEIdELIRKLE 1286
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKinklNSDLSKINSEIKNDK-EQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1287 DsdrKSDSLQSTIKRLEEdgiaKEALLLTEKQAHEATrmtLTEALEKNEELLKKIHD--DDKHILELQftIQRLEENTAa 1364
Cdd:TIGR04523 124 V---ELNKLEKQKKENKK----NIDKFLTEIKKKEKE---LEKLNNKYNDLKKQKEEleNELNLLEKE--KLNIQKNID- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1365 KENLLLREREQNDATTKAQIEsqeRNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGE 1444
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQ---KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1445 RNEELIMKIEDTDKKIEHLQNAIIKLEGDIEakDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQ 1524
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEIS--DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1525 KLQVDaISRLSSFVMEKQESDAAKRALTEARER-NEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNL 1603
Cdd:TIGR04523 346 QLKKE-LTNSESENSEKQRELEEKQNEIEKLKKeNQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410
....*....|..
gi 1002232322 1604 EAENQVLRQQAT 1615
Cdd:TIGR04523 425 EKEIERLKETII 436
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
886-1388 |
5.09e-08 |
|
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: 58.65 E-value: 5.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEKSK------VAEVSKLQAALneMEQRMQDVTAMQERESAKKAVEEALEQE 959
Cdd:pfam01576 571 LEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQkkfdqmLAEEKAISARY--AEERDRAEAEAREKETRALSLARALEEA 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 960 REKISsltsEIEGLKALLVAEQEE-----NDLTKKAHANAQERnEELSKEVEDADGKIKQLSDTVQ-------RLEETIQ 1027
Cdd:pfam01576 649 LEAKE----ELERTNKQLRAEMEDlvsskDDVGKNVHELERSK-RALEQQVEEMKTQLEELEDELQatedaklRLEVNMQ 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1028 ------EREallLAERQEKEEASAVIAESQARNeaFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVV 1101
Cdd:pfam01576 724 alkaqfERD---LQARDEQGEEKRRQLVKQVRE--LEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVK 798
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1102 QLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIA 1181
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKS 878
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEdADRRNNQLQDSLQRLEENVGAKESLLLTER 1261
Cdd:pfam01576 879 ALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELA-AERSTSQKSESARQQLERQNKELKAKLQEM 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQNASTLKLLAEAHLE--IDELIRKLEDSDRKSDSLQSTIKRLEEDgiAKEALLLTEKQAHEATRMtlTEALEKNEELLK 1339
Cdd:pfam01576 958 EGTVKSKFKSSIAALEakIAQLEEQLEQESRERQAANKLVRRTEKK--LKEVLLQVEDERRHADQY--KDQAEKGNSRMK 1033
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1002232322 1340 KIhdddKHILElqftiQRLEENTAAKENLLLREREQNDATTKAQIESQE 1388
Cdd:pfam01576 1034 QL----KRQLE-----EAEEEASRANAARRKLQRELDDATESNESMNRE 1073
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1301-1615 |
5.11e-08 |
|
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: 58.44 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1301 RLEEDGIAKEALL-LTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDAT 1379
Cdd:pfam02463 164 GSRLKRKKKEALKkLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1380 TKAQIEsQERNEQLLKRFVDVDRKIDL---LQDTIERIGENSTIKDALLLSERQEKdaiKKELVEAGERNEELIMKIEDT 1456
Cdd:pfam02463 244 ELLRDE-QEEIESSKQEIEKEEEKLAQvlkENKEEEKEKKLQEEELKLLAKEEEEL---KSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1457 DKKIEHLQNAIIKLEGDIEAKDI---SLEAAREENDTIRKSLAEAQEKNEELLRKISDneyrihlLQDTAQKLQVDAISR 1533
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKelkELEIKREAEEEEEEELEKLQEKLEQLEEELLA-------KKKLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1534 LSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSK---TITQLQETLQRLEGKSTNLEAENQVL 1610
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQgklTEEKEELEKQELKLLKDELELKKSED 472
|
....*
gi 1002232322 1611 RQQAT 1615
Cdd:pfam02463 473 LLKET 477
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
912-1591 |
6.97e-08 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 58.30 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 912 TDLEKSkvaeVSKLQAALNEMEqrmqdvTAMQERESAKKAVEEaleqEREKISSLTSEIEGLKALLV---AEQEENDLTK 988
Cdd:PTZ00440 453 NELKKS----INQLKTLISIMK------SFYDLIISEKDSMDS----KEKKESSDSNYQEKVDELLQiinSIKEKNNIVN 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 989 KAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETI--QEREALLLAERQEK----EEASAVIAESQARNEAFASKLE 1062
Cdd:PTZ00440 519 NNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIkdEKLKRSMKNDIKNKikyiEENVDHIKDIISLNDEIDNIIQ 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1063 DAEKQIDLLQETVQRFEEAITKLQSSV-TIEKQQHEETVVQLAEAQAKIDE----LLREAGDTDEKSTQLETTIQRLEEs 1137
Cdd:PTZ00440 599 QIEELINEALFNKEKFINEKNDLQEKVkYILNKFYKGDLQELLDELSHFLDdhkyLYHEAKSKEDLQTLLNTSKNEYEK- 677
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1138 LTEKDA--------LLTTERQETEATKKLLSEAQYKN---------EELLKKIEDADKSIAHYHDTTQRLE--------- 1191
Cdd:PTZ00440 678 LEFMKSdnidniikNLKKELQNLLSLKENIIKKQLNNieqdisnslNQYTIKYNDLKSSIEEYKEEEEKLEvykhqiinr 757
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1192 ------------ENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLT 1259
Cdd:PTZ00440 758 knefilhlyendKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQ 837
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1260 EREQNASTLKLLAEAHLE---------IDELIRKLEDSDRKSDSLQS---TIKRLEEDGIAKEALLLTEKQaheatrmtL 1327
Cdd:PTZ00440 838 LLQKFPTEDENLNLKELEkefnennqiVDNIIKDIENMNKNINIIKTlniAINRSNSNKQLVEHLLNNKID--------L 909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1328 TEALEKNEELLKK---IHDDDKHILE--LQFTIQRLEE--NTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDV 1400
Cdd:PTZ00440 910 KNKLEQHMKIINTdniIQKNEKLNLLnnLNKEKEKIEKqlSDTKINNLKMQIEKTLEYYDKSKENINGNDGTHLEKLDKE 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1401 DRKIDLLQDTIERIGENSTIKDAlllserQEKDAIKKELVEAGERNEELIMKI-----EDTDKKIEHLQNAIIKLEgdie 1475
Cdd:PTZ00440 990 KDEWEHFKSEIDKLNVNYNILNK------KIDDLIKKQHDDIIELIDKLIKEKgkeieEKVDQYISLLEKMKTKLS---- 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1476 AKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNeyrihllqdtaqKLQVDAISRLSSfvMEKQESDAAKRALTEAR 1555
Cdd:PTZ00440 1060 SFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDEN------------KNKLIEIKNKSH--EHVVNADKEKNKQTEHY 1125
|
730 740 750
....*....|....*....|....*....|....*.
gi 1002232322 1556 ERNEDLLkrnEDLLKRNDDLIKKIEESSKTITQLQE 1591
Cdd:PTZ00440 1126 NKKKKSL---EKIYKQMEKTLKELENMNLEDITLNE 1158
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
903-1311 |
8.03e-08 |
|
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: 57.66 E-value: 8.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 903 RLGLEKKLRTDLEKSKVAEVSKLQAALNEME--------QRMQDVTAMQERESAKKAVEEAlEQEREKISSLTSEIEGLK 974
Cdd:COG5185 181 IFGLTLGLLKGISELKKAEPSGTVNSIKESEtgnlgsesTLLEKAKEIINIEEALKGFQDP-ESELEDLAQTSDKLEKLV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 975 allvaeQEENDLTKKAHANAQERNEELSKEVEDAdgkIKQLSDTVQRLEETIQEREAlllaeRQEKEEASAVIAESQARN 1054
Cdd:COG5185 260 ------EQNTDLRLEKLGENAESSKRLNENANNL---IKQFENTKEKIAEYTKSIDI-----KKATESLEEQLAAAEAEQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EaFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETvVQLAEAQAKIDELlreagdtdekSTQLETTIQRL 1134
Cdd:COG5185 326 E-LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGE-VELSKSSEELDSF----------KDTIESTKESL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1135 EESLTekdALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAhyhdttQRLEENVTAVENSLKAERQHNGAIMKQ 1214
Cdd:COG5185 394 DEIPQ---NQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNE------EVSKLLNELISELNKVMREADEESQSR 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1215 LADAQVEIG-ELQRNLEDADRRNNQLQDSLQRLEEnvgakeslllTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSD 1293
Cdd:COG5185 465 LEEAYDEINrSVRSKKEDLNEELTQIESRVSTLKA----------TLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG 534
|
410
....*....|....*...
gi 1002232322 1294 SLQstIKRLEEDGIAKEA 1311
Cdd:COG5185 535 YAH--ILALENLIPASEL 550
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1011-1206 |
8.72e-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: 56.70 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1011 KIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSvt 1090
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1091 IEKQQHE---------------------------ETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDA 1143
Cdd:COG4942 99 LEAQKEElaellralyrlgrqpplalllspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1144 LLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQ 1206
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
890-1233 |
9.21e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQEResaKKAVEEALEQEREKISSLTSE 969
Cdd:COG4372 5 GEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLEEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 970 IEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAE 1049
Cdd:COG4372 82 LEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1050 SQARNEAFASKLEDAEKQiDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLET 1129
Cdd:COG4372 162 LQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1130 TIQRLEEsltEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNG 1209
Cdd:COG4372 241 ALELEED---KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
330 340
....*....|....*....|....
gi 1002232322 1210 AIMKQLADAQVEIGELQRNLEDAD 1233
Cdd:COG4372 318 LAALLELAKKLELALAILLAELAD 341
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
892-1276 |
1.19e-07 |
|
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: 57.36 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 892 KLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMeqrmqdVTAMQERESAKKAVEEALEQEREKISSLTSEIE 971
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM------LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 972 GLKALLvAEQEENDLTKKAHANAQER-------NEELSKEVEDADGKIKQLSDTVQR--LEETIQERealllaeRQEKEE 1042
Cdd:TIGR00606 762 RLKNDI-EEQETLLGTIMPEEESAKVcltdvtiMERFQMELKDVERKIAQQAAKLQGsdLDRTVQQV-------NQEKQE 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1043 ASAVIAESQARNEAFASKLEDAEKQIDLLQETVQrfEEAITKLQSSVTIEKQQHEETvvQLAEAQAKIDELLREAGDTDE 1122
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTN--ELKSEKLQIGTNLQRRQQFEE--QLVELSTEVQSLIREIKDAKE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1123 KSTQLETTI----QRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDA---------------DKSIAHY 1183
Cdd:TIGR00606 910 QDSPLETFLekdqQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGkddylkqketelntvNAQLEEC 989
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1184 HDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQV--EIGELQRNLEDADRRNNQLQ-----DSLQRLEEN---VGAK 1253
Cdd:TIGR00606 990 EKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRenELKEVEEELKQHLKEMGQMQvlqmkQEHQKLEENidlIKRN 1069
|
410 420
....*....|....*....|...
gi 1002232322 1254 ESLLLTeREQNASTLKLLAEAHL 1276
Cdd:TIGR00606 1070 HVLALG-RQKGYEKEIKHFKKEL 1091
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
881-1204 |
1.22e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.83 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 881 RDTQALKVAKEKLEERVEELTNRLG-LEKKLRTDLEK----------------SKVAEVSKLQAALNEMEQRM----QDV 939
Cdd:pfam07888 59 KEKERYKRDREQWERQRRELESRVAeLKEELRQSREKheeleekykelsasseELSEEKDALLAQRAAHEARIreleEDI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 940 TAMQEResakkAVEEALEQERekissLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTV 1019
Cdd:pfam07888 139 KTLTQR-----VLERETELER-----MKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1020 QRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSvtieKQQHEET 1099
Cdd:pfam07888 209 LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQA----RLQAAQL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1100 VVQLAEAQAKIDE-----------LLREAGDTDEKSTQLETTIQRLEESL----TEKDALLTTERQETEATKKLLSEAQY 1164
Cdd:pfam07888 285 TLQLADASLALREgrarwaqeretLQQSAEADKDRIEKLSAELQRLEERLqeerMEREKLEVELGREKDCNRVQLSESRR 364
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1002232322 1165 KNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAE 1204
Cdd:pfam07888 365 ELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1048-1248 |
1.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1048 AESQARNEAFASKLEDAEKQIDLLQETVQRF----------EEAITKLQSSVTIEKQQhEETVVQLAEAQAKIDELLREA 1117
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEFrqknglvdlsEEAKLLLQQLSELESQL-AEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1118 GDTDEKSTQL--ETTIQRLEESLTEkdalltTERQETEATKKLLSEA-QYKneELLKKIEDADKSIAH----YHDTTQRL 1190
Cdd:COG3206 250 GSGPDALPELlqSPVIQQLRAQLAE------LEAELAELSARYTPNHpDVI--ALRAQIAALRAQLQQeaqrILASLEAE 321
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1191 EENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRnleDADRRNNQLQDSLQRLEE 1248
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLER---EVEVARELYESLLQRLEE 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
877-1448 |
1.31e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 57.12 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 877 RMAARDTQALKVAKEKLEERVEELTnRLGLE---KKLRTDLEKSK--VAEVSKLQAALNEMEQRMQDVTAMQE--RESAK 949
Cdd:PRK10246 257 QEASRRQQALQQALAAEEKAQPQLA-ALSLAqpaRQLRPHWERIQeqSAALAHTRQQIEEVNTRLQSTMALRAriRHHAA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 950 KAVEEALEQ---------EREKISSLTSEIEGLKALLvaeqeendltkkahanAQERNEElskevedadgkiKQLSDTVQ 1020
Cdd:PRK10246 336 KQSAELQAQqqslntwlaEHDRFRQWNNELAGWRAQF----------------SQQTSDR------------EQLRQWQQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1021 RLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTI--------- 1091
Cdd:PRK10246 388 QLTHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQrnaalnemr 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1092 ----EKQQHEETVVQLAEAQAKIDELLR----------------------------EAGDTDEKSTQLETTIQRL-EESL 1138
Cdd:PRK10246 468 qrykEKTQQLADVKTICEQEARIKDLEAqraqlqagqpcplcgstshpaveayqalEPGVNQSRLDALEKEVKKLgEEGA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1139 T---EKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENvTAVENSLKAERQHNgAIMKQL 1215
Cdd:PRK10246 548 AlrgQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQ-EEHERQLRLLSQRH-ELQGQI 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1216 ADAQVEIGELQRNLEdadRRNNQLQDSLQRLEENVGAK--ESLLLTEREQNASTLKLLAEAHLEIDELIRKLE------- 1286
Cdd:PRK10246 626 AAHNQQIIQYQQQIE---QRQQQLLTALAGYALTLPQEdeEASWLATRQQEAQSWQQRQNELTALQNRIQQLTplletlp 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1287 DSDRKSDSLQSTI----KRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKH-----ILELQfTIQR 1357
Cdd:PRK10246 703 QSDDLPHSEETVAldnwRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDDQQaflaaLLDEE-TLTQ 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1358 LEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENST----IKDALLLSE--RQE 1431
Cdd:PRK10246 782 LEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQLRENTTrqgeIRQQLKQDAdnRQQ 861
|
650
....*....|....*..
gi 1002232322 1432 KDAIKKELVEAGERNEE 1448
Cdd:PRK10246 862 QQALMQQIAQATQQVED 878
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
914-1602 |
1.44e-07 |
|
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: 57.37 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 914 LEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEA-------------LEQEREKISSLTSEIEGLKALLVAE 980
Cdd:TIGR01612 512 MELYKPDEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAknwkkliheikkeLEEENEDSIHLEKEIKDLFDKYLEI 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 981 QEEN--------DLTKKAHaNAQERNE------ELSKEVEDADGKIKQLSDTVQ-RLEETIQEREALLLAERQE------ 1039
Cdd:TIGR01612 592 DDEIiyinklklELKEKIK-NISDKNEyikkaiDLKKIIENNNAYIDELAKISPyQVPEHLKNKDKIYSTIKSElskiye 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1040 ------KEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSvTIEKQQHE--ETVV---------- 1101
Cdd:TIGR01612 671 ddidalYNELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLS-NIENKKNEllDIIVeikkhihgei 749
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1102 ------------------------------QLAEAQAKIDELL--------------REAGDTDEKSTQLETTIQRLEES 1137
Cdd:TIGR01612 750 nkdlnkiledfknkekelsnkindyakekdELNKYKSKISEIKnhyndqinidnikdEDAKQNYDKSKEYIKTISIKEDE 829
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1138 LTE--------KDALL------------------TTERQETEATKKLLSEA----------------------------Q 1163
Cdd:TIGR01612 830 IFKiinemkfmKDDFLnkvdkfinfennckekidSEHEQFAELTNKIKAEIsddklndyekkfndskslineinksieeE 909
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1164 YKNEELLKKI-------EDADKSIAHYHDTTQRLEE----NVTAVENSLKAERQHNGAIMKQLADAQVEIGEL--QRNLE 1230
Cdd:TIGR01612 910 YQNINTLKKVdeyikicENTKESIEKFHNKQNILKEilnkNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAfkDASLN 989
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1231 DADRRNNQLQDSLQRLEENVGA-KESLLLTEREQN--------------------------ASTLKLLAEAHLEI----- 1278
Cdd:TIGR01612 990 DYEAKNNELIKYFNDLKANLGKnKENMLYHQFDEKekatndieqkiedanknipnieiaihTSIYNIIDEIEKEIgknie 1069
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1279 ---DELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLlteKQAHEATRM-----TLTEALEKNEELLKKIHD-DDKHIL 1349
Cdd:TIGR01612 1070 llnKEILEEAEINITNFNEIKEKLKHYNFDDFGKEENI---KYADEINKIkddikNLDQKIDHHIKALEEIKKkSENYID 1146
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1350 ELQFTIQRLE---ENTAAKENLLLREREQNDATTKaqIESQERNEQLLKRFVDVDRKIDLLQDTIERI-GENSTIKDAL- 1424
Cdd:TIGR01612 1147 EIKAQINDLEdvaDKAISNDDPEEIEKKIENIVTK--IDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVkGINLSYGKNLg 1224
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1425 -LLSERQEKDAIKKE-LVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISleaareeNDTIRKSLAEAQEKN 1502
Cdd:TIGR01612 1225 kLFLEKIDEEKKKSEhMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNIS-------HDDDKDHHIISKKHD 1297
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1503 EellrKISD-NEYRIHLLQDTAQKLQVDAISR-LSSFVMEKQESDAA--------------------KRALTEARERNED 1560
Cdd:TIGR01612 1298 E----NISDiREKSLKIIEDFSEESDINDIKKeLQKNLLDAQKHNSDinlylneianiynilklnkiKKIIDEVKEYTKE 1373
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1002232322 1561 LLKRNEDL---LKRNDDLIKKIEESSKTITQLQETLQRLEGKSTN 1602
Cdd:TIGR01612 1374 IEENNKNIkdeLDKSEKLIKKIKDDINLEECKSKIESTLDDKDID 1418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
878-1124 |
1.58e-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: 55.93 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 878 MAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKvaevSKLQAALNEMEQRMQDVTAMQeresakKAVEEALE 957
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEE----KALLKQLAALERRIAALARRI------RALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 958 QEREKISSLTSEIEGLKALLVAEQEE-NDLTKKAHANAQERNEELSKEVEDADGKI------KQLSDTVQRLEETIQERE 1030
Cdd:COG4942 80 ALEAELAELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAVrrlqylKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLAERQEKEEASAVIAESQARNEAfaskledaekQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKI 1110
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEE----------ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI 229
|
250
....*....|....
gi 1002232322 1111 DELLREAGDTDEKS 1124
Cdd:COG4942 230 ARLEAEAAAAAERT 243
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
890-1108 |
1.68e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEELTNRLgleKKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQEResakKAVEEALEQEREKISSLTSE 969
Cdd:COG3206 163 EQNLELRREEARKAL---EFLEEQLPELR-KELEEAEAALEEFRQKNGLVDLSEEA----KLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 970 IEGLKALL--VAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDT-------VQRLEETIQEREALLLAERQE- 1039
Cdd:COG3206 235 LAEAEARLaaLRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQRi 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1040 KEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEaitkLQSSVTIEKQQHEETVVQLAEAQA 1108
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
873-1086 |
2.17e-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: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 873 LRQLRmaaRDTQALKVAKEKLEERVEELTNRLgleKKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQERESAKKAV 952
Cdd:COG4942 29 LEQLQ---QEIAELEKELAALKKEEKALLKQL---AALERRIAALA-RRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 953 EEALEQEREKISSLTSEIEGLKALLVAEqEENDLTKKAHAnAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAL 1032
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLLSPE-DFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1033 LLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQ 1086
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1094-1613 |
2.46e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.07 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1094 QQHEETVVQLAEAQAKIDELL-REAGDTDEKSTQlettiQRLEESLtekDALLTTERQETEatkkllseaqykNEELLKK 1172
Cdd:PRK11281 29 AASNGDLPTEADVQAQLDALNkQKLLEAEDKLVQ-----QDLEQTL---ALLDKIDRQKEE------------TEQLKQQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1173 IEDADKSIAHYHDTTQRLEENVTAVENslkaerqhngaimKQLADAQVEigELQRNLedadrrnNQLQDSLQRLEENVGA 1252
Cdd:PRK11281 89 LAQAPAKLRQAQAELEALKDDNDEETR-------------ETLSTLSLR--QLESRL-------AQTLDQLQNAQNDLAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1253 KESLLLT-----EREQNAstlklLAEAHLEIDELIRKLEDSDRKSDSLQSTIKrleedgiakeALLLTEKQAHEAT---R 1324
Cdd:PRK11281 147 YNSQLVSlqtqpERAQAA-----LYANSQRLQQIRNLLKGGKVGGKALRPSQR----------VLLQAEQALLNAQndlQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1325 MTLTEALEKNEELLKKIHDddkhilELQFTIQRLEENTAAKENLLLRER-EQNDATTKAQIESQERNeqllkrfvdvdrk 1403
Cdd:PRK11281 212 RKSLEGNTQLQDLLQKQRD------YLTARIQRLEHQLQLLQEAINSKRlTLSEKTVQEAQSQDEAA------------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1404 idllqdtieRIGENStikdaLLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEA 1483
Cdd:PRK11281 273 ---------RIQANP-----LVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERNIKEQISVLKGSLLL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1484 AREENDTiRKSLAEAQEkNEELLRKISDneYRIHLLQDTAQKlqvDAISRLSSFVmEKQESDAAKRALTEARERNEDLLK 1563
Cdd:PRK11281 339 SRILYQQ-QQALPSADL-IEGLADRIAD--LRLEQFEINQQR---DALFQPDAYI-DKLEAGHKSEVTDEVRDALLQLLD 410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1564 RNEDLLkrnDDLIK----KIEESsktITqLQETLQRLEGKSTNLEAenqVLRQQ 1613
Cdd:PRK11281 411 ERRELL---DQLNKqlnnQLNLA---IN-LQLNQQQLLSVSDSLQS---TLTQQ 454
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1370-1622 |
4.56e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.31 E-value: 4.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1370 LREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIG-ENSTIKDALLlseRQEKDAIKKELVEAGERNEE 1448
Cdd:COG4913 237 LERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRlWFAQRRLELL---EAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1449 LIMKIEDTDKKIEHLQNAIIKLEGDieakdiSLEAAREENDTIRKSLAEAQEKNEELlrkisdneyrihllQDTAQKLQV 1528
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARL--------------EALLAALGL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1529 DAISRLSSFVMEKQESDAAKRALTEARERNEDLLkrnedllkrnDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQ 1608
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEAL----------AEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250
....*....|....*
gi 1002232322 1609 VLRQQ-ATATPPSTA 1622
Cdd:COG4913 444 ALRDAlAEALGLDEA 458
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1134-1612 |
4.82e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 55.36 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1134 LEESLTEKDALLTtERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMK 1213
Cdd:TIGR00618 158 LKAKSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1214 QLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKleDSDRKSD 1293
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ--QAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1294 SLQSTiKRLEEDGIAKEALLLTEKQAHEATRMTLtEALEKNEELLKKIHDDDKHILElqftiqRLEENTAAKENLLLRER 1373
Cdd:TIGR00618 315 ELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLL-QTLHSQEIHIRDAHEVATSIRE------ISCQQHTLTQHIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1374 EQNDATTK----AQIESQERNEQ-----LLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGE 1444
Cdd:TIGR00618 387 QKTTLTQKlqslCKELDILQREQatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1445 RNEELIMKIEdtDKKIEHLQNAIIKLEgdiEAKdiSLEAAREENDTIRKSLAEAQEKNEELL------RKISDNEYRIHL 1518
Cdd:TIGR00618 467 SLKEREQQLQ--TKEQIHLQETRKKAV---VLA--RLLELQEEPCPLCGSCIHPNPARQDIDnpgpltRRMQRGEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1519 LQDTAQKLQVDAIS---RLSSFVMEKQESDAAKRALTEARERNEDLLkrnEDLLKRNDDLIKKIEESSKTITQLQETLQR 1595
Cdd:TIGR00618 540 LETSEEDVYHQLTSerkQRASLKEQMQEIQQSFSILTQCDNRSKEDI---PNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
490
....*....|....*..
gi 1002232322 1596 LEGKsTNLEAENQVLRQ 1612
Cdd:TIGR00618 617 LLRK-LQPEQDLQDVRL 632
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
884-1514 |
4.90e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.35 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEE--LTNRL-GLEKKLRtDLEKSkVAEVSKLQAALNEMEQRM-QDVTA-------MQERESAKKAV 952
Cdd:PRK04863 493 EAWDVARELLRRLREQrhLAEQLqQLRMRLS-ELEQR-LRQQQRAERLLAEFCKRLgKNLDDedeleqlQEELEARLESL 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 953 EEALEQEREKISSLTSEIEGLKallvaeQEENDLTKKAHA--NAQERNEELSKEVEDADGKIKQLSDTVQRLEEtiQERE 1030
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQ------ARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLE--RERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 AlllaeRQEKEEasavIAESQARNEAFASKLEDAEKQIDllqETVQRFEE-----AITKLQSSVTIEKQ----------Q 1095
Cdd:PRK04863 643 L-----TVERDE----LAARKQALDEEIERLSQPGGSED---PRLNALAErfggvLLSEIYDDVSLEDApyfsalygpaR 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1096 HEETVVQLAEAQAKIDELlreaGDTDEKSTQLETTIQRLEESLTEKDALL------TTERQ------------ETEATKK 1157
Cdd:PRK04863 711 HAIVVPDLSDAAEQLAGL----EDCPEDLYLIEGDPDSFDDSVFSVEELEkavvvkIADRQwrysrfpevplfGRAAREK 786
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1158 LLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVtAVENSLKAERQHNGAimkqLADAQVEIGELQRNLEDADRRNN 1237
Cdd:PRK04863 787 RIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFI-GSHLAVAFEADPEAE----LRQLNRRRVELERALADHESQEQ 861
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1238 QLQDSLQRLEENVGAKESLLltereqnaSTLKLLAEAHL-----EIDELIRKLEDSDRKSDSLQSTIKRLEEdgIAkeAL 1312
Cdd:PRK04863 862 QQRSQLEQAKEGLSALNRLL--------PRLNLLADETLadrveEIREQLDEAEEAKRFVQQHGNALAQLEP--IV--SV 929
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1313 LLTEKQAHEATRMTLTEALEKNEELLKKIHDDD-----KHILELQFTIQRLEENTAAKENLL--LREREQNDATTKAQI- 1384
Cdd:PRK04863 930 LQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTevvqrRAHFSYEDAAEMLAKNSDLNEKLRqrLEQAEQERTRAREQLr 1009
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1385 ESQERNEQLLKRFVDV----DRKIDLLQDTIERIGENSTIKDALLLSE-RQEKDAIKKELVEAGERNEELIMKIEDTDKK 1459
Cdd:PRK04863 1010 QAQAQLAQYNQVLASLkssyDAKRQMLQELKQELQDLGVPADSGAEERaRARRDELHARLSANRSRRNQLEKQLTFCEAE 1089
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1460 IEHLQNAIIKLEGDIEAKDISLEAAR----------EENDTIRK------------SLAEAQEKNEELLR-KISDNEY 1514
Cdd:PRK04863 1090 MDNLTKKLRKLERDYHEMREQVVNAKagwcavlrlvKDNGVERRlhrrelaylsadELRSMSDKALGALRlAVADNEH 1167
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
884-1599 |
5.61e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEeRVEELTNRLGLEKKLRT---DLEKsKVAEVSKLQAALNEMEQRM-QDVTAMQEREsakkAVEEALEQE 959
Cdd:COG3096 492 QAWQTARELLR-RYRSQQALAQRLQQLRAqlaELEQ-RLRQQQNAERLLEEFCQRIgQQLDAAEELE----ELLAELEAQ 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 960 REKISSLTSEIEGLKALLVAEQEE-----NDLTKKAHA--NAQER----NEELSKEVEDADGKIKQLSDTVQRLEETIQE 1028
Cdd:COG3096 566 LEELEEQAAEAVEQRSELRQQLEQlrariKELAARAPAwlAAQDAlerlREQSGEALADSQEVTAAMQQLLEREREATVE 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1029 REalLLAERQEKeeasaviAESQARNEAFASKLEDAEkqidlLQETVQRFE-EAITKLQSSVTIEKQ----------QHE 1097
Cdd:COG3096 646 RD--ELAARKQA-------LESQIERLSQPGGAEDPR-----LLALAERLGgVLLSEIYDDVTLEDApyfsalygpaRHA 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1098 ETVVQLAEAQAKIDELlreaGDTDEKSTQLETTIQRLEESLTEKDAL------LTTERQ---ETEATKKLLSEAQYKNE- 1167
Cdd:COG3096 712 IVVPDLSAVKEQLAGL----EDCPEDLYLIEGDPDSFDDSVFDAEELedavvvKLSDRQwrySRFPEVPLFGRAAREKRl 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1168 ELLKkiEDADKSIAHYHDT------TQRLEEN---------VTAVENSLKAErqhngaimkqLADAQVEIGELQRNLEDA 1232
Cdd:COG3096 788 EELR--AERDELAEQYAKAsfdvqkLQRLHQAfsqfvgghlAVAFAPDPEAE----------LAALRQRRSELERELAQH 855
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1233 DRRNNQLQDSLQRLEENVGAKESLLltereqnaSTLKLLAEAHLE--IDELIRKLEDSDRKSDSLQSTIKRLEE-DGIAk 1309
Cdd:COG3096 856 RAQEQQLRQQLDQLKEQLQLLNKLL--------PQANLLADETLAdrLEELREELDAAQEAQAFIQQHGKALAQlEPLV- 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1310 eALLLTEKQAHEATRMTLTEALEKNEELlkkihddDKHILELQFTIQRLEE----------------NTAAKENLLLRER 1373
Cdd:COG3096 927 -AVLQSDPEQFEQLQADYLQAKEQQRRL-------KQQIFALSEVVQRRPHfsyedavgllgensdlNEKLRARLEQAEE 998
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1374 EQNDATTKAQiESQERNEQLLKRFVDV----DRKIDLLQDTIERIGEnstikdallLSERQEKDAIKKELVEAGERNEEL 1449
Cdd:COG3096 999 ARREAREQLR-QAQAQYSQYNQVLASLkssrDAKQQTLQELEQELEE---------LGVQADAEAEERARIRRDELHEEL 1068
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1450 IMkiedTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDN--EYRIHllqdtaqklq 1527
Cdd:COG3096 1069 SQ----NRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNdvERRLH---------- 1134
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1528 vdaisRLSSFVMEKQE----SDAAKRALTEARERNE---DLLKRNEDLLK------------------------RNDDLI 1576
Cdd:COG3096 1135 -----RRELAYLSADElrsmSDKALGALRLAVADNEhlrDALRLSEDPRRperkvqfyiavyqhlrerirqdiiRTDDPV 1209
|
810 820
....*....|....*....|...
gi 1002232322 1577 KKIEESSKTITQLQETLQRLEGK 1599
Cdd:COG3096 1210 EAIEQMEIELARLTEELTSREQK 1232
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
875-1132 |
6.45e-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: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLE---ERVEELtNRLGLEK-----KLRTDLE---KSKVAEVSKlQAALNEMEQRMQDVTAMQ 943
Cdd:pfam17380 352 RIRQEERKRELERIRQEEIAmeiSRMREL-ERLQMERqqkneRVRQELEaarKVKILEEER-QRKIQQQKVEMEQIRAEQ 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 944 E--RESAKKAVEEALEQEREKISSltSEIEGLKALLVAEQEENDLTKKAHanAQERNEELSKEVEDADGKI--KQLSDTV 1019
Cdd:pfam17380 430 EeaRQREVRRLEEERAREMERVRL--EEQERQQQVERLRQQEEERKRKKL--ELEKEKRDRKRAEEQRRKIleKELEERK 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1020 QRLEETIQEREALllaeRQEKEEASAVIAESQARNEAfaskLEDAEKQIDLlqETVQRFEEAITKlqssVTIEKQQheet 1099
Cdd:pfam17380 506 QAMIEEERKRKLL----EKEMEERQKAIYEEERRREA----EEERRKQQEM--EERRRIQEQMRK----ATEERSR---- 567
|
250 260 270
....*....|....*....|....*....|...
gi 1002232322 1100 vvqlAEAQAKIDELLREAGDTDEKSTQLETTIQ 1132
Cdd:pfam17380 568 ----LEAMEREREMMRQIVESEKARAEYEATTP 596
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
911-1507 |
7.09e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 911 RTDLEKSKvAEVSKLQAALNEMEqrMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKA 990
Cdd:pfam05557 1 RAELIESK-ARLSQLQNEKKQME--LEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 991 HANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDL 1070
Cdd:pfam05557 78 NRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1071 LQETVQRFEEAITKLQS-SVTIEKQQHEETVVQLAEA-QAKIDELLREAGDTDEKSTQLETTIqRLEESLTEKDALLTTE 1148
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSeLARIPELEKELERLREHNKHLNENI-ENKLLLKEEVEDLKRK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1149 RQETEATKKLLSEAQYKNEELLKKIEdADKSIAHYHDTTQRLEEnvtAVENSLKAERQHNGAIMKQLADAQVEIGELQRN 1228
Cdd:pfam05557 237 LEREEKYREEAATLELEKEKLEQELQ-SWVKLAQDTGLNLRSPE---DLSRRIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1229 LEDADRRNNQLQDSLqrLEENVGAKESLLLTEREQnastlKLLAEAHLEIDELIRKLEDSDRKsdslqstikrleedgia 1308
Cdd:pfam05557 313 RRELEQELAQYLKKI--EDLNKKLKRHKALVRRLQ-----RRVLLLTKERDGYRAILESYDKE----------------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1309 keallLTEKQaheaTRMTLTEALEKNEELLKKIHdddKHILELQFTIQRLEENTAAKenlllrereqndattKAQIESQE 1388
Cdd:pfam05557 369 -----LTMSN----YSPQLLERIEEAEDMTQKMQ---AHNEEMEAQLSVAEEELGGY---------------KQQAQTLE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1389 RNEQLLKRfvdvdrkidllQDTIERIGENSTIKDALllseRQEKDAIKKELVEAGERNEELIMKIE------DTD----K 1458
Cdd:pfam05557 422 RELQALRQ-----------QESLADPSYSKEEVDSL----RRKLETLELERQRLREQKNELEMELErrclqgDYDpkktK 486
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1002232322 1459 KIEHLQNAIIKLEgdiEAKDISLEAAREENDTIRKSLAEAQEKNEELLR 1507
Cdd:pfam05557 487 VLHLSMNPAAEAY---QQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1093-1613 |
7.53e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.36 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1093 KQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLseaqyknEELLKK 1172
Cdd:pfam05557 19 KQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYL-------EALNKK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1173 IEDADKSIAHYHDTTQRLEEnvtavenslkaerqhngaimkqladaqvEIGELQRNLEDAD----RRNNQLQDSLQRLEE 1248
Cdd:pfam05557 92 LNEKESQLADAREVISCLKN----------------------------ELSELRRQIQRAElelqSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1249 nVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEdgiakeallltekqaheatrmtlt 1328
Cdd:pfam05557 144 -LKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR------------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1329 eaLEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIEsQERNEQLLKRFVDVD------- 1401
Cdd:pfam05557 199 --IPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELE-KEKLEQELQSWVKLAqdtglnl 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1402 --------RKIDLLQDTIERIGENSTIKDALLLSERQEKDaIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLegd 1473
Cdd:pfam05557 276 rspedlsrRIEQLQQREIVLKEENSSLTSSARQLEKARRE-LEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLL--- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1474 ieAKDISLEAAREENDTIRKSLAEAQEKNEEllrkisdneyRIHLLQDTAQKLQVDAiSRLSSFVMEKQESDAAKRALTE 1553
Cdd:pfam05557 352 --TKERDGYRAILESYDKELTMSNYSPQLLE----------RIEEAEDMTQKMQAHN-EEMEAQLSVAEEELGGYKQQAQ 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1554 ARERNEDLLKRNEDLlkrnddlikkiEESSKTITQLQETLQRLEgkstNLEAENQVLRQQ 1613
Cdd:pfam05557 419 TLERELQALRQQESL-----------ADPSYSKEEVDSLRRKLE----TLELERQRLREQ 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
879-1108 |
9.17e-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: 9.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEELTNRLgleKKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAmqERESAKKAVEEALEQ 958
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAEL---DALQAELEELN-EEYNELQAELEALQAEIDKLQA--EIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 959 EREKISSL--TSEIEGLKALLVAEQEENDLTKKAHA--NAQERNEELSKEVEDAdgkIKQLSDTVQRLEETIQEREALLL 1034
Cdd:COG3883 88 LGERARALyrSGGSVSYLDVLLGSESFSDFLDRLSAlsKIADADADLLEELKAD---KAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1035 AERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQA 1108
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1421-1616 |
1.01e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1421 KDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAR--EENDTIRKSLAEA 1498
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1499 QEKNEELLRKIsdnEYRIHLLQDTAQKLQvdAISRLssfvmEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKK 1578
Cdd:COG4717 145 PERLEELEERL---EELRELEEELEELEA--ELAEL-----QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002232322 1579 IEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATA 1616
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLL 252
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1064-1397 |
1.10e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1064 AEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDA 1143
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1144 LLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVE-- 1221
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDel 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1222 IGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQS---- 1297
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELElail 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1298 --TIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQ 1375
Cdd:COG4372 269 veKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 1002232322 1376 NDATTKAQIESQERNEQLLKRF 1397
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
820-1245 |
1.20e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 820 AALKEFMFRKQNKATTHIQTQWRCHRDNSNYLKLKRAALTYQcawrRRVARRELRQLRMAARDTQALKVAKEKLEERVEE 899
Cdd:pfam12128 596 AASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKA----SREETFARTALKNARLDLRRLFDEKQSEKDKKNK 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 900 -LTNRLGLEKKLRTDLEKSKVAEVSKLQAALNE-----MEQRMQDVTAMQERESAKKAVEEALEQEREKissltsEIEGL 973
Cdd:pfam12128 672 aLAERKDSANERLNSLEAQLKQLDKKHQAWLEEqkeqkREARTEKQAYWQVVEGALDAQLALLKAAIAA------RRSGA 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 974 KALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLS---DTVQRLEETIQEREAL---LLAERQEKEEASA-- 1045
Cdd:pfam12128 746 KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAvrrQEVLRYFDWYQETWLQrrpRLATQLSNIERAIse 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1046 -------VIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLqsSVTIEKQQHEETVVQLAEAQAKIDELLREag 1118
Cdd:pfam12128 826 lqqqlarLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL--ATLKEDANSEQAQGSIGERLAQLEDLKLK-- 901
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1119 dTDEKSTQLETTIQRLEESLTEKDALLTTERQEteatkKLLSEAQYKNEELLKkiedadksIAHYHDTTQRLEENVTA-V 1197
Cdd:pfam12128 902 -RDYLSESVKKYVEHFKNVIADHSGSGLAETWE-----SLREEDHYQNDKGIR--------LLDYRKLVPYLEQWFDVrV 967
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1002232322 1198 ENSLKAERQhngaimkQLADAQVEIGELQRNLEDADRRNNQLQDSLQR 1245
Cdd:pfam12128 968 PQSIMVLRE-------QVSILGVDLTEFYDVLADFDRRIASFSRELQR 1008
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
893-1172 |
1.22e-06 |
|
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: 52.89 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 893 LEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQE------REKISSL 966
Cdd:pfam15905 78 LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKfsedgtQKKMSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 967 TSEIEGLKALLvaeqeenDLTKKAHANAQERNE----ELSKEVEDADGKIKQLSDTVQRLEETIQErealllaERQEKEE 1042
Cdd:pfam15905 158 SMELMKLRNKL-------EAKMKEVMAKQEGMEgklqVTQKNLEHSKGKVAQLEEKLVSTEKEKIE-------EKSETEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1043 ASAVIAESQARNEafasKLEDAEKQIDLLQETVQRFEEAITKLQSSVtiekqqheetvvqlaeaQAKIDELLREAGDTDE 1122
Cdd:pfam15905 224 LLEYITELSCVSE----QVEKYKLDIAQLEELLKEKNDEIESLKQSL-----------------EEKEQELSKQIKDLNE 282
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1123 KSTQLETTIQRLEESLTEKDALLTTERQETEatKKLLSEAQyKNEELLKK 1172
Cdd:pfam15905 283 KCKLLESEKEELLREYEEKEQTLNAELEELK--EKLTLEEQ-EHQKLQQK 329
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1043-1255 |
1.33e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1043 ASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDtde 1122
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1123 kstQLEtTIQRLEESLTEKDALLTTE------------RQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRL 1190
Cdd:COG3883 91 ---RAR-ALYRSGGSVSYLDVLLGSEsfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1191 EENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKES 1255
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1102-1409 |
1.79e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1102 QLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEkdallttERQETEATKKLLSEAQYKNEELLKKIEDADKSIA 1181
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQ-------ARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTER 1261
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 -EQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKK 1340
Cdd:COG4372 185 lDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1341 IHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQD 1409
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| Myo5b_CBD |
cd15477 |
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, ... |
1900-2025 |
2.24e-06 |
|
Cargo binding domain of myosin 5b; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5b-CBD, Rab11-family interacting protein 2.
Pssm-ID: 271261 Cd Length: 372 Bit Score: 52.17 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1900 AIVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHWSDNATREFAGSAw 1979
Cdd:cd15477 183 ALIRQLNTFHSIMCDQGLDPEIIQQVFKQLFYMINAVTLNNLLLRKDVCSWSTGMQLRYNISQLEEWLRGRNLHQSGAA- 261
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1002232322 1980 DALKHIRQAVDFLVISLKPMRTLKEIRTdVCPALSIQQLERIVSMY 2025
Cdd:cd15477 262 QTMEPLIQAAQLLQLKKKTSEDAEAICS-LCTALSTQQIVKILNLY 306
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1107-1604 |
2.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1107 QAKIDELLreAGDTDEKSTQLET--TIQRLEES-LTEKDAL--LTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIA 1181
Cdd:PRK01156 137 QGEMDSLI--SGDPAQRKKILDEilEINSLERNyDKLKDVIdmLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEENVTAVENS---LKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDS---LQRLEENVGAKES 1255
Cdd:PRK01156 215 ITLKEIERLSIEYNNAMDDynnLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELeerHMKIINDPVYKNR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1256 LLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQS-----TIKRLEEDGIAKEALLLTEKQaheatrMTLTEA 1330
Cdd:PRK01156 295 NYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyndyIKKKSRYDDLNNQILELEGYE------MDYNSY 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1331 LEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKaQIESQERNeqllkrfvdVDRKIDLLQDT 1410
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQ-DISSKVSS---------LNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1411 IERIGENSTIKDA--------LLLSERQEKDaIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDIS-- 1480
Cdd:PRK01156 439 LDELSRNMEMLNGqsvcpvcgTTLGEEKSNH-IINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINks 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1481 ------LEAAREENDTIRKSLAEAQEKneELLRKISDNEYRIHLLQDTAQKLQ--VDAISRLSSFVME--KQESDAAKRA 1550
Cdd:PRK01156 518 ineynkIESARADLEDIKIKINELKDK--HDKYEEIKNRYKSLKLEDLDSKRTswLNALAVISLIDIEtnRSRSNEIKKQ 595
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1551 LTEARER--------------NEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLE 1604
Cdd:PRK01156 596 LNDLESRlqeieigfpddksyIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID 663
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
950-1375 |
2.90e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 950 KAVEEALEQEREKISSLTsEIEGLKALLVAEQEENDLTK--KAHANAQERneelSKEVEDADGKIKQLSDTVQRLEETIQ 1027
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEylRAALRLWFA----QRRLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1028 EREALLLAERQEKEEASAVIAESQARN-EAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEA 1106
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1107 QAKIDELLREAgdtDEKSTQLETTIQRLEESLTEKDALLTTERQ-------ETEATKKLLSEAQYKNE-------ELLK- 1171
Cdd:COG4913 393 LEALEEELEAL---EEALAEAEAALRDLRRELRELEAEIASLERrksnipaRLLALRDALAEALGLDEaelpfvgELIEv 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1172 KIEDAD--KSI---------------AHY---------HDTTQRL-----------EENVTAVENSL------------- 1201
Cdd:COG4913 470 RPEEERwrGAIervlggfaltllvppEHYaaalrwvnrLHLRGRLvyervrtglpdPERPRLDPDSLagkldfkphpfra 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1202 --KAE----------------RQHNGAIM-------------------------------KQLADAQVEIGELQRNLEDA 1232
Cdd:COG4913 550 wlEAElgrrfdyvcvdspeelRRHPRAITragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1233 DRRNNQLQDSLQRLEENVGAKESLL----------------------LTEREQNASTLKLLAEahlEIDELIRKLEDSDR 1290
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAeyswdeidvasaereiaeleaeLERLDASSDDLAALEE---QLEELEAELEELEE 706
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1291 KSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKN-EELLKKIHDD---DKHILELQFTIQRLEENTAAKE 1366
Cdd:COG4913 707 ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDaveRELRENLEERIDALRARLNRAE 786
|
....*....
gi 1002232322 1367 NLLLREREQ 1375
Cdd:COG4913 787 EELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
921-1082 |
2.97e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 50.69 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 921 EVSKLQAALNEMEQRMQDVTA-MQERESAKKAVEEALEQEREKISSLTSEIEGLKALL--VAEQEENDLTKKAHANAQER 997
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAeLAELEDELAALEARLEAAKTELEDLEKEIKRLELEIeeVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 998 NEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAfasKLEDAEKQIDLLQETVQR 1077
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE---ELAELEAELEELEAEREE 167
|
....*
gi 1002232322 1078 FEEAI 1082
Cdd:COG1579 168 LAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
880-1156 |
3.05e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 880 ARDTQALKVAKEKLEERVEEltNRLGL-EKKLRTDLEKSKVAEvskLQAALNEME-QRMQDVTAMQERESAKKAVEeale 957
Cdd:pfam15921 582 GRTAGAMQVEKAQLEKEIND--RRLELqEFKILKDKKDAKIRE---LEARVSDLElEKVKLVNAGSERLRAVKDIK---- 652
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 958 QEREKissLTSEIEGLKALLVAEQEENDLTKKAHANAQErneelskEVEDADGKIK-QLSDTVQRLEETiqeREALllaE 1036
Cdd:pfam15921 653 QERDQ---LLNEVKTSRNELNSLSEDYEVLKRNFRNKSE-------EMETTTNKLKmQLKSAQSELEQT---RNTL---K 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1037 RQEKEEASAVIAESQARNEAFASKledaeKQIDLLQETVQRFEEAIT---KLQSSVTIEKQQHEETVVQLAEAQAKID-- 1111
Cdd:pfam15921 717 SMEGSDGHAMKVAMGMQKQITAKR-----GQIDALQSKIQFLEEAMTnanKEKHFLKEEKNKLSQELSTVATEKNKMAge 791
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1002232322 1112 -ELLR-EAGDTDEKSTQLETTIQRLEESLTEKDALLttERQETEATK 1156
Cdd:pfam15921 792 lEVLRsQERRLKEKVANMEVALDKASLQFAECQDII--QRQEQESVR 836
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
881-1205 |
4.03e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 881 RDTQALKVAKEKLeerVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAA------LNEMEQRMQD---VTAMQERESAK-- 949
Cdd:pfam05701 56 KQSEAAEAAKAQV---LEELESTKRLIEELKLNLERAQTEEAQAKQDSelaklrVEEMEQGIADeasVAAKAQLEVAKar 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 950 --------KAVEEALEQEREKISSLTSE---------------------IEGLKALLVAEQEENDLTKKAHANAQERNEE 1000
Cdd:pfam05701 133 haaavaelKSVKEELESLRKEYASLVSErdiaikraeeavsaskeiektVEELTIELIATKESLESAHAAHLEAEEHRIG 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1001 LS-----------KEVEDADGKIKQLSDTV---QRLEETIQEREALLLAERQE---------KEEASAVIAESQARN--- 1054
Cdd:pfam05701 213 AAlareqdklnweKELKQAEEELQRLNQQLlsaKDLKSKLETASALLLDLKAElaaymesklKEEADGEGNEKKTSTsiq 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASK---LEDAEKQIDLLQETVQRFEEAITKLQSSVtiEKQQHEETVVQLAEAQAKIDELLREAgdTDEKSTQLETTI 1131
Cdd:pfam05701 293 AALASAkkeLEEVKANIEKAKDEVNCLRVAAASLRSEL--EKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALV 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1132 QRLE----ESLTEKDALLTTERQETEATKKLlseAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAER 1205
Cdd:pfam05701 369 QAKEkearEKMVELPKQLQQAAQEAEEAKSL---AQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEK 443
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
953-1341 |
4.20e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 953 EEALEQEREKISSLTSEiEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLeetiqereal 1032
Cdd:PRK11281 38 EADVQAQLDALNKQKLL-EAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL---------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1033 llaerqeKEEASAVIAESqarneaFAS-KLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKID 1111
Cdd:PRK11281 107 -------KDDNDEETRET------LSTlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1112 ELLRE-AGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDT--TQ 1188
Cdd:PRK11281 174 QIRNLlKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQEAinSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1189 RL---EENVTAVENSLKAERQHNGAIMKQladaqveigELQRNLEDADR------RNNQL-QDSL-------------QR 1245
Cdd:PRK11281 254 RLtlsEKTVQEAQSQDEAARIQANPLVAQ---------ELEINLQLSQRllkateKLNTLtQQNLrvknwldrltqseRN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1246 LEENVGA-KESLLLT----EREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSL---QSTIKRLEEDgiakealllTEK 1317
Cdd:PRK11281 325 IKEQISVlKGSLLLSrilyQQQQALPSADLIEGLADRIADLRLEQFEINQQRDALfqpDAYIDKLEAG---------HKS 395
|
410 420
....*....|....*....|....
gi 1002232322 1318 QAHEATRMTLTEALEKNEELLKKI 1341
Cdd:PRK11281 396 EVTDEVRDALLQLLDERRELLDQL 419
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
879-1262 |
4.70e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.57 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEkLEERVEELTNRL-----GLEKKLRTDLEkskvAEVSKLQAALnemeQRMQDVTAmQERESakKAVE 953
Cdd:pfam05701 165 IKRAEEAVSASKE-IEKTVEELTIELiatkeSLESAHAAHLE----AEEHRIGAAL----AREQDKLN-WEKEL--KQAE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EALEQEREKISS---LTSEIE-------GLKALLVA--------EQEENDLTKKAHANAQERNEELSKEVEDADGKIKQL 1015
Cdd:pfam05701 233 EELQRLNQQLLSakdLKSKLEtasalllDLKAELAAymesklkeEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1016 SDTVQRLE---ETIQ---EREALLLAERQEKEE-ASAVIAESQArneafasKLEDAEKQIDLLQETVQRFEEAITKLQSS 1088
Cdd:pfam05701 313 KDEVNCLRvaaASLRselEKEKAELASLRQREGmASIAVSSLEA-------ELNRTKSEIALVQAKEKEAREKMVELPKQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1089 VTIEKQQHEETVvqlAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLseaQYKNEE 1168
Cdd:pfam05701 386 LQQAAQEAEEAK---SLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKALQ---ESESSA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1169 LLKKIEDADKSIahyhdtTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEE 1248
Cdd:pfam05701 460 ESTNQEDSPRGV------TLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEERKEALKI 533
|
410
....*....|....*...
gi 1002232322 1249 NVG----AKESLLLTERE 1262
Cdd:pfam05701 534 ALEkaekAKEGKLAAEQE 551
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
890-1402 |
4.70e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 4.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEELTNRLGLEKKLRTDLEK--SKVAEVSKLQAALNEMEQRMQDVT-----AMQERESAKKAVEEALEQEREK 962
Cdd:PRK01156 234 YNNLKSALNELSSLEDMKNRYESEIKTaeSDLSMELEKNNYYKELEERHMKIIndpvyKNRNYINDYFKYKNDIENKKQI 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 963 ISSLTSEI----EGLKALLVAEQEENDLTKKahanaQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAlllaERQ 1038
Cdd:PRK01156 314 LSNIDAEInkyhAIIKKLSVLQKDYNDYIKK-----KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEE----YSK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1039 EKEEASAVIAESQARNEAFAS-----------KLEDAEKQIDLLQETVQRFEEAITKLQSSVTI---------------- 1091
Cdd:PRK01156 385 NIERMSAFISEILKIQEIDPDaikkelneinvKLQDISSKVSSLNQRIRALRENLDELSRNMEMlngqsvcpvcgttlge 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1092 EKQQH--EETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESltekdallttERQETEATKKLLSEAQYKneel 1169
Cdd:PRK01156 465 EKSNHiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE----------EINKSINEYNKIESARAD---- 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1170 LKKIEDADKSIAHYHDTTQRLEENVtaveNSLKAE--RQHNGAIMKQLAD-AQVEIGELQRNLEDADRRNNQLQDSLQRL 1246
Cdd:PRK01156 531 LEDIKIKINELKDKHDKYEEIKNRY----KSLKLEdlDSKRTSWLNALAViSLIDIETNRSRSNEIKKQLNDLESRLQEI 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1247 EENVGAKESLlltereqNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDgiakeallLTEKQAHEATRMT 1326
Cdd:PRK01156 607 EIGFPDDKSY-------IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQ--------IAEIDSIIPDLKE 671
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1327 LTEALEKNEELLKKIHDddkhilELQFTIQRLEENTAAKENLLLREREQNDATTKAQiESQERNEQLLKRFVDVDR 1402
Cdd:PRK01156 672 ITSRINDIEDNLKKSRK------ALDDAKANRARLESTIEILRTRINELSDRINDIN-ETLESMKKIKKAIGDLKR 740
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1030-1507 |
4.73e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1030 EALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQidlLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAK 1109
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQE---RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1110 IDELLREAGDTDEKSTQLETT---IQRLEESLTEKdalltterqeteatKKLLSEAQYKNEELLKKIEDADKSIahyhdt 1186
Cdd:pfam07888 82 VAELKEELRQSREKHEELEEKykeLSASSEELSEE--------------KDALLAQRAAHEARIRELEEDIKTL------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1187 TQRLEENvtavENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNAS 1266
Cdd:pfam07888 142 TQRVLER----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1267 TLKLLAEAHLEIDELIRKLEDsdrksdsLQSTIKRLEedgiakealllTEKQAHEATRMTLTEALEKNEELLKKIHdddK 1346
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEE-------LRSLQERLN-----------ASERKVEGLGEELSSMAAQRDRTQAELH---Q 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1347 HILEL-QFTIQrleentAAKENLLLREREQNDAttkaqiesQERNEQLLKRFVDVDRKIDL---LQDTIERIGENSTIKD 1422
Cdd:pfam07888 277 ARLQAaQLTLQ------LADASLALREGRARWA--------QERETLQQSAEADKDRIEKLsaeLQRLEERLQEERMERE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1423 ALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNA-------IIKLEGDIE--AKDISLEAAREENDTIRK 1493
Cdd:pfam07888 343 KLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEkqelleyIRQLEQRLEtvADAKWSEAALTSTERPDS 422
|
490
....*....|....
gi 1002232322 1494 SLAEAQEKNEELLR 1507
Cdd:pfam07888 423 PLSDSEDENPEALQ 436
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
879-1094 |
4.77e-06 |
|
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: 51.00 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEELtnrlgleKKLRTDLEKSKVAEvsklQAALNEMEQRMQDVTAMQERESAKKAVEEALEQ 958
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKL-------EQQAEEAEKQRAAE----QARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 959 EREkissltseiegLKALLVAEQ---EENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAlllA 1035
Cdd:TIGR02794 121 AEE-----------AKAKQAAEAkakAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEA---E 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1036 ERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEA----ITKLQSSVTIEKQ 1094
Cdd:TIGR02794 187 AKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAelgdIFGLASGSNAEKQ 249
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1329-1611 |
4.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1329 EALEKNEELLKKIhdddkhILELQFTIQRLEENTAAKENL--LLREREQNDATTKAQIESQERNEQLLKRFVD-VDRKID 1405
Cdd:PRK03918 158 DDYENAYKNLGEV------IKEIKRRIERLEKFIKRTENIeeLIKEKEKELEEVLREINEISSELPELREELEkLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1406 LLQDTIERIGEnstiKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQnaiiKLEGDIEAKDISLEAAR 1485
Cdd:PRK03918 232 ELEELKEEIEE----LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK----ELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1486 EENDTIRK------SLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvDAISRLSSFVMEKQESDAAKRALTEARERNE 1559
Cdd:PRK03918 304 EYLDELREiekrlsRLEEEINGIEERIKELEEKEERLEELKKKLKELE-KRLEELEERHELYEEAKAKKEELERLKKRLT 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1560 DLLKrnedllkrnDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLR 1611
Cdd:PRK03918 383 GLTP---------EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
895-1304 |
5.02e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 52.14 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 895 ERVEELTNRLGLEKKLRTDLEKS--------KVAEVSKLQAALNEMEQRM------------QDV--TAMQERESAKKAV 952
Cdd:NF041483 829 ERASEDANRLRREAQEETEAAKAlaertvseAIAEAERLRSDASEYAQRVrteasdtlasaeQDAarTRADAREDANRIR 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 953 EEALEQEREKISSLTSEIEGLKALLVAEQEE--NDLTKKAHANAQERNEELSKEVEDADGKIKQL----SDTV----QRL 1022
Cdd:NF041483 909 SDAAAQADRLIGEATSEAERLTAEARAEAERlrDEARAEAERVRADAAAQAEQLIAEATGEAERLraeaAETVgsaqQHA 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1023 EETIQE-----REALLLAER---QEKEEASAVIAEsqARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQssvtiekq 1094
Cdd:NF041483 989 ERIRTEaervkAEAAAEAERlrtEAREEADRTLDE--ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQ-------- 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1095 qhEETVVQLAEAQAKIDELLREAGDTDEKSTQlETTIQ---RLEESLTEKDALLTTERQETEATKKllseaqyKNEELLK 1171
Cdd:NF041483 1059 --EEALRTTTEAEAQADTMVGAARKEAERIVA-EATVEgnsLVEKARTDADELLVGARRDATAIRE-------RAEELRD 1128
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1172 KIEdadKSIAHYHDTTQRleENVTAVENSLKAERQHNGAIMKQLADAQVEIGELqrnLEDADRRNNQLQDSLQRLEENvg 1251
Cdd:NF041483 1129 RIT---GEIEELHERARR--ESAEQMKSAGERCDALVKAAEEQLAEAEAKAKEL---VSDANSEASKVRIAAVKKAEG-- 1198
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1252 akeslLLTEREQNASTL-----KLLAEAHLEIDELI----RKLEDSDRKSDSLQSTIKRLEE 1304
Cdd:NF041483 1199 -----LLKEAEQKKAELvreaeKIKAEAEAEAKRTVeegkRELDVLVRRREDINAEISRVQD 1255
|
|
| fMyo2p_CBD |
cd15480 |
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin ... |
1912-2065 |
5.28e-06 |
|
cargo binding domain of fungal myosin 2; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271264 Cd Length: 363 Bit Score: 51.04 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1912 LRANHVPSILVHKLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHW------SDNATRefagsawdaLKHI 1985
Cdd:cd15480 182 MKSYYIEESVIRQVVTELLKLIGVTAFNDLLMRRNFLSWKRGLQINYNITRLEEWckshdiPEGTLQ---------LEHL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1986 RQAVDFLviSLKpMRTLKEIRT--DVCPALSIQQLERIVSMYwddingSNA-----ISAEFTSSLKSAVREESNTVTTFS 2058
Cdd:cd15480 253 MQATKLL--QLK-KATLEDIEIiyDVCWILTPAQIQKLISQY------YVAdyenpISPEILKAVAARVKPEDKSDHLLL 323
|
....*..
gi 1002232322 2059 ILLDDDS 2065
Cdd:cd15480 324 IPLVEEV 330
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
891-1304 |
5.41e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 51.38 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRlglekKLRTDLEKskvaeVSKL------QAALNEMEQRMQDVTAmqereSAKKAVEEALEQERE--- 961
Cdd:PRK04778 32 DELEERKQELENL-----PVNDELEK-----VKKLnltgqsEEKFEEWRQKWDEIVT-----NSLPDIEEQLFEAEElnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 962 --KISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQL-----------SDTVQRLEETIQE 1028
Cdd:PRK04778 97 kfRFRKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELrksllanrfsfGPALDELEKQLEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1029 REalllAERQEKEEASAVIAESQARNEafaskLEDAEKQIDLLQETVQRFEEAITKLQSSVtiekqqheetVVQLAEAQA 1108
Cdd:PRK04778 177 LE----EEFSQFVELTESGDYVEAREI-----LDQLEEELAALEQIMEEIPELLKELQTEL----------PDQLQELKA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1109 KIDELLREAGDTDEKstQLETTIQRLEESLTEKDALLTTERqeteatkklLSEAQYKNEELLKKIE----------DADK 1178
Cdd:PRK04778 238 GYRELVEEGYHLDHL--DIEKEIQDLKEQIDENLALLEELD---------LDEAEEKNEEIQERIDqlydilerevKARK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1179 SIAHYHDTTQRLEENVTAVENSLKAERQHngaiMKQ---LADAQVEIgelQRNLEdadRRNNQLQDSLQRLEENVGAKE- 1254
Cdd:PRK04778 307 YVEKNSDTLPDFLEHAKEQNKELKEEIDR----VKQsytLNESELES---VRQLE---KQLESLEKQYDEITERIAEQEi 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1255 --SLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKS-DSLQSTIKRLEE 1304
Cdd:PRK04778 377 aySELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEArEKLERYRNKLHE 429
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
884-1231 |
6.17e-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: 51.65 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEkLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKI 963
Cdd:pfam05483 426 QFEKIAEE-LKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKEL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 964 ----SSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQ----RLEETIQEREALLLA 1035
Cdd:pfam05483 505 tqeaSDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldKSEENARSIEYEVLK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1036 E--------------RQEKEEASAVIAESQARNEAFASKLEDAEKQIDL-----------LQETVQRFEEAITKLQSSVT 1090
Cdd:pfam05483 585 KekqmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeikvnkleleLASAKQKFEEIIDNYQKEIE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1091 IEKQQHEETVVQLAEAQAKIDELLREAGDTDekstqlettiQRLEESLTEKDALLTTERQETEatkkllseaqykneell 1170
Cdd:pfam05483 665 DKKISEEKLLEEVEKAKAIADEAVKLQKEID----------KRCQHKIAEMVALMEKHKHQYD----------------- 717
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1171 KKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLED 1231
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1079-1535 |
6.30e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1079 EEAITKLQSSVTIEKQQHEeTVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLtekdALLTTERQETEATKKL 1158
Cdd:COG3096 278 NERRELSERALELRRELFG-ARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHL----NLVQTALRQQEKIERY 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1159 ---LSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVtaveNSLKAerqhngaimkQLADaqveigeLQRNLEDADRR 1235
Cdd:COG3096 353 qedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEV----DSLKS----------QLAD-------YQQALDVQQTR 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1236 NNQLQDSLQRLEEnvgAKEsllltereqnastlkLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEedgiakealllt 1315
Cdd:COG3096 412 AIQYQQAVQALEK---ARA---------------LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELE------------ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1316 ekqaheaTRMTLTEA----LEKNEELLKKIHDDdkhilelqftIQRLEENTAAKEnLLLREREQ-NDATTKAQIESQERN 1390
Cdd:COG3096 462 -------QKLSVADAarrqFEKAYELVCKIAGE----------VERSQAWQTARE-LLRRYRSQqALAQRLQQLRAQLAE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1391 -EQLLKRFVDVDRkidLLQDTIERIGENSTIKDAL--LLSE-RQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHL-QN 1465
Cdd:COG3096 524 lEQRLRQQQNAER---LLEEFCQRIGQQLDAAEELeeLLAElEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELaAR 600
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1466 AIIKlegdIEAKDiSLEAAREENDTIRKSLAEAQEKNEELLRKisDNEYRIHLLQDTAQKLQVDA-ISRLS 1535
Cdd:COG3096 601 APAW----LAAQD-ALERLREQSGEALADSQEVTAAMQQLLER--EREATVERDELAARKQALESqIERLS 664
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
890-1066 |
7.76e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 890 KEKLEERVEElTNRLGLEKKLRTDLEKSKVAEVSKLQAalneMEQRMQDVTAMQERESAKKAVEEALEQEREKiSSLTSE 969
Cdd:PRK09510 77 AEEQRKKKEQ-QQAEELQQKQAAEQERLKQLEKERLAA----QEQKKQAEEAAKQAALKQKQAEEAAAKAAAA-AKAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 970 IEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREAlllAERQEKEEASAVIAE 1049
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAA---AEAKKKAAAEAKAAA 227
|
170
....*....|....*..
gi 1002232322 1050 SQARNEAFAskleDAEK 1066
Cdd:PRK09510 228 AKAAAEAKA----AAEK 240
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
875-1298 |
1.20e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.25 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMaardtqalkvaKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSklQAALNEmEQRMQDVTAMQERESaKKAVEE 954
Cdd:pfam02029 17 EERR-----------RQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG--QGGLDE-EEAFLDRTAKREERR-QKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREKISSLTSEIEGlkallVAEQEENdltkkahaNAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQER----E 1030
Cdd:pfam02029 82 ALERQKEFDPTIADEKES-----VAERKEN--------NEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENkwstE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDL-LQETVQRFEEAitklQSSVTIEKQQHEETVVQLAEAQAK 1109
Cdd:pfam02029 149 VRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKkVKYESKVFLDQ----KRGHPEVKSQNGEEEVTKLKVTTK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1110 IDELLREAGDTDEKST--QLETTiQRLEESLTEKDAlltTERQETEATKKLLSEAQYKNEELLKKIEDADKSiahyhdtt 1187
Cdd:pfam02029 225 RRQGGLSQSQEREEEAevFLEAE-QKLEELRRRRQE---KESEEFEKLRQKQQEAELELEELKKKREERRKL-------- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1188 qrLEENvtavENSLKAERqhngaimkqlADAQVEIGELQRNL-EDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNAS 1266
Cdd:pfam02029 293 --LEEE----EQRRKQEE----------AERKLREEEEKRRMkEEIERRRAEAAEKRQKLPEDSSSEGKKPFKCFSPKGS 356
|
410 420 430
....*....|....*....|....*....|..
gi 1002232322 1267 TLKllaeahleIDELIRKLEDSDRKSDSLQST 1298
Cdd:pfam02029 357 SLK--------ITERAEFLNKSLQKSSSVKKT 380
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
881-1221 |
1.20e-05 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 50.10 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 881 RDTQALKVAKEKLEErveeLTNRLGLEkklRTDLEKSK-VAEVSK--LQAALNEMEQRMQD-VTAMQEreSAKKAVEE-- 954
Cdd:pfam03528 51 RQNAVLQEAQVELDA----LQNQLALA---RAEMENIKaVATVSEntKQEAIDEVKSQWQEeVASLQA--IMKETVREye 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 -----ALEQEREKIS----SLTSEIEGLKALLVAEQEENDLTKKAHaNAQERNEELSKEVEDADGKIKQLSDTVQRLEET 1025
Cdd:pfam03528 122 vqfhrRLEQERAQWNqyreSAEREIADLRRRLSEGQEEENLEDEMK-KAQEDAEKLRSVVMPMEKEIAALKAKLTEAEDK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1026 IQEREAlllaeRQEKEEASAVIAESQARN--EAFASKLEdaeKQIDLLQETVQRFEEAITKLQSSVTIEKQQHeetvvql 1103
Cdd:pfam03528 201 IKELEA-----SKMKELNHYLEAEKSCRTdlEMYVAVLN---TQKSVLQEDAEKLRKELHEVCHLLEQERQQH------- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1104 aeaqakidellreagdtdeksTQLETTIQRLEESLTEKDALLTTERQETEAtkkLLSEAQYKNEELLKKIEDADKSIAHY 1183
Cdd:pfam03528 266 ---------------------NQLKHTWQKANDQFLESQRLLMRDMQRMES---VLTSEQLRQVEEIKKKDQEEHKRART 321
|
330 340 350
....*....|....*....|....*....|....*...
gi 1002232322 1184 HDTtqrleenvtavENSLKAERQHNGAIMKQLADAQVE 1221
Cdd:pfam03528 322 HKE-----------KETLKSDREHTVSIHAVFSPAGVE 348
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
914-1183 |
1.20e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 914 LEKSKVAEVSK----LQAALNEMEQRMqdvtAMQER--ESAKKAVEEALEQEREKISSLTSEIEGLKALLvaeqeendlt 987
Cdd:PHA02562 171 LNKDKIRELNQqiqtLDMKIDHIQQQI----KTYNKniEEQRKKNGENIARKQNKYDELVEEAKTIKAEI---------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 988 kkahANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQ--EREALLLAE-------RQEKEEASAVIAESQARNEAFA 1058
Cdd:PHA02562 237 ----EELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1059 SKLEDAEKQIDLLQETVQRFEEAITK---LQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDtdeKSTQLETTIQRLE 1135
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEQSKKlleLKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD---NAEELAKLQDELD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1002232322 1136 EsLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHY 1183
Cdd:PHA02562 390 K-IVKTKSELVKEKYHRGIVTDLLKDSGIKASIIKKYIPYFNKQINHY 436
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
886-1166 |
1.35e-05 |
|
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: 50.34 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSK-LQAALNEME--------QRMQDVTAMQERESAKKA----- 951
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQeLEESKRETEtgiqnltaEIEQGQESLTENLEAIKEeieni 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 952 -VEEALEQEREKISSLTSEIEGLK--------ALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRL 1022
Cdd:COG5185 367 vGEVELSKSSEELDSFKDTIESTKesldeipqNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNEL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1023 EETIQEREALLLAERQEK--EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKlqssvtiekqQHEETV 1100
Cdd:COG5185 447 ISELNKVMREADEESQSRleEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER----------QLEGVR 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1101 VQLAEAQAKIDELLREAGdtDEKSTQLETTIQrlEESLTEKDALLTTERQETEATKKLLSEAQYKN 1166
Cdd:COG5185 517 SKLDQVAESLKDFMRARG--YAHILALENLIP--ASELIQASNAKTDGQAANLRTAVIDELTQYLS 578
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
924-1140 |
1.40e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 48.49 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 924 KLQAALNEMEQrmqdvtaMQEREsakKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSK 1003
Cdd:pfam00261 2 KMQQIKEELDE-------AEERL---KEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1004 EVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAIT 1083
Cdd:pfam00261 72 AADESERGRKVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002232322 1084 -------KLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTE 1140
Cdd:pfam00261 152 vvgnnlkSLEASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEA 215
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1262-1510 |
1.74e-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: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKI 1341
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1342 HDDDKHILELQFTIQRLEENTAAKenLLLREREQNDAttkaqiesqERNEQLLKRFVDVDRK-IDLLQDTIERIGEnsti 1420
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLA--LLLSPEDFLDA---------VRRLQYLKYLAPARREqAEELRADLAELAA---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1421 KDALLLSERQEKDAIKKELveagerneelimkiedtdkkiehlQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQE 1500
Cdd:COG4942 165 LRAELEAERAELEALLAEL------------------------EEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250
....*....|
gi 1002232322 1501 KNEELLRKIS 1510
Cdd:COG4942 221 EAEELEALIA 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
876-1063 |
2.00e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 876 LRMAARDTQ--ALKVAKEKLEERVEELTNRLgleKKLRTDLEKSKvAEVSKLQAALNEMEQRMQDVTAMQEResakkaVE 953
Cdd:COG1579 10 LDLQELDSEldRLEHRLKELPAELAELEDEL---AALEARLEAAK-TELEDLEKEIKRLELEIEEVEARIKK------YE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EALEQ---EREkISSLTSEIEGLKallvaeqEENDLTKKAHANAQERNEELSKEVEDADgkikqlsdtvQRLEETIQERE 1030
Cdd:COG1579 80 EQLGNvrnNKE-YEALQKEIESLK-------RRISDLEDEILELMERIEELEEELAELE----------AELAELEAELE 141
|
170 180 190
....*....|....*....|....*....|...
gi 1002232322 1031 ALLLAERQEKEEASAVIAESQARNEAFASKLED 1063
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1313-1606 |
2.07e-05 |
|
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: 49.51 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1313 LLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHIL-----ELQFTIQRLEENTA-AKENLLLREREQNDATTKAQIES 1386
Cdd:pfam07888 35 RLEECLQERAELLQAQEAANRQREKEKERYKRDREQWerqrrELESRVAELKEELRqSREKHEELEEKYKELSASSEELS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1387 QERNEQLLKRFVDVDRkIDLLQDTIERIGENSTIKDALL--LSERQEKDAIKKELVEAgeRNEELIMKIEDTDKKIEHLQ 1464
Cdd:pfam07888 115 EEKDALLAQRAAHEAR-IRELEEDIKTLTQRVLERETELerMKERAKKAGAQRKEEEA--ERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1465 NAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEK---NEELLRKISDNEYRIHLLQDTAQKLQVDaisrLSSFVMEK 1541
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKeaeNEALLEELRSLQERLNASERKVEGLGEE----LSSMAAQR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1542 QESDAA-KRALTEARERNEDLLKRNEDL-------------LKRNDDLIK-KIEESSKTITQLQETLQRLEGKSTNLEAE 1606
Cdd:pfam07888 268 DRTQAElHQARLQAAQLTLQLADASLALregrarwaqeretLQQSAEADKdRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| Myo5p-like_CBD_DIL_ANK |
cd15473 |
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ... |
1721-1945 |
2.13e-05 |
|
cargo binding domain of myosin 5-like of dil and ankyrin domain containing protein; DIL and ankyrin domain-containing protein are a group of fungal proteins that contain a domain homologous to the cargo binding domain of class V myosins and ankyrin repeats. Their function is unknown.
Pssm-ID: 271257 [Multi-domain] Cd Length: 316 Bit Score: 48.71 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1721 KPVAALLIYQCL--SHWRSFEAMKTGVFDSILQAINSATEA-QNDTRALAYWLSNLSTLTVLLQRsfkttrtaistpqrr 1797
Cdd:cd15473 30 RPVPANLLFLCAryAHYHCSPELLEDLLLGALDRIEDVVEAnPWDMTLLAFWLSNVTLLLHYLKK--------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1798 rfsserifhasqtsNAGLAYLSGQpvvgaaglpqveakypallFKQQLVDLIEKVYGMISDSVKKELNPLLElciqdprt 1877
Cdd:cd15473 95 --------------DAGLVEATPE-------------------FQQELAELINEIFVLIIRDAERRIDKLLD-------- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1878 sHSPAKghanglgqknqlghwlaIVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRLLLRR 1945
Cdd:cd15473 134 -ASPRN-----------------ITSLLSSTLYVLELYDVHPAIIIQALSQLFYWLGCELFNRILTNK 183
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1011-1175 |
2.38e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1011 KIKQLSDtVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQ---S 1087
Cdd:COG1579 5 DLRALLD-LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEeqlG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1088 SVTIEKQ----QHEetvvqLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEA----TKKLL 1159
Cdd:COG1579 84 NVRNNKEyealQKE-----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEelaeLEAEL 158
|
170
....*....|....*.
gi 1002232322 1160 SEAQYKNEELLKKIED 1175
Cdd:COG1579 159 EELEAEREELAAKIPP 174
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1238-1501 |
2.45e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1238 QLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEedgiakeallltek 1317
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE-------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1318 qaheatrmtltealEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKenLLLREREQNDATTKAQIeSQERNEQLLKRF 1397
Cdd:COG4942 90 --------------KEIAELRAELEAQKEELAELLRALYRLGRQPPLA--LLLSPEDFLDAVRRLQY-LKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1398 VDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAk 1477
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR- 231
|
250 260
....*....|....*....|....
gi 1002232322 1478 dISLEAAREENDTIRKSLAEAQEK 1501
Cdd:COG4942 232 -LEAEAAAAAERTPAAGFAALKGK 254
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
875-1108 |
2.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLgleKKLRTDLEKSKvAEVSKLQAALNEMEQRMQD--------VTAMQERE 946
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEY---NELQAELEALQ-AEIDKLQAEIAEAEAEIEErreelgerARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 947 SAKKAVEEALEQEreKISSLTSEIEGLKALLVAEQEENDLTKKAhanaQERNEELSKEVEDadgKIKQLSDTVQRLEETI 1026
Cdd:COG3883 100 GSVSYLDVLLGSE--SFSDFLDRLSALSKIADADADLLEELKAD----KAELEAKKAELEA---KLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1027 QEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEA 1106
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
..
gi 1002232322 1107 QA 1108
Cdd:COG3883 251 AA 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
880-1091 |
4.55e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 880 ARDTQALKVAKEKLEERVEELTNRLG-LEKKLRTDLEKSKV----AEVSKLQAALNEMEQRMQDVTA-MQERESAKKAVE 953
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEeAEAALEEFRQKNGLvdlsEEAKLLLQQLSELESQLAEARAeLAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 954 EALEQEREKISSLTS--EIEGLKALLV-AEQEENDLTKK---AHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQ 1027
Cdd:COG3206 247 AQLGSGPDALPELLQspVIQQLRAQLAeLEAELAELSARytpNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1028 EREALLLAERQEKEEASAVIAESQARneafASKLE-DAEKQIDLLQETVQRFEEAitKLQSSVTI 1091
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAE----LRRLErEVEVARELYESLLQRLEEA--RLAEALTV 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1176-1388 |
4.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1176 ADKSIAHYHDTTQRLEENVTAVENSLKAerqhngaIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKES 1255
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDA-------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1256 LL------LTEREQNASTLKLLAEAHlEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEAllltEKQAHEATRMTLTE 1329
Cdd:COG3883 87 ELgeraraLYRSGGSVSYLDVLLGSE-SFSDFLDRLSALSKIADADADLLEELKADKAELEA----KKAELEAKLAELEA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1330 ALEKNEELLKKIhddDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQE 1388
Cdd:COG3883 162 LKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1192 |
4.99e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 880 ARDTQALKVAKEKLEERVEELTN----RLGLEKKLRTDLEKSKVAEVSKLQAAlnemEQRMQDVTAMQERESAKKAVEEA 955
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKaeeaKIKAEELKKAEEEKKKVEQLKKKEAE----EKKKAEELKKAEEENKIKAAEEA 1667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQEREKissltseieglKALLVAEQEENDltKKAHANAQERNEELSKEVEDADgkiKQLSDTVQRLEETIQEREallla 1035
Cdd:PTZ00121 1668 KKAEEDK-----------KKAEEAKKAEED--EKKAAEALKKEAEEAKKAEELK---KKEAEEKKKAEELKKAEE----- 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1036 ERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVtIEKQQHEETVVQLAEAQAKIDELLR 1115
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV-IEEELDEEDEKRRMEVDKKIKDIFD 1805
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1116 EAGDTDE---KSTQLETTIQRLEESLTEKDALLT-TERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLE 1191
Cdd:PTZ00121 1806 NFANIIEggkEGNLVINDSKEMEDSAIKEVADSKnMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIE 1885
|
.
gi 1002232322 1192 E 1192
Cdd:PTZ00121 1886 E 1886
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
884-1175 |
5.20e-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: 48.48 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEELTNRLGLEKKLRTDLEKskvaEVSKLQAALNEMEQRMqdvtamqeresakkaveealEQEREKI 963
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNLDNTR--------------------ESLETQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 964 SSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEa 1043
Cdd:TIGR04523 471 KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1044 saviaesqarnEAFASKLEDAEKQIDLLQETVQRFEEAITKL---QSSVTIEKQQHEETVV----QLAEAQAKIDELLRE 1116
Cdd:TIGR04523 550 -----------DDFELKKENLEKEIDEKNKEIEELKQTQKSLkkkQEEKQELIDQKEKEKKdlikEIEEKEKKISSLEKE 618
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1117 AGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIED 1175
Cdd:TIGR04523 619 LEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1055-1395 |
5.78e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.21 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKLEDAEKQIDLLQETVQRFEEA---ITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTI 1131
Cdd:pfam09731 78 ESKEPKEEKKQVKIPRQSGVSSEVAEEekeATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1132 QRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSiahyhDTTQRLEENVTAVENsLKAERQHNGAI 1211
Cdd:pfam09731 158 AVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQS-----EEEAAPPLLDAAPET-PPKLPEHLDNV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1212 MKQLADAQVE---IGELQRNLEDADrrnNQLQDSLQRLEENV--GAKESLLLTEREQNAstlkLLAEAHLEIDELIRKLE 1286
Cdd:pfam09731 232 EEKVEKAQSLaklVDQYKELVASER---IVFQQELVSIFPDIipVLKEDNLLSNDDLNS----LIAHAHREIDQLSKKLA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1287 DSDRKSD-SLQSTIKRLEEDGIAKEALL---LTEKQAHEATRMTLtEALEKNEELLKKIHDDDKHILELQFTI--QRLEE 1360
Cdd:pfam09731 305 ELKKREEkHIERALEKQKEELDKLAEELsarLEEVRAADEAQLRL-EFEREREEIRESYEEKLRTELERQAEAheEHLKD 383
|
330 340 350
....*....|....*....|....*....|....*
gi 1002232322 1361 NTAAKENLLLREREQNdatTKAQIEsQERNEQLLK 1395
Cdd:pfam09731 384 VLVEQEIELQREFLQD---IKEKVE-EERAGRLLK 414
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1381-1606 |
5.93e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1381 KAQIESQERNEQLLKRFVD-VDRKIDLLQDTIERI----GENSTIKDALLLSERQEKDAIKKELVEAGERNEELIMKIED 1455
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDhIQQQIKTYNKNIEEQrkknGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1456 TDKKIEHLQNAIIKLEGDIE--AKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQdtaqklqvDAISR 1533
Cdd:PHA02562 253 PSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLD--------TAIDE 324
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1534 LSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEES----SKTITQLQETLQRLEGKSTNLEAE 1606
Cdd:PHA02562 325 LEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdnAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
891-1030 |
6.14e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.65 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLE----------KSKVAEVSKLQAALNEMEQRMQDVTAM-----QERESAKKAVEEA 955
Cdd:PRK09039 56 DRLNSQIAELADLLSLERQGNQDLQdsvanlraslSAAEAERSRLQALLAELAGAGAAAEGRagelaQELDSEKQVSARA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQerekISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDA-DGKIKQL----SDTVQRLEETIQERE 1030
Cdd:PRK09039 136 LAQ----VELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVAlAQRVQELnryrSEFFGRLREILGDRE 211
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
943-1168 |
6.39e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 943 QERESAKKAveealEQEREKissltseieglkallVAEQEENDLTKKAhANAQERNEELSKEVEDADGKIKQlsdtvqrl 1022
Cdd:PRK09510 69 QQQKSAKRA-----EEQRKK---------------KEQQQAEELQQKQ-AAEQERLKQLEKERLAAQEQKKQ-------- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1023 eeTIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIdllQETVQRFEEAITKLQSSVTIEKQQHEETVVQ 1102
Cdd:PRK09510 120 --AEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKA---AAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1103 L-AEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDAlltteRQETEATKKLLSEAQYKNEE 1168
Cdd:PRK09510 195 AaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA-----AAEKAAAAKAAEKAAAAKAA 256
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
908-1449 |
7.18e-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: 47.81 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 908 KKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKkavEEALeqeREKIssltseieglkallvaeqEENDLT 987
Cdd:pfam05557 26 KRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEA---EEAL---REQA------------------ELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 988 KKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEeasaviaESQARNEAFASKLEDAEKQ 1067
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELE-------ELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1068 IDLLQETVQRFEEAITKLQS-SVTIEKQQHEETVVQLAEA-QAKIDELLREAGDTDEKSTQLETTIqRLEESLTEKDALL 1145
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSeLARIPELEKELERLREHNKHLNENI-ENKLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1146 TTERQETEATKKLLSEAQYKNEELLKKI-----------------EDADKSIAHYHDTTQRLEENVTAVENSLKAERqhn 1208
Cdd:pfam05557 234 KRKLEREEKYREEAATLELEKEKLEQELqswvklaqdtglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQLE--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1209 gaimKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENV--------GAKESLL-----LTEREQNASTLKLLAEAH 1275
Cdd:pfam05557 311 ----KARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkerdGYRAILEsydkeLTMSNYSPQLLERIEEAE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1276 LEIDELIRKLEDSDRKSDSLQSTIK--RLEEDGIAKEALLLTEKQAHE---ATRMTLTEALEKNEELLKKIH--DDDKHI 1348
Cdd:pfam05557 387 DMTQKMQAHNEEMEAQLSVAEEELGgyKQQAQTLERELQALRQQESLAdpsYSKEEVDSLRRKLETLELERQrlREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1349 LELQFTIQRLEENTAAKENLLLREREqnDATTKAQIESQERNEQL---LKRFVDVDRKIDLLQDTIERIGENSTIKDall 1425
Cdd:pfam05557 467 LEMELERRCLQGDYDPKKTKVLHLSM--NPAAEAYQQRKNQLEKLqaeIERLKRLLKKLEDDLEQVLRLPETTSTMN--- 541
|
570 580
....*....|....*....|....
gi 1002232322 1426 lseRQEKDAIKKELVEAGERNEEL 1449
Cdd:pfam05557 542 ---FKEVLDLRKELESAELKNQRL 562
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
915-1288 |
7.91e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 47.71 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 915 EKSKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEglkallvaeqeendltkkahana 994
Cdd:pfam05667 296 KGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQ----------------------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 995 qerneELSKEVEDADGKIKQLSDTVQRLEETIQEREalllaerqekeeasaviaesqarneafaSKLEDAEKQIDLLQET 1074
Cdd:pfam05667 353 -----ELEKEIKKLESSIKQVEEELEELKEQNEELE----------------------------KQYKVKKKTLDLLPDA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1075 vqrfEEAITKLQSSVtiekQQHEETVVQLAEAQAK-----IDELLREAgdtDEKSTQLETTIQRLEE--SLTEKdalltt 1147
Cdd:pfam05667 400 ----EENIAKLQALV----DASAQRLVELAGQWEKhrvplIEEYRALK---EAKSNKEDESQRKLEEikELREK------ 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1148 erqeteaTKKLLSEAQYKNE---ELLKKIEDADKSI--AHYhdtTQRLEENVtavenslkaerqhnGAIMKQLADAQ--- 1219
Cdd:pfam05667 463 -------IKEVAEEAKQKEElykQLVAEYERLPKDVsrSAY---TRRILEIV--------------KNIKKQKEEITkil 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1220 VEIGELQRNLedadrrnNQLQDSLQRLEENVgakESLLLTEREQNAST---LKLLAEAHLEIDELIRKLEDS 1288
Cdd:pfam05667 519 SDTKSLQKEI-------NSLTGKLDRTFTVT---DELVFKDAKKDESVrkaYKYLAALHENCEQLIQTVEET 580
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1147-1533 |
8.21e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1147 TERQETEATKKLLSEA-QYKNEELLKKIEdadksiahyhdTTQRLEEnvtaVENSLKAERQHNGAIMKQLADAQVEIG-E 1224
Cdd:pfam17380 285 SERQQQEKFEKMEQERlRQEKEEKAREVE-----------RRRKLEE----AEKARQAEMDRQAAIYAEQERMAMERErE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1225 LQR-NLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLE 1303
Cdd:pfam17380 350 LERiRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1304 EDGIAKEALLLTEKQAHEATRMTLTEalekneellkkihdddkhiLELQFTIQRLeentaakenlllREREQNDATTKAQ 1383
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEE-------------------QERQQQVERL------------RQQEEERKRKKLE 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1384 IESQERNEQLLKrfvDVDRKIdLLQDTIERigenstiKDALLLSERqekdaiKKELVEagerneelimkiedtdKKIEHL 1463
Cdd:pfam17380 479 LEKEKRDRKRAE---EQRRKI-LEKELEER-------KQAMIEEER------KRKLLE----------------KEMEER 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1464 QNAIIKLEGDIEA-----KDISLEAAREENDTIRK-----SLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQVDAISR 1533
Cdd:pfam17380 526 QKAIYEEERRREAeeerrKQQEMEERRRIQEQMRKateerSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIYR 605
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1014-1286 |
8.23e-05 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 47.76 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1014 QLSDTVQRLEETIQEReaLLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTiEK 1093
Cdd:COG4192 59 KLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRAAVADLRNLLQQLDSLLT-QR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1094 QQHEEtvvQLAEAQAKIDELLREAGDT-----DEKSTQLETTI------QRLEESLTEKDALLTTERQETEAtKKLLSEA 1162
Cdd:COG4192 136 IALRR---RLQELLEQINWLHQDFNSEltpllQEASWQQTRLLdsvettESLRNLQNELQLLLRLLAIENQI-VSLLREV 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1163 QYkneellkkIEDADKSIAHYHdttqRLEENVTAVENSLKAERQHNGAIM-KQLADAQVEIGELQRNLEDADRRNNQLQD 1241
Cdd:COG4192 212 AA--------ARDQADVDNLFD----RLQYLKDELDRNLQALKNYPSTITlRQLIDELLAIGSGEGGLPSLRRDELAAQA 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1002232322 1242 SLQRLEEnvgAKESLLlteREQNASTLKLLAEAHLEIDELIRKLE 1286
Cdd:COG4192 280 TLEALAE---ENNSIL---EQLRTQISGLVGNSREQLVALNQETA 318
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1336-1512 |
9.87e-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: 46.07 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1336 ELLKKIHDDDKHILELQFTIQRLEENTAAKENLL--LREREQNDATTKAQIESQ-ERNEQLLKrfvDVDRKIDLLQdtiE 1412
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELaaLEARLEAAKTELEDLEKEiKRLELEIE---EVEARIKKYE---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1413 RIGENSTIKDAlllserqekDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDT-- 1490
Cdd:COG1579 81 QLGNVRNNKEY---------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEel 151
|
170 180
....*....|....*....|....
gi 1002232322 1491 --IRKSLAEAQEKNEELLRKISDN 1512
Cdd:COG1579 152 aeLEAELEELEAEREELAAKIPPE 175
|
|
| Myo5a_CBD |
cd15478 |
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, ... |
1841-2053 |
1.12e-04 |
|
Cargo binding domain of myosin 5a; Class V myosins are well studied unconventional myosins, represented by three paralogs (Myo5a,b,c) in vertebrates. Their C-terminal cargo binding domains (CBDs) are important for the binding of a diverse set of cargos, including membrane vesicles, organelles, proteins and mRNA. They interact with several adaptor proteins, in case of Myo5a-CBD, melanophilin (MLPH), Rab interacting lysosomal protein-like 2 (RILPL2), and granuphilin. Mutations in human Myo5a (many of which map to the cargo binding domain) lead to Griscelli syndrome, a severe neurological disease.
Pssm-ID: 271262 Cd Length: 375 Bit Score: 46.95 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1841 FKQQLVDLIEKVYGMISDSVKKELNPLLELCIQDPRTSHSPAKGHANGLGQKNQL----GHWL--AIVKVLTNYLDVLRA 1914
Cdd:cd15478 118 YRQVLSDLAIQIYQQLVRVLENILQPMIVSGMLEHETIQGVSGVKPTGLRKRTSSiadeGTYTldSILRQLNSFHSVMCQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1915 NHVPSILVHKLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHWSDNATREFAGsAWDALKHIRQAVDFLVI 1994
Cdd:cd15478 198 HGMDPELIKQVVKQMFYIIGAITLNNLLLRKDMCSWSKGMQIRYNVSQLEEWLRDKNLMNSG-AKETLEPLIQAAQLLQV 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1995 SLKPMRTLKEIrTDVCPALSIQQLERIVSMYWDDINGSNAISAEFTSSLKSAVREESNT 2053
Cdd:cd15478 277 KKKTDDDAEAI-CSMCNALTTAQIVKVLNLYTPVNEFEERVSVSFIRTIQMRLRDRKDS 334
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
973-1113 |
1.15e-04 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 45.28 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 973 LKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREallLAERQEKEEAsavIAESQA 1052
Cdd:pfam15619 58 LPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKN---LAEREELQKK---LEQLEA 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1053 RNEAFASKLEDAEKQIDLLQETVQRfeeaitklqsSVTIEKQQHEETVVQLAEAQAKIDEL 1113
Cdd:pfam15619 132 KLEDKDEKIQDLERKLELENKSFRR----------QLAAEKKKHKEAQEEVKILQEEIERL 182
|
|
| Myo5p-like_CBD_fungal |
cd15474 |
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin ... |
1748-2050 |
1.52e-04 |
|
cargo binding domain of fungal myosin V -like proteins; Yeast myosin V travels along actin cables, actin filaments that are bundled by fimbrin, in the presence of tropomyosin. This is in contrast to the other vertebrate class V myosins. Like other class V myosins, fungal myosin 2 and 4 contain a C-terminal cargo binding domain. In case of Myo4 it has been shown to bind to the adapter protein She3p (Swi5p-dependent HO expression 3), which in turn anchors myosin 4 to its cargos, zip-coded mRNP (messenger ribonucleoprotein particles) and tER (tubular endoplasmic reticulum). Myo 2 binds to Vac17, vacuole-specific cargo adaptor, and Mmr1, mitochondria-specific cargo adaptor. Both adaptors bind competitivly at the same site.
Pssm-ID: 271258 Cd Length: 352 Bit Score: 46.26 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1748 SILQAINSATEAQNDTRALAYWLSNLSTLtvllqRSFKTTR-TAISTPQRRRFSSErifhasqtsnaglaylsgqpvvga 1826
Cdd:cd15474 65 SYIASIVDSLPKKETIPDGAFWLANLHEL-----RSFVVYLlSLIEHSSSDEFSKE------------------------ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1827 aglpQVEAKYPAllfKQQLVDLIEKVYGMISDSVKKELNPLLE------LCIQDPRTSHSPAKGHANGLGQKNQLghwla 1900
Cdd:cd15474 116 ----SEEYWNTL---FDKTLKHLSNIYSTWIDKLNKHLSPKIEgavlvlLTSLDLSELIDLNKEFFNKPKKKMAD----- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1901 IVKVLTNYLDVLRANHVPSILVHKLFTQIFSLIDVQLFNRLLLRRECCSFSNGEYVKVGLAELKHWsdnATREFAGSAWD 1980
Cdd:cd15474 184 LITFLNEVYDLLQSFSVQPELLNAIVSSTLQYINVEAFNSLITKRSALSWKRGSQISYNVSRLKEW---CHQHGLSDANL 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1981 ALKHIRQAVDFLVISLKPMRTLKEIRtDVCPALSIQQLERIVSMYwDDINGSNAISAEFTSSLKSAVREE 2050
Cdd:cd15474 261 QLEPLIQASKLLQLRKDDENDFKIIL-SVCYALNPAQIQKLLDKY-QPANYEAPVPKEFLNALEKLIKKE 328
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
877-1568 |
1.56e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 47.13 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 877 RMAARDTQALKVAKEKLEERVEElTNRLGLEKKLRTDLEKSKVAE-VSKLQAALNEMEQRMQDvtamqerESAKKAVEEA 955
Cdd:NF041483 579 RLHTEAEERLTAAEEALADARAE-AERIRREAAEETERLRTEAAErIRTLQAQAEQEAERLRT-------EAAADASAAR 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 956 LEQEREKI---SSLTSEIEGLKAllvAEQEENDLTKKAHANAQER-----NEELSKEVEDADGKIKQLSDTVQRL-EETI 1026
Cdd:NF041483 651 AEGENVAVrlrSEAAAEAERLKS---EAQESADRVRAEAAAAAERvgteaAEALAAAQEEAARRRREAEETLGSArAEAD 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1027 QEREAlllaERQEKEE--ASAVIAESQARNEAfASKLEDAEKQIdllQETVQRFEEAITKLQSSVTIEKQQHEETVVQLA 1104
Cdd:NF041483 728 QERER----AREQSEEllASARKRVEEAQAEA-QRLVEEADRRA---TELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLR 799
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1105 EAQAKIDELLReaGDTDEKSTQLETTIQRLEESLTEKDALLTTE-RQETEATKKL----LSEAqykneellkkIEDADKS 1179
Cdd:NF041483 800 SAAEHAAERTR--TEAQEEADRVRSDAYAERERASEDANRLRREaQEETEAAKALaertVSEA----------IAEAERL 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1180 IAHYHDTTQRLEenvTAVENSLKAERQhngAIMKQLADAQVEIGELQRNL-EDADRRNNQLQDSLQRLEENVGAKESLLL 1258
Cdd:NF041483 868 RSDASEYAQRVR---TEASDTLASAEQ---DAARTRADAREDANRIRSDAaAQADRLIGEATSEAERLTAEARAEAERLR 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1259 TEREQNAStlKLLAEAHLEIDELIRK-LEDSDRKSDSLQSTIKRLEEDG--IAKEALLLTEKQAHEATRMTlTEALEKNE 1335
Cdd:NF041483 942 DEARAEAE--RVRADAAAQAEQLIAEaTGEAERLRAEAAETVGSAQQHAerIRTEAERVKAEAAAEAERLR-TEAREEAD 1018
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1336 ELLKKIHDD-DKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQerneqllkrfvdVDRKIDLLQDTIERI 1414
Cdd:NF041483 1019 RTLDEARKDaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQ------------ADTMVGAARKEAERI 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1415 GENSTIK------------DALLLSERQEKDAIKkelveagERNEELIMKIEdtdKKIEHLQN-------AIIKLEGdiE 1475
Cdd:NF041483 1087 VAEATVEgnslvekartdaDELLVGARRDATAIR-------ERAEELRDRIT---GEIEELHErarresaEQMKSAG--E 1154
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1476 AKDISLEAAREEndtirksLAEAQEKNEELLRKISDNEYRIHLLQ-DTAQKLQVDAISRLSSFVMEKQE--SDA---AKR 1549
Cdd:NF041483 1155 RCDALVKAAEEQ-------LAEAEAKAKELVSDANSEASKVRIAAvKKAEGLLKEAEQKKAELVREAEKikAEAeaeAKR 1227
|
730
....*....|....*....
gi 1002232322 1550 ALTEARERNEDLLKRNEDL 1568
Cdd:NF041483 1228 TVEEGKRELDVLVRRREDI 1246
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
925-1152 |
1.56e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 925 LQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLkALLVAEQEE--NDLTKKAHA-----NAQER 997
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAA-ALQPGEEEEleEERRRLSNAeklreALQEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 998 NEELSkevEDADGKIKQLSDTVQRLEEtIQEREALLLAERQEKEEASAVIAESQARNEAFASKLE-DAEKqidlLQETVQ 1076
Cdd:COG0497 232 LEALS---GGEGGALDLLGQALRALER-LAEYDPSLAELAERLESALIELEEAASELRRYLDSLEfDPER----LEEVEE 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1077 RFEeAITKLqssvtieKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQET 1152
Cdd:COG0497 304 RLA-LLRRL-------ARKYGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAARKKA 371
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1104-1505 |
1.58e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 46.98 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1104 AEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQE----------TEATKKLLSEAQYKnEELLKKI 1173
Cdd:pfam13166 92 IEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKkikrkknsalSEALNGFKYEANFK-SRLLREI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1174 EDADKSIAHYHDTTQRLEENVTAVENSLKAERQ-----------HNGAIMKQ-LADAQVEIGELQRNLedadrrnnQLQD 1241
Cdd:pfam13166 171 EKDNFNAGVLLSDEDRKAALATVFSDNKPEIAPltfnvidfdalEKAEILIQkVIGKSSAIEELIKNP--------DLAD 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1242 SLQR-LEENVGAKESLLLTEREQNASTLKLLaEAHLEidelirklEDSDRKSDSLQSTIKRLEEDGIAKEALLltekqah 1320
Cdd:pfam13166 243 WVEQgLELHKAHLDTCPFCGQPLPAERKAAL-EAHFD--------DEFTEFQNRLQKLIEKVESAISSLLAQL------- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1321 eATRMTLTEALEKNEELLKKIHDD-DKHILELQFTIQRLEentaAKENLLLREREQNDATTKAQIESQerneqllkrfvd 1399
Cdd:pfam13166 307 -PAVSDLASLLSAFELDVEDIESEaEVLNSQLDGLRRALE----AKRKDPFKSIELDSVDAKIESIND------------ 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1400 vdrKIDLLQDTIERigENSTIKDallLSERQEKDAIKKELVEAgERNEELIMKIED----TDKKIEHLQNAIIKLEGDIE 1475
Cdd:pfam13166 370 ---LVASINELIAK--HNEITDN---FEEEKNKAKKKLRLHLV-EEFKSEIDEYKDkyagLEKAINSLEKEIKNLEAEIK 440
|
410 420 430
....*....|....*....|....*....|
gi 1002232322 1476 AKDislEAAREENDTIRKSLAEAQEKNEEL 1505
Cdd:pfam13166 441 KLR---EEIKELEAQLRDHKPGADEINKLL 467
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1381-1618 |
1.61e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1381 KAQIESQERNEqLLKRFVDVDRKIDLLQDTIERIGENstiKDAlllsERQEKDAIKKELVEAGERNEElimkiedtdkkI 1460
Cdd:PRK02224 193 KAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQ---REQ----ARETRDEADEVLEEHEERREE-----------L 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1461 EHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISdneyrihlLQDTAQKLQVDAISRLSSFVME 1540
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1541 KQESDAAKR-ALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQATATP 1618
Cdd:PRK02224 326 LRDRLEECRvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1055-1282 |
1.69e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 45.40 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRL 1134
Cdd:pfam00261 11 DEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENRALKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1135 EESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQ 1214
Cdd:pfam00261 91 EEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEASEEKASER 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1215 LADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNastLKLLAEAHLEIDELI 1282
Cdd:pfam00261 171 EDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKY---KAISEELDQTLAELN 235
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
986-1475 |
1.78e-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: 46.56 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 986 LTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQrleeTIQEREALLLAERQEKEEasavIAESQArneaFASKLEDAE 1065
Cdd:pfam05667 172 RKGKTLKNSKELKEFYSEYLPPVTAQPSSRASVVP----SLLERNAAELAAAQEWEE----EWNSQG----LASRLTPEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1066 KQIDLLQETVQRFEEAITKLQssvtiekQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLettiqrleesltekdall 1145
Cdd:pfam05667 240 YRKRKRTKLLKRIAEQLRSAA-------LAGTEATSGASRSAQDLAELLSSFSGSSTTDTGL------------------ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1146 tTERQETEATKKLlseaQYKNEellkkiedADKSIAHYHDTTQRLEEnvtavensLKAERQhngaimkqladaqVEIGEL 1225
Cdd:pfam05667 295 -TKGSRFTHTEKL----QFTNE--------APAATSSPPTKVETEEE--------LQQQRE-------------EELEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1226 QRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNAS----------TLKLLAEAhleiDELIRKLEdsdrksDSL 1295
Cdd:pfam05667 341 QEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEElekqykvkkkTLDLLPDA----EENIAKLQ------ALV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1296 QSTIKRLEEdgIAKEallltekqaHEATRMTLTEALEKNEELLKKIHDDDKHILE----LQFTIQRLEENTAAKENL--- 1368
Cdd:pfam05667 411 DASAQRLVE--LAGQ---------WEKHRVPLIEEYRALKEAKSNKEDESQRKLEeikeLREKIKEVAEEAKQKEELykq 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1369 LLREREQ--NDAT----------TKAQIESQERN-EQLLKRFVDVDRKIDLLQDTIERigeNSTIKDALLLSERQEKDAI 1435
Cdd:pfam05667 480 LVAEYERlpKDVSrsaytrrileIVKNIKKQKEEiTKILSDTKSLQKEINSLTGKLDR---TFTVTDELVFKDAKKDESV 556
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1002232322 1436 K---KELVEAGERNEELIMKIEDTDKKiehlQNAIIKLEGDIE 1475
Cdd:pfam05667 557 RkayKYLAALHENCEQLIQTVEETGTI----MREIRDLEEQIE 595
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
900-1388 |
1.89e-04 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 46.60 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 900 LTNRLGLEKKLRTDLEKskvaeVSKLQAALNEMEQRMQDVTAMQERESAKKAVE--EALEQ-EREKISSLTSEIEGLKAL 976
Cdd:COG5244 71 LLNGNAAYEKIKGGLVC-----ESKGMDKDGEIKQENHEDRIHFEESKIRRLEEtiEALKStEKEEIVELRRENEELDKI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 977 --LVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLaERQEKEEASAVIAESQARN 1054
Cdd:COG5244 146 nlSLRERISSEEPELNKDGSKLSYDELKEFVEESRVQVYDMVELVSDISETLNRNGSIQR-SSVRECERSNIHDVLFLVN 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKledaekqIDLLQETVQRFEEAITKLQSSVTIEKQQH---EETVVQLAEAQAKIDeLLREAGDTDEKSTQLETTI 1131
Cdd:COG5244 225 GILDGV-------IDELNGELERLRRQLVSLMSSHGIEVEENsrlKATLEKFQSLELKVN-TLQEELYQNKLLKKFYQIY 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1132 QRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKsIAHYHDTTQRLEENVTAVENSLKAERQHNGAI 1211
Cdd:COG5244 297 EPFAQAALSSQLQYLAEVIESENFGKLENIEIHIILKVLSSISYALH-IYTIKNTPDHLETTLQCFVNIAPISMWLSEFL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1212 MKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLL-LTEREQNASTLKLLAEAH--LEIDELIRKLEDS 1288
Cdd:COG5244 376 QRKFSSKQETAFSICQFLEDNKDVTLILKILHPILETTVPKLLAFLrTNSNFNDNDTLCLIGSLYeiARIDKLIGKEEIS 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1289 DRKSDSLQSTIKRLEEDGIAKeaLLLTEKQaheATRMTLTEALEKN----EELLKKIHDDDKHILELQFTIQRL-EENTA 1363
Cdd:COG5244 456 KQDNRLFLYPSCDITLSSILT--ILFSDKL---EVFFQGIESLLENitifPEQPSQQTSDSENIKENSLLSDRLnEENIR 530
|
490 500
....*....|....*....|....*
gi 1002232322 1364 AKENLLLREREQNDATTKAQIESQE 1388
Cdd:COG5244 531 LKEVLVQKENMLTEETKIKIIIGRD 555
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
879-1077 |
1.95e-04 |
|
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: 45.99 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAAlNEMEQRMQDVTAMQERESAKKAVEEALEQ 958
Cdd:TIGR02794 73 LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE-EAKAKQAAEAKAKAEAEAERKAKEEAAKQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 959 EREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNEELSKEVEDADGKIKQlsDTVQRLEetiQEREALLLAERQ 1038
Cdd:TIGR02794 152 AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAA--EAAAKAE---AEAAAAAAAEAE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1002232322 1039 EKEEASAVIAESQARNEAFASKLEDAEKQ---------IDLLQETVQR 1077
Cdd:TIGR02794 227 RKADEAELGDIFGLASGSNAEKQGGARGAaagsevdkyAAIIQQAIQQ 274
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1188-1533 |
2.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1188 QRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNAST 1267
Cdd:COG4372 20 PKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1268 LKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEedgiAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKH 1347
Cdd:COG4372 100 QEELESLQEEAEELQEELEELQKERQDLEQQRKQLE----AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1348 IL--ELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALL 1425
Cdd:COG4372 176 LSeaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1426 LSERQEKDAIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEEL 1505
Cdd:COG4372 256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
330 340
....*....|....*....|....*...
gi 1002232322 1506 LRKISDNEYRIHLLQDTAQKLQVDAISR 1533
Cdd:COG4372 336 LAELADLLQLLLVGLLDNDVLELLSKGA 363
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
891-1076 |
2.21e-04 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 44.18 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLG-LEKKLRTDLEKskvaevsKLQAALNEMEQRMQDVTAM--QERESAKKAVEEALEQEREKISSLT 967
Cdd:pfam01442 7 DELSTYAEELQEQLGpVAQELVDRLEK-------ETEALRERLQKDLEEVRAKlePYLEELQAKLGQNVEELRQRLEPYT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 968 SEiegLKALLVAEQEEndLTKKAHANAQERNEELSKEVEDADGkikQLSDTVQRLEETIQER-EALllaerqeKEEASAV 1046
Cdd:pfam01442 80 EE---LRKRLNADAEE--LQEKLAPYGEELRERLEQNVDALRA---RLAPYAEELRQKLAERlEEL-------KESLAPY 144
|
170 180 190
....*....|....*....|....*....|.
gi 1002232322 1047 IAESQARNEAFASKL-EDAEKQIDLLQETVQ 1076
Cdd:pfam01442 145 AEEVQAQLSQRLQELrEKLEPQAEDLREKLD 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1008-1206 |
2.37e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1008 ADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQS 1087
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1088 SVTIEKQQ------------------HEETVVQLAEAQAK-IDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTE 1148
Cdd:COG3883 94 ALYRSGGSvsyldvllgsesfsdfldRLSALSKIADADADlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1149 RQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQ 1206
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
947-1238 |
2.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 947 SAKKAVEEALEQEREKISSLTSEIEGLKallvaeQEENDLTKKAHANAQERNeELSKEVEDADGKIKQLSDTVQRLEETI 1026
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK------EKRDELNEELKELAEKRD-ELNAQVKELREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1027 QErealLLAERQE-KEEASAVIAE-SQARNEafASKLEDAEKQIDLLQETVQRFEEaitKLQSSV-TIEKQQheetvvQL 1103
Cdd:COG1340 74 KE----LKEERDElNEKLNELREElDELRKE--LAELNKAGGSIDKLRKEIERLEW---RQQTEVlSPEEEK------EL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1104 AEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDAL---LTTERQETEATKKLLSEAQYKNEELLKKIEDADKSI 1180
Cdd:COG1340 139 VEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIhkkIKELAEEAQELHEEMIELYKEADELRKEADELHKEI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1181 ahyhdttqrleenvtaVENSLKAERQHNG--AIMKQLADAQVEIGELQRNLEDADRRNNQ 1238
Cdd:COG1340 219 ----------------VEAQEKADELHEEiiELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
891-1199 |
2.85e-04 |
|
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: 46.00 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQ---RMQDVTAMQERESAKKAVEEALEQ--------E 959
Cdd:pfam06160 182 EKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQLEENLALlenleldeA 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 960 REKISSLTSEIEGLKALLvaEQEendltKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEE--TIQEREALLLAER 1037
Cdd:pfam06160 262 EEALEEIEERIDQLYDLL--EKE-----VDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsyTLNENELERVRGL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1038 QEK--------EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSvtiEKqqheetvvqlaEAQAK 1109
Cdd:pfam06160 335 EKQleelekryDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKD---EL-----------EAREK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1110 IDELlreagdtdekSTQLETTIQRLEES----LTEK-DALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYH 1184
Cdd:pfam06160 401 LDEF----------KLELREIKRLVEKSnlpgLPESyLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLY 470
|
330
....*....|....*
gi 1002232322 1185 DTTQRLEENVTAVEN 1199
Cdd:pfam06160 471 EKTEELIDNATLAEQ 485
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
875-1144 |
2.86e-04 |
|
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: 46.12 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALneMEQRMQDVTAMQERESAKKAVEE 954
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL--LASRQLALQKMQSEKEQLTYWKE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQEREKISSLTSEIEGLKALlVAEQEENDLTKKAHANAQErneELSKEVEdadGKIKQLSDTVQRLEETIQEREAL-L 1033
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDRE-FNEIENASSSLGSDLAARE---DALNQSL---KELMHQARTVLKARTEAHFNNNEeV 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1034 LAERQEKEEASAVIAESQARNEAFAsklEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDEL 1113
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLRE---EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
250 260 270
....*....|....*....|....*....|.
gi 1002232322 1114 LREAGDTDEKSTQLETTIQRLEESLTEKDAL 1144
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1322-1558 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1322 ATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVD 1401
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1402 RKIDLLQD-------TIERIGENSTIKdaLLLSERQEKDAIKkelveAGERNEELIMKIEDTDKKIEHLQNAIIKLEGDI 1474
Cdd:COG4942 97 AELEAQKEelaellrALYRLGRQPPLA--LLLSPEDFLDAVR-----RLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1475 EAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDN----EYRIHLLQDTAQKLQvDAISRLssfvmEKQESDAAKRA 1550
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKElaelAAELAELQQEAEELE-ALIARL-----EAEAAAAAERT 243
|
....*...
gi 1002232322 1551 LTEARERN 1558
Cdd:COG4942 244 PAAGFAAL 251
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
908-1474 |
3.95e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 45.98 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 908 KKLRTDLEKSKVAEVSKLQAALNEMEQRMQDVtamqeresakkaveeaLEQEREKISSLTSEIEGLKAllvaeqEENDLT 987
Cdd:PTZ00440 691 KNLKKELQNLLSLKENIIKKQLNNIEQDISNS----------------LNQYTIKYNDLKSSIEEYKE------EEEKLE 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 988 KKAHANAQERNEELSKEVEDAdgkiKQLSDTVQRLEETIQEREALLLAERQEKEEASAViaesqarneafaskledaEKQ 1067
Cdd:PTZ00440 749 VYKHQIINRKNEFILHLYEND----KDLPDGKNTYEEFLQYKDTILNKENKISNDINIL------------------KEN 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1068 IDLLQETVQRFEEAITKLQSSVTiekqQHEETVVQLAEAQAKIDELLREAGDTDE---KSTQLETTIQRLEESLTEKDAL 1144
Cdd:PTZ00440 807 KKNNQDLLNSYNILIQKLEAHTE----KNDEELKQLLQKFPTEDENLNLKELEKEfneNNQIVDNIIKDIENMNKNINII 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1145 --LTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKA--ERQHNGAIMKQL---AD 1217
Cdd:PTZ00440 883 ktLNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINTDNIIQKNEKLNLLNNLNKEKEkiEKQLSDTKINNLkmqIE 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1218 AQVEI---------GELQRNLEDADRRNNQLQDSLQRLEenvgakeSLLLTEREQNASTLKLLAEAHLEIDELIRKLEDS 1288
Cdd:PTZ00440 963 KTLEYydkskeninGNDGTHLEKLDKEKDEWEHFKSEID-------KLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKE 1035
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1289 DRKS--DSLQSTIKRLEEDGIAKEALLLT---EKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQftiQRLEENTA 1363
Cdd:PTZ00440 1036 KGKEieEKVDQYISLLEKMKTKLSSFHFNidiKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIK---NKSHEHVV 1112
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1364 AKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDtierigenstIKDALLLSERQEKDAIKKELVEAG 1443
Cdd:PTZ00440 1113 NADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNE----------VNEIEIEYERILIDHIVEQINNEA 1182
|
570 580 590
....*....|....*....|....*....|.
gi 1002232322 1444 ERNEELIMKIEDTDKKIEHLQNAIIKLEGDI 1474
Cdd:PTZ00440 1183 KKSKTIMEEIESYKKDIDQVKKNMSKERNDH 1213
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1233-1620 |
4.01e-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: 45.33 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1233 DRRNNQLQDSlQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLE-EDGIAKEA 1311
Cdd:COG5185 140 VEKLDEIADI-EASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKEsETGNLGSE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1312 LLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLREREQNDATTKAQIESQERNE 1391
Cdd:COG5185 219 STLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKI 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1392 QLLKRFVDVDRKIDLLQDTIERIGENSTIKDALllSERQEKdaIKKELVEAGERNEELIMKIEDTDKKIEHLQNAIIKLE 1471
Cdd:COG5185 299 AEYTKSIDIKKATESLEEQLAAAEAEQELEESK--RETETG--IQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSK 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1472 GDIEAKDIS--LEAAREENDTIRKslaEAQEKNEELLRKISDNeYRIHLLQdtAQKLQVDAISRLSSFVMEKQESDAAKR 1549
Cdd:COG5185 375 SSEELDSFKdtIESTKESLDEIPQ---NQRGYAQEILATLEDT-LKAADRQ--IEELQRQIEQATSSNEEVSKLLNELIS 448
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1550 ALTEARERNEDLLKRN--EDLLKRNDDLIKKIEESSKTITQLQETL----QRLEGKSTNLEAENQVLRQQATATPPS 1620
Cdd:COG5185 449 ELNKVMREADEESQSRleEAYDEINRSVRSKKEDLNEELTQIESRVstlkATLEKLRAKLERQLEGVRSKLDQVAES 525
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
891-1174 |
4.42e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 891 EKLEERVEELTNRLGLEKKLRTDLEK----------SKVAEVSKLQAALNEM-EQRMQDVTAMQERESAKKAVEEALEQE 959
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEelkelaekrdELNAQVKELREEAQELrEKRDELNEKVKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 960 REKISSLTSEiegLKALLVAEQEENDLTKK-AHANAQERNEELSKEVEdadgkiKQLSDTVQRLEETIQEREALLLAERQ 1038
Cdd:COG1340 91 REELDELRKE---LAELNKAGGSIDKLRKEiERLEWRQQTEVLSPEEE------KELVEKIKELEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1039 ekeeasavIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLqssvtieKQQHEETVVQLAEAQAKIDELLREAG 1118
Cdd:COG1340 162 --------LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL-------YKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1119 DTDEKSTQLETTIQRLEESLTEKDallttERQETEATKKLLSEAQYKNEELLKKIE 1174
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLR-----KKQRALKREKEKEELEEKAEEIFEKLK 277
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1384-1612 |
4.75e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1384 IESQERNEQLLKRFVDVDR---KIDLLQDTIERIGENSTIKDALLLSERQEKDAIK---KELVEAGERNEELIMKIEDTD 1457
Cdd:PRK03918 141 LESDESREKVVRQILGLDDyenAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKekeKELEEVLREINEISSELPELR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1458 KKIEHLQNAIIKLEGDIEakdiSLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQ-----VDAIS 1532
Cdd:PRK03918 221 EELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelkekAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1533 RLSSFvmeKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQ 1612
Cdd:PRK03918 297 KLSEF---YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
|
| CCDC14 |
pfam15254 |
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ... |
1114-1323 |
4.93e-04 |
|
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.
Pssm-ID: 464594 Cd Length: 857 Bit Score: 45.18 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 LREAGDTDEKSTQLETTIQRLeeSLTEKDALLTTERQETEATKKLLseaQYKNEELLKKIEDADKSIAHYHDTTQRLEEn 1193
Cdd:pfam15254 410 LREQEKTEKTSGSGDCNLELF--SLQSLNMSLQNQLQESLKSQELL---QSKNEELLKVIENQKEENKKLTKIFKEKEQ- 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1194 vTAVENslkaeRQH----NGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDSL-QRLEENVGAKEsllLTEREQNaSTL 1268
Cdd:pfam15254 484 -TLLEN-----KQQfdieTTRVKIELEEALVNMKSFQFKLEAAEKENQILGITLrQRDAEVTRLRE---LTRTLQG-SMA 553
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1269 KLLAEahLEIDELIRKLEDSDRKS-----------------DSLQSTIKRLEEDGIAKEALLLTEKQAHEAT 1323
Cdd:pfam15254 554 KLLSD--LSMDTARPKPGNNLTKSllniydkqlqhdpapahTSIMSYLKKLETNHSFTHSEPLSTIKNEETI 623
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
944-1091 |
4.98e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 944 ERESAKKAVEeALEQEREKISSLTSE------IEGLKALLVA--------EQEENDLTKKAHANAQERNEELSKEVEDAD 1009
Cdd:COG2433 334 ERDALAAALK-AYDAYKNKFERVEKKvppdvdRDEVKARVIRglsieealEELIEKELPEEEPEAEREKEHEERELTEEE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1010 GKIKQLSDTVQRLE--------------ETIQEREA---LLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQ 1072
Cdd:COG2433 413 EEIRRLEEQVERLEaeveeleaeleekdERIERLERelsEARSEERREIRKDREISRLDREIERLERELEEERERIEELK 492
|
170
....*....|....*....
gi 1002232322 1073 ETVQRFEEAITKLQSSVTI 1091
Cdd:COG2433 493 RKLERLKELWKLEHSGELV 511
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
884-1040 |
5.02e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.59 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEELTnrlglekKLRTDLEKSKVAEVSKLQAALNEMEQRMQDV-TAMQEResaKKAVEEALEQERE- 961
Cdd:cd00176 43 EALEAELAAHEERVEALN-------ELGEQLIEEGHPDAEEIQERLEELNQRWEELrELAEER---RQRLEEALDLQQFf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 962 -KISSLTSEIEGLKALLVAEQEENDLTKKAhaNAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEK 1040
Cdd:cd00176 113 rDADDLEQWLEEKEAALASEDLGKDLESVE--ELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEE 190
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1068 |
5.03e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKsKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEE 954
Cdd:COG4913 679 RLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 AL--EQEREKISSLTSEIEGLKALLvaEQEENDLTKKAHA-NAQERNE--ELSKEVEDADGKIKQLsdtvQRLEETIqer 1029
Cdd:COG4913 758 ALgdAVERELRENLEERIDALRARL--NRAEEELERAMRAfNREWPAEtaDLDADLESLPEYLALL----DRLEEDG--- 828
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1002232322 1030 eallLAERQEKeeasavIAESQARNE-----AFASKLEDAEKQI 1068
Cdd:COG4913 829 ----LPEYEER------FKELLNENSiefvaDLLSKLRRAIREI 862
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
913-1192 |
5.11e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 913 DLEKSkVAEVSKLQAALNEMEQRMQDVTAMQERESAKKA----VEEALEQEREKISSLTSEIEGLKALLVAE----QEEN 984
Cdd:PLN02939 157 DLEKI-LTEKEALQGKINILEMRLSETDARIKLAAQEKIhveiLEEQLEKLRNELLIRGATEGLCVHSLSKEldvlKEEN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 985 DLTKkahANAQERNEELSkEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEkeeasaVIAESQARNEAFASKLEDA 1064
Cdd:PLN02939 236 MLLK---DDIQFLKAELI-EVAETEERVFKLEKERSLLDASLRELESKFIVAQED------VSKLSPLQYDCWWEKVENL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1065 EkqiDLLQETVQRFEEAITKLqssvtiekQQHEEtvvqLAEAQAKIDELLREAGDTDEKSTQLETTIQRLeesltekdal 1144
Cdd:PLN02939 306 Q---DLLDRATNQVEKAALVL--------DQNQD----LRDKVDKLEASLKEANVSKFSSYKVELLQQKL---------- 360
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1002232322 1145 ltterqeteatKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEE 1192
Cdd:PLN02939 361 -----------KLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE 397
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
995-1365 |
5.90e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 995 QERNEELSKEVEDADGKIKQLSDTVQRLEETIQeREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQET 1074
Cdd:PLN02939 48 KKRGKNIAPKQRSSNSKLQSNTDENGQLENTSL-RTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1075 VQRFEEAITKLQSSvtiekqqhEETVVQLAEAQAkidellreagdtdekstqleTTIQRLEESLTEKDAL------LTTE 1148
Cdd:PLN02939 127 DFQLEDLVGMIQNA--------EKNILLLNQARL--------------------QALEDLEKILTEKEALqgkiniLEMR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1149 RQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRN 1228
Cdd:PLN02939 179 LSETDARIKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEER 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1229 LEDADRRNNQLQDSLQRLEEN-VGAKESLL-LTEREQNA-----STLK-LLAEAHLEIDELIRKLEDSDRKSDSLQSTIK 1300
Cdd:PLN02939 259 VFKLEKERSLLDASLRELESKfIVAQEDVSkLSPLQYDCwwekvENLQdLLDRATNQVEKAALVLDQNQDLRDKVDKLEA 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1301 RLEEDGIAKEALLLTEKQAHEATrmTLTEALEK-NEELLKKIHDDDKHILELQFTIQRLEENTAAK 1365
Cdd:PLN02939 339 SLKEANVSKFSSYKVELLQQKLK--LLEERLQAsDHEIHSYIQLYQESIKEFQDTLSKLKEESKKR 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1017-1557 |
5.93e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1017 DTVQRLEETIQE----REALLLAERQEK------EEASAVIAESQARNEafaskledaekqidllqetvqrfEEAITKLQ 1086
Cdd:PRK04863 230 KAFQDMEAALREnrmtLEAIRVTQSDRDlfkhliTESTNYVAADYMRHA-----------------------NERRVHLE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1087 SSVTIEKQQHEeTVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLtekdALLTTERQETEATKKL---LSEAQ 1163
Cdd:PRK04863 287 EALELRRELYT-SRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL----NLVQTALRQQEKIERYqadLEELE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1164 YKNEELLKKIEDADKSIAhyhdttqRLEENVTAVENSLKAerqhngaIMKQLADAQVEIGELQRnledadrRNNQLQDSL 1243
Cdd:PRK04863 362 ERLEEQNEVVEEADEQQE-------ENEARAEAAEEEVDE-------LKSQLADYQQALDVQQT-------RAIQYQQAV 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1244 QRLEEnvgAKEsllltereqnastlkLLAEAHLEIDELIRKLEDSDRKSDSLqstikrleedgiakealllTEKQAHEAT 1323
Cdd:PRK04863 421 QALER---AKQ---------------LCGLPDLTADNAEDWLEEFQAKEQEA-------------------TEELLSLEQ 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1324 RMTLTEA----LEKNEELLKKIHDDdkhilelqftIQRLEENTAAKENLLLREREQNDATTKAQIESQERN-EQLLKRFV 1398
Cdd:PRK04863 464 KLSVAQAahsqFEQAYQLVRKIAGE----------VSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSElEQRLRQQQ 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1399 DVDRkidLLQDTIERIGENSTIKDAL--LLSERQEK-DAIKKELVEAGERNEELIMKIEDTDKKIEHLqnaiiklegdiE 1475
Cdd:PRK04863 534 RAER---LLAEFCKRLGKNLDDEDELeqLQEELEARlESLSESVSEARERRMALRQQLEQLQARIQRL-----------A 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1476 AKDISLEAAREENDTIRKSLAEAQEKNEELlrkisdneyrIHLLQDTAQKLQvdaisrlsSFVMEKQESDAAKRALTEAR 1555
Cdd:PRK04863 600 ARAPAWLAAQDALARLREQSGEEFEDSQDV----------TEYMQQLLERER--------ELTVERDELAARKQALDEEI 661
|
..
gi 1002232322 1556 ER 1557
Cdd:PRK04863 662 ER 663
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
945-1538 |
5.97e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.20 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 945 RESAKKAVEEALEQEREKISSLTSEIEGLkaLLVAEQEENDLTKKAHANAQERN---EEL-SKEVEDADGKIKQLSDTVQ 1020
Cdd:NF041483 184 RAEAERLAEEARQRLGSEAESARAEAEAI--LRRARKDAERLLNAASTQAQEATdhaEQLrSSTAAESDQARRQAAELSR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1021 RLEETIQEREALLlaeRQEKEEASAVIAESQarnEAFASKLEDAEKQIDLLQETVQrfeEAITKLQSSVTIEKQQHEETV 1100
Cdd:NF041483 262 AAEQRMQEAEEAL---REARAEAEKVVAEAK---EAAAKQLASAESANEQRTRTAK---EEIARLVGEATKEAEALKAEA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQ-LAEAQAKIDELLREAGD------TDEKSTQLETTIQRLEESLT--EKDALLTTeRQETEATKKLLSEAQYKNEELLK 1171
Cdd:NF041483 333 EQaLADARAEAEKLVAEAAEkartvaAEDTAAQLAKAARTAEEVLTkaSEDAKATT-RAAAEEAERIRREAEAEADRLRG 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1172 KIED-ADKSIAHYHDTTQrlEENVTAVENSLKAERQHNGAimKQLADAQVEIGELQRNledADRRnnqlqDSLQRLEENV 1250
Cdd:NF041483 412 EAADqAEQLKGAAKDDTK--EYRAKTVELQEEARRLRGEA--EQLRAEAVAEGERIRG---EARR-----EAVQQIEEAA 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1251 GAKESlLLTEREQNASTLKLLAEAHLEI--DELIRKLEDSDRKSD-SLQSTikRLEEDGIAKEALLLTEKQAHEATRmtl 1327
Cdd:NF041483 480 RTAEE-LLTKAKADADELRSTATAESERvrTEAIERATTLRRQAEeTLERT--RAEAERLRAEAEEQAEEVRAAAER--- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1328 tEALEKNEELLKKIHDDDKHILElqfTIQRLeeNTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLL 1407
Cdd:NF041483 554 -AARELREETERAIAARQAEAAE---ELTRL--HTEAEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1408 QDTIERIGENSTIKDALLLSE-RQEKDAIKKEL-VEAGERNEELIMKIEDTDKKI----------------EHLQNAIIK 1469
Cdd:NF041483 628 QAQAEQEAERLRTEAAADASAaRAEGENVAVRLrSEAAAEAERLKSEAQESADRVraeaaaaaervgteaaEALAAAQEE 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1470 LEGDIEAKDISLEAAREENDTIRKSlaeAQEKNEELL---RKisdneyRIHLLQDTAQKLQVDAISRLSSFV 1538
Cdd:NF041483 708 AARRRREAEETLGSARAEADQERER---AREQSEELLasaRK------RVEEAQAEAQRLVEEADRRATELV 770
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
879-1092 |
6.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKvaKEKLEERVEELtnrlgleKKLRTDLEKSKVAEVSKLQAALNEMEQRmqdvtamqeresakkavEEALEQ 958
Cdd:PRK12704 47 AKKEAEAIK--KEALLEAKEEI-------HKLRNEFEKELRERRNELQKLEKRLLQK-----------------EENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 959 EREKIssltseieglkallvaEQEENDLTKKAHaNAQERNEELSKEVEDADGKIKQLsdtVQRLEE----TIQEREALLL 1034
Cdd:PRK12704 101 KLELL----------------EKREEELEKKEK-ELEQKQQELEKKEEELEELIEEQ---LQELERisglTAEEAKEILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1035 --AERQEKEEASAVI--AESQARneafasklEDAEKQI-DLLQETVQRF--EEAITKLQSSVTIE 1092
Cdd:PRK12704 161 ekVEEEARHEAAVLIkeIEEEAK--------EEADKKAkEILAQAIQRCaaDHVAETTVSVVNLP 217
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1060-1307 |
7.28e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1060 KLEDAEKQIDLLQETVQRFE----EAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDE-------KSTQLE 1128
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRkkngENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAalnklntAAAKIK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1129 TTIQRL--EESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIahyhdttQRLEEnvtavenslkaerq 1206
Cdd:PHA02562 269 SKIEQFqkVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI-------DELEE-------------- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1207 hngaIMKQLADAQVEIGELQRNLEDADR-------RNNQLQDSLQRLEEnvgakesllltEREQNASTLKLLAEahlEID 1279
Cdd:PHA02562 328 ----IMDEFNEQSKKLLELKNKISTNKQslitlvdKAKKVKAAIEELQA-----------EFVDNAEELAKLQD---ELD 389
|
250 260
....*....|....*....|....*...
gi 1002232322 1280 ELIRKLEDSDRKSDSLQSTIKRLEEDGI 1307
Cdd:PHA02562 390 KIVKTKSELVKEKYHRGIVTDLLKDSGI 417
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
607-632 |
7.30e-04 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 42.33 E-value: 7.30e-04
10 20
....*....|....*....|....*.
gi 1002232322 607 RFKVQLHELMETLSSTEPHYIRCVKP 632
Cdd:cd01363 145 IINESLNTLMNVLRATRPHFVRCISP 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
875-1053 |
7.40e-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: 44.37 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRlglEKKLRTDLEKSKvAEVSKLQAALNEMEQR--------MQDVTAMQERE 946
Cdd:COG4942 63 RIAALARRIRALEQELAALEAELAELEKE---IAELRAELEAQK-EELAELLRALYRLGRQpplalllsPEDFLDAVRRL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 947 SAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHANAQERNE-----------ELSKEVEDADGKIKQL 1015
Cdd:COG4942 139 QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEalkaerqkllaRLEKELAELAAELAEL 218
|
170 180 190
....*....|....*....|....*....|....*...
gi 1002232322 1016 SDTVQRLEETIQEREAllLAERQEKEEASAVIAESQAR 1053
Cdd:COG4942 219 QQEAEELEALIARLEA--EAAAAAERTPAAGFAALKGK 254
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
944-1346 |
9.05e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 944 ERESAKKAVEEALEQEREkissltSEIEGLKALLVAEQEENdltkkAHANAQERNEELSKEVEDADGkikqLSDTVQRLE 1023
Cdd:pfam02029 8 ARERRRRAREERRRQKEE------EEPSGQVTESVEPNEHN-----SYEEDSELKPSGQGGLDEEEA----FLDRTAKRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1024 ETIQER--EALllaERQEKEEASAVIAESQARNEafaskledaEKQIDLLQETVQRFEEAITKLQSSVTIEkqqhEETVV 1101
Cdd:pfam02029 73 ERRQKRlqEAL---ERQKEFDPTIADEKESVAER---------KENNEEEENSSWEKEEKRDSRLGRYKEE----ETEIR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1102 QLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEesltekdalltTERQETEATKKLLSEAQYKNEELLKKIEDADKsiA 1181
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVP-----------TENFAKEEVKDEKIKKEKKVKYESKVFLDQKR--G 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1182 HYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIgELQRNLEDADRRNnqlqdslQRLEEnvgaKESLLLTER 1261
Cdd:pfam02029 204 HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFL-EAEQKLEELRRRR-------QEKES----EEFEKLRQK 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1262 EQnastlkllaEAHLEIDELIRKLEDsDRKSDSLQSTIKRLEED--GIAKEALLLTEKQAHEATRMtltEALEKNEELLK 1339
Cdd:pfam02029 272 QQ---------EAELELEELKKKREE-RRKLLEEEEQRRKQEEAerKLREEEEKRRMKEEIERRRA---EAAEKRQKLPE 338
|
....*..
gi 1002232322 1340 KIHDDDK 1346
Cdd:pfam02029 339 DSSSEGK 345
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1091-1248 |
9.26e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1091 IEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEEsltekdalltterqeteatkkllseaqyKNEELL 1170
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEA----------------------------EVEELE 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002232322 1171 KKIEDADKSIAHYHDttqRLEENVTAVENSLKAERQHNgaIMKQladaqvEIGELQRNLEDADRRNNQLQDSLQRLEE 1248
Cdd:COG2433 434 AELEEKDERIERLER---ELSEARSEERREIRKDREIS--RLDR------EIERLERELEEERERIEELKRKLERLKE 500
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
886-1613 |
1.02e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEKsKVAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQerekISS 965
Cdd:PTZ00440 800 INILKENKKNNQDLLNSYNILIQKLEAHTEK-NDEELKQLLQKFPTEDENLNLKELEKEFNENNQIVDNIIKD----IEN 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 966 LTSEIEGLKALlvaeqeenDLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRlEETIQEREALLLAERQEKEEAsa 1045
Cdd:PTZ00440 875 MNKNINIIKTL--------NIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIINT-DNIIQKNEKLNLLNNLNKEKE-- 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1046 vIAESQARNEAFASKLEDAEKQIDLLQETVQRFEE---------------------AITKLQSSV--------TIEKQQH 1096
Cdd:PTZ00440 944 -KIEKQLSDTKINNLKMQIEKTLEYYDKSKENINGndgthlekldkekdewehfksEIDKLNVNYnilnkkidDLIKKQH 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1097 EETVVQlaeaqakIDELLREAG-DTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIED 1175
Cdd:PTZ00440 1023 DDIIEL-------IDKLIKEKGkEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDE 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1176 ADKSIAhyhDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLEDADRRNNQLQDslqrleenvgAKES 1255
Cdd:PTZ00440 1096 NKNKLI---EIKNKSHEHVVNADKEKNKQTEHYNKKKKSLEKIYKQMEKTLKELENMNLEDITLNE----------VNEI 1162
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1256 LLLTEReqnastlkllaeahLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEALLLTEKQAHeATRMTLTEALEKNE 1335
Cdd:PTZ00440 1163 EIEYER--------------ILIDHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDH-LTTFEYNAYYDKAT 1227
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1336 ELLKKIHDDDKHILELqftiqRLEENTAAKENLLLREREQNDATTKAQIESQERNEQLLKRFVDVDrkiDLLQDT-IERI 1414
Cdd:PTZ00440 1228 ASYENIEELTTEAKGL-----KGEANRSTNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMY---EFLISIdSEKI 1299
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1415 GENstIKDALLLSERQEKDAiKKELveagERNEELIMKIEDtdkKIEHLQNAIIKLEGDIEAKDI-----SLEAAREEND 1489
Cdd:PTZ00440 1300 LKE--ILNSTKKAEEFSNDA-KKEL----EKTDNLIKQVEA---KIEQAKEHKNKIYGSLEDKQIddeikKIEQIKEEIS 1369
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1490 TIRKSL-------AEAQEKNEELLRKISDNEYRIHLLQDTAQ-----KLQVDAISRLSSFVMEKQESDAAKRALTEARER 1557
Cdd:PTZ00440 1370 NKRKEInkylsniKSNKEKCDLHVRNASRGKDKIDFLNKHEAiepsnSKEVNIIKITDNINKCKQYSNEAMETENKADEN 1449
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002232322 1558 NEDLLKRNEDLLK-RNDDLI--------KKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQQ 1613
Cdd:PTZ00440 1450 NDSIIKYEKEITNiLNNSSIlgkktkleKKKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNEQ 1514
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1238-1612 |
1.03e-03 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 43.90 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1238 QLQDSLQRLEENVGAKESLLLTEREQNaSTLK----LLAEAHL----EIDELIRKLEDSDRKSDSLQSTIKRLEEDgiAK 1309
Cdd:pfam15742 17 QLRQNLQRLQILCTSAEKELRYERGKN-LDLKqhnsLLQEENIkikaELKQAQQKLLDSTKMCSSLTAEWKHCQQK--IR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1310 EALLLTEKQAHEatRMTLTEALEKNEELLKKIHDDDKHILELQftiQRLE-------ENTAAKENLLLRERE----QNDA 1378
Cdd:pfam15742 94 ELELEVLKQAQS--IKSQNSLQEKLAQEKSRVADAEEKILELQ---QKLEhahkvclTDTCILEKKQLEERIkeasENEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1379 TTKAQIESQERNEQLLkrfvdvDRKIDLLQDTIE--RIGENS-TIKDALLLSERQEKDAIKKELveagernEELIMKIED 1455
Cdd:pfam15742 169 KLKQQYQEEQQKRKLL------DQNVNELQQQVRslQDKEAQlEMTNSQQQLRIQQQEAQLKQL-------ENEKRKSDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1456 TDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDneyriHLLQDTAQKLQvdAISRLS 1535
Cdd:pfam15742 236 HLKSNQELSEKLSSLQQEKEALQEELQQVLKQLDVHVRKYNEKHHHHKAKLRRAKD-----RLVHEVEQRDE--RIKQLE 308
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1536 SfvmekqESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQ 1612
Cdd:pfam15742 309 N------EIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEELIKNNKRTISSVQNRVNFLDEENKQLQE 379
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
979-1133 |
1.04e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 979 AEQEENDLTKKAHANAQERN----EELSKEVEDADGKIKQLSDTVQRLEETIQEREALLlaerqEKEEasaviAESQARN 1054
Cdd:PRK12704 47 AKKEAEAIKKEALLEAKEEIhklrNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL-----EKRE-----EELEKKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1055 EAFASKLEDAEKQIDLLQETVQrfeEAITKLQ--SSVTIE--KQQHEETVVQLA--EAQAKIDELLREAGDTDEKSTQ-- 1126
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIE---EQLQELEriSGLTAEeaKEILLEKVEEEArhEAAVLIKEIEEEAKEEADKKAKei 193
|
....*..
gi 1002232322 1127 LETTIQR 1133
Cdd:PRK12704 194 LAQAIQR 200
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1121-1287 |
1.04e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1121 DEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAhyhdttqRLEENVTAVENS 1200
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------KYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1201 lkaerqhngaimKQLADAQVEIgelqrnlEDADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDE 1280
Cdd:COG1579 89 ------------KEYEALQKEI-------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
....*..
gi 1002232322 1281 LIRKLED 1287
Cdd:COG1579 150 ELAELEA 156
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1385-1596 |
1.11e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1385 ESQERNEQLLKRFVDVDRKIDLLQDTIErigENSTIKDALLLSERQEKDAIKKELVEAGERNEElimKIEDTDKKIEHLQ 1464
Cdd:PRK05771 40 LSNERLRKLRSLLTKLSEALDKLRSYLP---KLNPLREEKKKVSVKSLEELIKDVEEELEKIEK---EIKELEEEISELE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1465 NAIIKLEGDIEA----KDISLEAARE-ENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQD---------TAQKLQVDA 1530
Cdd:PRK05771 114 NEIKELEQEIERlepwGNFDLDLSLLlGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDkgyvyvvvvVLKELSDEV 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002232322 1531 ISRLSSFVMEKQE---SDAAKRALTEARERNEDLLKRNEDLL-------KRNDDLIKKIEESSKTITQLQETLQRL 1596
Cdd:PRK05771 194 EEELKKLGFERLEleeEGTPSELIREIKEELEEIEKERESLLeelkelaKKYLEELLALYEYLEIELERAEALSKF 269
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1400-1509 |
1.24e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1400 VDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGER-NEELIMKIEDTDKKIEHLQNAI--IKLEGDIEA 1476
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAeVEELEAELEEKDERIERLERELseARSEERREI 461
|
90 100 110
....*....|....*....|....*....|....
gi 1002232322 1477 -KDISLEAAREENDTIRKSLAEAQEKNEELLRKI 1509
Cdd:COG2433 462 rKDREISRLDREIERLERELEEERERIEELKRKL 495
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1453-1632 |
1.27e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1453 IEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRIHLLQDTAQKLQvdais 1532
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQ----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1533 rlssfvmekQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAENQVLRQ 1612
Cdd:COG4372 108 ---------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE 178
|
170 180
....*....|....*....|
gi 1002232322 1613 QATATPPSTAKSSASRSKIT 1632
Cdd:COG4372 179 AEAEQALDELLKEANRNAEK 198
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
879-1067 |
1.34e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEE-----RVEELTNRLGLEKKLRTD-------LEKSKVAEVSKLQaalnemEQRMQDVTAMQERE 946
Cdd:pfam15709 333 ASRDRLRAERAEMRRLEverkrREQEEQRRLQQEQLERAEkmreeleLEQQRRFEEIRLR------KQRLEEERQRQEEE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 947 SAKKAVEEALEQEREKissLTSEIEGLKALLVAEQEENDLTKKAHANAQERneelsKEVEdadgkiKQLSDTVQRLEETI 1026
Cdd:pfam15709 407 ERKQRLQLQAAQERAR---QQQEEFRRKLQELQRKKQQEEAERAEAEKQRQ-----KELE------MQLAEEQKRLMEMA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1002232322 1027 QEREALLLAERQEKEEASAVIAESQARNEAFASKL--EDAEKQ 1067
Cdd:pfam15709 473 EEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLalEEAMKQ 515
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
875-992 |
1.35e-03 |
|
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: 43.59 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 875 QLRMAARDTQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKVAEVSKLQAALNEMEQRMQdvtamqerESAKKAVEE 954
Cdd:pfam09731 331 ELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQ--------REFLQDIKE 402
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1002232322 955 ALEQER----EKISSLTSEIEGLKALLVAEQEENDLTKKAHA 992
Cdd:pfam09731 403 KVEEERagrlLKLNELLANLKGLEKATSSHSEVEDENRKAQQ 444
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
877-1112 |
1.39e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.32 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 877 RMAARDTQALK-VAKEKLEE---------RVEEL-TNRLGLEKKLR----TDLEKS------------------------ 917
Cdd:COG2268 112 RFLGRDPEEIEeLAEEKLEGalravaaqmTVEELnEDREKFAEKVQevagTDLAKNglelesvaitdledennyldalgr 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 918 -KVAEVSKLQA-ALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENdlTKKAHANAQ 995
Cdd:COG2268 192 rKIAEIIRDARiAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA--RAEAEAAYE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 996 ERNEELSKEVEdadgkikqlsdtvQRLEETIQEREALLL---AERQEKEEASAVIAESQARNEAfASKLEDAEKQIDLLQ 1072
Cdd:COG2268 270 IAEANAEREVQ-------------RQLEIAEREREIELQekeAEREEAELEADVRKPAEAEKQA-AEAEAEAEAEAIRAK 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1002232322 1073 -----ETVQRFEEAITKLQSSVTIEK--QQHEETVVQLAEAQAKIDE 1112
Cdd:COG2268 336 glaeaEGKRALAEAWNKLGDAAILLMliEKLPEIAEAAAKPLEKIDK 382
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1232-1616 |
1.40e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1232 ADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAE-------AHLEIDELIRKLEDSDRKSDSLQ----STIK 1300
Cdd:pfam12128 207 EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHFGYKSDETLIASRQeerqETSA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1301 RLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKhilelQFTIQRLEENTAAKENL--------LLRE 1372
Cdd:pfam12128 287 ELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHG-----AFLDADIETAAADQEQLpswqseleNLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1373 R------EQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERigENSTIKDALLLSERQEKDAIKKELVEAGERN 1446
Cdd:pfam12128 362 RlkaltgKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDR--QLAVAEDDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1447 EELIMKIEDTDKKIEHLQnAIIKLEGDIEAKDISLEAAREENDTIRKS-------LAEAQEKNEELLRKISDNEYR---- 1515
Cdd:pfam12128 440 YRLKSRLGELKLRLNQAT-ATPELLLQLENFDERIERAREEQEAANAEverlqseLRQARKRRDQASEALRQASRRleer 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1516 ------------------IHLLQDTAQ--------------------------------------KLQVDAISRLSSFVM 1539
Cdd:pfam12128 519 qsaldelelqlfpqagtlLHFLRKEAPdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAAS 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1540 EKQ---ESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLeaenQVLRQQATA 1616
Cdd:pfam12128 599 EEElreRLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSE----KDKKNKALA 674
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
884-1029 |
1.41e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 884 QALKVAKEKLEERVEELTNRLGLEKKLRTDLE---KSKVAEVSKLQAALNEMeQRMQDVTAMQ-ERESAKKAVEEALEQE 959
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNV-RNNKEYEALQkEIESLKRRISDLEDEI 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 960 REkissLTSEIEGLKALLVAEQEENDLTKKAHANAQernEELSKEVEDADGKIKQLSDTVQRLEETIQER 1029
Cdd:COG1579 113 LE----LMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
883-1250 |
1.42e-03 |
|
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: 43.69 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 883 TQALKVAKEKLEERVEELTNRLGLEKKLRTDLEKSKV--AEVSK---------------LQAALNEME---QRMQDVTAM 942
Cdd:pfam06160 92 EELLDDIEEDIKQILEELDELLESEEKNREEVEELKDkyRELRKtllanrfsygpaideLEKQLAEIEeefSQFEELTES 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 943 QERESAKKAVEEA---LEQEREKISSLTSEIEGLKALLVAEQEEndlTKKAHANAQERNEELskEVEDADGKIKQLSDTV 1019
Cdd:pfam06160 172 GDYLEAREVLEKLeeeTDALEELMEDIPPLYEELKTELPDQLEE---LKEGYREMEEEGYAL--EHLNVDKEIQQLEEQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1020 QRLEETIqerealllaERQEKEEASAviaesqarneafasKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEET 1099
Cdd:pfam06160 247 EENLALL---------ENLELDEAEE--------------ALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1100 VVQLAEAQAKIDELLRE---AGDTDEKSTQLETTIQRLEESLTEkdallttERQETEATKKLLSEAQYKNEELLKKIEDA 1176
Cdd:pfam06160 304 EEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDE-------IVERLEEKEVAYSELQEELEEILEQLEEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1177 DKSIAHYHDTTQRLEENVTAVENSLK------------AERQH----NGAIMKQLADAQVEIGELQRNLE----DADRRN 1236
Cdd:pfam06160 377 EEEQEEFKESLQSLRKDELEAREKLDefklelreikrlVEKSNlpglPESYLDYFFDVSDEIEDLADELNevplNMDEVN 456
|
410
....*....|....*..
gi 1002232322 1237 NQL---QDSLQRLEENV 1250
Cdd:pfam06160 457 RLLdeaQDDVDTLYEKT 473
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1214-1513 |
1.44e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1214 QLADAQVEIGELQRNLEDADRRNNQLQDSL-----QRLEENVGAKE--SLLLTEREQNASTLKLLAEAHLEIDELIRKLE 1286
Cdd:COG1340 9 SLEELEEKIEELREEIEELKEKRDELNEELkelaeKRDELNAQVKElrEEAQELREKRDELNEKVKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1287 DSDRKSDSLQSTIKRLEEDGIAKEALlltEKQAHEATRMTLTEALEKNEEllKKIHDddkhilelqfTIQRLEEntaake 1366
Cdd:COG1340 89 ELREELDELRKELAELNKAGGSIDKL---RKEIERLEWRQQTEVLSPEEE--KELVE----------KIKELEK------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1367 nlLLREREQndattkaQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERN 1446
Cdd:COG1340 148 --ELEKAKK-------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002232322 1447 EELIMKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREEndtirKSLAEAQEKNEELLRKISDNE 1513
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE-----KEKEELEEKAEEIFEKLKKGE 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1451-1606 |
1.51e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1451 MKIEDTDKKIEHLQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLRKISDNEYRihllQDTAQKL-QVD 1529
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ----LGNVRNNkEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002232322 1530 AISR-LSSFVMEKQESDAAKRALTEARERNEDLLKRNEDLL-KRNDDLIKKIEESSKTITQLQETLQRLEGKSTNLEAE 1606
Cdd:COG1579 93 ALQKeIESLKRRISDLEDEILELMERIEELEEELAELEAELaELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CR6_interact |
pfam10147 |
Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family ... |
923-1043 |
1.53e-03 |
|
Growth arrest and DNA-damage-inducible proteins-interacting protein 1; Members of this family of proteins act as negative regulators of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occur also in the absence of GADD45 proteins. Furthermore, they act as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity.
Pssm-ID: 431088 [Multi-domain] Cd Length: 204 Bit Score: 42.15 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 923 SKLQAALNEMEQRMQ--DVTAMQERESAKKAVEEALEQERE-----KISSLTSEIEGLKALLVAEQEENDLTKKAHANAQ 995
Cdd:pfam10147 71 SAEQLEELEAEEREWypSLAQMLESNRAQKAEKEARRQAREqeiakKMAKMPQWIADWNAQKAKREAEAQAAKERKERLV 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1002232322 996 ER-NEELSKEVEDADGKIKQLsdtVQRLEEtiQEREALLLAERQEKEEA 1043
Cdd:pfam10147 151 AEaREHFGFKVDPRDERFKEM---LQQKEK--EDKKKVKEAKRKEKEEK 194
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
886-1117 |
1.78e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 886 LKVAKEKLEERVEELTNRLGLEKKLRTDLEKSK--------------VAEVSKLQAALNEMEQRMQDVTAMQERESAKKA 951
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNeeqaewkelekeeeREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 952 VE-EALEQEREKISSLTSEIEGLKALLVAEQeendltkkahanaQERNEELsKEVEDADGKIKQLSDTVQRLEETIQERE 1030
Cdd:pfam13868 184 REiARLRAQQEKAQDEKAERDELRAKLYQEE-------------QERKERQ-KEREEAEKKARQRQELQQAREEQIELKE 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1031 ALLLAERQEKEEASAVIAESQArnEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKI 1110
Cdd:pfam13868 250 RRLAEEAEREEEEFERMLRKQA--EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAER 327
|
....*..
gi 1002232322 1111 DELLREA 1117
Cdd:pfam13868 328 RERIEEE 334
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1132-1478 |
1.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1132 QRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAI 1211
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1212 MKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEenvgaKESLLLTEREQNASTlkllaeahlEIDELIRKLEDSDRK 1291
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ-----KERQDLEQQRKQLEA---------QIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1292 SDSLQSTIKRLEEDGIAKEALLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLR 1371
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1372 EREQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGENSTIKDALLLSERQEKDAIKKELVEAGERNEELIM 1451
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330 340
....*....|....*....|....*..
gi 1002232322 1452 KIEDTDKKIEHLQNAIIKLEGDIEAKD 1478
Cdd:COG4372 312 ALEDALLAALLELAKKLELALAILLAE 338
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
883-1192 |
2.10e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 883 TQALKVAKEKLEERVEELTNRLGLEKKLRT----------DLEKSKVAEVSKLQAALNEMEQRMqdvtamqeresakkav 952
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNREeveqlkdlyrELRKSLLANRFSFGPALDELEKQL---------------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 953 eEALEQEREKISSLTSEIEGLKA---LLVAEQEENDLTKKAhanaqERNEELSKEVE-DADGKIKQLSDTVQRLEE---- 1024
Cdd:PRK04778 175 -ENLEEEFSQFVELTESGDYVEAreiLDQLEEELAALEQIM-----EEIPELLKELQtELPDQLQELKAGYRELVEegyh 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1025 ----TIQEREALLLAERQEkeeASAVIAESQArnEAFASKLEDAEKQIDLLQETVQRfeEAITKLQssvtIEKQQhEETV 1100
Cdd:PRK04778 249 ldhlDIEKEIQDLKEQIDE---NLALLEELDL--DEAEEKNEEIQERIDQLYDILER--EVKARKY----VEKNS-DTLP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1101 VQLAEAQAKIDELLRE----------AGDTDEKSTQLETTIQRLEESLTEKDalltterQETEATKKLLSEAQYKNEELL 1170
Cdd:PRK04778 317 DFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEIT-------ERIAEQEIAYSELQEELEEIL 389
|
330 340
....*....|....*....|..
gi 1002232322 1171 KKIEDADKSIAHYHDTTQRLEE 1192
Cdd:PRK04778 390 KQLEEIEKEQEKLSEMLQGLRK 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1296-1483 |
2.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1296 QSTIKRLEE--DGIAKEAllltEKQAHEATRMTLTEAlekNEELLKKIHDDDKHILELQFTIQRLEENTAAKENLLLRER 1373
Cdd:PRK12704 30 EAKIKEAEEeaKRILEEA----KKEAEAIKKEALLEA---KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1374 EQNDAtTKAQIESQE-----RNEQLLKRFVDVDRKIDLLQDTIERIGEnstikdallLSERQEKDAIKKELVEagERNEE 1448
Cdd:PRK12704 103 ELLEK-REEELEKKEkeleqKQQELEKKEEELEELIEEQLQELERISG---------LTAEEAKEILLEKVEE--EARHE 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1002232322 1449 LIMKIedtdKKIEhlqnAIIKLEGDIEAKDISLEA 1483
Cdd:PRK12704 171 AAVLI----KEIE----EEAKEEADKKAKEILAQA 197
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
979-1123 |
3.27e-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: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 979 AEQEENDLTKKAHANAQERNEELSKEVEdadgKIKQLSDTVQRLEETIQEREALLLAERQEKEEASA---VIAESQARNE 1055
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQA----RQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAkakQAAEAKAKAE 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002232322 1056 AFASK--LEDAEKQidllQETVQRFEE-AITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEK 1123
Cdd:TIGR02794 138 AEAERkaKEEAAKQ----AEEEAKAKAaAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
927-1133 |
3.36e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.97 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 927 AALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLvaeQEENDLTKKAHANAQERNEELSKEVE 1006
Cdd:cd22656 94 AEILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKL---TDFENQTEKDQTALETLEKALKDLLT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1007 DADGKI--KQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITK 1084
Cdd:cd22656 171 DEGGAIarKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEK 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1085 LQSS-VTIEKqqheetvvQLAEAQAKIDELLREAGDTDEKSTQLETTIQR 1133
Cdd:cd22656 251 LQGAwQAIAT--------DLDSLKDLLEDDISKIPAAILAKLELEKAIEK 292
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1034-1284 |
3.39e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1034 LAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAkIDEL 1113
Cdd:pfam12795 5 LEKAKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLS-LEEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1114 LREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAqyknEELLKKIEDADKSIAHyhdtTQRleen 1193
Cdd:pfam12795 84 EQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQI----RNRLNGPAPPGEPLSE----AQR---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1194 vtaveNSLKAERQHNGAIMKQL------ADAQVEIGELQRNLedADRRNNQLQDSLQRLEENVGAKeslLLTEREQNAST 1267
Cdd:pfam12795 152 -----WALQAELAALKAQIDMLeqellsNNNRQDLLKARRDL--LTLRIQRLEQQLQALQELLNEK---RLQEAEQAVAQ 221
|
250
....*....|....*..
gi 1002232322 1268 LKLLAEAHLEIDELIRK 1284
Cdd:pfam12795 222 TEQLAEEAAGDHPLVQQ 238
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
921-1129 |
3.48e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.96 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 921 EVSKLQAALNEMEQRMQDVTAMQERESAKKAVEEALEQEREKissltseieglKALLVAEQEENDLTKKAhanAQERnEE 1000
Cdd:COG1842 31 AIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEE-----------KARLALEKGREDLAREA---LERK-AE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1001 LSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQAR---NEAFAS-KLEDAEkqidllqETVQ 1076
Cdd:COG1842 96 LEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvNEALSGiDSDDAT-------SALE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1077 RFEEAITKLqssvtiekqqheetvvqlaEAQAKIDELLREAGDTDEKSTQLET 1129
Cdd:COG1842 169 RMEEKIEEM-------------------EARAEAAAELAAGDSLDDELAELEA 202
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1035-1177 |
3.60e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1035 AERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQssvtiEKQQheetvvQLAEAQAKIDELL 1114
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAA-----LKQK------QAEEAAAKAAAAA 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002232322 1115 REAGDTDEKstQLETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDAD 1177
Cdd:PRK09510 146 KAKAEAEAK--RAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAE 206
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
1235-1346 |
3.66e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 40.66 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1235 RNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHL-EIDELIRKL-------EDSDRKSDSLQSTIkRLEEDG 1306
Cdd:pfam15619 75 RLRRLQEKERDLERKLKEKEAELLRLRDQLKRLEKLSEDKNLaEREELQKKLeqleaklEDKDEKIQDLERKL-ELENKS 153
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1002232322 1307 IAKEalLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDK 1346
Cdd:pfam15619 154 FRRQ--LAAEKKKHKEAQEEVKILQEEIERLQQKLKEKER 191
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1033-1276 |
3.76e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1033 LLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRFEEAitKLQSsvtIEKQQHEETVVQLAEAQaKIDE 1112
Cdd:COG0497 153 LEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAA--ALQP---GEEEELEEERRRLSNAE-KLRE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1113 LLREA-----GDTDEKSTQLETTIQRLEEsLTEKDALLtterqetEATKKLLSEAQYKneellkkIEDADKSIAHYHDTT 1187
Cdd:COG0497 227 ALQEAlealsGGEGGALDLLGQALRALER-LAEYDPSL-------AELAERLESALIE-------LEEAASELRRYLDSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1188 ----QRLEEnvtaVENSL----KAERQHNGAImKQLADAQVEIGELQRNLEDADRRNNQLQDSLQRLEENVgAKESLLLT 1259
Cdd:COG0497 292 efdpERLEE----VEERLallrRLARKYGVTV-EELLAYAEELRAELAELENSDERLEELEAELAEAEAEL-LEAAEKLS 365
|
250
....*....|....*...
gi 1002232322 1260 E-REQNASTLKLLAEAHL 1276
Cdd:COG0497 366 AaRKKAAKKLEKAVTAEL 383
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
931-1196 |
4.60e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 41.48 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 931 EMEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSEIEGLKALLVAEQEENDLTKKAHA---NAQERNEELSKEVED 1007
Cdd:pfam09728 2 AARELMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkaiLAKSKLEKLCRELQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1008 ADGKIKQLSDTVQRLEET----IQEREALLLAERQEK-EEASAVIAESQARNEAFASKLEDAEKQIDLLQETVQRF---- 1078
Cdd:pfam09728 82 QNKKLKEESKKLAKEEEEkrkeLSEKFQSTLKDIQDKmEEKSEKNNKLREENEELREKLKSLIEQYELRELHFEKLlktk 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1079 ----EEAITKL-QSSVTIEKQQHEETVVQLAEAQAKIDELLREAGdtdEKSTQLETTIQRLEE---SLTEKDALLTTERQ 1150
Cdd:pfam09728 162 elevQLAEAKLqQATEEEEKKAQEKEVAKARELKAQVQTLSETEK---ELREQLNLYVEKFEEfqdTLNKSNEVFTTFKK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1002232322 1151 ETEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTA 1196
Cdd:pfam09728 239 EMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEK 284
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
893-1200 |
4.63e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 893 LEERVEELTN-RLGLEKKLRTDLEKskvaEVSKLQAALNE--MEQRMQDVTAMQERESAKKAVEEALEQEREKISSLTSE 969
Cdd:PRK05771 33 IEDLKEELSNeRLRKLRSLLTKLSE----ALDKLRSYLPKlnPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 970 IEGLKallvaeqeendltkkahaNAQERNEELSKEVE-----DADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEas 1044
Cdd:PRK05771 109 ISELE------------------NEIKELEQEIERLEpwgnfDLDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVEN-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1045 aVIAESQARNE---AFASKLEDAEKQIDLLQETvqRFEEAITKLQSSVTIEKQQHEEtvvQLAEAQAKIDELLREAGDTD 1121
Cdd:PRK05771 169 -VEYISTDKGYvyvVVVVLKELSDEVEEELKKL--GFERLELEEEGTPSELIREIKE---ELEEIEKERESLLEELKELA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1122 EKstqLETTIQRLEEsltekdaLLTTERQETEATKKLLSEAQY----------KNEELLKKIEDA--DKSIAHYHDTTQR 1189
Cdd:PRK05771 243 KK---YLEELLALYE-------YLEIELERAEALSKFLKTDKTfaiegwvpedRVKKLKELIDKAtgGSAYVEFVEPDEE 312
|
330
....*....|.
gi 1002232322 1190 LEENVTAVENS 1200
Cdd:PRK05771 313 EEEVPTKLKNP 323
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
879-1566 |
4.86e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.12 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 879 AARDTQALKVAKEKLEERVEEL--TNRLGLEK--KLRTDLEkskvAEVSKLQAALNEMEQRMQDVTAMQERESAKKAVEE 954
Cdd:NF041483 363 AAQLAKAARTAEEVLTKASEDAkaTTRAAAEEaeRIRREAE----AEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVEL 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 955 ALEQERekissLTSEIEGLKALLVAEQEEndLTKKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQER---EA 1031
Cdd:NF041483 439 QEEARR-----LRGEAEQLRAEAVAEGER--IRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERvrtEA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1032 LLLA---ERQEKE-------EASAVIAESQARNEAFASKLEDAEKQidlLQETVQRFEEA--------ITKLQSSVTIEK 1093
Cdd:NF041483 512 IERAttlRRQAEEtlertraEAERLRAEAEEQAEEVRAAAERAARE---LREETERAIAArqaeaaeeLTRLHTEAEERL 588
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1094 QQHEETvvqLAEAQAKIDELLREAGDTDEK------------STQLETTIQRLEeslTEKDALLTTERQETEATK-KLLS 1160
Cdd:NF041483 589 TAAEEA---LADARAEAERIRREAAEETERlrteaaerirtlQAQAEQEAERLR---TEAAADASAARAEGENVAvRLRS 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1161 EAQYKNEELLKKIED-ADKSIAHYHDTTQRL----------------------EENVTAVENSLKAERQHN--------G 1209
Cdd:NF041483 663 EAAAEAERLKSEAQEsADRVRAEAAAAAERVgteaaealaaaqeeaarrrreaEETLGSARAEADQERERAreqseellA 742
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1210 AIMKQLADAQveiGELQRNLEDADRRNN-----------QLQDSLQRLEENVGAKESLLLTEREQNASTLKllAEAHLEI 1278
Cdd:NF041483 743 SARKRVEEAQ---AEAQRLVEEADRRATelvsaaeqtaqQVRDSVAGLQEQAEEEIAGLRSAAEHAAERTR--TEAQEEA 817
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1279 D--------ELIRKLEDSDR-------KSDSLQSTIKRLEEDGIAkEALLLTEKQAHEATRMTlTEAlekNEELLKKIHD 1343
Cdd:NF041483 818 DrvrsdayaERERASEDANRlrreaqeETEAAKALAERTVSEAIA-EAERLRSDASEYAQRVR-TEA---SDTLASAEQD 892
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1344 DDKHILELQFTIQRLEENTAAKENLLLRE------REQNDATTKAQIESQERNEQLLKRFVDVDRKIDLLQDTIERIGEN 1417
Cdd:NF041483 893 AARTRADAREDANRIRSDAAAQADRLIGEatseaeRLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAER 972
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1418 ------STIKDALLLSER--QEKDAIKKELVEAGERNEEliMKIEDTDKKIEHLQNAIIKLEGDI-EAKDISLEAAREEN 1488
Cdd:NF041483 973 lraeaaETVGSAQQHAERirTEAERVKAEAAAEAERLRT--EAREEADRTLDEARKDANKRRSEAaEQADTLITEAAAEA 1050
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1489 DtirKSLAEAQEkneELLRKISDNEYRIHLL----QDTAQKLQVDAISRLSSFVmEKQESDA------AKRALTEARERN 1558
Cdd:NF041483 1051 D---QLTAKAQE---EALRTTTEAEAQADTMvgaaRKEAERIVAEATVEGNSLV-EKARTDAdellvgARRDATAIRERA 1123
|
....*...
gi 1002232322 1559 EDLLKRNE 1566
Cdd:NF041483 1124 EELRDRIT 1131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1428-1559 |
4.95e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1428 ERQEKDAIKKELVEAGERNEELIMKIEDTDKKiehlQNAIIKLEGDIEAKDISLEAAREENDTIRKSLAEAQEKNEELLR 1507
Cdd:PRK09510 109 ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAK----AAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK 184
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1002232322 1508 KISDNEYRIHLLQDTAQKLQVDAisrlssfvMEKQESDAAKRALTEARERNE 1559
Cdd:PRK09510 185 KKAEAEAAAKAAAEAKKKAEAEA--------KKKAAAEAKKKAAAEAKAAAA 228
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
988-1067 |
6.28e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 39.95 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 988 KKAHANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQ 1067
Cdd:pfam05266 101 KDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAADKEIARLKSEAEKLEQEIQDVELE 180
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1050-1226 |
6.59e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1050 SQARNEAFASKLEDAEKQIDLLQETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLreagdTDEKSTQLET 1129
Cdd:cd22656 105 DATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLL-----TDEGGAIARK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1130 TIQRLEESLTEkdalltterqeteATKKLLSEAQYKNEELLKKIEDADKSIAHyhdtTQRLEENVTAVENSLKaerqhng 1209
Cdd:cd22656 180 EIKDLQKELEK-------------LNEEYAAKLKAKIDELKALIADDEAKLAA----ALRLIADLTAADTDLD------- 235
|
170
....*....|....*..
gi 1002232322 1210 AIMKQLADAQVEIGELQ 1226
Cdd:cd22656 236 NLLALIGPAIPALEKLQ 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1438-1597 |
8.21e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1438 ELVEAGERNEELIMKI---EDTDKKIEHLQNAIIKLEGDIEAKDISLeaAREENdtIRKSLAEAQEKNEELLRKISDNEY 1514
Cdd:PRK03918 139 AILESDESREKVVRQIlglDDYENAYKNLGEVIKEIKRRIERLEKFI--KRTEN--IEELIKEKEKELEEVLREINEISS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1515 RIHLLQDtaqklQVDAISRlssfvmEKQESDAAKRALTEARERNEDLLKRNEDLLKRNDDLIKKIEESSKTITQLQETLQ 1594
Cdd:PRK03918 215 ELPELRE-----ELEKLEK------EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK 283
|
...
gi 1002232322 1595 RLE 1597
Cdd:PRK03918 284 ELK 286
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
894-1222 |
8.38e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 40.67 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 894 EERVEELtNRLGLEKKLRTDLEKsKVAEVSKLQAALNEMEQRMQDVtAMQERESAKKAVEEALEQEREK----ISSLTSE 969
Cdd:pfam13868 5 SDELREL-NSKLLAAKCNKERDA-QIAEKKRIKAEEKEEERRLDEM-MEEERERALEEEEEKEEERKEErkryRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 970 IEGLKALLVAEQEENDLTKKA--HANAQERNEELSKEVEDADGKIKQLSDTVQRLEETIQEREALLLAERQEKEEASAVI 1047
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQEREQmdEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1048 AESQARNEAFASKLEDAEKQIDLLQetvqrfeEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQL 1127
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREI-------ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1128 ETTIQRLEESLTEKDALLTTERQETEATKKLLSEAQYKNEELLKKIEDAD--KSIAHYHDTTQRLEENVTAVENSLKAER 1205
Cdd:pfam13868 235 QELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRrmKRLEHRRELEKQIEEREEQRAAEREEEL 314
|
330
....*....|....*..
gi 1002232322 1206 QHNGAIMKQLADAQVEI 1222
Cdd:pfam13868 315 EEGERLREEEAERRERI 331
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
913-1408 |
8.69e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 913 DLEKSKVAEvSKLQAALNEMEQRmqdvtAMQERESAKKAVEEAleqEREKISSLTSEIEglkallvAEQEENDLTKKAHA 992
Cdd:COG3064 3 EALEEKAAE-AAAQERLEQAEAE-----KRAAAEAEQKAKEEA---EEERLAELEAKRQ-------AEEEAREAKAEAEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 993 NAQERNEELSKEVEDADGKIKQL-SDTVQRLEETIQEREALLLAERQEKEEASAVIAESQARNEAFASKLEDAEKQIDLL 1071
Cdd:COG3064 67 RAAELAAEAAKKLAEAEKAAAEAeKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1072 QETVQRFEEAITKLQSSVTIEKQQHEETVVQLAEAQAKIDELLREAGDTDEKSTQLETTIQRLEESLTEKDALLTTERQE 1151
Cdd:COG3064 147 EAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1152 TEATKKLLSEAQYKNEELLKKIEDADKSIAHYHDTTQRLEENVTAVENSLKAERQHNGAIMKQLADAQVEIGELQRNLED 1231
Cdd:COG3064 227 AASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1232 ADRRNNQLQDSLQRLEENVGAKESLLLTEREQNASTLKLLAEAHLEIDELIRKLEDSDRKSDSLQSTIKRLEEDGIAKEA 1311
Cdd:COG3064 307 LLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002232322 1312 LLLTEKQAHEATRMTLTEALEKNEELLKKIHDDDKHILELQFTIQRLEENTAAK-ENLLLREREQNDATTKAQIESQERN 1390
Cdd:COG3064 387 AGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLvADLAGGLVGIGKALTGDADALLGIL 466
|
490
....*....|....*...
gi 1002232322 1391 EQLLKRFVDVDRKIDLLQ 1408
Cdd:COG3064 467 KAVALDGGAVLADLLLLG 484
|
|
| |
