|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
585-1321 |
0e+00 |
|
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: 1036.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV---PKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQ 820
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 821 RAVWRVLAAIYHLGAAGACK---VGRKQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRwGLEDEETS 897
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ-ESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 898 SGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGKDRAATFEELCHNYAHERLQL 977
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 978 LFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLERL 1057
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLERL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1058 CAAFEKKGAGTeGSSALRTCEQPLQCEIFHQLGWDPVRYDLTGWLHRAKPNLSALDAPQVLHQSKREelrslfqaraklp 1137
Cdd:cd01386 480 FSHYGDKEGGK-GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1138 pvcravaglegtsqqalqrsrmvrrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRSGQESP 1217
Cdd:cd01386 546 ------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTSS 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1218 PPpqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGIDERKAV 1297
Cdd:cd01386 596 PA----------AGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKAV 665
|
730 740
....*....|....*....|....
gi 1034629690 1298 EELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01386 666 EELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
586-1321 |
2.67e-96 |
|
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: 326.47 E-value: 2.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV-----PKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVmekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKIRATFTVLRAFGsvsmaHSRS-----ATRFSMVMSLDFNATG 729
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFG-----NAKTvrndnSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---HQMADSSSFGMGVWSKPEDKQKAAAAFAQL 806
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 807 QGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKhhlR 876
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 877 QIIqqmtfgpsrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSS--HHLSMASIMVVDSPGFQNPR 953
Cdd:cd00124 309 TIK-----------VGGETITKPLTVEQaEDARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 954 HQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVVDQNPSqvrlpagggaqda 1032
Cdd:cd00124 378 VNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKPL------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1033 rGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1112
Cdd:cd00124 437 -GILSLLDEECLFPKGTDATFLEKLYSAHGSH-----PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFLEKNKDTLP-- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1113 dapqvlhqskrEELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIK 1192
Cdd:cd00124 507 -----------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTLN 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1193 RSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1272
Cdd:cd00124 532 STQPHFVRCIKPND----------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKR 589
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1034629690 1273 FQVLDAPLLKKLMSTSEgiderKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd00124 590 YRILAPGATEKASDSKK-----AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
566-1333 |
3.38e-91 |
|
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: 312.94 E-value: 3.38e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 566 NPPELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKvpkGRRDG-LPAHIGS 638
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPykqlpiYTDEVIKKYR---GKSRGeLPPHVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 639 MAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRF 717
Cdd:smart00242 78 IADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEdQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 718 SMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQmadSSSFG---MGVWSK-- 792
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS---PEDYRylnQGGCLTvd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 793 -PEDKqkaaAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFmrfewaNYAAEALGC 861
Cdd:smart00242 235 gIDDA----EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEEL------SNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 862 EYEELNTA-TFKhhlrqiiqQMTFGpsrwgleDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMA 939
Cdd:smart00242 305 DPEELEKAlTKR--------KIKTG-------GEVITKPLNVEQAlDARDALAKALYSRLFDWLVKRINQSLSFKDGSTY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 940 SIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ----FDLpdpspGTTVAVVD 1015
Cdd:smart00242 370 FIGVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTfidfFDN-----QDCIDLIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1016 QNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCeqplqceiF---HQLGwd 1092
Cdd:smart00242 439 KKP--------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTE--------FiikHYAG-- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1093 PVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravaglegtSQQALQRSRMVRRTFASslaavr 1172
Cdd:smart00242 495 DVTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLF-------------------PSGVSNAGSKKRFQTVG------ 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1173 rkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEA 1252
Cdd:smart00242 549 -----SQFKEQLNELMDTLNSTNPHFIRCIKPNE--EKKPGD--------------------FDSSLVLHQLRYLGVLEN 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1253 LRLHRTGYADHMGLTRFRRQFQVLDAPLLKklmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQR 1332
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 1034629690 1333 E 1333
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
510-2085 |
1.66e-75 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 279.27 E-value: 1.66e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 510 WYEA-EKVWLA---QKDGFTLATVlkpdEGTADLPAGRVrlwIDADKTITEVDEEhvhraNPPELDQVEDLASLISVNES 585
Cdd:COG5022 13 WIPDeEKGWIWaeiIKEAFNKGKV----TEEGKKEDGES---VSVKKKVLGNDRI-----KLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGpsVPSAG-----KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:COG5022 81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPyRD--LGIYTddiiqSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQ 737
Cdd:COG5022 159 GESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 738 TMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISE 817
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 818 SEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQqmtfgpsrwGLEDEE 895
Cdd:COG5022 318 EEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVK---RQIKT---------GGEWIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 896 TSSGLKMTgVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:COG5022 386 VPLNLEQA-LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNS------FEQLCINYTNEKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 976 QLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVL 1054
Cdd:COG5022 459 QQFFNQHMFKLEQEEYVKEGIEWSFiDYFDNQP-CIDLIEKKNPL--------------GILSLLDEECVMPHATDESFT 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1055 ERLCAAFEKKgagtegSSALRTCEQPLQCEIF--HQLGwDpVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQA 1132
Cdd:COG5022 524 SKLAQRLNKN------SNPKFKKSRFRDNKFVvkHYAG-D-VEYDVEGFLDKNKDPLN-DDLLELLKASTNEFVSTLFDD 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1133 RaklppvcravaglegtsQQALQRSRmvRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRS 1212
Cdd:COG5022 595 E-----------------ENIESKGR--FPTLG------------SRFKESLNSLMSTLNSTQPHYIRCIKPN---EEKS 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1213 gqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGiD 1292
Cdd:COG5022 641 -------------------PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKE-D 700
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1293 ERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQKN 1372
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1373 VAVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEK----SEKLRNELRQNTDLLESKIADltSDLAD 1448
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKAK 858
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1449 ERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQkKLGDVNKQLE----EAQQKIQLNDLERNptggdewqmrfdca 1524
Cdd:COG5022 859 KRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELEseiiELKKSLSSDLIENL-------------- 923
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1525 QMENEFLrKRLQQCEERLDSELTARKELEQK--LGELQSAydgakkmahqlkrkchhlTCDLEDTCVLLENqqsrnhELE 1602
Cdd:COG5022 924 EFKTELI-ARLKKLLNNIDLEEGPSIEYVKLpeLNKLHEV------------------ESKLKETSEEYED------LLK 978
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1603 KKqkkfdlqlaqalgesvfEKGLREKVTQENTSVRW--ELGQLQQQLKQKEQEASQLKQQVEMLQDHKREllgspslgen 1680
Cdd:COG5022 979 KS-----------------TILVREGNKANSELKNFkkELAELSKQYGALQESTKQLKELPVEVAELQSA---------- 1031
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1681 cvaglkERLWKLESSALEQQK-IQSQQENTIKQLEQLRQRFE---LEIERmkqmhQKDREDQEEELEDVRqscqkrlhql 1756
Cdd:COG5022 1032 ------SKIISSESTELSILKpLQKLKGLLLLENNQLQARYKalkLRREN-----SLLDDKQLYQLESTE---------- 1090
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1757 emQLEQEYEEKQMVLhEKQDLEGLIGTLcdqighrDFDVEKRLRRDL-RRTHALLSdvqLLLGTMEDGKTSVSKEELE-- 1833
Cdd:COG5022 1091 --NLLKTINVKDLEV-TNRNLVKPANVL-------QFIVAQMIKLNLlQEISKFLS---QLVNTLEPVFQKLSVLQLEld 1157
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1834 --KVHSQLEQSEAKCEEALKTQKVLTADleSMHSEL--ENMTRNKSLVDE--QLYRLQFE---KADLLKRIDEDQDDLNE 1904
Cdd:COG5022 1158 glFWEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSSSEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPTE 1235
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1905 LMQKHKDliAQSAADIGQiqelqlqlEEAKKEKHKLQEQL-QVAQMRIEYLEQSTVDRAIVsrqeavicdlenKTEFQKV 1983
Cdd:COG5022 1236 YSTSLKG--FNNLNKKFD--------TPASMSNEKLLSLLnSIDNLLSSYKLEEEVLPATI------------NSLLQYI 1293
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1984 QIKRFEVLVIRLRDSLIKMGEELSQaatseSQQRESSQYYQRRLEELKADMEELVQReaeasRRCMELEKY-VEELAAVR 2062
Cdd:COG5022 1294 NVGLFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQA-----VKVLQLLKDdLNKLDELL 1363
|
1610 1620
....*....|....*....|....
gi 1034629690 2063 QTLQTDLETSIRRI-ADLQAALEE 2085
Cdd:COG5022 1364 DACYSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
573-1321 |
4.07e-71 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 253.74 E-value: 4.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 573 VEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAY 644
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiYSEDMIKAyrGK----RRGELPPHIFAIADEAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 645 WALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:pfam00063 77 RSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGM-GVWSKP 793
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyHYLSQSGCYTIdGIDDSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 794 EDKqkaaaafaQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANYAAEALGCEYEEL 866
Cdd:pfam00063 236 EFK--------ITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 867 NTATFKhhlRQIiqqmtfgpsrwgledeETSSGLKMTGVDC------VEGMASGLYQELFAAVVSLINRSFSSHHLSMAS 940
Cdd:pfam00063 304 EKALCK---RRI----------------KTGRETVSKPQNVeqanyaRDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 941 -IMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVV 1014
Cdd:pfam00063 365 fIGVLDIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFiDFGDNQP--CIDLI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1015 DQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEK----KGAGTEGSSALRtceqplqceIFHQLG 1090
Cdd:pfam00063 433 EKKP--------------LGILSLLDEECLFPKATDQTFLDKLYSTFSKhphfQKPRLQGETHFI---------IKHYAG 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1091 wdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKlppvcRAVAGLEGTSQQALQRSRMVRRTFASslaa 1170
Cdd:pfam00063 490 --DVEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITVG---- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1171 vrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHIL 1250
Cdd:pfam00063 558 -------SQFKESLGELMKTLNSTNPHYIRCIKPNE--KKRAGV--------------------FDNSLVLHQLRCNGVL 608
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 1251 EALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMStsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:pfam00063 609 EGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-----DAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
585-1321 |
4.49e-53 |
|
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: 200.00 E-value: 4.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVP---KGRRDGLPAHIGSMAQRAYWALLN----QRRDQS 655
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsiPDLYSEERMLlyhGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 656 IVALGWSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSV----EKIRATFTVLRAFGSVSMAHSRSATRFS 718
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLgsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 719 MVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEDKq 797
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 798 kaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRkQFMRFewanyAAEALGCEYEELN 867
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfesendtTVLEDATTL-QSLKL-----AAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 868 TATFKHHL----RQIIQQMTFGPSRwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMV 943
Cdd:cd14890 312 KALLTRQLfvggKTIVQPQNVEQAR-----------------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 944 VDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPSQVRL 1023
Cdd:cd14890 375 LDIYGFEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFND-NQACLEL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1024 PAGGGAQDArGLFWVLDEEVHVEGS-SDSVVLERLCAAFekkGAGTEGSSALRTCEQ------P-----LQCEIFHQLGw 1091
Cdd:cd14890 438 IEGKVNGKP-GIFITLDDCWRFKGEeANKKFVSQLHASF---GRKSGSGGTRRGSSQhphfvhPkfdadKQFGIKHYAG- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1092 dPVRYDLTGWLHRAKPNLSAldapqvlhqskreELRSLfqaraklppvcravaglegtsqqalqrsrmvrrtFASSLAAV 1171
Cdd:cd14890 513 -DVIYDASGFNEKNNETLNA-------------EMKEL----------------------------------IKQSRRSI 544
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1172 RRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILE 1251
Cdd:cd14890 545 REVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA----------------------PGKFDGLDCLRQLKYSGMME 602
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629690 1252 ALRLHRTGYA---DHmglTRFRRQFQVLDapllkklmSTSEGIDErkAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14890 603 AIQIRQQGFAlreEH---DSFFYDFQVLL--------PTAENIEQ--LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
4.11e-50 |
|
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: 190.99 E-value: 4.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP----SAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPY-KNLPiyseNIIEMYRGKkRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRI 731
Cdd:cd14920 80 GESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 732 TAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFgMGVWSKPEDKQKAAAAFAQLQGAME 811
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRF-LSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 812 MLGISESEQRAVWRVLAAIYHLGAAGACKvGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsRWGL 891
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 892 EDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNY 970
Cdd:cd14920 311 QKAQTKEQADFA----VEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 971 AHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEG 1047
Cdd:cd14920 381 TNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP--------------GVLALLDEECWFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1048 SSDSVVLERLcaafekkgAGTEGS-SALRTCEQP---LQCEIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQS 1121
Cdd:cd14920 446 ATDKTFVEKL--------VQEQGShSKFQKPRQLkdkADFCIIHYAG--KVDYKADEWLMK---NMDPLndNVATLLHQS 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1122 KREELRSLFQARAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14920 513 SDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVG------------QLYKESLTKLMATLRNTNPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1202 LVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14920 581 IIPNH--EKRAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629690 1282 KKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14920 639 PKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
586-1276 |
1.07e-49 |
|
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: 189.45 E-value: 1.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAgkvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPfkdvplYGNEFITA----YRQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG---IEnEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 819 EQRAVWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKHHLRqiiqqmtfgpsrwg 890
Cdd:cd01383 234 DQEHIFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQ-------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 891 LEDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSF-SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd01383 295 AGGDKIVKKLTLQqAIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlpdpspgTTVAVVDqNPSQVRL----PAgggaqdarGLFWVLDEEVH 1044
Cdd:cd01383 369 NYANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFED-NQECLDLiekkPL--------GLISLLDEESN 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1045 VEGSSDSVVLERL--------CAAFEKKGAGTegssalrtceqplqceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1116
Cdd:cd01383 430 FPKATDLTFANKLkqhlksnsCFKGERGGAFT----------------IRHYAG--EVTYDTSGFLEKNRDLLHS-DLIQ 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1117 VLHQSKreelRSLFQARAklppvcravAGLEGTSQQALQRSRMvrrtfasSLAAVRRKAPCSQIKLQMDALTSMIKRSRL 1196
Cdd:cd01383 491 LLSSCS----CQLPQLFA---------SKMLDASRKALPLTKA-------SGSDSQKQSVATKFKGQLFKLMQRLENTTP 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1197 HFIHCLVPNPV-VESRSGQEsppppqpgrdkpgaggpLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQV 1275
Cdd:cd01383 551 HFIRCIKPNNKqLPGVFDQD-----------------LVLQ------QLRCCGVLEVVRISRSGYPTRMTHQEFARRYGF 607
|
.
gi 1034629690 1276 L 1276
Cdd:cd01383 608 L 608
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
586-1278 |
4.96e-47 |
|
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: 182.46 E-value: 4.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALL-------NQRRD 653
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPF-KHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRrrlhepgASKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 726 -----NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--DSSSFGMGVWSKPEDKQK 798
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQRNDGVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 799 AAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANYAAE 857
Cdd:cd14895 241 DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 858 ALGCEYEELNTATFKhhlRQIiqqmtfgpsrwGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLIN-----RSF 931
Cdd:cd14895 321 LFAVDQDELVSALTT---RKI-----------SVGGETFHANLSLAQCgDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 932 SSHHLSMAS------IMVVDSPGFQnprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPD 1004
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1005 PSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagteGSSALRTCEQPLQCE 1084
Cdd:cd14895 461 NS--VCLEMLEQRPS--------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS----NFSASRTDQADVAFQ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1085 IFHQLGwdPVRYDLTGWL--HRAKPNLSALDapqVLHQSKREELRSLfqaraklppvCRAVAGLEgTSQQALQRSRMVRR 1162
Cdd:cd14895 521 IHHYAG--AVRYQAEGFCekNKDQPNAELFS---VLGKTSDAHLREL----------FEFFKASE-SAELSLGQPKLRRR 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1163 TfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRV 1242
Cdd:cd14895 585 S--SVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND--ESASDQ--------------------FDMAKVSS 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 1034629690 1243 QLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1278
Cdd:cd14895 638 QLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
586-1206 |
1.02e-45 |
|
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: 177.58 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSV-----------PSAGKVPkgrrdglpaHIGSMAQRAYWALLNQRR 652
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfkTIPGLysdemllkfiqPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 653 DQSIVALGWSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT- 728
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 729 --------GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-------------DLDLRTELNLHQMA-DSSSFG 786
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeenDEKLAKGADAKPISiDMSSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 787 MGVWSKPEDKQKAAAAFA--------QLQGAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 852
Cdd:cd14888 232 PHLKFRYLTKSSCHELPDvddleefeSTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 853 NYAAEALGCEYEEL-NTATFkhhlRQIIQQmtfgpsrwgleDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRS 930
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA-----------HEFYTKPLRVDeAEDVRDALARALYSCLFDKVVERTNES 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 931 FS-SHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFdl 1002
Cdd:cd14888 377 IGySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIswnPLDF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1003 pdPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTceQPLQ 1082
Cdd:cd14888 445 --PDNQDCVDLLQEKPL--------------GIFCMLDEECFVPGGKD----QGLCNKLCQKHKGHKRFDVVKT--DPNS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1083 CEIFHQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglegtsqqalqrsrMVRR 1162
Cdd:cd14888 503 FVIVHFAG--PVKYCSDGFLEKNKDQLS-VDAQEVIKNSKNPFISNLFSA--------------------------YLRR 553
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034629690 1163 TFASSLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNP 1206
Cdd:cd14888 554 GTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
585-1321 |
1.88e-45 |
|
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: 177.09 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPedKQKAAAAF 803
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP--GVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEyeelNTATFK--HHLRQIIQQ 881
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 882 MT--FGPSRWGL-EDEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgK 957
Cdd:cd14911 303 MTraFLTPRIKVgRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE------I 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 958 DRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlpagggaqdARG 1034
Cdd:cd14911 377 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGL-DLQP--TIDLIDK---------------PGG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1035 LFWVLDEEVHVEGSSDSVVLERLCAA------FEKkgAGTEGSSALrtceqplqcEIFHQLGwdPVRYDLTGWLHRakpN 1108
Cdd:cd14911 439 IMALLDEECWFPKATDKTFVDKLVSAhsmhpkFMK--TDFRGVADF---------AIVHYAG--RVDYSAAKWLMK---N 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1109 LSALDapqvlhqskrEELRSLFQArAKLPPVCR--AVAGLEGTSQQALQRSRMVRRTFASSLAAVrrkapcSQI-KLQMD 1185
Cdd:cd14911 503 MDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTV------SHLyKEQLA 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1186 ALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgAGGPLALDipalrvQLAGFHILEALRLHRTGYADHMG 1265
Cdd:cd14911 566 KLMDTLRNTNPNFVRCIIPNH--EKRAGK--------------IDAPLVLD------QLRCNGVLEGIRICRQGFPNRIP 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1266 LTRFRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14911 624 FQEFRQRYELLTPNVIPKGF-----MDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
585-1321 |
1.90e-45 |
|
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: 176.75 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP---------SAGKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQS 655
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPY-KELPiytqdivkqYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 656 IVALGWSGAGKTTCCEQVLEHLVgmagSVDGRVS-VE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14883 76 VIISGESGAGKTETTKLILQYLC----AVTNNHSwVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAG--LDLDLRTELNLHQMAD------SSSFGMGVWSKPEDkqkaaaaFAQ 805
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDyhylnqSGCIRIDNINDKKD-------FDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 806 LQGAMEMLGISESEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEA--LGCEYEELNTA-TFKHhlRQIIQ 880
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 881 QMTFGPsrwgledeetssgLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd14883 303 NVTEIP-------------LKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQF-------DLPDPSPgttvavvdqnpsqvrlpaggga 1029
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP---------------------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1030 qdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQceifHQLGwdPVRYDLTGWLHRAKPNL 1109
Cdd:cd14883 422 ---LGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK----HYAG--EVTYTVQGFLDKNKDTQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1110 SaLDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEGTSQqalqrsrmvRRTfasslaavRRKAP--CSQIKLQMDAL 1187
Cdd:cd14883 493 Q-DDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS---------RGT--------SKGKPtvGDTFKHQLQSL 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1188 TSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1267
Cdd:cd14883 555 VDVLSATQPWYVRCIKPNSLKE----------------------PNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFK 612
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 1268 RFRRQFQVLDapllkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14883 613 EFVDRYLCLD-----PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
586-1318 |
4.67e-45 |
|
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: 175.35 E-value: 4.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPS--AGKVPKGrrdgLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQL 736
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNlhqmaDSSSFGMGVWSKPEDKQKAAAAF--AQLQGAMEMLG 814
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG-----SSAAYGYLSLSGCIEVEGVDDVAdfEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 815 ISESEQRAVWRVLAAIYHLG------AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTAtFKHHLRQIIQQmtfGPSR 888
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 889 WGLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQ----NprhqgkdraaTF 963
Cdd:cd14872 306 IPLTPAQ--------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAGGGaqdarGLFWVLDEEV 1043
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFE----------HIDFIDNQPVLDLIEKKQP-----GLMLALDDQV 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1044 HVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd14872 433 KIPKGSD----ATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAG--DVTYDITGFLEKNKDTLQK-DLYVLLSSSKN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1124 EELRSLFqaraklPPvcraVAGLEGTSQQALqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14872 506 KLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRCVK 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1204 PNpvvesrsgqesppppQPGRDKPGAGgplALDIPALRvqLAGfhILEALRLHRTGYAdhmgltrFR---RQFQVLDAPL 1280
Cdd:cd14872 554 PN---------------QEKRARLFDG---FMSLEQLR--YAG--VFEAVKIRKTGYP-------FRyshERFLKRYRFL 604
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629690 1281 LKKlMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQV 1318
Cdd:cd14872 605 VKT-IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
585-1277 |
8.44e-45 |
|
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: 174.58 E-value: 8.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAG---KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQwlPELYTEEqhsKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ---------------MADSSSFgmgvwskpedkqkaaaafA 804
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANecaytganktikiegMSDRKHF------------------A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANYAAEALGCEYEELNTATFKH 873
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 874 HLRQIIQQMTFgpsrwGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPR 953
Cdd:cd14903 296 TMRAAGDVYTV-----PLKKDQAE--------DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 954 HQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVdqnpsqvrlpagggaQDA 1032
Cdd:cd14903 363 HN------SFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRwAHIDFADNQ--DVLAVI---------------EDR 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1033 RGLFWVLDEEV-HVEGSSDSVVLeRLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAK----P 1107
Cdd:cd14903 420 LGIISLLNDEVmRPKGNEESFVS-KLSSIHKDEQDVIEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdallP 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1108 NLSALdapqvLHQSKREELRSLFQARaklppvcravAGLEGTSQQALQRSRMVRRTFASSLAAVRrkapcSQIKLQMDAL 1187
Cdd:cd14903 492 DLSDL-----MRGSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNEL 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1188 TSMIKRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLT 1267
Cdd:cd14903 552 MTTIRSTNVHYVRCIKPNS----------------------IKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHE 609
|
730
....*....|
gi 1034629690 1268 RFRRQFQVLD 1277
Cdd:cd14903 610 EFLDKFWLFL 619
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
585-1321 |
1.78e-44 |
|
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: 174.05 E-value: 1.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKkRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQGAMEM 812
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQ--DDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 813 LGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglE 892
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSI--LTPRIKVG------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 893 DEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYA 971
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 972 HERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGS 1048
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP--------------GVLALLDEECWFPKA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1049 SDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREEL 1126
Cdd:cd14921 447 TDKSFVEKLC---TEQGNHPKFQKPKQLKDKTEFS-IIHYAG--KVDYNASAWLTK---NMDPLndNVTSLLNASSDKFV 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1127 RSLFQARAKlppvcraVAGLEgtsqqalQRSRMVRRTFASslAAVRRKAPCSQI----KLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14921 518 ADLWKDVDR-------IVGLD-------QMAKMTESSLPS--ASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1203 VPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1282
Cdd:cd14921 582 IPNH--EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIP 639
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629690 1283 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14921 640 KGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
582-1320 |
2.12e-44 |
|
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: 173.50 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 582 VNESSVLNTLLQRYKAQLLHTCTGPD-LIVLQP--RGPSV--PSAGK-------VPKGRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPykYLSSNsdASLGEygseyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 650 QRRDQSIVALGWSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHqmaDSSSFGMGvWS--------KP--EDkqk 798
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYALL-ASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 799 aAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVgrkqfmrfewANY-----AAEALGCEY 863
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnleftydhegGEESAVV----------KNTdvldiVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 864 EELNTA-TFKhhlrqiiqqmtfgpsrwgledeetssgLKMTGVDCVEGM-------------ASGLYQELFAAVVSLINR 929
Cdd:cd14879 303 EDLETSlTYK---------------------------TKLVRKELCTVFldpegaaaqrdelARTLYSLLFAWVVETINQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 930 SFSSHHLSMAS-IMVVDSPGFQNprhQGKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSpg 1008
Cdd:cd14879 356 KLCAPEDDFATfISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSV----PATS-- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1009 ttvaVVDqNPSQVRLPAGGGAqdarGLFWVLDEEV-HVEGSSDSVVLERLCAAFEKK-------GAGTEGSSALRTceqp 1080
Cdd:cd14879 427 ----YFD-NSDCVRLLRGKPG----GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHssfiavgNFATRSGSASFT---- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1081 lqceIFHQLGwdPVRYDLTGWLHRakpNLSALDApqvlhqskreELRSLfqaraklppvcravagLEGTSQqalqrsrmv 1160
Cdd:cd14879 494 ----VNHYAG--EVTYSVEGFLER---NGDVLSP----------DFVNL----------------LRGATQ--------- 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1161 rrtFASSLaavrrkapcsqiklqmDALTSMIKRSRLHFIHCLVPNPvvesrsgqeSPPPPQPGRDKpgaggplaldipaL 1240
Cdd:cd14879 530 ---LNAAL----------------SELLDTLDRTRLWSVFCIRPND---------SQLPNSFDKRR-------------V 568
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1241 RVQLAGFHILEALRLHRTGYADHMGLTRFrrqfqvldaplLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1320
Cdd:cd14879 569 KAQIRSLGLPELAARLRVEYVVSLEHAEF-----------CERYKSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
586-1130 |
7.26e-44 |
|
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: 171.41 E-value: 7.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR------RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKP-LPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-----HQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLG 814
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 815 ISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFE---WANYAAEALGCEYEELNTAtfkhhlrqIIQQMTFgpsrwgL 891
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAdeyPLHAVAKLLGIDEVELTEA--------LISNVNT------I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 892 EDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHL-----SMASIMVVDSPGFQNPRHQGkdraatFEE 965
Cdd:cd14897 306 RGERIQSWKSLrQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHV 1045
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL--------------GILPLLDEESTF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1046 EGSSDSVVLERLcaafEKKGagteGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd14897 445 PQSTDSSLVQKL----NKYC----GESPRYVASPGNRVAfgIRHYAE--QVTYDADGFLEKNRDNLSS-DIVGCLLNSNN 513
|
....*..
gi 1034629690 1124 EELRSLF 1130
Cdd:cd14897 514 EFISDLF 520
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
586-1321 |
9.83e-44 |
|
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: 171.49 E-value: 9.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATF--------TVLRAFGSVSMAHSRSATRFSMVMSLDFNATG 729
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGM-------GVWSKPEDKqkaaaa 802
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltidGVDDAEEFK------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 803 faQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELNTATFKHHL---R 876
Cdd:cd01377 232 --LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 877 QIIQQmtfgpsrwgledeetssGLKMTGVDC-VEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----N 951
Cdd:cd01377 310 EWVTK-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 952 prhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVD--QNPSQvrlp 1024
Cdd:cd01377 373 ----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfglDLQ--------PTIDliEKPNM---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1025 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegsSALRTCEQPLQCE----IFHQLGwdPVRYDLTG 1100
Cdd:cd01377 431 ---------GILSILDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEahfiLKHYAG--DVEYNIDG 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1101 WLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQI 1180
Cdd:cd01377 493 WLEKNKDPLNE-NVVALLKKSSDPLVASLF-----------KDYEESGGGGGKKKKKGGSFRTVS------------QLH 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1181 KLQMDALTSMIKRSRLHFIHCLVPNpvvESRsgqesppppQPGR-DKpgaggPLALDipalrvQLA--GfhILEALRLHR 1257
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPN---EEK---------KPGKiDA-----PLVLH------QLRcnG--VLEGIRICR 603
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629690 1258 TGYADHMGLTRFRRQFQVLDAPLLKKlmstseGIDERKAVEELLETLDLEKKAV-AVGHSQVFLK 1321
Cdd:cd01377 604 KGFPNRIIFAEFKQRYSILAPNAIPK------GFDDGKAACEKILKALQLDPELyRIGNTKVFFK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
588-1321 |
4.34e-43 |
|
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: 169.56 E-value: 4.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 588 LNTLLQRYKAQLLHTCTGPDLIVLQPRG--------PSVPSAGKVPKGRRDGLPaHIGSMAQRAYWAL----LNQRRDQS 655
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKsipllydvPGFDSQRKEEATASSPPP-HVFSIAERAYRAMkgvgKGQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 656 IVALGWSGAGKTTCCEQVLEHLV-------GMAGSVDGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLD 724
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLAtasklakGASTSKGAANAHESIEECVllsnLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 725 FNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFA 804
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgackvgrkqfmRFEwANYAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNV-----------RFE-ENADDEDVFAQSADGVNVAKAAGLLGVDAAELM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 885 GPSRWgledEETSSG------LKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSSH----HLSMAS------IMVVD 945
Cdd:cd14892 310 FKLVT----QTTSTArgsvleIKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 946 SPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFDlpDPSPgtTVAVVDQNPSqv 1021
Cdd:cd14892 386 IFGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ--DNQD--CLDLIQKKPL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1022 rlpagggaqdarGLFWVLDEEVHV-EGSSDSVVLERLCAAFEKKGAgtegssalrTCEQP-LQCEIF---HQLGwdPVRY 1096
Cdd:cd14892 453 ------------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHP---------HYAKPrFECDEFvlrHYAG--DVTY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1097 DLTGWLhrAKPNLSaldapqvLHqskrEELRSLfqaraklppvcravaglegtsqqaLQRSRMVRRtfasslaavrrkap 1176
Cdd:cd14892 510 DVHGFL--AKNNDN-------LH----DDLRDL------------------------LRSSSKFRT-------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1177 csqiklQMDALTSMIKRSRLHFIHCLVPNPVvesrsgqespppPQPGrdkpGAGGPLALDipalrvQLAGFHILEALRLH 1256
Cdd:cd14892 539 ------QLAELMEVLWSTTPSYIKCIKPNNL------------KFPG----GFSCELVRD------QLIYSGVLEVVRIR 590
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 1257 RTGYADHMGLTRFRRQFQVLDAPLLKKLMS--TSEGIDERKAVeELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14892 591 REGFPIRRQFEEFYEKFWPLARNKAGVAASpdACDATTARKKC-EEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
632-1321 |
1.69e-42 |
|
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: 167.72 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 632 LPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKIR----ATFTVLRAFGSVS 707
Cdd:cd01378 52 VPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIA--AVSGGSESEVERVKdmllASNPLLEAFGNAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 708 MAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ--------- 778
Cdd:cd01378 130 TLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpeqyyyysk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 779 --------MADSSSFgmgvwskpedkqkaaaafAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGR 843
Cdd:cd01378 210 sgcfdvdgIDDAADF------------------KEVLNAMKVIGFTEEEQDSIFRILAAILHLGniqfaedEEGNAAISD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 844 KQFMRFewanyAAEALGCEYEELNTA-TFkhhlRQIIqqmtfgpSRWGlEDEETSSGLKMTGVDCV-EGMASGLYQELFA 921
Cdd:cd01378 272 TSVLDF-----VAYLLGVDPDQLEKAlTH----RTIE-------TGGG-GRSVYEVPLNVEQAAYArDALAKAIYSRLFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 922 AVVSLINRSFSSHHLSMASIM-VVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---P 997
Cdd:cd01378 335 WIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS------FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 998 VQF-------DLpdpspgttvavVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEG-SSDSVVLERLCAAFEKKGAGTE 1069
Cdd:cd01378 409 IKYfnnkiicDL-----------IEEKP--------------PGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFEC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1070 GSSALrtcEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravagLEG 1148
Cdd:cd01378 464 PSGHF---ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDLLFK-DLKELMQSSSNPFLRSLF---------------PEG 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1149 TSQQALQRSrmvrrTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgrdkpg 1228
Cdd:cd01378 523 VDLDSKKRP-----PTAG-----------TKFKNSANALVETLMKKQPSYIRCIKPN---DNKS---------------- 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1229 aggPLALDIPALRVQLAGFHILEALRLHRTGYAdhmgltrFRRQFqvlDAPLLK-KLMS--TS---EGIDeRKAVEELLE 1302
Cdd:cd01378 568 ---PGEFDEELVLHQVKYLGLLENVRVRRAGFA-------YRQTY---EKFLERyKLLSpkTWpawDGTW-QGGVESILK 633
|
730
....*....|....*....
gi 1034629690 1303 TLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01378 634 DLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
586-1205 |
1.60e-41 |
|
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: 164.37 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 662 SGAGKTTCCEQVLEHLVGMaGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLL 741
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTE---LNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 819 EQRAVWRVLAAIYHLG-------AAGACKVGRKQFMRFEWANYAAEALGCEYEElntatfkhhlrqiiqqmtfgpsrwgL 891
Cdd:cd01379 241 EVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADE-------------------------L 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 892 EDEETSSGLKMTG------------VDCVEGMASGLYQELFAAVVSLINR--SFSSHHLSMA-SIMVVDSPGFQNPRHQg 956
Cdd:cd01379 296 QEALTSHSVVTRGetiirnntveeaTDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPS-----QVRLpagggaqd 1031
Cdd:cd01379 375 -----SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVD----------LIEYEDNRPLldmflQKPM-------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1032 arGLFWVLDEEVHVEGSSDSVVLERlcaaFEKkgaGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSA 1111
Cdd:cd01379 432 --GLLALLDEESRFPKATDQTLVEK----FHN---NIKSKYYWRPKSNALSFGIHHYAG--KVLYDASGFLEKNRDTLPP 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1112 lDAPQVLHQSKreelrslfqaraklppvcravaglegtsqqalqrSRMVRRTFAS----SLaavrrkapcsqiklqMDAL 1187
Cdd:cd01379 501 -DVVQLLRSSE----------------------------------NPLVRQTVATyfrySL---------------MDLL 530
|
650
....*....|....*...
gi 1034629690 1188 TSMIKrSRLHFIHCLVPN 1205
Cdd:cd01379 531 SKMVV-GQPHFVRCIKPN 547
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
585-1205 |
2.46e-41 |
|
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: 163.96 E-value: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-SVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQIlPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGN-CLTCEGRDDAAEFADIRSAMKVLMFTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 819 EQRAVWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANYAAEALGCEYEELNTATFKHHLrqiiqqMTFGpsr 888
Cdd:cd01381 236 EIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTI------FTRG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 889 wgledEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSF---SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd01381 302 -----ETVVSPLSAEQaLDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSQVRLpagggAQDARGLFWVLDEEVH 1044
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQH----------IEFVDNQDVLDLI-----ALKPMNIMSLIDEESK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKRE 1124
Cdd:cd01381 436 FPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT-----SFGINHFAG--VVFYDTRGFLEKNRDTFSA-DLLQLVQSSKNK 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1125 ELRSLFQAraklppvCRAvAGLEGtsqqalqrsrmvrrtfasslaavRRKAP--CSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd01381 508 FLKQLFNE-------DIS-MGSET-----------------------RKKSPtlSSQFRKSLDQLMKTLSACQPFFVRCI 556
|
...
gi 1034629690 1203 VPN 1205
Cdd:cd01381 557 KPN 559
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
586-1321 |
3.89e-41 |
|
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: 163.68 E-value: 3.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvyNPEVVEGYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAAFAQLQ 807
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEilvASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKALCF--P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 RWGLEDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14913 305 RVKVGNEYVTKGQTVDQVHhAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLpdpspGTTVAVVdqnpsqVRLpagggAQDARGLFWVLDEEVHV 1045
Cdd:cd14913 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC------IEL-----IEKPMGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1046 EGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1125
Cdd:cd14913 443 PKATDTSFKNKLYDQHLGKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKSSNRL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1126 LRSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14913 519 LAHLYAtfATADADSGKKKVAKKKGSSFQ--------------TVSALFRE--------NLNKLMSNLRTTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14913 577 PN---ETKT-------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPE 634
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629690 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14913 635 ----GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
585-1321 |
8.50e-41 |
|
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: 162.89 E-value: 8.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKYLPIYSEEIVNmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQL 806
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPgqQDK----ELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 807 QGAMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFG 885
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNM-SFKKERNSDQASMPDDTAAQKV-CHLLGMNVTDFT---RAILSpRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 886 psRWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFE 964
Cdd:cd14932 311 --RDYVQKAQTQEQAEFA----VEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqvrlPAGggaqdARGLFWVLDE 1041
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQP--CIELIEK-------PNG-----PPGILALLDE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1042 EVHVEGSSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSALD--APQVLH 1119
Cdd:cd14932 444 ECWFPKATDKSFVEKVV---QEQGNNPKFQKPKKLKDDADFC-IIHYAG--KVDYKANEWLMK---NMDPLNenVATLLN 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1120 QSKREELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFI 1199
Cdd:cd14932 515 QSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVG------------QLYKEQLMNLMTTLRNTNPNFV 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1200 HCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1279
Cdd:cd14932 582 RCIIPNH--EKKAGKLAH--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 639
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1034629690 1280 LLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14932 640 AIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
586-1273 |
1.09e-40 |
|
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: 163.14 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP--SVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALL-NQR 651
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPlpDLYSESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 652 RDQSIVALGWSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADS---SSFGMGVWSKPEDKQKAA 800
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 801 AAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANyAAEALGCEYEELNTATFKH 873
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 874 HLRQIIQQMTFGPSRWGLEDEETSsglkmtgvdcvegMASGLYQELFAAVVSLIN---------RSFSSHHLSMASIMVV 944
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGS-------------LAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 945 DSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqvrlp 1024
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWK-NISYPSNAACLALFDDKSN----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1025 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagtegssalrtceqplQCEIFHQLGwdPVRYDLTGWLHR 1104
Cdd:cd14902 456 ---------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAG--RVCYNVEQFVEK 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1105 AKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEgtsqqalQRSRMVRrtfASSLAAvrrkapcsQIKLQM 1184
Cdd:cd14902 509 NTDALPA-DASDILSSSSNEVVVAIGADENRDSPGADNGAAGR-------RRYSMLR---APSVSA--------QFKSQL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1185 DALTSMIKRSRLHFIHCLVPNPVvesrsgqesppppqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHM 1264
Cdd:cd14902 570 DRLIVQIGRTEAHYVRCLKPNEV----------------------KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRL 627
|
....*....
gi 1034629690 1265 GLTRFRRQF 1273
Cdd:cd14902 628 AHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
586-1260 |
1.74e-40 |
|
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: 161.65 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKGRrDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESE 819
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 820 QRAVWRVLAAIYHLGAAGACKVGRK--QFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQQmtfgpsrwgledeETS 897
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEALCN---RSVVTR-------------NES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 898 SGLKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSS-HHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHE 973
Cdd:cd14904 304 VTVPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 974 RLQLLFYQRTFVSTLQRYQEEGvpVQFD-LPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSV 1052
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREG--LQWDhIEYQDNQGIVEVIDGK---------------MGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1053 VLERLCAAFEKKGAGT--EGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLF 1130
Cdd:cd14904 441 LVNKIRTNHQTKKDNEsiDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTELF 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1131 QAraklppvcravagLEGTSQQALQRSRmvRRTFAsslaavrRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvES 1210
Cdd:cd14904 513 GS-------------SEAPSETKEGKSG--KGTKA-------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPN---AN 567
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1211 RSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGY 1260
Cdd:cd14904 568 KS-------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
585-1321 |
1.89e-40 |
|
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: 161.55 E-value: 1.89e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPS-AGKVPKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPykRYPVYTNrCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-HQMADSSSFGMGVWSKPedKQKAAAAFAQLQGAMEM 812
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVP--NVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 813 LGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMR---FEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRw 889
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 890 gleDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHN 969
Cdd:cd14909 318 ---QQVTNS---------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 970 YAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLpdpspgttVAVVDQnpsqvrlpagggAQDARGLFWVLDEEVH 1044
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL------------IEKPMGILSILEEESM 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldaPQVLHQSKRE 1124
Cdd:cd14909 440 FPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAG--CVSYNITGWLEKNKDPLN----DTVVDQFKKS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1125 ELRSLFQARAKLPPVCRAVAGLEGTsqqalqrsrmvRRTFASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLVP 1204
Cdd:cd14909 514 QNKLLIEIFADHAGQSGGGEQAKGG-----------RGKKGGGFATVS-----SAYKEQLNSLMTTLRSTQPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1205 NPVvesrsgqespppPQPGrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1284
Cdd:cd14909 578 NEM------------KQPG----------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQGE 635
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629690 1285 MstsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14909 636 E------DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
585-1321 |
3.06e-40 |
|
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: 160.91 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKwlpvyqKEVMAAYK--GKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGldldlrtELNLHQM----ADSSSFGM---GVWSKpeDKQKAAAAFAQLQ 807
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSG-------KKELRDLllvsANPSDFHFcscGAVAV--ESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFG-----NMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKGLIH--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14929 299 RIKVGNEYVTRSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEG---VPVQFDLpdpspgTTVAVVDQnpsqvrlpagggAQDARGLFWVLDEEV 1043
Cdd:cd14929 373 CINFTNEKLQQFFNQHMFVLEQEEYRKEGidwVSIDFGL------DLQACIDL------------IEKPMGIFSILEEEC 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1044 HVEGSSDSVVLERLC-AAFEKKGAGTEGSSALRTCEqpLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSAlDAPQVLHQSK 1122
Cdd:cd14929 435 MFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNKDLLNE-TVVAVFQKSS 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1123 REELRSLFQARAklppvcravaglegTSQQALQRSRMVRRTFASSlaavrrKAPCSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14929 510 NRLLASLFENYI--------------STDSAIQFGEKKRKKGASF------QTVASLHKENLNKLMTNLKSTAPHFVRCI 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1203 VPNPvvesrsgqesppppqpgRDKPGAGGP-LALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDApll 1281
Cdd:cd14929 570 NPNV-----------------NKIPGVLDPyLVLQ------QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP--- 623
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629690 1282 kKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14929 624 -RTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
3.56e-40 |
|
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: 161.03 E-value: 3.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQLQGAMEML 813
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPgqQDK----DMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALGcEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNI-VFKKERNTDQASMPDNTAAQKVS-HLLGINVTDFTRGI--LTPRIKVG------RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 973 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVavvdqnpsqVRLPAGggaqdARGLFWVLDEEVHVEGSS 1049
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDL---------IEKPAG-----PPGILALLDEECWFPKAT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1050 DSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELR 1127
Cdd:cd14919 445 DKSFVEKV---VQEQGTHPKFQKPKQLKDKADFC-IIHYAG--KVDYKADEWLMK---NMDPLndNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1128 SLFQARAKlppvcraVAGLE---GTSQQALQRSRMVRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1204
Cdd:cd14919 516 ELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1205 NPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1284
Cdd:cd14919 581 NH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629690 1285 MstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14919 639 F-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
585-1321 |
4.17e-40 |
|
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: 160.58 E-value: 4.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAG----KVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPY-KWLPIYGarvaNMYKGKkRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14934 80 GESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSF-----GMGVWSKPEDkqkaAAAFAQLQGA 809
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYhwvsqGVTVVDNMDD----GEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 810 MEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELntatfkhhlrqiiqQMTFGP 886
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGEL--------------QKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 887 SRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEE 965
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCnNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLD 1040
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFidfglDLQ--------ACIDL------------LEKPMGIFSILE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1041 EEVHVEGSSDSVV--------LERLCAAFEKKGAGTEGSSAlrtceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSal 1112
Cdd:cd14934 434 EQCVFPKATDATFkaalydnhLGKSSNFLKPKGGKGKGPEA--------HFELVHYAG--TVGYNITGWLEKNKDPLN-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1113 dapqvlhqskrEELRSLFQARAKLppVC----RAVAGLEGTSQQALQRSRMVRRTFasslaavrrkapcsqIKLQMDALT 1188
Cdd:cd14934 502 -----------ETVVGLFQKSSLG--LLallfKEEEAPAGSKKQKRGSSFMTVSNF---------------YREQLNKLM 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1189 SMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTR 1268
Cdd:cd14934 554 TTLHSTAPHFVRCIVPNEFKQSG----------------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPE 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1034629690 1269 FRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14934 612 FKQRYQVLNPNVIPQGF-----VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
587-1321 |
2.04e-39 |
|
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: 158.36 E-value: 2.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14918 307 KVGNEYVTKGQTVQQVyNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1048
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PLGIFSILEEECMFPKA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1049 SDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQ-SKREELR 1127
Cdd:cd14918 446 TDTSFKNKLYDQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLN--DTVVGLYQkSAMKTLA 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1128 SLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14918 521 SLFStyASAEADSGAKKGAKKKGSSFQ--------------TVSALFRE--------NLNKLMTNLRSTHPHFVRCIIPN 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1206 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1285
Cdd:cd14918 579 ---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE-- 634
|
730 740 750
....*....|....*....|....*....|....*.
gi 1034629690 1286 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14918 635 --GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1321 |
2.30e-39 |
|
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: 158.33 E-value: 2.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSA-GKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPykQLPIYTEAiVEMYRGKkRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFT---VLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRkepgVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkaAAAFAQLQGAMEML 813
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE---RELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRAL--LTPRIKVG------RD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 973 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSS 1049
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPwtfLDFGL-DLQPCIDLIERPANPP--------------GLLALLDEECWFPKAT 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1050 DSVVLERLCaafEKKGAGTEGSSAlRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKReelrsl 1129
Cdd:cd14930 447 DKSFVEKVA---QEQGGHPKFQRP-RHLRDQADFSVLHYAG--KVDYKANEWLMKNMDPLND-NVAALLHQSTD------ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1130 fQARAKLPPVCRAVAGLEGTSQQAL-QRSRMVRRTFASSLAAVRRKApcsqiklqMDALTSMIKRSRLHFIHCLVPNPvv 1208
Cdd:cd14930 514 -RLTAEIWKDVEGIVGLEQVSSLGDgPPGGRPRRGMFRTVGQLYKES--------LSRLMATLSNTNPSFVRCIVPNH-- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1209 ESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMsts 1288
Cdd:cd14930 583 EKRAGKLEP--------------RLVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF--- 639
|
730 740 750
....*....|....*....|....*....|...
gi 1034629690 1289 egIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14930 640 --MDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
586-1205 |
2.99e-39 |
|
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: 157.80 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP----RGPSVPSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyfdiPKLYSSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLH--QMADSSSFGmgvwskpedkqkaaaafaQLQGAMEMLGISES 818
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKdpLLDDVGDFI------------------RMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 819 EQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanYAAEALGCEYEELntatfKHHLRQIIQQMTFGPS- 887
Cdd:cd01382 222 EKLDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 ----RWGLEDEETSSGLkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSShhlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd01382 294 gtviKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQnpsqvrlpagggaQD--------AR 1033
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVDN-------------QDcidlieakLV 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1034 GLFWVLDEEVHVEGSSD----SVVLE------RLCAAFEKKGAGTEgssALRTCEQPLqceIFHQLGwdPVRYDLTGWLH 1103
Cdd:cd01382 414 GILDLLDEESKLPKPSDqhftSAVHQkhknhfRLSIPRKSKLKIHR---NLRDDEGFL---IRHFAG--AVCYETAQFIE 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1104 RakpNLSALDAP--QVLHQSKREELRSLFQARAKLPPVCRAVAGlegtsqqalqrsrmvRRTFASslaaVRRKapcsqIK 1181
Cdd:cd01382 486 K---NNDALHASleSLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FK 538
|
650 660
....*....|....*....|....
gi 1034629690 1182 LQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd01382 539 TQLNLLMDKLRSTGTSFIRCIKPN 562
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
586-1321 |
1.14e-38 |
|
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: 156.03 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpvynAEVVAAYRGKK--RSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFAQLQ 807
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPS 887
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGN-----------MKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14917 305 RVKVGNEYVTKGQNVQQVIYATGaLAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVLDE 1041
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgmDLQ--------ACIDL------------IEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1042 EVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1121
Cdd:cd14917 439 ECMFPKATDMTFKAKLFDNHLGKSNNFQKPRNIKG-KPEAHFSLIHYAGT--VDYNIIGWLQKNKDPLNE-TVVGLYQKS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1122 KREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMvrrtfaSSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14917 515 SLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1202 LVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14917 575 IIPN---ETKS-------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629690 1282 KKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14917 633 PE----GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
585-1321 |
2.05e-38 |
|
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: 155.50 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYK--GKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT-------------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 726 NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAA 802
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVttvDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 803 FAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQfmRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQM 882
Cdd:cd14927 235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNM---KFKQKQ--REE----QAEADGTESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 883 TFGPSRWGleDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVyAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLF 1036
Cdd:cd14927 378 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL------------IEKPLGIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1037 WVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSALDAPq 1116
Cdd:cd14927 438 SILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVP--YNIVGWLDKNKDPLNETVVA- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1117 VLHQSKREELRSLFQARAKLPPVCRAVAGLEGtsqqalqrsrmvRRTFASSLAAVrrkapcSQI-KLQMDALTSMIKRSR 1195
Cdd:cd14927 515 IFQKSQNKLLATLYENYVGSDSTEDPKSGVKE------------KRKKAASFQTV------SQLhKENLNKLMTNLRATQ 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1196 LHFIHCLVPNpvvESRSgqesppppqpgrdkPGAGGPLaLDIPALRVQlagfHILEALRLHRTGYADHMGLTRFRRQFQV 1275
Cdd:cd14927 577 PHFVRCIIPN---ETKT--------------PGVMDPF-LVLHQLRCN----GVLEGIRICRKGFPNRILYADFKQRYRI 634
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1034629690 1276 LDAPLLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14927 635 LNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
586-1321 |
2.32e-38 |
|
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: 154.95 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEqySRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL------NLHQMADSssfgmGVWSkpEDKQKAAAAFAQLQ 807
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVE--DKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNYAAEALGCEYEELNTAtfkhhlrqIIQQM 882
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDA--------LTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 883 TFgpsrwgLEDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14873 302 MF------LRGEEILTPLNVqQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPSPGTTVAVVDQNpsqvrlpagggaqdaRGLFWVLDE 1041
Cdd:cd14873 369 HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGL-VWEDIDWIDNGECLDLIEKK---------------LGLLALINE 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1042 EVHVEGSSDSVVLERLcaafekKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1121
Cdd:cd14873 433 ESHFPQATDSTLLEKL------HSQHANNHFYVKPRVAVNNFGVKHYAG--EVQYDVRGILEKNRDTFRD-DLLNLLRES 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1122 KREELRSLFQARAKlppvcravAGLEGTSQQALQRsrmvrrtfasslaavRRKAPCSQIKLQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14873 504 RFDFIYDLFEHVSS--------RNNQDTLKCGSKH---------------RRPTVSSQFKDSLHSLMATLSSSNPFFVRC 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1202 LVPNpvVESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYAdhmgltrFRRQFQvldaPLL 1281
Cdd:cd14873 561 IKPN--MQKMPDQFDQ--------------AVVLN------QLRYSGMLETVRIRKAGYA-------VRRPFQ----DFY 607
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1034629690 1282 KKLMSTSEGI----DERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14873 608 KRYKVLMRNLalpeDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1321 |
2.33e-38 |
|
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: 155.27 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFA 804
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEitvPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKALCY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 885 gpSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14915 306 --PRVKVGNEYVTKGQTVQQVyNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1043
Cdd:cd14915 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1044 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskr 1123
Cdd:cd14915 443 MFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN------------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1124 EELRSLFQaRAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAS--SLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHC 1201
Cdd:cd14915 507 ETVVGLYQ-KSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSfqTVSALFRE--------NLNKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1202 LVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1281
Cdd:cd14915 578 LIPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAI 635
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629690 1282 KKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14915 636 PE----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
587-1016 |
2.60e-38 |
|
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: 154.76 E-value: 2.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfkRLPHLYDAHMMEqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 662 SGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGMGVWSKPEDkqkaaaaFAQLQGAMEML 813
Cdd:cd01384 163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 814 GISESEQRAVWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANyAAEALGCEYEELNTATFKhhlRQIIqqmtfg 885
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVIV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 886 psrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQnprhQGKDRaaTFE 964
Cdd:cd01384 305 -----TPDGIITKPLDPDAaTLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKTN--SFE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-------DLPDPSPGTTVAVVDQ 1016
Cdd:cd01384 374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKPGGIIALLDE 435
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
586-1321 |
6.15e-38 |
|
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: 154.12 E-value: 6.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFA 804
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYDYPFVSQGEISVASiddQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEElnTATFKHHLRQIIQQMTF 884
Cdd:cd14912 235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREE----QAEPDGTEVAD--KAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 885 GPSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVtNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEV 1043
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK---------------PMGIFSILEEEC 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1044 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAldapQVLHQSKR 1123
Cdd:cd14912 443 MFPKATDTSFKNKLYEQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE----TVVGLYQK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1124 EELRSLfqarAKLPPVCRAVAGlEGTSQQALQRSRMVRRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14912 516 SAMKTL----AYLFSGAQTAEG-ASAGGGAKKGGKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCII 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14912 582 PN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE 639
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629690 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14912 640 ----GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
587-1276 |
1.29e-37 |
|
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: 152.75 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR-----RDGLPAHIGSMAQRAYWALLNQ----RRDQSIV 657
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKY-LHIYEKEVSQKykcekKSSLPPHIFAVADRAYQSMLGRlargPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 658 ALGWSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQL 736
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKpEDKQKAAAAFAQLQGAMEMLGIS 816
Cdd:cd14889 158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 817 ESEQRAVWRVLAAIYHLGA-------AGACKVGRKQfmrFEWANYAAEALGCEYEEL-----NTATF-------KHHLRQ 877
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNitfemddDEALKVENDS---NGWLKAAAGQFGVSEEDLlktltCTVTFtrgeqiqRHHTKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 878 IIQqmtfgpsrwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFS---SHHLSMASIMVVDSPGFQnprH 954
Cdd:cd14889 314 QAE-------------------------DARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---N 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 955 QGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQVRLPAgggaqDARG 1034
Cdd:cd14889 366 FAVNR---FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWK----------EITYKDNKPILDLFLN-----KPIG 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1035 LFWVLDEEVHVEGSSDSVVLERLCAAFekKGAGTEGSSALRTceqPLqCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlda 1114
Cdd:cd14889 428 ILSLLDEQSHFPQATDESFVDKLNIHF--KGNSYYGKSRSKS---PK-FTVNHYAG--KVTYNASGFLEKNRDTIPA--- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1115 pqvlhqSKREE-LRSLFQARAKLPPVCRAVAGLEGTSQQALQRSrmvrrtfASSLAAVRRKAPCSQIKLQMDALTSMIKR 1193
Cdd:cd14889 497 ------SIRTLfINSATPLLSVLFTATRSRTGTLMPRAKLPQAG-------SDNFNSTRKQSVGAQFKHSLGVLMEKMFA 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1194 SRLHFIHCLVPNPVvesrsgqespppPQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1273
Cdd:cd14889 564 ASPHFVRCIKPNHV------------KVPGQ----------LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERY 621
|
...
gi 1034629690 1274 QVL 1276
Cdd:cd14889 622 KIL 624
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
586-1321 |
1.41e-37 |
|
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: 152.91 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVAAYRgkkRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 662 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAG-----LDLDLRTElNLHQMADSSSFGMGVWSKPEDKqkaaaAFAQ 805
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNkkpelLDMLLVTN-NPYDYAFVSQGEVSVASIDDSE-----ELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFG 885
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGN-----------MKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 886 PSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14916 304 HPRVKVGNEYVTKGQSVQQVyYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqvrlpagggAQDARGLFWVL 1039
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFidfgmDLQ--------ACIDL------------IEKPMGIMSIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1040 DEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLH 1119
Cdd:cd14916 438 EEECMFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVVGLYQ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1120 QSKREELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMVRrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFI 1199
Cdd:cd14916 514 KSSLKLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTHPHFV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1200 HCLVPNPvvesrsgqesppppqpgRDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAP 1279
Cdd:cd14916 575 RCIIPNE-----------------RKAPG-----VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1034629690 1280 LLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14916 633 AIPE----GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
586-1321 |
2.51e-37 |
|
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: 152.19 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVTAYRgkkRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 662 SGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14910 309 KVGNEYVTKGQTVQQVyNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVHVEGS 1048
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECMFPKA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1049 SDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREEL 1126
Cdd:cd14910 448 TDTSFKNKL---YEQHLGKSNNFQKPKPAKGKVEAHfsLIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSMKTL 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1127 RSLFQARAKLPpvCRAVAGLEGTSQQAlqrsrmvrRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLVPNp 1206
Cdd:cd14910 522 ALLFSGAAAAE--AEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPN- 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1207 vvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlms 1286
Cdd:cd14910 582 --ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE--- 637
|
730 740 750
....*....|....*....|....*....|....*
gi 1034629690 1287 tSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14910 638 -GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
586-994 |
2.68e-37 |
|
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: 151.54 E-value: 2.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRY-KAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvPKGRRDglPaHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPyedlpiYGEDIIQAysGQ-NMGELD--P-HIFAIAEEAYRQMARDEKNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 657 VALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd01380 78 IVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqmADSSSF---GMGvwSKPE-DKQKAAAAFAQLQGAME 811
Cdd:cd01380 158 MRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL---GSAEDFfytNQG--GSPViDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 812 MLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFEWA---NYAAEALGCEYEElntatFKHHL-RQIIQQMTfgps 887
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDehlQIACELLGIDESQ-----LAKWLcKRKIVTRS---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 rwgledEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MASIMVVDSPGFQ----Nprhqgkdra 960
Cdd:cd01380 304 ------EVIVKPLTLQqAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN--------- 368
|
410 420 430
....*....|....*....|....*....|....
gi 1034629690 961 aTFEELCHNYAHERLQLLFYQRTFvstlQRYQEE 994
Cdd:cd01380 369 -SFEQFCINYANEKLQQQFNQHVF----KLEQEE 397
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
585-1321 |
3.73e-37 |
|
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: 151.76 E-value: 3.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQG 808
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQ--DKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 809 AMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFGps 887
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNM-SFKKERHTDQASMPDNTAAQKV-CHLMGMNVTDFT---RAILSpRIKVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 888 RWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEEL 966
Cdd:cd15896 311 RDYVQKAQTQEQAEFA----VEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFEQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEV 1043
Cdd:cd15896 381 CINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQPCIDLIEKPASPP--------------GILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1044 HVEGSSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1123
Cdd:cd15896 446 WFPKATDKSFVEKV---LQEQGTHPKFFKPKKLKDEADFC-IIHYAG--KVDYKADEWLMKNMDPLND-NVATLLNQSTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1124 EELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTfasslaavrrkapcSQI-KLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd15896 519 KFVSELWKDVDRIVGLDK-VSGMSEMPGAFKTRKGMFRTV--------------GQLyKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1203 VPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1282
Cdd:cd15896 584 IPNH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP 641
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629690 1283 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd15896 642 KGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1321 |
3.18e-36 |
|
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: 148.68 E-value: 3.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMA-----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFAQ 805
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEvtvASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFg 885
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGLCC- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 886 pSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14923 305 -PRVKVGNEYVTKGQNVQQVtNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqvrlpagggaqdARGLFWVLDEEVH 1044
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK---------------PMGIFSILEEECM 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1045 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQSKRE 1124
Cdd:cd14923 443 FPKATDTSFKNKLYDQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN--ETVVGLYQKSSL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1125 ELRS-LFQARAKlppvcrAVAGLEGTSQQALQRsrmvRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1203
Cdd:cd14923 518 KLLSfLFSNYAG------AEAGDSGGSKKGGKK----KGSSFQTVSAVFRE--------NLNKLMTNLRSTHPHFVRCLI 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1204 PNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1283
Cdd:cd14923 580 PN---ETKT-------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPE 637
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629690 1284 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14923 638 ----GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
586-1320 |
8.10e-36 |
|
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: 147.24 E-value: 8.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-----------RGPSVPSAGKVPKGRRDgLPAHIGSMAQRAYWALLNQRR-- 652
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 653 --DQSIVALGWSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAF 803
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfMRFEWANYAAEALGCEYEELNTATFKHHL--RQIIQQ 881
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 882 MTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSSHHLSMASIMVVDSPGF----QNprhq 955
Cdd:cd14901 320 GEYITMPLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGL 1035
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF-VEYPNNDACVAMFEARPT--------------GL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1036 FWVLDEEVHVEGSSDsvvlERLCAAFekkgagtegssalrtceqplqceifhqlgwdpvrYDLTGwlhrAKPNLSAldap 1115
Cdd:cd14901 445 FSLLDEQCLLPRGND----EKLANKY----------------------------------YDLLA----KHASFSV---- 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1116 qvlhqSKREELRSLFQARAKLPPVCRAVAGL-----EGTSQQALQRSRMVRRTFASSLAAvrrkapcSQIKLQMDALTSM 1190
Cdd:cd14901 479 -----SKLQQGKRQFVIHHYAGAVCYATDGFcdknkDHVHSEALALLRTSSNAFLSSTVV-------AKFKVQLSSLLEV 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1191 IKRSRLHFIHCLVPNPVVESRSgqesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFR 1270
Cdd:cd14901 547 LNATEPHFIRCIKPNDVLSPSE----------------------FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFV 604
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1271 RQFQVLDAPLLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1320
Cdd:cd14901 605 HTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
585-1205 |
1.18e-35 |
|
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: 146.71 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALLNQR 651
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykQIDNLFSEEVMqmykeqiiqngEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 652 RDQSIVALGWSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRS 713
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 714 ATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSFGMGVWSK 792
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL--KNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 793 PE----DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRfewanYAAEA 858
Cdd:cd14907 239 SNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ-----IIAKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 859 LGCEYEELNTA-TFKhhLRQIIQQMTFGPsrwgledeetssglkMTGVDCV---EGMASGLYQELFAAVVSLINRSFSSH 934
Cdd:cd14907 314 LGIDEEELKEAlTTK--IRKVGNQVITSP---------------LSKKECInnrDSLSKELYDRLFNWLVERLNDTIMPK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 935 HLS--------MASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLP 1003
Cdd:cd14907 377 DEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylNQLSYT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1004 DPSPgtTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAafekkgagTEGSSALRTCEQPLQC 1083
Cdd:cd14907 451 DNQD--VIDLLDKPPI--------------GIFNLLDDSCKLATGTDEKLLNKIKK--------QHKNNSKLIFPNKINK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1084 EIF---HQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglEGTSQQALQRSRMV 1160
Cdd:cd14907 507 DTFtirHTAK--EVEYNIEGFREKNKDEIS-QSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQSKQKK 569
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1034629690 1161 RRtfasslaaVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14907 570 SQ--------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN 606
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
551-1358 |
1.26e-35 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 148.25 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 551 DKTITEVDEEHVHRANPP-ELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR 628
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 629 R----DGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV-GMAGSVDGRVSvEKIRATFTVLRAF 703
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQ-NAIMAANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 704 GSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--- 780
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEeyk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 781 -------------DSSSFGMGVWSkpedkqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLGAA----------- 836
Cdd:PTZ00014 314 yinpkcldvpgidDVKDFEEVMES------------------FDSMGLSESQIEDIFSILSGVLLLGNVeiegkeegglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 837 -GACKVGRKQfmrfEWANYAAEALGCEYEELntatfKHHLrqIIQQMTFGP----SRWGLEDEETSsglkmtgvdcVEGM 911
Cdd:PTZ00014 376 dAAAISDESL----EVFNEACELLFLDYESL-----KKEL--TVKVTYAGNqkieGPWSKDESEML----------KDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 912 ASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVST 987
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 988 LQRYQEEGVP---VQFdlpdpspgTTvavvdqNPSQVRLPAGGGaqdaRGLFWVLDEEVHVEGSSDsvvlERLCAAFEKK 1064
Cdd:PTZ00014 505 SKLYKDEGISteeLEY--------TS------NESVIDLLCGKG----KSVLSILEDQCLAPGGTD----EKFVSSCNTN 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1065 gagTEGSSALRTCE--QPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcra 1142
Cdd:PTZ00014 563 ---LKNNPKYKPAKvdSNKNFVIKHTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF------------ 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1143 vaglEGtsqQALQRSRMVRRTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqp 1222
Cdd:PTZ00014 625 ----EG---VEVEKGKLAKGQLIG-----------SQFLNQLDSLMSLINSTEPHFIRCIKPN---ENKK---------- 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1223 grdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLlkklmSTSEGIDERKAVEELLE 1302
Cdd:PTZ00014 674 ---------PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-----SNDSSLDPKEKAEKLLE 739
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 1303 TLDLEKKAVAVGHSQVFLKAGVISRL-EKQREKLVS-QSIV-LFQAACKGFLSRQEFKK 1358
Cdd:PTZ00014 740 RSGLPKDSYAIGKTMVFLKKDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
586-1321 |
5.92e-35 |
|
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: 144.83 E-value: 5.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSV-PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKflPIYnPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 662 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGmgvwskpEDKQKAAAAFAQLQGAMEML 813
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 814 GISESEQRAVWRVLAAIYHLgaagackvGRKQFMRfeWANYAAEALGCEYEE-LNTATfkhHLRQIIQQMtfgpsrwgLE 892
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIIS---ELLRVKEET--------LL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 893 DEETSSGLKMTGVDCV------------EGMASGLYQELFAAVV-----SLINRSFSSHHlSMASIMVVDSPGFQNPRHQ 955
Cdd:cd01385 292 EALTTKKTVTVGETLIlpyklpeaiatrDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFdlpdpspgttvavVDqNPSQVRLPAGggaqDA 1032
Cdd:cd01385 371 ------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISwhnIEY-------------TD-NTGCLQLISK----KP 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1033 RGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegssalRTCEQPLQCE----IFHQLGwdPVRYDLTGWLHRAKPN 1108
Cdd:cd01385 427 TGLLCLLDEESNFPGATNQTLLAKFKQQHKDN----------KYYEKPQVMEpafiIAHYAG--KVKYQIKDFREKNLDL 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1109 LSAlDAPQVLHQSK----RE-------------ELRSLFQARAKLPPVCRA----VAGLEGTSQQALQRSRMVRRTfass 1167
Cdd:cd01385 495 MRP-DIVAVLRSSSsafvREligidpvavfrwaVLRAFFRAMAAFREAGRRraqrTAGHSLTLHDRTTKSLLHLHK---- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1168 laavRRKAPCSQIKLQ--MDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLA 1245
Cdd:cd01385 570 ----KKKPPSVSAQFQtsLSKLMETLGQAEPFFIRCIKSN------------------AEK----KPLRFDDELVLRQLR 623
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1246 GFHILEALRLHRTGYADHMGLTRFRRQFQVLdapLLKKLMSTSEGIderkavEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd01385 624 YTGMLETVRIRRSGYSVRYTFQEFITQFQVL---LPKGLISSKEDI------KDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
585-1260 |
8.24e-33 |
|
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: 137.96 E-value: 8.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAtGRITAAQLQTML 740
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVT-EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---------HQMADSSSFGMGvwskpedkqkAAAAFAQLQGAME 811
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLqeaekyfylNQGGNCEIAGKS----------DADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 812 MLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMRfewanYAAEALGCEYEELNTA-TFKhhLRQII 879
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGnvyfhkrqlrhGQEGVSVGSDAEIQ-----WVAHLLQISPEGLQKAlTFK--VTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 880 QQMTFGPsrwgLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd01387 302 RERIFTP----LTIDQ--------ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGTTVAVVDQNPSQVRLpagggAQDARGLFWVL 1039
Cdd:cd01387 366 --SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPVINLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1040 DEEVHVEGSSDSVVLERlCaafEKKGAGTEGSSALRTCEQPLQceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLH 1119
Cdd:cd01387 429 DDECNFPQATDHSFLEK-C---HYHHALNELYSKPRMPLPEFT--IKHYAG--QVWYQVHGFLDKNRDQLRQ-DVLELLV 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1120 QSKREELRSLF-----QARAKLPpvcravAGLEGTSQQALQRSRMVRRTFASSLaavrrkapcsqiklqMDALTSMiKRS 1194
Cdd:cd01387 500 SSRTRVVAHLFsshraQTDKAPP------RLGKGRFVTMKPRTPTVAARFQDSL---------------LQLLEKM-ERC 557
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1195 RLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAGFHILEALRLHRTGY 1260
Cdd:cd01387 558 NPWFVRCLKPN------------------HKK----EPMLFDMDVVMAQLRYSGMLETIRIRKEGY 601
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
585-1276 |
9.28e-32 |
|
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: 134.52 E-value: 9.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP----SVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSlplfSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQTML 740
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSF----GMGVWSKPEDKqkaaAAFAQLQGAMEMLGIS 816
Cdd:cd14896 159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDA----QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 817 ESEQRAVWRVLAAIYHLGaaGACkvgrkqFMRFEWANYAAEALGCEYEELNTATFKH----HLRQII-QQMTFGPSRWgl 891
Cdd:cd14896 234 AEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARLLQvppeRLEGAVtHRVTETPYGR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 892 edeeTSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFS--SHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCH 968
Cdd:cd14896 304 ----VSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdLPDPSPgttvavvdQNPSQVRLPAGggaqDARGLFWVLDEEVHVEGS 1048
Cdd:cd14896 374 NLASERLQLFSSQTLLAQEEEECQRELLPW---VPIPQP--------PRESCLDLLVD----QPHSLLSILDDQTWLSQA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1049 SDSVVLErlcaafekKGAGTEGSSALRTCEQpLQCEIF---HQLGwdPVRYDLTGWLHRakpNLSALDaPQVLH---QSK 1122
Cdd:cd14896 439 TDHTFLQ--------KCHYHHGDHPSYAKPQ-LPLPVFtvrHYAG--TVTYQVHKFLNR---NRDQLD-PAVVEmlaQSQ 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1123 REELRSLFQaraklppvcravaglEGTSQQALQRSRmvrrtfaSSLAavrrkapcSQIKLQMDALTSMIKRSRLHFIHCL 1202
Cdd:cd14896 504 LQLVGSLFQ---------------EAEPQYGLGQGK-------PTLA--------SRFQQSLGDLTARLGRSHVYFIHCL 553
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 1203 VPNPVvesrsgqesppppqpgrDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14896 554 NPNPG-----------------KLPG-----LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
586-1209 |
6.46e-31 |
|
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: 132.41 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 660 GWSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT-G 729
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 730 RITAAQLQTMLLEKSRVARQPEGES-NFLVFSQMLAGLDLDLRTELNLHQMADS-----------SSF---GMGVWSKPE 794
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKyryldarddviSSFksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 795 DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEwanyaAEALGCEYEELnTATFKHH 874
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFE-----EDSDFSKYAYQ-KDKVTAS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 875 LRQIIQQMTFGPSRWglEDEETSSGLKMTGVDCV--------------EGMASGLYQELFAAVVSLINRSF----SSHHL 936
Cdd:cd14906 305 LESVSKLLGYIESVF--KQALLNRNLKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSNDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 937 SMAS-------IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGT 1009
Cdd:cd14906 383 AGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PWS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1010 TVAVVDqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERlcaaFEKKGAGTEgSSALRTCEQpLQCEIFHQL 1089
Cdd:cd14906 447 NSNFID-NKECIELI----EKKSDGILSLLDDECIMPKGSEQSLLEK----YNKQYHNTN-QYYQRTLAK-GTLGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1090 GwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPvcravaglegTSQQalqrsrmvRRTFASSLA 1169
Cdd:cd14906 516 G--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTK--------KQTQSNTVS 574
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1034629690 1170 avrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVE 1209
Cdd:cd14906 575 --------GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
633-1063 |
1.36e-30 |
|
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: 130.93 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV--GMAGSVDGRVSVEKIRATFT------------ 698
Cdd:cd14891 55 PYAIAEMAYQQMCLGSGRMQNQSIVISGESGAGKTETSKIILRFLTtrAVGGKKASGQDIEQSSKKRKlsvtslderlmd 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 699 ---VLRAFGSVSMAHSRSATRFSMVMSLDFNATG-RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL 774
Cdd:cd14891 135 tnpILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 775 NLhqmadsssfgmgvwSKPEDKQKAAAAF-------------AQLQGAMEMLGISESEQRAVWRVLAAIYHLG------- 834
Cdd:cd14891 215 LL--------------LSPEDFIYLNQSGcvsddniddaanfDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdee 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 835 --AAGACKVGRKQFMrfEWANYAAEALGCEYEELntatfkhhLRQIIQQ--MTFGPSRWGLEDEETSSGLKmtgvdcvEG 910
Cdd:cd14891 281 dtSEGEAEIASESDK--EALATAAELLGVDEEAL--------EKVITQReiVTRGETFTIKRNAREAVYSR-------DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 911 MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14891 344 IAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES-----FETKNDFEQLLINYANEALQATFNQQVFIAEQEL 418
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 991 YQEEGVPV-QFDLPDpspgttvavvdqNPSQVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK 1063
Cdd:cd14891 419 YKSEGIDVgVITWPD------------NRECLDLI----ASKPNGILPLLDNEARNPNPSDAKLNETLHKTHKR 476
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
635-1211 |
1.61e-30 |
|
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: 131.31 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 635 HIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKIRATFTVLRAFGSVSMAHS 711
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 712 RSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLdlrtelnlhqmadSSSFGMGVWS 791
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA-------------AATQKSSAGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 792 K-PEdkqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfmRFEWANYAAEALGC--------- 861
Cdd:cd14887 210 GdPE-----STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPE--TSKKRKLTSVSVGCeetaadrsh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 862 --EYEELN-----TATFKHHLRQIIQQMTFGPSRWGLED----------EETSSGLKMTGVDCVEGMAS-GLYQELFAAV 923
Cdd:cd14887 283 ssEVKCLSsglkvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 924 VSLINRSFSSHHLSMAS--------------IMVVDSPGFQNPRHQGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQ 989
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 990 RYQEEGVPVQFDL-PDPSPGTTVAVVDQNPSQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLE-------RLCA-- 1059
Cdd:cd14887 440 LYTQEGVFQNQDCsAFPFSFPLASTLTSSPSSTSPFSPTPSFRSSSAFATSPSLPSSLSSLSSSLSSsppvwegRDNSdl 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1060 AFEKKGAGTEGSSALRTCEQPLQCE-----IFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskrEELRSLFQAra 1134
Cdd:cd14887 520 FYEKLNKNIINSAKYKNITPALSREnleftVSHFAC--DVTYDARDFCRANREATS-------------DELERLFLA-- 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 1135 klppvCRAVaglegTSQQALQRSRMVRrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESR 1211
Cdd:cd14887 583 -----CSTY-----TRLVGSKKNSGVR------AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
585-1289 |
7.99e-30 |
|
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: 128.39 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKVPKGRR-DGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPykelpiYSTMVSQLYLSSSGQLcSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 658 ALGWSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDF-NATGRITAAQ 735
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwskPEDKQKAAAAFAQLQ-----GAM 810
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM---REDVSTAERSLNREKlavlkQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 811 EMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNtatfkhhlrQIIQQMTFGPsrwg 890
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGD-----------IRFTALTEADSAFVSDLQLLE---------QVAGMLQVST---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 891 ledEETSSGLkMTGVDCVEG------------------MASGLYQELFAAVVSLINRSFSSHH----LSMASIMVVDSPG 948
Cdd:cd14878 292 ---DELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKSLYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 949 FQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLpdpSPGTTVAVVD---QNPSqvrlpa 1025
Cdd:cd14878 368 FEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAY---SPGNQTGVLDfffQKPS------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1026 gggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGT------EGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1099
Cdd:cd14878 433 --------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAvyspmkDGNGNVALKDQGTAFTVMHYAG--RVMYEIV 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1100 GWLHRAKPNLSaldapQVLhqskreelrsLFQARaklppvcravaglegTSQQALqrsrmVRRTFASSLAAVrrkapCSQ 1179
Cdd:cd14878 503 GAIEKNKDSLS-----QNL----------LFVMK---------------TSENVV-----INHLFQSKLVTI-----ASQ 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1180 IKLQMDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgrdkpGAGGPLALDIPALRVQLAGFHILEALRLHRTG 1259
Cdd:cd14878 543 LRKSLADIIGKLQKCTPHFIHCIKPN----------------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYG 600
|
730 740 750
....*....|....*....|....*....|..
gi 1034629690 1260 YADHMGLTRFRRQFQVLDAPLL--KKLMSTSE 1289
Cdd:cd14878 601 YPVRLSFSDFLSRYKPLADTLLgeKKKQSAEE 632
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
631-1273 |
2.47e-29 |
|
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: 127.23 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 631 GLPAHIGSMAQRAYWALLNQ-RRDQSIVALGWSGAGKTTCCEQVLEHLVGMA----GSVDGRVSVEKIRATFT----VLR 701
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDENLKwsnpVME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 702 AFGSVSMAHSRSATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL-NLHQM 779
Cdd:cd14875 133 SFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 780 AD------SSSF-GMGVWSKPEDKqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFE-- 850
Cdd:cd14875 213 QDykclngGNTFvRRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLME-----------VEFEsd 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 851 ------WANYAAEALGCEYEELNTATfkhhLRQIIqqmtfgpsrwgLEDEETSSGLKMTGVDCVEGM----ASGLYQELF 920
Cdd:cd14875 279 qndkaqIADETPFLTACRLLQLDPAK----LRECF-----------LVKSKTSLVTILANKTEAEGFrnafCKAIYVGLF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 921 AAVVSLINRSFSSHH--LSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPV 998
Cdd:cd14875 344 DRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 999 -QFDLPDPSpgTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTC 1077
Cdd:cd14875 418 pKIEFPDNS--ECVNMFDQKRT--------------GIFSMLDEECNFKGGTT----ERFTTNLWDQWANKSPYFVLPKS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1078 EQPLQCEIFHQLGWdpVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELRSLFQARAKLPpvcravaglegtsqqalQ 1155
Cdd:cd14875 478 TIPNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA-----------------R 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1156 RSRMVRRTFASSLAAVRrkapcsqiklqmdaltSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLAL 1235
Cdd:cd14875 536 RKQTVAIRFQRQLTDLR----------------TELESTETQFIRCIKPNMEAS----------------------PSFL 577
|
650 660 670
....*....|....*....|....*....|....*...
gi 1034629690 1236 DIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1273
Cdd:cd14875 578 DNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
586-1205 |
4.40e-28 |
|
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: 122.72 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPK--------------GRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqKLPGLYSSDTMAKyllsfearssstrnKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 650 QRR----DQSIVALGWSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKIRATFTVLRAFGSVSMAHSRSAT 715
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 716 RFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSssfgmgvwskped 795
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMDA------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 796 kqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NYAAEALGCEYEE 865
Cdd:cd14900 228 --------------MDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 866 LNTATfkhHLRQIIQQMTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRSF-----SSHHLSMAS 940
Cdd:cd14900 294 LEKAL---SVRRIRAGTDFVSMKLSAAQANNAR----------DALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 941 IMVVDSPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDqNPS 1019
Cdd:cd14900 361 IGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKY----------VEFCD-NQD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1020 QVRLPagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtEGSSALRTCEQPLQCEIFHQLGwdPVRYDLT 1099
Cdd:cd14900 423 CVNLI----SQRPTGILSLIDEECVMPKGSDTTLASKLYRACGSH----PRFSASRIQRARGLFTIVHYAG--HVEYSTD 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1100 GWLHRAKpnlsaldapQVLHQskreELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQ 1179
Cdd:cd14900 493 GFLEKNK---------DVLHQ----EAVDLFVY--------------------------------------------GLQ 515
|
650 660
....*....|....*....|....*.
gi 1034629690 1180 IKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14900 516 FKEQLTTLLETLQQTNPHYVRCLKPN 541
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
586-996 |
1.12e-27 |
|
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: 121.16 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGK--VPKGRRDGLPaHIGSMAQRAYWALLNQRrDQSIVALGWSG 663
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMkaYLKNYSHVEP-HVYDVAEASVQDLLVHG-NQTIVISGESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 664 AGKTTCCEQVLEHLV-GMAGSVdgrvSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNatGRITAAQLQTMLL 741
Cdd:cd14898 80 SGKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqmADSSSFGmgvwSKPEDKQKAAAAFAQLQGAMEMLGISESeqR 821
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCASKRLNIKNDF-----IDTSSTA----GNKESIVQLSEKYKMTCSAMKSLGIANF--K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 822 AVWRVLAAIYHLGAAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlrqiiqqmtfGPSRWGLEDEETSSGLK 901
Cdd:cd14898 223 SIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVK------------FSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 902 mTGVDCVEGMASGLYQELFAAVVSLINRSFSSHhlSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQ 981
Cdd:cd14898 291 -QARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDFIK 361
|
410
....*....|....*
gi 1034629690 982 RTFVSTLQRYQEEGV 996
Cdd:cd14898 362 KMFRAKQGMYKEEGI 376
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
585-1205 |
1.34e-27 |
|
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: 121.50 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAgKVPKGRRD--------GLPAHIGSMAQRAYWALLNQRR--DQ 654
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKP-VPQL-YSPELMREyhaapqpqKLKPHIFTVGEQTYRNVKSLIEpvNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 655 SIVALGWSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSsfgmgvWSKPEDKQKAAAAFAQLQ 807
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLG---------AAGACKV--GRKQFMRFewanyAAEALGCEYEELNTATFKHHLR 876
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGniqfadsedEAQPCQPmdDTKESVRT-----SALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 877 QIIQQMTF-GPSRWGLEDeetssglkmTGVDCvegMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQNPRH 954
Cdd:cd14880 308 AGKQQQVFkKPCSRAECD---------TRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 955 QgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSpgTTVAVVDQNPSQVrlpagggaqdar 1033
Cdd:cd14880 376 N------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFiNYQDNQ--TCLDLIEGSPISI------------ 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1034 glFWVLDEEVHVEGSSDSVVLErlcAAFEKKGAGTEGSSALRTCEQPlQCEIFHQLGwdPVRYDLTGWLHRAK----PNL 1109
Cdd:cd14880 436 --CSLINEECRLNRPSSAAQLQ---TRIESALAGNPCLGHNKLSREP-SFIVVHYAG--PVRYHTAGLVEKNKdpvpPEL 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1110 SaldapQVLHQSKREELRSLFQARAKlppvcravaglEGTSQQALQRSRmvrrtfASSLAAVrrkapcSQIKLQMDALTS 1189
Cdd:cd14880 508 T-----RLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SKFKASLEQLLQ 559
|
650
....*....|....*.
gi 1034629690 1190 MIKRSRLHFIHCLVPN 1205
Cdd:cd14880 560 VLHSTTPHYIRCIKPN 575
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
587-1321 |
3.58e-26 |
|
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: 117.01 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP-------------RGPSVPSAGKvpkgrrdgLPAHIGSMAQRAYWALLNQRRD 653
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirKYRDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 654 QSIVALGWSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMAD-----SSSFGMGVWSKPEDkqkaaaaFAQLQ 807
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEykflnPKCLDVPGIDDVAD-------FEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 808 GAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQFMRFEwanYAAEALGCEYEELNTATFKHHL------RQIIQQ 881
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 882 MTF-GP----SRWGLEDEETssgLKMTgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQg 956
Cdd:cd14876 301 VTKaGGqeieGRWTKDDAEM---LKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPvqfdlpdpspgTTVAVVDQNPSQVRLPAGGGaqdaRGLF 1036
Cdd:cd14876 370 -----SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIP-----------TAELEYTSNAEVIDVLCGKG----KSVL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1037 WVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQ 1116
Cdd:cd14876 430 SILEDQCLAPGGSD----EKFVSACVSKLKSNGKFKPAKV-DSNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELVE 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1117 VLHQSKREELRSLFqaraklppvcravaglEGtsqQALQRSRMVRrtfaSSLAAvrrkapcSQIKLQMDALTSMIKRSRL 1196
Cdd:cd14876 502 VVQASTNPVVKALF----------------EG---VVVEKGKIAK----GSLIG-------SQFLKQLESLMGLINSTEP 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1197 HFIHCLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14876 552 HFIRCIKPN---ETKK-------------------PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1034629690 1277 DAPLlkklmSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1321
Cdd:cd14876 610 DLGI-----ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
586-1283 |
4.68e-25 |
|
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: 113.46 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGK--VPKGRRDG------------LPAHIGSMAQRAYWALLN-Q 650
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPF-QRLPLYGKeiLESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 651 RRDQSIVALGWSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFG------MGVWSKPE 794
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLpnefhyTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 795 -DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNYAAEALGCE 862
Cdd:cd14908 241 lREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 863 YEELNTAtfkhhLRQIIQQMTFGPSRWGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MAS 940
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKAY--------DARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 941 IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDpspgttvavvdqNPS 1019
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD------------NQD 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1020 QVRLPAGggaqDARGLFWVLDEEvhvegssdsvvlerlCAAFEKkgaGTEGSSALRTCEQPLQceifhqlgwdpvrydlt 1099
Cdd:cd14908 445 CLDTIQA----KKKGILTMLDDE---------------CRLGIR---GSDANYASRLYETYLP----------------- 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1100 gwlhrakpnlsalDAPQVLHQSKREELRSLfqARAKLppvCRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRKAPCSQ 1179
Cdd:cd14908 486 -------------EKNQTHSENTRFEATSI--QKTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQQ 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1180 IKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTG 1259
Cdd:cd14908 548 FKAQLHSLIEMIEDTDPHYIRCIKPNDAAK----------------------PDLVTRKRVTEQLRYGGVLEAVRVARSG 605
|
730 740
....*....|....*....|....
gi 1034629690 1260 YADHMGLTRFRRQFQVLdAPLLKK 1283
Cdd:cd14908 606 YPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
587-996 |
3.97e-23 |
|
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: 107.28 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPKGRR--------DGLPAHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 657 VALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSlILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMaDSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLgI 815
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 816 SESEQRAVWRVLAAIYHLGAAGACKVGRkqfMRFEwaNYAAEALGCEYEEL------NTATFKHHLRQ---IIQQMTFgp 886
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAAQAIITkvvVINNETI-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 887 srwgledeeTSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14886 312 ---------ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQL 376
|
410 420 430
....*....|....*....|....*....|
gi 1034629690 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGV 996
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1401-2085 |
4.10e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.22 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1480
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEAQQKIqlndlernptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1560
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEEL------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1561 SAYDGAKKMAHQLKRKchhltcdledtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVfEKGLREKVTQENT------ 1634
Cdd:TIGR02168 400 NEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERleeale 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1635 SVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGspsLGENCVAGLKERLWKlessaleqqkiqSQQENTIKQLE 1714
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGL------------SGILGVLSELI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1715 QLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDqig 1789
Cdd:TIGR02168 530 SVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1790 HRDFDVEKRL------------------RRDLRRTHALLSDVQL---LLG-----TMEDGKTSVS----KEELEKVHSQL 1839
Cdd:TIGR02168 607 LVKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdLVRpggviTGGSAKTNSSilerRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1840 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAAD 1919
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1920 IGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDS 1998
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1999 LIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2078
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*..
gi 1034629690 2079 LQAALEE 2085
Cdd:TIGR02168 927 LELRLEG 933
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
585-1274 |
5.74e-23 |
|
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: 107.36 E-value: 5.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP---SVPSAGKVPKGRRDGL-----------PAHIGSMAQRAYWALLNQ 650
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPlpiYTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 651 RRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KIRATFTVLRAFGSVSMAHSRSATRFSM 719
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 720 VMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLD--LRTELNLHQMADssSFGMGVWSKPE--D 795
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVN--EFVMLKQADPLatN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 796 KQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfewANYAAEALGCEYEELNT 868
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 869 ATFKHHLRQ---IIQQMTFGPSRWGLED-EETSSGLKMTGV----DCVEGMASGLYQELFAAVVSLIN-------RSFSS 933
Cdd:cd14893 313 ILLAAKLLEvepVVLDNYFRTRQFFSKDgNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 934 HHLSMAS--IMVVDSPGFQN--PRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDpspGT 1009
Cdd:cd14893 393 SNIVINSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTV---NS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1010 TVAVVDQNPSQVRLpaggGAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK--------KGAGTEGSSALRTCEQPL 1081
Cdd:cd14893 464 NVDITSEQEKCLQL----FEDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSKDWRL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1082 QCEIFHQLGwdPVRYDLTGWLHRAKPNLSALDApQVLHQSKREELRSLFQARAklppvcrAVAGLEGTSQQALQRSRmVR 1161
Cdd:cd14893 540 LFIVQHHCG--KVTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS-TS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1162 RTFASSLAAVRR-----KAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALD 1236
Cdd:cd14893 609 SKFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEG----------------------VFD 666
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629690 1237 IPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1274
Cdd:cd14893 667 SAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
585-1276 |
1.25e-21 |
|
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: 102.26 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKgrrdglPAHIGSMAQRAYWALL-NQRRDQSIVALGWSG 663
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIK------KCHISGVAENALDRIKsMSSNAESIVFGGESG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 664 AGKTTCCEQVLEHLVGMAGSvdgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQ-TMLLE 742
Cdd:cd14874 75 SGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKyTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 743 KSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMadSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRA 822
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 823 VWRVLAAIYHLGaagackvgrKQFMRFEWANYAAEALGcEYEELNTATFKHHLRQI-IQQMtfgpSRWGLEDEETSSGLK 901
Cdd:cd14874 229 IYKIISTILHIG---------NIYFRTKRNPNVEQDVV-EIGNMSEVKWVAFLLEVdFDQL----VNFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 902 M-TGVDCVEGMASGLYQELFAAVVSLINRSFSShHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFY 980
Cdd:cd14874 295 LnAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 981 QRTFVSTLQRYQEEGVPVQFDLPDP-SPGTTVAVVDQNPsqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCA 1059
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKP--------------YGLLPLLTDECKFPKGSHESYLEHCNL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1060 AFEKKGAGTEGSSALRtceqpLQCEIFHQLG--WdpvrYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQARAKlp 1137
Cdd:cd14874 434 NHTDRSSYGKARNKER-----LEFGVRHCIGttW----YNVTDFFSRNKRIIS-LSAVQLLRSSKNPIIGLLFESYSS-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1138 pvcravagleGTSQQALQRSRMVRRTfASSLAavrrkapcsqiklqmdaltSMIKRSRLHFIHCLvpnpvvesRSGQESp 1217
Cdd:cd14874 502 ----------NTSDMIVSQAQFILRG-AQEIA-------------------DKINGSHAHFVRCI--------KSNNER- 542
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 1218 pppQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1276
Cdd:cd14874 543 ---QPKK----------FDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1326-2094 |
8.02e-21 |
|
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: 100.91 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1326 SRLEKQREKL--VSQSIVLFQAACKgfLSRQEFKKLKIRRLAAQCIQknvAVFLAVKDWPWWQLLGSLQPLLsatigtEQ 1403
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALE------RQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1404 LRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKHEQ 1483
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----------LGEEEQLRVK--EKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1484 VQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQmenefLRKRLQQCEERLDSELTARKELEQKLGELQSAY 1563
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1564 DGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALgesvfeKGLREKVTQ---ENTSVRWEL 1640
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAI------AGIEAKINEleeEKEDKALEI 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1641 gqlqqqlKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLES--SALEQQKIQSQQE----------- 1707
Cdd:TIGR02169 451 -------KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRelAEAEAQARASEERvrggraveevl 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1708 --------NTIKQLEQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQL---EMQLEQEYEEkqmVL 1771
Cdd:TIGR02169 517 kasiqgvhGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLS---IL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1772 HEkqdlEGLIGTLCDQIghrDFDVEKR-----------LRRDLRRTHALLSDVQLLL---------GTM------EDGKT 1825
Cdd:TIGR02169 594 SE----DGVIGFAVDLV---EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMVTlegelfeksGAMtggsraPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1826 SVSKEELEKVHS------QLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLvdeQLYRLQFEKADLLKRIDEDQ 1899
Cdd:TIGR02169 667 LFSRSEPAELQRlrerleGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1900 DDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLqvAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKt 1978
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKlEEEVSRIEARLREIEQK- 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1979 efqkvqIKRFEVLVIRLRDsliKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2058
Cdd:TIGR02169 821 ------LNRLTLEKEYLEK---EIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
810 820 830
....*....|....*....|....*....|....*.
gi 1034629690 2059 AAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTE 2094
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
586-1053 |
8.35e-21 |
|
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: 99.80 E-value: 8.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgpsvpsagkvpkgRRDGLPAHIGSMAQRA-YWALLN-------QRRD---- 653
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY-------------RDVGNPLTLTSTRSSPlAPQLLKvvqeavrQQSEtgyp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATR---FSMVMSLDfnatGR 730
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRighFIEVQVTD----GA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL--HQMADSS--SFGMGVWSKPEDKqkaaAAFAQL 806
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRylSHGDTRQNEAEDA----ARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 807 QGAMEMLGISESEqraVWRVLAAIYHLG--------AAGACKVGRKQFmrfewaNYAAEALGCE----YEELNTATfkHH 874
Cdd:cd14881 221 KACLGILGIPFLD---VVRVLAAVLLLGnvqfidggGLEVDVKGETEL------KSVAALLGVSgaalFRGLTTRT--HN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 875 LR-QIIQQmtfgpsrwgLEDEETSSGLKmtgvDCvegMASGLYQELFAAVVSLINR-----SFSSHHLSMASIMVVDSPG 948
Cdd:cd14881 290 ARgQLVKS---------VCDANMSNMTR----DA---LAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 949 FQNPrhqgkdRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDlpdpspgttVAVVDQNP-----SQVRL 1023
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVE---------VDYVDNVPcidliSSLRT 418
|
490 500 510
....*....|....*....|....*....|
gi 1034629690 1024 pagggaqdarGLFWVLDEEVHVEGSSDSVV 1053
Cdd:cd14881 419 ----------GLLSMLDVECSPRGTAESYV 438
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
585-1205 |
3.64e-20 |
|
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: 98.24 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPS--AGKVPKG--------------RRDGLPAHIGSMAQRAYWALL 648
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPF-QDLPQlyGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 649 NQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KIRATFTVLRAFGSVSMAHSR 712
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 713 SATRFSMVMSLDFNATGR-ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELN--LHQMADSSSFGM-- 787
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKqvLALSGGPQSFRLln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 788 -GVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGA---------------AGACKVGRKQFMRFEW 851
Cdd:cd14899 240 qSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 852 ANYAAEALGCEYEELNTATFKhhlrqiiqqmtfgpsRWGLEDEETSsglkMTGVDCVEG------MASGLYQELFAAVVS 925
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTK---------------RWLHASNETL----VVGVDVAHArntrnaLTMECYRLLFEWLVA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 926 LINRSFSSH---------------HLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14899 381 RVNNKLQRQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 991 YQEEGVPVQFdLPDPSPGTTVAVVDQNPSqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEG 1070
Cdd:cd14899 455 YRDEGIRWSF-VDFPNNRACLELFEHRPI--------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPHF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1071 SSAlRTCEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLfqARAKLPPVCRAVAGLEGTS 1150
Cdd:cd14899 520 RSA-PLIQRTTQFVVAHYAGC--VTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQAL--AAGSNDEDANGDSELDGFG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1034629690 1151 QQALQRSRmvrrtfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14899 594 GRTRRRAK-------SAIAAV---SVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1386-2070 |
2.96e-19 |
|
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: 95.63 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1386 QLLGSLQPLLSATIGTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvaCQVLESER 1464
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1465 AERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDS 1544
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ-EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1545 ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfEKG 1624
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EKA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1625 LREKVTQENTSVRWElgqlqqqLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESS--------- 1695
Cdd:pfam01576 616 ISARYAEERDRAEAE-------AREKETRALSLARALEEALEAKEEL-------ERTNKQLRAEMEDLVSSkddvgknvh 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1696 -------ALEQQ----KIQSQQ-ENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQE 1763
Cdd:pfam01576 682 elerskrALEQQveemKTQLEElEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1764 YEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQlllgtmedgktsvskEELEKVHSQLEQSE 1843
Cdd:pfam01576 762 RKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQ---------------RELEEARASRDEIL 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1844 AKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMqkhkdliaqsaadiGQI 1923
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE--------------ARI 891
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1924 QELQLQLEEAKKEKHKLQEQLQVAQMRIEYL------EQSTVDRAIVSRQEAVICDLENKTEFQKV--QIK-RFEVLVIR 1994
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLttelaaERSTSQKSESARQQLERQNKELKAKLQEMegTVKsKFKSSIAA 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1995 LRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL--------------KADMEELVQREAEASRRCMELEKYVEELAA 2060
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqvederrhadqyKDQAEKGNSRMKQLKRQLEEAEEEASRANA 1051
|
730
....*....|
gi 1034629690 2061 VRQTLQTDLE 2070
Cdd:pfam01576 1052 ARRKLQRELD 1061
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1402-2067 |
1.01e-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: 93.97 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEEAqqKIQLNDLERNPTGGDEWQ---------MRFDCAQMENEFLRKRLQQCEERLDSELTARKEL 1552
Cdd:TIGR02168 389 AQLELQIASLNNEIERL--EARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1553 EQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE------DTCVLLENQQSRNH-------ELEKKQKKFDLQLAQALGES 1619
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIEAALGGR 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1620 VfekglrEKVTQENTSVRW---------ELGQLQQQLKQKEQEASQLKQQVEMLQDHKR------ELLGSPSLGENCVAG 1684
Cdd:TIGR02168 547 L------QAVVVENLNAAKkaiaflkqnELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1685 LKERLWKLES--SALEQQKIQS-------------------------------QQENTIKQLEQLRQRFELEIERMKQ-- 1729
Cdd:TIGR02168 621 LLGGVLVVDDldNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1730 -MHQKDREDQEEELEDVR---QSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRR 1805
Cdd:TIGR02168 701 aELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1806 THALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQ 1885
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1886 FEKADLLKRIDEDQDDLNEL----------MQKHKDLIAQSAADI----GQIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1951
Cdd:TIGR02168 859 AEIEELEELIEELESELEALlnerasleeaLALLRSELEELSEELreleSKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1952 EYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlVIRLRDSLIKMGeELSQAATSESQQressqyYQRRLEELK 2031
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-----LKRLENKIKELG-PVNLAAIEEYEE------LKERYDFLT 1006
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629690 2032 ADMEELVqrEAEASrrcmeLEKYVEEL-AAVRQTLQT 2067
Cdd:TIGR02168 1007 AQKEDLT--EAKET-----LEEAIEEIdREARERFKD 1036
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
586-999 |
2.21e-17 |
|
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: 88.64 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVP-----SAGKVPKGRRDGLPaHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEypqefHAKYRCKSRSDNAP-HIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 661 WSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd14882 81 ESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 741 LEKSRVARQPEGESNFLVFSQMLAGL-------DLDLRTELNLHQM----ADSSSFGMGVWSKPEDKQKAAAAFAQLQGA 809
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFIeaqnrlkEYNLKAGRNYRYLrippEVPPSKLKYRRDDPEGNVERYKEFEEILKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 810 MEMlgiSESEQRAVWRVLAAIYHLGAAGACKV-GRKQFMRFEWANYAAEALGceyeeLNTATFKHHLRQIIQQMTFGPSR 888
Cdd:cd14882 239 LDF---NEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 889 WGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINrsfssHHLSMA--------SIMVVDSPGFQNPRHQGkdra 960
Cdd:cd14882 311 RKHTTEEAR--------DARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR---- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034629690 961 atFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ 999
Cdd:cd14882 374 --LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTI 410
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1403-2089 |
2.27e-17 |
|
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: 89.46 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVA----------CQVLESERAERLQAFR 1472
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDTLDTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1473 EVQELKSKHEQvqkKLGDVNKQLEEAQQ--KIQLNDL-ERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEE--------- 1540
Cdd:pfam01576 317 AQQELRSKREQ---EVTELKKALEEETRshEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1541 ------RLDSElTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQL-- 1612
Cdd:pfam01576 394 rtlqqaKQDSE-HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1613 AQALG--ESVFEKGLREKVTQ---ENTSVRWELGQLQQQLKQKEQEASQLKQQvemLQDHKREllgspslgencvagLKE 1687
Cdd:pfam01576 473 TQELLqeETRQKLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQ---LSDMKKK--------------LEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1688 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSC------QKRLHQL---EM 1758
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkQKKFDQMlaeEK 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1759 QLEQEY-EEKQMVLHEKQDLEGLIGTLCdqighRDFDVEKRLRRDLRRTHALL-SDVQLLLGTMEDGKTSVskEELEKVH 1836
Cdd:pfam01576 615 AISARYaEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTNKQLrAEMEDLVSSKDDVGKNV--HELERSK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1837 SQLEQSeakcEEALKTQkvltadLESMHSELEnMTRNKSL---VDEQLYRLQFE-------------KADLLKRIDEDQD 1900
Cdd:pfam01576 688 RALEQQ----VEEMKTQ------LEELEDELQ-ATEDAKLrleVNMQALKAQFErdlqardeqgeekRRQLVKQVRELEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1901 DLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLeQSTVDRAIVSRQEAVICDLENKTef 1980
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1981 qkvQIKRFEVLVIRLRDSLI--------------KMGEELSQAATSESQQRESsqyyQRRLEELKADMEELVQREAEAS- 2045
Cdd:pfam01576 834 ---KLKNLEAELLQLQEDLAaserarrqaqqerdELADEIASGASGKSALQDE----KRRLEARIAQLEEELEEEQSNTe 906
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 2046 -------RRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASS 2089
Cdd:pfam01576 907 llndrlrKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGT 960
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
585-999 |
2.34e-17 |
|
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: 88.92 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGA 664
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 665 GKTTCCEQVLE-HLVGMagSVDGRVSVEKIRATFtVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEK 743
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 744 SRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPE-DKQKAAAAFAQLQGAMEMLGISESeqra 822
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNMHDMKDD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 823 VWRVLAAIYHLG--------AAGACKVGRKQFMRFEWANYAAEALGCEYEEL-NTATFKHhlRQIIQQMTFGPsrwgLED 893
Cdd:cd14937 234 LFLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 894 EETSSGLKMTGVDcvegmasgLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHE 973
Cdd:cd14937 308 EESVSICKSISKD--------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANE 373
|
410 420
....*....|....*....|....*.
gi 1034629690 974 RLQLLFYQRTFVSTLQRYQEEGVPVQ 999
Cdd:cd14937 374 EIHSIYLYIVYEKETELYKAEDILIE 399
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
586-1205 |
2.68e-17 |
|
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: 88.81 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-------------------SVPSAGKVPkgrrdglPAHIGSMAQRAYWA 646
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPlkelydqdvmnvylhkksnSAASAAPFP-------KAHIYDIANMAYKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 647 LLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFN 726
Cdd:cd14884 75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 727 A---------TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-DLDL---RTELNLH----------QMADSS 783
Cdd:cd14884 155 EventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvygllnpdesHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 784 SFGMGVWSK-----PEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGackvgrkqfmrfewANYAAEA 858
Cdd:cd14884 235 KGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRA--------------YKAAAEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 859 LGCEYEELNTaTFKHHLRQIIQQMTFGPSRwglEDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINR--------- 929
Cdd:cd14884 301 LQIEEEDLEN-VIKYKNIRVSHEVIRTERR---KENATST---------RDTLIKFIYKKLFNKIIEDINRnvlkckekd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 930 SFSSHHLSM---ASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPS 1006
Cdd:cd14884 368 ESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1007 PGTTVAVVDQNPSQV----RLPAgGGAQDARGLFW---------VLDEEVHVEGSsdsvVLERLCAAFEKKGAGTEGSSA 1073
Cdd:cd14884 441 YSDTLIFIAKIFRRLdditKLKN-QGQKKTDDHFFryllnnerqQQLEGKVSYGF----VLNHDADGTAKKQNIKKNIFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1074 LRtceqplqceifHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSlfqaraklppvcravAGLEGTSQQA 1153
Cdd:cd14884 516 IR-----------HYAG--LVTYRINNWIDKNSDKIET-SIETLISCSSNRFLRE---------------ANNGGNKGNF 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 1154 LQRSRMVrrtfasslaavrrkapcsqIKlQMDALTSMIKRSRLHFIHCLVPN 1205
Cdd:cd14884 567 LSVSKKY-------------------IK-ELDNLFTQLQSTDMYYIRCFLPN 598
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1402-1956 |
3.92e-17 |
|
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: 88.15 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLAD---ERFKGDVACQVLES--ERAERLQAfrEVQE 1476
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKkiQKNKSLES--QISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1477 LKSKH-------EQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLdSELT 1547
Cdd:TIGR04523 223 LKKQNnqlkdniEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-SDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1548 ARKE-------------LEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQ-QSRNHELEKKQKKfdLQLA 1613
Cdd:TIGR04523 302 NQKEqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----SESEnSEKQRELEEKQNE--IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1614 QALGESVFEKglREKVTQENTSVRWELgqlqqqlKQKEQEASQLKQQVEMLQDHKRELLGspslgencvaglkerlwkle 1693
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1694 ssalEQQKIQSQ---QENTIKQLEQLRQRFELEIERMKQMhqkdREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQ-- 1768
Cdd:TIGR04523 427 ----EIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNT----RESLETQLKVLSRSINKIKQNLE-QKQKELKSKEke 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1769 --MVLHEKQDLEGLIGTLCDQIghrdfdvekrlrrdlrrthallsdvqlllgtmedgktSVSKEELEKVHSQLEQSEAKC 1846
Cdd:TIGR04523 498 lkKLNEEKKELEEKVKDLTKKI-------------------------------------SSLKEKIEKLESEKKEKESKI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1847 EEalktqkvLTADLESMHSEL--ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQ 1924
Cdd:TIGR04523 541 SD-------LEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590
....*....|....*....|....*....|..
gi 1034629690 1925 ELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1956
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-2085 |
1.42e-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: 87.03 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1408 EEELTTLRRKLEKSEKLRnELRQntDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1487
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYK-ELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1488 LGDVNKQLEEAQQK-----IQLNDLERNPTGGDEwqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1562
Cdd:TIGR02168 276 VSELEEEIEELQKElyalaNEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1563 YDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfekgLREKVTQentsvrwelgq 1642
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLER----------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1643 lqqqlkqkeqeasqLKQQVEMLQDHKRELLGSPSLGEncvagLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL 1722
Cdd:TIGR02168 412 --------------LEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1723 EIERMKQmhqkdREDQEEELedvrQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfDVEKRLRRD 1802
Cdd:TIGR02168 473 AEQALDA-----AERELAQL----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEAA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1803 LRRthALLSDVQLLLgtMEDgktsvsKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVD 1878
Cdd:TIGR02168 539 IEA--ALGGRLQAVV--VEN------LNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1879 EqlYRLQFEKA--DLLKR--IDEDQDDLNELMQKHK----------DLIA-------QSAADIGQIQELQLQLEEAKKEK 1937
Cdd:TIGR02168 609 K--FDPKLRKAlsYLLGGvlVVDDLDNALELAKKLRpgyrivtldgDLVRpggvitgGSAKTNSSILERRREIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1938 HKLQEQLQVAQMRIEYLEQSTVDraivsrqeavicdLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQr 2017
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL- 752
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629690 2018 essqyyQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:TIGR02168 753 ------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
586-1057 |
2.88e-16 |
|
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: 85.14 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVPK-GRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWS 662
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRylPFLHSQELVRNyNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 663 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLE 742
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 743 KSRVARQPEGESNFLVFSQMLAGLDLDlrtELNLHQMADSSSF-------GMGVWSKPEDKqkaaaAFAQLQGAMEMLGI 815
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDE---EKAAYQLGDINSYhylnqggSISVESIDDNR-----VFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 816 SESEQRAVWRVLAAIYHLGAAgackvgrkQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRWGLEDEE 895
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 896 TssglkmtgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMaSIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:cd14905 305 S--------------LARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 976 QLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgTTVAVVDQNPSqvrlpagggAQDARGLFWVLDEEVHVEGSSDSVVLE 1055
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWM---------TPISFKDNEES---------VEMMEKIINLLDQESKNINSSDQIFLE 425
|
..
gi 1034629690 1056 RL 1057
Cdd:cd14905 426 KL 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1402-2070 |
1.44e-15 |
|
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: 83.69 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNEL-RQNTDLLESKIA---------DLTSDLADERFKGDVACQVLES---ERAERL 1468
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNAlqeqlqaetELCAEAEEMRARLAARKQELEEilhELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1469 QAFRE-VQELKSKHEQVQKKLGDVNKQLEE---AQQKIQlndLERNPTGGDEWQMRFDCAQME--NEFLRKRLQQCEERL 1542
Cdd:pfam01576 85 EEEEErSQQLQNEKKKMQQHIQDLEEQLDEeeaARQKLQ---LEKVTTEAKIKKLEEDILLLEdqNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1543 DSELTARKELEQKLgelqsaydgakKMAHQLKRKCHHLTCDLEDTcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFE 1622
Cdd:pfam01576 162 SEFTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1623 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL---------------GSPSLGENCVAgLKE 1687
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraarnkaekQRRDLGEELEA-LKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1688 RLWKLESSALEQQKIQSQQENTI----KQLEQLRQRFELEIERMKQMHQKDREDQEEELED---VRQSCQKRLHQLEMQL 1760
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQEVtelkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1761 EQEYEEKQMVLHEKQDLEgligtlcdqigHRdfdvEKRLRRDLRRTHALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLE 1840
Cdd:pfam01576 387 AELQAELRTLQQAKQDSE-----------HK----RKKLEGQLQELQARLSESERQRAELAE-KLSKLQSELESVSSLLN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1841 QSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI 1920
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1921 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY------------------LEQSTVDraiVSRQEAVICDLENKTefqk 1982
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrlqqeLDDLLVD---LDHQRQLVSNLEKKQ---- 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1983 vqiKRFEVLVIRLRDSLIKMGEELSQA----------ATSESQQRESSQYYQRRLEE----LKADMEELVQREAEASRRC 2048
Cdd:pfam01576 604 ---KKFDQMLAEEKAISARYAEERDRAeaeareketrALSLARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKNV 680
|
730 740
....*....|....*....|..
gi 1034629690 2049 MELEKYVEELAAVRQTLQTDLE 2070
Cdd:pfam01576 681 HELERSKRALEQQVEEMKTQLE 702
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1384-2021 |
3.36e-15 |
|
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: 82.32 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1384 WW--QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdllESKIADLTSDLADERFKGDVACQVLE 1461
Cdd:TIGR00618 243 AYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1462 SERAERLQAFREVQELKSKHEQVQKKLGDVNKQLeeaQQKIQLNDLERNPTGgdeWQMRFDCAQMENEFLRKRLQQCEER 1541
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATS---IREISCQQHTLTQHIHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1542 LDSELTARKELEQKLGEL-QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGES 1619
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQeSAQSLKER 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1620 VFEKGLREKVTQENTSVRWELGQLQQQLKQKEQE--ASQLKQQVEMLQDHKRELLGSPSL-GENCVAGLKERLWKLE--- 1693
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYhql 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1694 SSALEQQKIQSQQENTIKQ----LEQLRQRFELEIERMKQMHQKDREDQEEELEDvRQSCQKRLHQLEMQLEQEYEEKQM 1769
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQsfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-EDMLACEQHALLRKLQPEQDLQDV 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1770 VLHEKQ----------DLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVS--KEELEKVHS 1837
Cdd:TIGR00618 631 RLHLQQcsqelalkltALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1838 QLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1917
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1918 ADIGQIQELQLQLEEAKKEKHKLQEQLQvaQMRIEYLEQSTV-DRAIVSRQEAVICDLENKTEfqkvqikrfevLVIRLR 1996
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLqCETLVQEEEQFLSRLEEKSA-----------TLGEIT 848
|
650 660
....*....|....*....|....*
gi 1034629690 1997 DSLIKMGEELSQAATSESQQRESSQ 2021
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1472-2101 |
3.47e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1472 REVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENefLRKRLQQCEERLDSELTARKE 1551
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE--LKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1552 LEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdledtcvllenqqsrnhELEKKQKKFdlqlaQALGEsvfekgLREKVTQ 1631
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELK------------------ELKEKAEEY-----IKLSE------FYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1632 ENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvAGLKERLWKLESSALEQQKIQSQQENtik 1711
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKKEE--- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1712 qLEQLRQRFE-LEIERMKQMHQKDREDQEEELEDVRQSCQKRlhqleMQLEQEYEEKQMVLHEkqdLEGLIGTlCDQIGh 1790
Cdd:PRK03918 374 -LERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARI-----GELKKEIKELKKAIEE---LKKAKGK-CPVCG- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1791 RDFDVEKRLRRdLRRTHALLSDVqlllgtmedgktSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTAdLESMHSELENm 1870
Cdd:PRK03918 443 RELTEEHRKEL-LEEYTAELKRI------------EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKE- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1871 trnkslVDEQLYRLQFEKadlLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMR 1950
Cdd:PRK03918 508 ------LEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1951 IEYLEQSTVDraivsrqeavicDLENKTEFQKVQIKRFevlvIRLRDSLIKMGEELSQAATSESQQRESSQYYQR---RL 2027
Cdd:PRK03918 579 LEELGFESVE------------ELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAEtekRL 642
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2028 EELKADMEEL-----VQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVD 2101
Cdd:PRK03918 643 EELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1408-2088 |
1.42e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLE--SKIA----DLTSDLadERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLErqAEKAeryrELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENE--FLRKRLQQCEERLDSELTARKELEQKLGEL 1559
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiaRLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1560 QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWE 1639
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1640 LGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpslgencVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQR 1719
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1720 FELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ---LEMQLEQEYEEkqmvlhekqDLEGLIGTLCDQIGHRDFDVE 1796
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavaVLIGVEAAYEA---------ALEAALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1797 KRLRRDLRRtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSL 1876
Cdd:COG1196 560 AAAIEYLKA-AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1877 VDEQLYRLQFEKADLlkridedqddlnelmqkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1956
Cdd:COG1196 639 AVTLAGRLREVTLEG-------------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1957 STVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDsLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEE 2036
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 2037 L------VQREAEasrrcmELEKYVEELAAVRQTLQ---TDLETSIRRI-----ADLQAALEEVAS 2088
Cdd:COG1196 779 LgpvnllAIEEYE------ELEERYDFLSEQREDLEearETLEEAIEEIdretrERFLETFDAVNE 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1829-2097 |
2.30e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1908
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1909 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENKTEFQKVQIKRF 1988
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1989 EVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2068
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....*....
gi 1034629690 2069 LETSIRRIADLQAALEEVASSDSDTESVQ 2097
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1686-2122 |
2.36e-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: 79.45 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1686 KERLWKLESSALEQQKIQSQ--QENTIKQlEQLRQRFEL--EIERMKQMhqkdREDQEEELEDVrqscqkrLHQLEMQLE 1761
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMRAR----LAARKQELEEI-------LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1762 QEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEE--LEKVHSQL 1839
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEE-AARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERklLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1840 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNkslvdEQLYRLQFEKADllKRIDEDQDDLNElmqkhkdliaqsaad 1919
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-----EEKGRQELEKAK--RKLEGESTDLQE--------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1920 igQIQELQLQLEEAKKEKHKLQEQLQVAQMRieyLEQSTVDRAIVSRQ----EAVICDLE----------NKTEFQKVQI 1985
Cdd:pfam01576 223 --QIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKirelEAQISELQedleseraarNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1986 -KRFEVLVIRLRDSL----------IKMGEELSQ--------AATSESQQRESSQYYQRRLEELKADMEELVQREAEASR 2046
Cdd:pfam01576 298 gEELEALKTELEDTLdttaaqqelrSKREQEVTElkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 2047 RCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQT-AVDCGSSGRKEMDNVSILSSQPEG 2122
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAeLAEKLSKLQSELESVSSLLNEAEG 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1942 |
1.19e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLR---NELRQNTDLLESKIADLTSDLaderfkgdvacqvleSERAERLqafrevQELK 1478
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKI---------------RELEERI------EELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1479 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggDEWQMRFDCAQMENEFLRKRLQQCEERLD--SELTAR-KELEQK 1555
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIKLSEFY------EEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERlEELKKK 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1556 LGELQSAYDGAKKmAHQLkrkchhltcdLEDTCVLLENQQsrnhELEKKQKKFDLQLAQALGESVFEKglREKVTQENTS 1635
Cdd:PRK03918 347 LKELEKRLEELEE-RHEL----------YEEAKAKKEELE----RLKKRLTGLTPEKLEKELEELEKA--KEEIEEEISK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1636 VRWELGQLQQQLKQKEQEASQLKQ--------QVEMLQDHKRELLGSPSLG----ENCVAGLKERLWKLESSALEQQKIQ 1703
Cdd:PRK03918 410 ITARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1704 SQQENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLHQLEMQLEQEYE---EKQMVLHEKQDL 1777
Cdd:PRK03918 490 KKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEKLEElkkKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1778 EGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGtmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLT 1857
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETE 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1858 ADLESMHSELENMTRNKSLVD-EQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKE 1936
Cdd:PRK03918 640 KRLEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKA 719
|
....*.
gi 1034629690 1937 KHKLQE 1942
Cdd:PRK03918 720 LERVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1433-2097 |
1.74e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.55 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1433 DLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREvQELKSKHEQVQKkLGDVNKQLEEAQQKIQLNDlernpt 1512
Cdd:TIGR00618 171 NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQV-LEKELKHLREALQQTQQSH------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1513 ggdEWQMRFDCAQMENEFLRKRLQQCEERLDsELTArkeLEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLE 1592
Cdd:TIGR00618 243 ---AYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA---QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1593 nQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEA-----SQLKQQVEMLQDH 1667
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1668 KRELLGSPSLGENCVAGLKERLwkLESSALEQQKI--QSQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEELE 1743
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRT--SAFRDLQGQLAhaKKQQELQQRYAELCAAAITctAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1744 dvrqscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfdvekrlrrdlrrTHALLSDvqlllgtmEDG 1823
Cdd:TIGR00618 473 -------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-------------PARQDID--------NPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1824 KTSVSKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID--- 1896
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkls 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1897 EDQDDLNELMQKHKDLIAQSAADIGQIQEL-QLQLEEAKKEKHKLQEQLQVAQMRI-EYLEQSTVDRA-IVSRQEAVICD 1973
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKeLLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1974 LENKTEF---------QKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESS------QYYQRRLEELKADMEELV 2038
Cdd:TIGR00618 685 MQSEKEQltywkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2039 QREAEASRRCMELEKYvEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQ 2097
Cdd:TIGR00618 765 NNNEEVTAALQTGAEL-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-2085 |
2.59e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRnELRQNTDLLESKIADLTSDL--ADERFKGDVACQVLESERAERLQAFREVQ--EL 1477
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVrkAEELRKAEDARKAEAARKAEEERKAEEARkaED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1478 KSKHEQVqKKLGDVNKQLEEAQQKiqlnDLERNptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLG 1557
Cdd:PTZ00121 1223 AKKAEAV-KKAEEAKKDAEEAKKA----EEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1558 ELQSAYDgaKKMAHQLKRKChhltcdledtcvllenQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ-ENTSV 1636
Cdd:PTZ00121 1294 EAKKAEE--KKKADEAKKKA----------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEAA 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1637 RWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK--ERLWKLESSALEQQKIQSQQENtIKQLE 1714
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEE-KKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1715 QLRQRFEleiERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEmqLEQEYEEKQMVLHEKQDLEgligtlcdqighrdfd 1794
Cdd:PTZ00121 1435 EAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAE---------------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1795 vEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSvskEELEKVHSQLEQSEA-KCEEALKTQKVLTADLESMHSELENMTRN 1873
Cdd:PTZ00121 1494 -EAKKKADEAKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1874 KSlvDEQLYRLQFEKADLLKRIDEDQddLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKhklQEQLQVAQMRIEY 1953
Cdd:PTZ00121 1570 KK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKE 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1954 LEQstVDRAIVSRQEavicdlENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAatsESQQRESSQYYQRRLEElKAD 2033
Cdd:PTZ00121 1643 AEE--KKKAEELKKA------EEENKIKAAEEAKKA-------EEDKKKAEEAKKA---EEDEKKAAEALKKEAEE-AKK 1703
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 2034 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1401-1945 |
2.86e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSK 1480
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfDCAQMENEFLRKRLQQcEERLDSELTARKELEQKLGELQ 1560
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA-----------EAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1561 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWEL 1640
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1641 GQLQQQLKQKEQEASQLKQQVEMLQDH------KRELLGSPSLGENCVAGLKERLWKLESSALEQqkiqsqqentikqle 1714
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--------------- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1715 qlrqrfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDF- 1793
Cdd:COG1196 542 ------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARy 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1794 -----------DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLES 1862
Cdd:COG1196 616 yvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1863 MHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELqLQLEEAKKEKHKLQE 1942
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLER 774
|
...
gi 1034629690 1943 QLQ 1945
Cdd:COG1196 775 EIE 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1403-2057 |
8.29e-12 |
|
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: 70.91 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1403 QLRAKEEELTTLRRKLEKSEKLRNELR-QNTDL---LESKIADlTSDLADERFKGDVACQVLESERAerlQAFREVQELK 1478
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQfENEKVslkLEEEIQE-NKDLIKENNATRHLCNLLKETCA---RSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1479 SKHEQVQKKLGDVNkqleeaqqkiqlNDLERNPTGGDEWQMRFDCAQMENEFLRK----RLQQCEERLDSELTARK---- 1550
Cdd:pfam05483 176 YEREETRQVYMDLN------------NNIEKMILAFEELRVQAENARLEMHFKLKedheKIQHLEEEYKKEINDKEkqvs 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1551 -------ELEQKLGELQSAYDGAKKMAHQLKRKC--------------HHLTCDLEDTCVLLENQQSRNHELEKkqkkfD 1609
Cdd:pfam05483 244 llliqitEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEE-----D 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1610 LQLAQalgESVFEkglrekVTQENTSVRWELGqlqQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERL 1689
Cdd:pfam05483 319 LQIAT---KTICQ------LTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1690 WKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKRLHQLEMQLEQEYEEK 1767
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1768 QMVLHEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALL---SDVQLLLGTMEDGKTSVSKEElEKVHSQLEQSEa 1844
Cdd:pfam05483 467 EHYLKEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTqeaSDMTLELKKHQEDIINCKKQE-ERMLKQIENLE- 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1845 kceealKTQKVLTADLESMHSEL---------------ENMTRNKSLV---DEQLYRLQFEKADLLKRIDEDQDDLNELM 1906
Cdd:pfam05483 541 ------EKEMNLRDELESVREEFiqkgdevkckldkseENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1907 QKHKDLIAQSAADIGQ-------IQELQLQLEEAKKekhKLQEQLQVAQMRIEYLEQS------TVDRAIVSRQEAVICD 1973
Cdd:pfam05483 615 QENKALKKKGSAENKQlnayeikVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAVKLQ 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1974 LENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL-SQAATSESQQRESSQyyqrrleeLKADME-ELVQREAE--ASRRCM 2049
Cdd:pfam05483 692 KEIDKRCQH-KIAEMVALMEKHKHQYDKIIEERdSELGLYKNKEQEQSS--------AKAALEiELSNIKAEllSLKKQL 762
|
....*...
gi 1034629690 2050 ELEKYVEE 2057
Cdd:pfam05483 763 EIEKEEKE 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1822-2087 |
1.92e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1822 DGKTSVSKEELEKVHSQLEQSEAKCEE-------------------ALKTQK------VLTADLESMHSELENMTRNKSL 1876
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrerekaeryqALLKEKreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1877 VDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI--------GQIQELQLQLEEAKKEKHKLQEQLQVAQ 1948
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1949 MRIEyleqstvdraivsRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLE 2028
Cdd:TIGR02169 329 AEID-------------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2029 ELKADMEELvqrEAEASRRCMELEKYVEELAAVRQtlqtDLETSIRRIADLQAALEEVA 2087
Cdd:TIGR02169 396 KLKREINEL---KRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA 447
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1402-2085 |
2.11e-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: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTS-DLADERFKGDVACQVLE-----SERAERLQAF--RE 1473
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSrKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNhqRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1474 VQELKSKHEQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQ---MRFDCAQMENEfLRKRLQQCEERLDSELTA 1548
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTelLVEQGRLQLQADRHQehiRARDSLIQSLA-TRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1549 R--------------KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSrnhelEKKQKKFDLQLAQ 1614
Cdd:TIGR00606 393 KnfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1615 ALGESVFEKglrekvTQENTSVRWELgqlqqQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGL---KERLWK 1691
Cdd:TIGR00606 468 GSSDRILEL------DQELRKAEREL-----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1692 LESSALEQ----QKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLHQLEMQLEQEYE 1765
Cdd:TIGR00606 537 MEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1766 EKQMVLHEKQDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSdvqlllgtMEDGKTSVSKEELEKVHSQLEQSEA 1844
Cdd:TIGR00606 616 SKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRA--------MLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1845 KCEEALKTQKVL---TADLESM-------HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIA 1914
Cdd:TIGR00606 682 VCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1915 QSAADIGQiQELQLQLEEAKKEKHKLQeQLQVAQMRIEYLEQSTVDRAI---VSRQEAVICDLENKTEFQKVQIKRFEVl 1991
Cdd:TIGR00606 762 RLKNDIEE-QETLLGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIaqqAAKLQGSDLDRTVQQVNQEKQEKQHEL- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1992 virlrDSLIKMGEELSQAAtseSQQRESSQYYQRRLEELKADMEELvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2071
Cdd:TIGR00606 839 -----DTVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
730
....*....|....
gi 1034629690 2072 SIRRIADLQAALEE 2085
Cdd:TIGR00606 907 AKEQDSPLETFLEK 920
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1696-2092 |
3.58e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1696 ALEQQKIQSQQENTIKQLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQ----KRLHQLEMQLEQEYEEKQMVL 1771
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELER----LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1772 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVqlllgtmedgktsvsKEELEKVHSQLEQSEAKceealk 1851
Cdd:COG4913 359 RRRARLE----ALLAALGLPLPASAEEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAA------ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1852 tQKVLTADLESMHSELENMTRNKSLVDEQLYRLqfeKADLLKRIDEDQDDLN---ELMQ-KHKDLIAQSAAdigqiqELQ 1927
Cdd:COG4913 414 -LRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAELPfvgELIEvRPEEERWRGAI------ERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1928 L------------QLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD---------------------RAIVSRQEAVIC 1972
Cdd:COG4913 484 LggfaltllvppeHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfrawlEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1973 dLENKTEFQKVqikRFEVlvirLRDSLIKMGEELSQAATsesQQRESSQYY-----QRRLEELKADMEELVQREAEASRR 2047
Cdd:COG4913 564 -VDSPEELRRH---PRAI----TRAGQVKGNGTRHEKDD---RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 2048 CMELEKYVEELAAVRQTLQT---------DLETSIRRIADLQAALEEVASSDSD 2092
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDD 686
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-1890 |
3.63e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELttlrRKLEKSEKLRNELRQNTDllESKIADLTSDLADERFKGDVACQVLESER-AERL----QAFREVQE 1476
Cdd:PTZ00121 1401 EEDKKKADEL----KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKkAEEAkkkaEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1477 LKSKHEQvQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDEWQmrfdcaQMENEFLRKRLQQCEERLDSELTARKELEQK 1555
Cdd:PTZ00121 1475 AKKKAEE-AKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAK------KAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1556 LGELQSAYDGAK----KMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ 1631
Cdd:PTZ00121 1548 ADELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1632 ENtSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK----------ERLWKLESSALEQQK 1701
Cdd:PTZ00121 1628 AE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1702 IQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE--EEL---EDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQD 1776
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1777 LE-------------------------GLIGTLCDQIGHRDFDVEKR---LRRDLRRTHALLSDVQLLLGTMEDGKTSVS 1828
Cdd:PTZ00121 1787 EEdekrrmevdkkikdifdnfaniiegGKEGNLVINDSKEMEDSAIKevaDSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKAD 1890
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1479-2085 |
3.71e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 65.43 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1479 SKHEQVQKKLGDVNKQLEEAQQKIQlnDLERNPTGGDEwqmrfDCAQMENEFlrKRLQQCEERLDSELTARKeleQKLGE 1558
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELK--NLDKNLNKDEE-----KINNSNNKI--KILEQQIKDLNDKLKKNK---DKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1559 LQSaydGAKKMAHQLKRKchhltcdlEDTCVLLENQQSRnheLEKKQKKFDLQLAQALGESVFEKGLREKVTQENtsvrw 1638
Cdd:TIGR04523 101 LNS---DLSKINSEIKND--------KEQKNKLEVELNK---LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1639 elgqlqqqlkqkeqeaSQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQ 1718
Cdd:TIGR04523 162 ----------------NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1719 RFElEIERMKQMHQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMVLHEKQ-DLE---GLIGTLCDQIghrdfd 1794
Cdd:TIGR04523 226 QNN-QLKDNIEKKQQEINEKTTEISNTQT-------QLN-QLKDEQNKIKKQLSEKQkELEqnnKKIKELEKQL------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1795 vekrlrrdlrrtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNK 1874
Cdd:TIGR04523 291 ------------NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1875 SLVDEQLYrlqfEKADLLKRIDEDQDDLNELMQKHKDliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL 1954
Cdd:TIGR04523 359 SEKQRELE----EKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1955 EQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSqyyQRRLEELKAD 2033
Cdd:TIGR04523 425 EKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKE 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 2034 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1682-2102 |
4.75e-10 |
|
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: 65.46 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1682 VAGLKERlwKLESsaleQQKIQSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRLH 1754
Cdd:TIGR02168 167 ISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1755 QLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLGTMEdGKTSVSKEELE 1833
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLE-QQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1834 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1913
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1914 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAvicdLENKTEfqkvqikRFEVLVI 1993
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQE-------ELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1994 RLrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSi 2073
Cdd:TIGR02168 462 AL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD- 532
|
410 420 430
....*....|....*....|....*....|..
gi 1034629690 2074 rriADLQAALEEVASSDSD---TESVQTAVDC 2102
Cdd:TIGR02168 533 ---EGYEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1398-1858 |
1.43e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1398 TIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvlesERAERLQAFREVQEL 1477
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELR------------EELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1478 KSKHEQVQKKLGDVNKQLEEAQQKIQ-LNDLERnptggdewqmrfDCAQMENEFLRKRLQQCEERLDSELTARKELEQ-- 1554
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEeLRELEE------------ELEELEAELAELQEELEELLEQLSLATEEELQDla 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1555 -KLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQEN 1633
Cdd:COG4717 199 eELEELQQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1634 -----------TSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK-RELLGSPSLGENcvaGLKERLWKLESSALEQQK 1701
Cdd:COG4717 275 iagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAALGLPPD---LSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1702 IQSQQENTIKQLEQlrQRFELEIER-MKQMHQKDREDQEEELEDVRQSCQ--KRLHQLEMQLEQEYEEKQMVL--HEKQD 1776
Cdd:COG4717 352 LLREAEELEEELQL--EELEQEIAAlLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLeaLDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1777 LEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGktsvskEELEKVHSQLEQSEAKCEEALKTQKVL 1856
Cdd:COG4717 430 LEEELEELEEEL--------EELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAAL 495
|
..
gi 1034629690 1857 TA 1858
Cdd:COG4717 496 KL 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1654-2096 |
1.53e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1654 ASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES------SALEQQKIQSQQENtiKQLEQLRQRFELEIERM 1727
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrDRLEECRVAAQAHN--EEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1728 KQMHQK----------------DREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghr 1791
Cdd:PRK02224 359 EELREEaaeleseleeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1792 dfdveKRLRRDLRRTHALLsdvqlllgtmEDGKTSVSKEELEKvhSQLEQSEAKCEEALKTQKVLTADLESMHSELEN-M 1870
Cdd:PRK02224 436 -----RTARERVEEAEALL----------EAGKCPECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEErL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1871 TRNKSLV--DEQLYRLQfEKADLLK--------RIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKL 1940
Cdd:PRK02224 499 ERAEDLVeaEDRIERLE-ERREDLEeliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1941 QEQLQVAQMRIEYLEqstvdraivsRQEAVICDLENktefqkvqikrfevlvirLRDSLIKMGEELSQAATSESQQRESS 2020
Cdd:PRK02224 578 NSKLAELKERIESLE----------RIRTLLAAIAD------------------AEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2021 QYYQRRLEELKAD-----MEELVQREAEASRRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASSDSD 2092
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
....
gi 1034629690 2093 TESV 2096
Cdd:PRK02224 710 LEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1589-2084 |
1.63e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1589 VLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1668
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1669 R--ELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR 1746
Cdd:COG4717 126 QllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1747 QSCQkrlhqlemQLEQEYEEKQMVLHE-KQDLEGLigtlcdQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLGTMEDGKT 1825
Cdd:COG4717 206 QRLA--------ELEEELEEAQEELEElEEELEQL------ENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1826 SVskeelekvhsqleqseakceeaLKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQfekaDLLKRIDEDQDDLNEL 1905
Cdd:COG4717 271 LI----------------------LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----ALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1906 MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEylEQSTVDRAIVSRQEAVICDLENKTEFQKVQi 1985
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1986 KRFEVLVIRLRDSLIKMGEELsqAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEK--YVEELAAVRQ 2063
Cdd:COG4717 402 EELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELE 479
|
490 500
....*....|....*....|.
gi 1034629690 2064 TLQTDLETSIRRIADLQAALE 2084
Cdd:COG4717 480 ELKAELRELAEEWAALKLALE 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1402-2286 |
2.05e-09 |
|
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: 63.21 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKS-EKLRNELRQNTDLLESKIADLTSDLAderfkgdVACQVLESERAERLQAFREVQELKsk 1480
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQFSQESGNLD-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 hEQVQKKLGDVNKQ-----LEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEflrkRLQQCEERLDSEltARKELEQK 1555
Cdd:pfam15921 377 -DQLQKLLADLHKRekelsLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE--CQGQMERQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1556 LGELQSAYDGAKKMAhqlkrkchHLTCDLEDTCVLL----ENQQSRNHELEKKQKKFDlQLAQALGESvfEKGLrEKVTQ 1631
Cdd:pfam15921 450 MAAIQGKNESLEKVS--------SLTAQLESTKEMLrkvvEELTAKKMTLESSERTVS-DLTASLQEK--ERAI-EATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1632 ENTSVRwelgqlqqqlkqkeqeaSQLKQQVEMLQDHKREllgspslGENcvaglkerlwkLESSALEQQKIQSQQENTIK 1711
Cdd:pfam15921 518 EITKLR-----------------SRVDLKLQELQHLKNE-------GDH-----------LRNVQTECEALKLQMAEKDK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1712 QLEQLRQrfelEIERMKQM-HQKDREDQEEELEdvrqscqkrlhqlEMQLEQEYEEKQMVLHEKQDLEgligtlcdqigh 1790
Cdd:pfam15921 563 VIEILRQ----QIENMTQLvGQHGRTAGAMQVE-------------KAQLEKEINDRRLELQEFKILK------------ 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1791 rdfdvEKRLRRdLRRTHALLSDVQL----LLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMH 1864
Cdd:pfam15921 614 -----DKKDAK-IRELEARVSDLELekvkLVNAGSERLRAVKdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1865 SELEnMTRNKslvdeqlYRLQFEKADllkridedqddlNELMQKHKDLIAQSAADiGQIQELQLQLEEAKKEKhklQEQL 1944
Cdd:pfam15921 688 EEME-TTTNK-------LKMQLKSAQ------------SELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAK---RGQI 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1945 QVAQMRIEYLEQSTVDraivsrqeavicdlENKTefqkvqiKRFevlvirLRDSLIKMGEELSQAATSESQ---QRESSQ 2021
Cdd:pfam15921 744 DALQSKIQFLEEAMTN--------------ANKE-------KHF------LKEEKNKLSQELSTVATEKNKmagELEVLR 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2022 YYQRRLEELKADMEELVQREAEASRRCMELEKYvEELAAVRQTLQTDLETS------IRRIADLQAALEEVASSDSDTES 2095
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKelqgpgYTSNSSMKPRLLQPASFTRTHSN 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2096 VQTAVDCGSSGRKEMDNVSILSSQPEGSLQSWLSCTLSL-----ATDTMRTPSRQSATSSRILSPRINEEAgdterTQSA 2170
Cdd:pfam15921 876 VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCI-----IESS 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2171 LALSRARSTNVHSKTSGDKpVSPHFVRRQKYCHFGDGEVLAVQRKSTERLEPASSPLASRSTNTSPlsrEKLPSPSaALS 2250
Cdd:pfam15921 951 LRSDICHSSSNSLQTEGSK-SSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSP---KKSPVHS-LLT 1025
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1034629690 2251 EFVEGLRRKRAQRGQGSTL----GLEDWPTLPIyQTTGAS 2286
Cdd:pfam15921 1026 SSAEGSIGSSSQYRSAKTIhspdSVKDSQSLPI-ETTGKT 1064
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1539-2085 |
2.16e-09 |
|
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: 63.45 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1539 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdLEDTCVLLENQ--QSRNHELEKKQKKFDLQLAQAL 1616
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKlnEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1617 GESVFEKglrEKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspSLGENCVAGLKERLWKLESSA 1696
Cdd:pfam02463 258 QEIEKEE---EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1697 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRLHQLEMQLEQEYEEKQMV--L 1771
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAAKLKEEELELKSEEEKEAqlL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1772 HEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKT-SVSKEELEKVHSQLEQSEAKCEEAL 1850
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1851 KTQKVLTAD-LESMHSELENMtrNKSLVDEQLYRLQFEKADLLKRIDE-DQDDLNELMQKHKDLIAQSAADIGQIQELQL 1928
Cdd:pfam02463 491 SRQKLEERSqKESKARSGLKV--LLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1929 QLEEAKKEKHKLQEQLQVAQMRIeyleqstVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ 2008
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL-------KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 2009 AATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1410-2096 |
2.20e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 63.32 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1410 ELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADErfKGDVACQVLESERAE-RLQAFRE--VQELKSKHEQ--- 1483
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAA--DAAVAKDRSELEALEdQHGAFLDadIETAAADQEQlps 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1484 VQKKLGDVNKQ---LEEAQQKIQ-------LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELtaRKELE 1553
Cdd:pfam12128 352 WQSELENLEERlkaLTGKHQDVTakynrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1554 QKLGELQSAYDGAKKMAHQLKRKCHHLTCDlEDTCVLLENQQSRNHELEKKQKK-----FDLQLAQALGESVFEKGLrEK 1628
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAanaevERLQSELRQARKRRDQAS-EA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1629 VTQENTSVRWELGQLQQQLKQKEQEASQL----KQQVEMLQDH-----KRELLG----SPSLGENCVAG----------- 1684
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSigkviSPELLHrtdlDPEVWDGSVGGelnlygvkldl 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1685 --------------LKERLWKLESSALEQQKIQSQQEntiKQLEQLRQRFE---LEIERMKQMHQKDREDQeEELEDVRQ 1747
Cdd:pfam12128 588 kridvpewaaseeeLRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFARTALKNARLDL-RRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1748 SCQKRLHQlemqleQEYEEKQMVLHEKQDLEGLIGTLcdQIGHRDFDVEKRlRRDLRRTHALLSDVQLLLGTMEDGKTSV 1827
Cdd:pfam12128 664 SEKDKKNK------ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1828 sKEELEKVHSQLEQSEAKCEEALKT---------QKV--LTADLESMHSELENMTRNKSLVDE--QLYRLQF--EKADLL 1892
Cdd:pfam12128 735 -KAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERIAVRRQEVLRyfDWYQETWlqRRPRLA 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1893 KRIDEDQDDLNELMQkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL----EQSTVDRAIVSRQE 1968
Cdd:pfam12128 814 TQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGSIGE 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1969 AVIC--DLENKTEFQKVQIKRFevlvIRLRDSLI--KMGEELsqAATSESqQRESSQYYQRRLEELKADMEELVQREAEA 2044
Cdd:pfam12128 891 RLAQleDLKLKRDYLSESVKKY----VEHFKNVIadHSGSGL--AETWES-LREEDHYQNDKGIRLLDYRKLVPYLEQWF 963
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 2045 SRRCMELEKYVEELAAVRQTLQTD----LETSIRRIADLQAALEEVASSDSDTESV 2096
Cdd:pfam12128 964 DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1402-2068 |
2.63e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEE--ELTTLRRKLEKSEKlRNELRQNTDLLESKiADLTSDLADERFKGDVACQVLESERAERLQAFREVQEL-K 1478
Cdd:PTZ00121 1293 DEAKKAEEkkKADEAKKKAEEAKK-ADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1479 SKHEQVQKKLGDVNKQLEEAQQKIQL-NDLERNPTGGDEWQMRfDCAQMENEFLRKRLQqcEERLDSELTARKELEQKLG 1557
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKADELKKA-AAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1558 ELQSAYDGAKKmAHQLKRKCHhltcdledtcvllenQQSRNHELEKK-QKKFDLQLAQALGESVFEKGLREKVTQENTSV 1636
Cdd:PTZ00121 1448 EAKKKAEEAKK-AEEAKKKAE---------------EAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1637 RWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGEncvaglKERLWKLES--SALEQQKIQSQQENTIKQLE 1714
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKK------AEELKKAEEkkKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1715 QLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhqlEMQLEQEYEEKQMVLHEKQDLEGligtlcdqighrdfd 1794
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAE--------------- 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1795 vEKRLRRDLRRthallsdvqlllgtmEDGKTSVSKEELEKvhsQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNk 1874
Cdd:PTZ00121 1645 -EKKKAEELKK---------------AEEENKIKAAEEAK---KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA- 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1875 slvdEQLYRLQFE---KADLLKRIDEDQDDLNELMQKhkdliaQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQmRI 1951
Cdd:PTZ00121 1705 ----EELKKKEAEekkKAEELKKAEEENKIKAEEAKK------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE-EI 1773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1952 EYLEQSTVDRAIVSRQEAVICDLENKTefqKVQIKRFEVLV-------IRLRDSLIKMGEELSQAATSESQQRESSQYYQ 2024
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVDKKI---KDIFDNFANIIeggkegnLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034629690 2025 RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2068
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1405-1871 |
4.41e-09 |
|
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: 62.11 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1405 RAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDladerfKGDVACQVLESERAERLqAFREVQELKSKHEQV 1484
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1485 QKKLG---------DVNKQLEEAQqkiqlndLERnptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSE-------LTA 1548
Cdd:pfam01576 705 EDELQatedaklrlEVNMQALKAQ-------FER------DLQARDEQGEEKRRQLVKQVRELEAELEDErkqraqaVAA 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1549 RKELEQKLGELQSAYDGA-----------KKMAHQLKrkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1617
Cdd:pfam01576 772 KKKLELDLKELEAQIDAAnkgreeavkqlKKLQAQMK----DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1618 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgencvagLKERLWKLESSAL 1697
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-------LNDRLRKSTLQVE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1698 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQkdredqeeELEDVRQSCQK--------RLHQLEMQLEQEYEEKQM 1769
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLQ--------EMEGTVKSKFKssiaaleaKIAQLEEQLEQESRERQA 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1770 VlhekqdlegligtlcdqighrdfdvekrlRRDLRRTHALLSDVqLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1849
Cdd:pfam01576 993 A-----------------------------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
490 500
....*....|....*....|..
gi 1034629690 1850 LKTQKVLTADLESMHSELENMT 1871
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDAT 1064
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1402-2079 |
5.19e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 5.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEEAQQKiqLNDLERnptggdewqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ------- 1554
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEE--YDRVEK----------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhg 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1555 ---KLGELQSAYDGAKKMAhqLKRKCHHLTCDLEDTCV-----LLENQQSRNHEL---EKKQKKFDLQLAQALGESVFEK 1623
Cdd:TIGR02169 526 tvaQLGSVGERYATAIEVA--AGNRLNNVVVEDDAVAKeaielLKRRKAGRATFLplnKMRDERRDLSILSEDGVIGFAV 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1624 GLREKVTQENTSVRWELGQLQQqlkqkeqeasqlkqqVEMLqDHKRELLGspslgencvaglKERLWKLESSALEQQKIQ 1703
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLV---------------VEDI-EAARRLMG------------KYRMVTLEGELFEKSGAM 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1704 SQQENTIKQLEQLRQRFELEIERMKqmhqkdreDQEEELEDVRQSCQKRLHQLEMQLEQeyeekqmVLHEKQDLEGLIGT 1783
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLR--------ERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1784 LCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGKTSV--SKEELEKVHSQLEQSEAKCEEALktqkvltADLE 1861
Cdd:TIGR02169 721 IEKEI--------EQLEQEEEKLKERLEELEEDLSSLEQEIENVksELKELEARIEELEEDLHKLEEAL-------NDLE 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1862 SM--HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHK 1939
Cdd:TIGR02169 786 ARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1940 LQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ------AATS 2012
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgEDEE 945
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 2013 ESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADL 2079
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1883-2085 |
6.07e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1883 RLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdra 1962
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1963 ivsrqeavicDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREA 2042
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034629690 2043 EASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1682-2188 |
1.24e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 60.90 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1682 VAGLKERLwkLESSAL-EQQKIQSQQenTIKQLEQLRQRFELEIERMKQMHQKDREDQEeeleDVRQSCQKRLHQLEmql 1760
Cdd:pfam15921 87 VKDLQRRL--NESNELhEKQKFYLRQ--SVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQNTVHELE--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1761 eqeyEEKQMvlheKQDLEGLIGTLCDQighrdfdvekrLRRDLRRTHALLSDVQLLLGTMEDGKTsvskeelEKVHSQLE 1840
Cdd:pfam15921 156 ----AAKCL----KEDMLEDSNTQIEQ-----------LRKMMLSHEGVLQEIRSILVDFEEASG-------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1841 QSeakceealktqkvlTADLESMHSELENMTRNkslVDEQLYRLQ---FEKADLLKRI-DEDQDDLNELMQKHKDLIAQ- 1915
Cdd:pfam15921 210 MS--------------TMHFRSLGSAISKILRE---LDTEISYLKgriFPVEDQLEALkSESQNKIELLLQQHQDRIEQl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1916 -SAADIgQIQELQLQLEEAKKEKHKLQEQLQVAQmrieylEQSTVDRAIVSRQeavICDLEN-----KTEFQKVQiKRFE 1989
Cdd:pfam15921 273 iSEHEV-EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQ---LSDLEStvsqlRSELREAK-RMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1990 VLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEelvQREAEASrrcmeLEKYVEELAAVRQT----- 2064
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELS-----LEKEQNKRLWDRDTgnsit 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2065 ---LQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSgrKEMDNVSILSSQPEGSLQSWLSCTLSLATDTMRT 2141
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 2142 PSRQSATSSriLSPRINEEAGDTERTQSALALSRAR-----STNVHSKTSGD 2188
Cdd:pfam15921 492 ESSERTVSD--LTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGD 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1829-2085 |
1.87e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1908
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1909 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKR- 1987
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1988 FEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQT 2067
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|....*...
gi 1034629690 2068 DLETSIRRIADLQAALEE 2085
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1403-1950 |
3.30e-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: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSdladerfKGDVACQVLESERAErLQafREVQELKSKHE 1482
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE-------KKDHLTKELEDIKMS-LQ--RSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1483 QVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMEnEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1562
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1563 ydgaKKMAHQLKRKCHHLTCDL-EDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGESVFEkgLREKVTQENTSVRWel 1640
Cdd:pfam05483 397 ----TKFKNNKEVELEELKKILaEDEKLLDEKKQFEKIAEELKGKEQELIfLLQAREKEIHD--LEIQLTAIKTSEEH-- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1641 gqlqqqlkqkeqeasQLKQQVEMLQDHKRELLGSPSLGENCvaglkeRLWKLESSALEQQ------KIQSQQENTIKQLE 1714
Cdd:pfam05483 469 ---------------YLKEVEDLKTELEKEKLKNIELTAHC------DKLLLENKELTQEasdmtlELKKHQEDIINCKK 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1715 QlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFD 1794
Cdd:pfam05483 528 Q-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1795 VEKRLR--RDLRRTHALLSDVqlllGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTADLESMHSELENMT 1871
Cdd:pfam05483 603 IENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEEKLLEEVE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1872 RNKSLVDEQLyRLQFEkadLLKRIDEDQDDLNELMQKHK---DLIA----------------QSAADIGQIQEL------ 1926
Cdd:pfam05483 679 KAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAALEIELsnikae 754
|
570 580 590
....*....|....*....|....*....|
gi 1034629690 1927 ------QLQLEEAKKEKHKLQEQLQVAQMR 1950
Cdd:pfam05483 755 llslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1796-2086 |
1.17e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1796 EKRLRRDLRRTHALlsdvqlllgtmedGKTSVSK-EELEKVHSQLEQSEAKCEEALKTQKVLTADLE---SMHSELENMT 1871
Cdd:COG4913 591 EKDDRRRIRSRYVL-------------GFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQerrEALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1872 RNKSLVDEQLYRLQfEKADLLKRIDEDQDDLNELMQKHKDLIAQsaadigqIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1951
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1952 EYLeQSTVDRAIVSRQEAVICDLENKteFQKVQI-KRFEVLVIRLRDSLIKMGEELSQAATS-ESQQR------------ 2017
Cdd:COG4913 730 DEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEElERAMRafnrewpaetad 806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 2018 -----ESSQYYQRRLEELKADmeELVQREAEASRRCMELEKyvEELAAVRQTLQTDLETSIRRIADLQAALEEV 2086
Cdd:COG4913 807 ldadlESLPEYLALLDRLEED--GLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1402-1908 |
1.28e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.34 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSD---LADERFKGDVACQVLESERAERLQafrEVQELK 1478
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQ---EIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1479 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaQMENEFlrKRLQQCEERLDSELtarKELEQKLGE 1558
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------LLEKEI--ERLKETIIKNNSEI---KDLTNQDSV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1559 LQSAYDGAKKMAHQLKRKchhltcdLEDtcvlLENQ-QSRNHELEKKQKKFDLQlaqalgesvfekglrekvtqentsvr 1637
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQ-------LKV----LSRSiNKIKQNLEQKQKELKSK-------------------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1638 welgqlqqqlkqkeqeasqlKQQVEMLQDHKRELlgspslgENCVAGLKErlwKLESSALEQQKIqsqqENTIKQLEQLR 1717
Cdd:TIGR04523 495 --------------------EKELKKLNEEKKEL-------EEKVKDLTK---KISSLKEKIEKL----ESEKKEKESKI 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1718 QRFELEIERMKQMHQKdredqeEELEDVRQSCQKRLHQLEMQ---LEQEYEEKQMVLHEKQDlegLIGTLCDQIGHRDFD 1794
Cdd:TIGR04523 541 SDLEDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEK---EKKDLIKEIEEKEKK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1795 VEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE------------- 1861
Cdd:TIGR04523 612 ISS-LEKELEKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiielmkdwlkel 689
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034629690 1862 SMHSE--LENMTRNKSLvdEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1908
Cdd:TIGR04523 690 SLHYKkyITRMIRIKDL--PKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1711-2090 |
1.57e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1711 KQLEQLRqRFELEIE-RMKQMHQKDREDQE--EELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEK---QDLEGLIGTL 1784
Cdd:pfam05483 85 KEAEKIK-KWKVSIEaELKQKENKLQENRKiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1785 CDQIGHRDFDVEKRlRRDLRRTHA-LLSDVQLLLGTMEDGKTSVSKEELEkVHSQLEQSEAKCEEALktqkvltadlESM 1863
Cdd:pfam05483 164 CARSAEKTKKYEYE-REETRQVYMdLNNNIEKMILAFEELRVQAENARLE-MHFKLKEDHEKIQHLE----------EEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1864 HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK-------DLIAQSAADIGQIQELQLQLEEAKKE 1936
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1937 KHKLQEQLQVAQMRIEYL--------EQSTVDRA----IVSRQEAVICDLEnktEFQKVQIKRFEvlviRLRDSLIKMGE 2004
Cdd:pfam05483 312 QKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLE---ELLRTEQQRLE----KNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2005 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALE 2084
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
....*.
gi 1034629690 2085 EVASSD 2090
Cdd:pfam05483 461 AIKTSE 466
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1386-2059 |
1.64e-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: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1386 QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKlrnelRQNTDLLESKIADLTSDLADerfkgdvacqVLESERA 1465
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKSLQNEKAD----------LDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1466 ErlqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNdlernptggdEWQMRFDCAQMENEFLRKRlqQCEERLDSE 1545
Cdd:TIGR00606 520 L-----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI----------KSRHSDELTSLLGYFPNKK--QLEDWLHSK 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1546 LTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE-------DTCVlLENQQSRNHELEKKQKKFDLQLAQALGE 1618
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfDVCG-SQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1619 SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESSALE 1698
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAPG 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1699 QQKIQSQQENTIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDVR------QSCQKRLHQLEMQLEQEYEEKQMVLH 1772
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKN----DIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1773 EKQDLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVskEELEKVHSQLEQSEAKCEEALKT 1852
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQR 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1853 QKVLTADLESMHSELENM------TRNKSLVDEQ-LYRLQFEKADLLKRIDED----QDDLNELMQKHKDLIAQSAADIG 1921
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLireikdAKEQDSPLETfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIEN 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1922 QIQE---------------LQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTV---DRAIVSRQEAVICDLENKTEFQKV 1983
Cdd:TIGR00606 963 KIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKQHLK 1042
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1984 QIKRFEVLviRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELA 2059
Cdd:TIGR00606 1043 EMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1827-2086 |
2.61e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1827 VSKEELEKVHSQLEQSEaKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL- 1905
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1906 --MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraivsrqeavICDLENKTEFQKv 1983
Cdd:PRK03918 221 eeLEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-------------IEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1984 QIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL---KADMEELVQREAEASRRCMELEKYVEELAA 2060
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270
....*....|....*....|....*....|.
gi 1034629690 2061 VRQtLQTDLET-----SIRRIADLQAALEEV 2086
Cdd:PRK03918 367 AKA-KKEELERlkkrlTGLTPEKLEKELEEL 396
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1702-2083 |
2.98e-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: 55.67 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1702 IQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQEEELEDVRQSCQkRLHQLEMQLEQEYEEKQMVLHEKQDLE 1778
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1779 GLIGTLCDQIGHRDFDVEKRLRRdlrrthaLLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVL 1856
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELErmKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1857 TADLESMHSELENMTRNKSLVDEQLYRLQfekadllkridedqDDLNELMQKhkdliaqsaadIGQIQELQLQLEEAKKE 1936
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQ--------------DTITTLTQK-----------LTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1937 KHKLQEQLQVAQMRIEYLEQSTvdRAIVSRQEAVICDLeNKTEFQKVQikrfevLVIRLRDSLIKMGEELSQAATSESQQ 2016
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2017 RESSQYYQRRLEELKAD---MEELVQREAeasrrcMELEKYVEELAAVRQTLQTDLETSIRRIADLQAAL 2083
Cdd:pfam07888 310 QQSAEADKDRIEKLSAElqrLEERLQEER------MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1682-2171 |
3.64e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1682 VAGLKERLWKLESSaLEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLE 1761
Cdd:pfam15921 233 ISYLKGRIFPVEDQ-LEALKSESQN-----KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1762 QEYEEKQMVLHEKQDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLSDvqlllgtmedgktsvSKEELEK--VHSQL 1839
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---------------SQLRSELREAKRMYED---------------KIEELEKqlVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1840 EQSEAKCEEALKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQFEKA------DLLKRideDQDDLNELMQKHKD 1911
Cdd:pfam15921 357 ELTEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1912 LIA------------QSAADIG------QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAvicd 1973
Cdd:pfam15921 434 LLKamksecqgqmerQMAAIQGknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEK---- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1974 lENKTEFQKVQIKRFEVLV-IRLRD--SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADME--------------- 2035
Cdd:pfam15921 509 -ERAIEATNAEITKLRSRVdLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtaga 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2036 ---ELVQREAEASRRCMELEKYveelaavrQTLQTDLETSIR----RIADLQaaLEEVASSDSDTESVQTAVDCgssgRK 2108
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRVSDLE--LEKVKLVNAGSERLRAVKDI----KQ 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629690 2109 EMDNVSILSSQPEGSLQSwLSCTLSLATDTMRTPSRQSATSSRILSPRINEEAGDTERTQSAL 2171
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1923-2177 |
3.79e-07 |
|
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: 55.42 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1923 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIV----------SRQEAVICDLEN-KTEFQKVQiKRFEVL 1991
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1992 VIRlRDSLIKMGEElsqaATSESQQREssqyyqRRLEELKAD----MEEL-----VQREAEASRRC-------------- 2048
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGaalareqdklnwek 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2049 ------MELEKYVEELAAVRQtLQTDLETSIRRIADLQA--------ALEEVASSDSDTE----SVQTAVDcgsSGRKEM 2110
Cdd:pfam05701 227 elkqaeEELQRLNQQLLSAKD-LKSKLETASALLLDLKAelaaymesKLKEEADGEGNEKktstSIQAALA---SAKKEL 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629690 2111 DNV--SILSSQPE--------GSLQSWLSCTLS-LATdtmrtpSRQSATSSRILSPRINEEagdTERTQSALALSRAR 2177
Cdd:pfam05701 303 EEVkaNIEKAKDEvnclrvaaASLRSELEKEKAeLAS------LRQREGMASIAVSSLEAE---LNRTKSEIALVQAK 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1830-2099 |
3.94e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1830 EELEKvhsQLEQSEAKCEEALKTQKvLTADLEsmhselenmtrnksLVDEQLYRLQFEKADllKRIDEDQDDLNELMQKH 1909
Cdd:COG1196 196 GELER---QLEPLERQAEKAERYRE-LKEELK--------------ELEAELLLLKLRELE--AELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1910 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlenktefqkvQIKRFE 1989
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------------------------DIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1990 VLVIRLRDSLIKMGEELSQAATSESQQREssqyyqrRLEELKADMEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDL 2069
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270
....*....|....*....|....*....|
gi 1034629690 2070 ETSIRRIADLQAALEEVASSDSDTESVQTA 2099
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1899-2087 |
4.70e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1899 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAIVSRQEAvicdLEN 1976
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1977 KTEFQKVQIKRFEVLvirlrdSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVE 2056
Cdd:COG3883 91 RARALYRSGGSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|.
gi 1034629690 2057 ELAAVRQTLQTDLETSIRRIADLQAALEEVA 2087
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1847-2082 |
7.41e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1847 EEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAqsaadigQIQEL 1926
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1927 QLQLEEAKKEkhkLQEQLQVAQM--RIEYLE----QSTVDRAIVSRQ--EAVICDLENKTEFQKVQIKRfevlVIRLRDS 1998
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRlgRQPPLAlllsPEDFLDAVRRLQylKYLAPARREQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1999 LIKMGEELSQAATSESQQRessqyyqRRLEELKADMEELVqreAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2078
Cdd:COG4942 169 LEAERAELEALLAELEEER-------AALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 1034629690 2079 LQAA 2082
Cdd:COG4942 239 AAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1811-2085 |
8.96e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1811 SDVQLLLGTMEDGKtsvsKEELEKVHSQLEQSEAKceEALKTQKVLTADLESMHSELENMTRNKSLVDEQLyrlqfEKAD 1890
Cdd:PRK02224 172 SDARLGVERVLSDQ----RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-----DEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1891 L-LKRIDEDQDDLNELMQkhkdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLE--------QSTVDR 1961
Cdd:PRK02224 241 EvLEEHEERREELETLEA--------------EIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1962 AIVSRQEAVICDLENKTEF-------QKVQIKRFEVLVIRLRDSLIKMGEEL----SQAATSESQ---QRESSQYYQRRL 2027
Cdd:PRK02224 307 ADAEAVEARREELEDRDEElrdrleeCRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESEleeAREAVEDRREEI 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629690 2028 EELKADMEELVQREAEASRRCMELEKYVEELAAVRQ-------TLQTDLETSIRRIADLQAALEE 2085
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereaELEATLRTARERVEEAEALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1868-2097 |
1.02e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1868 ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK--DLIAQSAADIGQIQELQLQLEEAkkekhklQEQLQ 1945
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-------RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1946 VAQMRIEYLEQ---STVDRAIVSRQEAVICDLenKTEFQKVQIKRFEVLViRLRDSLIKMGEELSQAATSESQQRESSqy 2022
Cdd:COG3206 237 EAEARLAALRAqlgSGPDALPELLQSPVIQQL--RAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQLQQEA-- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2023 yQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQT---LQTDLETSIRRIADLQAALEEV-ASSDSDTESVQ 2097
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1464-2114 |
1.76e-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: 53.69 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1464 RAERLQAfrEVQELKSKHEQVQK-KLGDVNKQLEEA-QQKIQ---LNDLE-RNPTGGDEWQMRFDCAQMENEFLRKRLQQ 1537
Cdd:pfam12128 242 EFTKLQQ--EFNTLESAELRLSHlHFGYKSDETLIAsRQEERqetSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1538 CEERLDSeLTARKELEQKLGELQSAYDgaKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKFDLQLAQALg 1617
Cdd:pfam12128 320 DRSELEA-LEDQHGAFLDADIETAAAD--QEQLPSWQSELENLEERLK---ALTGKHQDVTAKYNRRRSKIKEQNNRDI- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1618 eSVFEKGLREkvtQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLES 1694
Cdd:pfam12128 393 -AGIKDKLAK---IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLksrLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1695 SALEQQKIQSQQENTIKQLE-------QLRQRFELEIERMKQMHQKdredqeeeLEDVRQSCQKRLHQLEMQleqeyeeK 1767
Cdd:pfam12128 469 FDERIERAREEQEAANAEVErlqselrQARKRRDQASEALRQASRR--------LEERQSALDELELQLFPQ-------A 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1768 QMVLH----EKQDLEGLIGTLCD--QIGHRDFDVEKrlrrdlrrTHALLSDVQLLLGTMEDGKtSVSKEELEKVHSQLEQ 1841
Cdd:pfam12128 534 GTLLHflrkEAPDWEQSIGKVISpeLLHRTDLDPEV--------WDGSVGGELNLYGVKLDLK-RIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1842 SEAKCEEALKTQKVLTADLESMHSELenmtrNKSLvDEQLYRLQFEKADlLKRIDEDQDDLNELMQKHKDLIAQSAADIG 1921
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQA-----NGEL-EKASREETFARTA-LKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1922 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQST-------------------VDRAIVSRQEAV-----ICDLENK 1977
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywqvvegaldaqlalLKAAIAARRSGAkaelkALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1978 TEFQKVQIKrfEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQR-----------RLEELKADMEEL------VQR 2040
Cdd:pfam12128 758 RDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprlatQLSNIERAISELqqqlarLIA 835
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629690 2041 EAEASRRCMELEKYVEELAAVRQT-LQTDLETSIRRIADLQaaleEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2114
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSeNLRGLRCEMSKLATLK----EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1596-1877 |
1.99e-06 |
|
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: 53.20 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1596 SRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQ--DHKRELlg 1673
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeERKREL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1674 sPSLGENCVAGLKERLWKLESSALEQQ----KIQSQQENTIKQ--LEQLRQR------FELEIERMKQMHQKDR------ 1735
Cdd:pfam17380 363 -ERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVkiLEEERQRkiqqqkVEMEQIRAEQEEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1736 EDQEEELEDVRQSCQKRLHQLEM--QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDv 1813
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 1814 qlllgTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRNKSLV 1877
Cdd:pfam17380 521 -----EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1691-1956 |
2.53e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1691 KLESSALEQQKIQSQQENTIKQLEQLRQR----------FELEIERMKQM--HQKDREDQEE--ELEDVRQSCQKRLHQL 1756
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARieeleedlhkLEEALNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1757 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKE------ 1830
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdelea 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1831 ELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkSLVDEQLYRLQFEKADLLKrIDEDQDDLNELMQKHK 1910
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIR 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034629690 1911 DLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1956
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1402-1835 |
2.86e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLeSKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSKH 1481
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEI-------NGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVN---KQLEEAQQKI-QLNDLERNPTGgdewqMRFDCAQMENEFLRKRLQQCEERLdSELTARK-ELEQKL 1556
Cdd:PRK03918 348 KELEKRLEELEerhELYEEAKAKKeELERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEI-SKITARIgELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1557 GELQSAYDGAKKMahqlKRKC---------HH-------LTCDLED-----------------------TCVLLENQQSR 1597
Cdd:PRK03918 422 KELKKAIEELKKA----KGKCpvcgrelteEHrkelleeYTAELKRiekelkeieekerklrkelreleKVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1598 NH-------ELEKKQKKFDLQLAQALGESvFEKGLRE--KVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1668
Cdd:PRK03918 498 LKelaeqlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1669 RELLgspSLGENCVAGLKERLWKLES------------SALE-----QQKIQSQQENTIKQLEQLRQRFELEIERMKQMH 1731
Cdd:PRK03918 577 KELE---ELGFESVEELEERLKELEPfyneylelkdaeKELEreekeLKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1732 QKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVlheKQDLEGLigtlcdqigHRDFDVEKRLRRDLRRTHALLS 1811
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKL---------KEELEEREKAKKELEKLEKALE 721
|
490 500
....*....|....*....|....
gi 1034629690 1812 DVQLLLGTMEDGKTSVSKEELEKV 1835
Cdd:PRK03918 722 RVEELREKVKKYKALLKERALSKV 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1685-2091 |
5.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1685 LKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQE-EELEDVRQSCQKRLHQLEMQL 1760
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1761 eQEYEEKQmvlHEKQDLEGLIGTLCDQI----GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDgktsvSKEELEKVH 1836
Cdd:COG4717 156 -EELRELE---EELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1837 SQLEQSEAKCEEALKTQK---------------------------------VLTADLESMHSELENMTRNKSLVDEQLYR 1883
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1884 LQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmrIEYLEQstvdrai 1963
Cdd:COG4717 307 LQ----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQ------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1964 vsrqeavicdlENKTEFQKVQIKrfevlvirLRDSLIKMGEELSQAAtsesQQRESSQYYQRRLEELKADMEELVQREAE 2043
Cdd:COG4717 371 -----------EIAALLAEAGVE--------DEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1034629690 2044 AsrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2091
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1388-1759 |
6.90e-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: 51.66 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1388 LGSLQPLLSATigTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAER 1467
Cdd:pfam15921 463 VSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1468 lqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERL--DSE 1545
Cdd:pfam15921 541 ----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1546 LTARKELEQKLGELQ--------------SAYDGAKKMAHQLKRKCHHLTCDL----EDTCVLLENQQSRNHELEKKQKK 1607
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1608 FDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGENcvaglKE 1687
Cdd:pfam15921 697 LKMQLKSAQSE-------LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNAN-----KE 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1688 R-LWKLESSALEQQ--KIQSQQENTIKQLEQLR---QRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKRL 1753
Cdd:pfam15921 764 KhFLKEEKNKLSQElsTVATEKNKMAGELEVLRsqeRRLKEKVANMEvaldkaslQFAECQDIIQRQEQESVRLKLQHTL 843
|
....*.
gi 1034629690 1754 HQLEMQ 1759
Cdd:pfam15921 844 DVKELQ 849
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1473-1961 |
7.12e-06 |
|
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: 51.39 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1473 EVQELKSK-HEQVQKKLGDVNKQLEEAQQkiqLNDlernptggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKE 1551
Cdd:pfam06160 46 KFEEWRKKwDDIVTKSLPDIEELLFEAEE---LND-----------KYRFKKAKKALDEIEELLDDIEEDIKQILEELDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1552 LEQKLGELQSAYDGAKKMAHQLKRKchhltcdledtcvLLENqqsrNHELEKKQKKFDLQLAQAlgESVFEKglrekVTQ 1631
Cdd:pfam06160 112 LLESEEKNREEVEELKDKYRELRKT-------------LLAN----RFSYGPAIDELEKQLAEI--EEEFSQ-----FEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1632 ENTSvrwelgqlqqqlkQKEQEASQLKQQVEMLQDHKRELLGS-PSLGENCVAGLKERLWKLES--SALEQQKIQSQQEN 1708
Cdd:pfam06160 168 LTES-------------GDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyREMEEEGYALEHLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1709 TIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDvrqscqkRLHQLEMQLEQEYEEKQMVLHEKQDLEgligtlcDQI 1788
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEKNLPEIE-------DYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1789 GHRDfDVEKRLRRDLRRT---------------------HALLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAK 1845
Cdd:pfam06160 301 EHAE-EQNKELKEELERVqqsytlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSelQEELEEILEQLEEIEEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1846 CEEALKTQKVLTAD-------LESMHSELENM-----TRNKSLVDEQlYRLQFEKA-DLLKRIDED-------------- 1898
Cdd:pfam06160 380 QEEFKESLQSLRKDelearekLDEFKLELREIkrlveKSNLPGLPES-YLDYFFDVsDEIEDLADElnevplnmdevnrl 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1899 ----QDDLNELMQKHKDLIaQSAADIGQ-IQ----------ELQLQLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVDR 1961
Cdd:pfam06160 459 ldeaQDDVDTLYEKTEELI-DNATLAEQlIQyanryrssnpEVAEALTEAELlfRNYDYEKALEIAATALEKVEPGAYER 537
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1694-2086 |
8.71e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1694 SSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----HQLEMQLEQ--EYEE 1766
Cdd:PTZ00440 891 RSNSNKQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYD 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1767 KQmvlheKQDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAK 1845
Cdd:PTZ00440 970 KS-----KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKE 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1846 CEEalKTQKVLTAdLESMHSELENMTRNK-------SLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS-- 1916
Cdd:PTZ00440 1040 IEE--KVDQYISL-LEKMKTKLSSFHFNIdikkyknPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdk 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1917 ------------AADIG----QIQELQLQLEEAKKEKHKLQEqlqVAQMRIEYleqstvDRAIVSRQEAVICDLENKTEF 1980
Cdd:PTZ00440 1117 eknkqtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILIDHIVEQINNEAKKSKT 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1981 QKVQIKRFEVLVIRLRDSLIKmgEELSQAATSESQQressqyYQRRLEELKADMEELVQrEAEASRRCMELEKYVEELAA 2060
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSK--ERNDHLTTFEYNA------YYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKE 1258
|
410 420
....*....|....*....|....*.
gi 1034629690 2061 VRQTLQTDLETSIRRIADLQAALEEV 2086
Cdd:PTZ00440 1259 IKLQVFSYLQQVIKENNKMENALHEI 1284
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1702-2027 |
1.31e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1702 IQSQQENTIKQLEQLrqrfeleiERMKQMHQKDrEDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLI 1781
Cdd:PLN02939 102 MQRDEAIAAIDNEQQ--------TNSKDGEQLS-DFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1782 GTLcdqighrdfdvEKRLRRdlrrthallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---SEAKCEEA-------LK 1851
Cdd:PLN02939 173 NIL-----------EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVHSlskeldvLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1852 TQKV-LTADLESMHSELENMT----------RNKSLVDEQLYRLQFE----KADLLK----RID---EDQDDLNELMQKH 1909
Cdd:PLN02939 233 EENMlLKDDIQFLKAELIEVAeteervfkleKERSLLDASLRELESKfivaQEDVSKlsplQYDcwwEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1910 KDLIAQSAADIGQ-------IQELQLQLEEAKKEKHKLqEQLQVAQMRIEYLEqstvdraivSRQEAviCDLENKTefqk 1982
Cdd:PLN02939 313 TNQVEKAALVLDQnqdlrdkVDKLEASLKEANVSKFSS-YKVELLQQKLKLLE---------ERLQA--SDHEIHS---- 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034629690 1983 vQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRL 2027
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1697-2101 |
1.56e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.51 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1697 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE-DQEEELEDVRQSCQKRLH--------QLEM--------- 1758
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAeaeealreQAELnrlkkkyle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1759 ---QLEQEYEEKQMVLHEKQD-LEGLIGTLCDQIGHRDFDVE------KRLRRDLRRTHALLSDVQLLLGTMEdGKTSVS 1828
Cdd:pfam05557 87 alnKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQstnselEELQERLDLLKAKASEAEQLRQNLE-KQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVhSQLE---QSEAKCEEALKTQKVLTADLESMHSELE----------NMTRNKSLVDEQLYRLQFEkadlLKRI 1895
Cdd:pfam05557 166 AEAEQRI-KELEfeiQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRK----LERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1896 DEDQDDLNELMQKHKDLIA--QSAADIGQIQEL-------------QLQLEEA--KKEKHKLQEQLQVAQMRIEYLEQSt 1958
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQelQSWVKLAQDTGLnlrspedlsrrieQLQQREIvlKEENSSLTSSARQLEKARRELEQE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1959 vdraiVSRQEAVICDLENKTEFQKVQIKRFE---VLVIRLRDSLIKMGEELSqaatSESQQRESSQYYQRRLEELkADME 2035
Cdd:pfam05557 320 -----LAQYLKKIEDLNKKLKRHKALVRRLQrrvLLLTKERDGYRAILESYD----KELTMSNYSPQLLERIEEA-EDMT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 2036 ELVQREAEASRrcMELEKYVEELAAVRQTLQTD-LETSIRRiadLQAALEEVASSDSDTESVQTAVD 2101
Cdd:pfam05557 390 QKMQAHNEEME--AQLSVAEEELGGYKQQAQTLeRELQALR---QQESLADPSYSKEEVDSLRRKLE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1402-1762 |
2.12e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKL-EKSEKLRNELRQNT-------DLLESKIADLTSDLadERFkgdvacqVLESERAERLQAFRE 1473
Cdd:PRK04778 129 QELLESEEKNREEVEQLkDLYRELRKSLLANRfsfgpalDELEKQLENLEEEF--SQF-------VELTESGDYVEAREI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1474 VQELKSKHEQVQKKLGDVNKQLEEAQQKI--QLNDLErnpTGGDEWQM---RFDCAQMENEF--LRKRLQQC-------- 1538
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELpdQLQELK---AGYRELVEegyHLDHLDIEKEIqdLKEQIDENlalleeld 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1539 -----------EERLDS-------ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLtcdledtcvllenQQSR--N 1598
Cdd:PRK04778 277 ldeaeekneeiQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV-------------KQSYtlN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1599 HELEKKQKKFDLQLAQAlgESVFEKgLREKVTQENTSvrwelgqlqqqlkqkeqeASQLKQQVEMLQDHkrellgspslg 1678
Cdd:PRK04778 344 ESELESVRQLEKQLESL--EKQYDE-ITERIAEQEIA------------------YSELQEELEEILKQ----------- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1679 encvaglkerlwklessaLEQqkIQSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEELE 1743
Cdd:PRK04778 392 ------------------LEE--IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMFF 451
|
410
....*....|....*....
gi 1034629690 1744 DVrqscQKRLHQLEMQLEQ 1762
Cdd:PRK04778 452 EV----SDEIEALAEELEE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1829-2045 |
2.63e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRnkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1908
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1909 HKDLIAQSAAD--IGQIQELQLQLEEAKK---EKH----KLQEQLQVAQmrieyleqstvdRAIVSRQEAVICDLENKTE 1979
Cdd:COG3206 256 LPELLQSPVIQqlRAQLAELEAELAELSArytPNHpdviALRAQIAALR------------AQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1980 FQKVQIKrfevlviRLRDSLIKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEAS 2045
Cdd:COG3206 324 ALQAREA-------SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1830-2058 |
3.21e-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: 47.72 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1830 EELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKH 1909
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1910 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAI--VSRQEAVICDLENKTEFQKVQIKR 1987
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVELEEELKVVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 1988 FEVlvirlrdslikmgeelsqaATSESQQRESSqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2058
Cdd:pfam00261 160 LEA-------------------SEEKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1401-1568 |
4.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1480
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE-------AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEAQQKIQlndlERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERldsELTAR-KELEQKLGEL 1559
Cdd:COG1340 80 RDELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK---ELVEKiKELEKELEKA 152
|
....*....
gi 1034629690 1560 QSAYDGAKK 1568
Cdd:COG1340 153 KKALEKNEK 161
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1408-2016 |
4.91e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLES---KIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQV 1484
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1485 QKklgdVNKQLEEAQQKIQLNDLERNP-TGGDEWQMRF--DCAQMENEFLRK---------RLQQCEERLDSELTARKEL 1552
Cdd:PRK01156 252 NR----YESEIKTAESDLSMELEKNNYyKELEERHMKIinDPVYKNRNYINDyfkykndieNKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1553 EQKLGELQSAYDGAKKMAHQ---LKRKCHHLTCDLEDTCVLLENQQSRN---HELEKKQKKFDLQLAQALGESVFE---- 1622
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDpdai 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1623 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGE----NCVAGLKERLWKLESSALE 1698
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEeksnHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1699 QQKIQSQQENTIKQLEQLRQRFEL-EIERMKQMHQKdREDQEEELEDVRQScQKRLHQLEMQLEQEYEE-KQMVLhekQD 1776
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNK-IESARADLEDIKIK-INELKDKHDKYEEIKNRyKSLKL---ED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1777 LEGLIGTLCDQIGHRD-FDVEK-RLRRDlrrthallsDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTqk 1854
Cdd:PRK01156 563 LDSKRTSWLNALAVISlIDIETnRSRSN---------EIKKQLNDLESRLQEI-EIGFPDDKSYIDKSIREIENEANN-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1855 vltadLESMHSELENmtrNKSLVDEqlyrLQFEKADLLKRI---DEDQDDLNELMQKhkdlIAQSAADIGQIQElqlQLE 1931
Cdd:PRK01156 631 -----LNNKYNEIQE---NKILIEK----LRGKIDNYKKQIaeiDSIIPDLKEITSR----INDIEDNLKKSRK---ALD 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1932 EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavicdleNKTEFQKVQIKRFEVLVIRLRDSLIKMG------EE 2005
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDI--------------NETLESMKKIKKAIGDLKRLREAFDKSGvpamirKS 757
|
650
....*....|.
gi 1034629690 2006 LSQAATSESQQ 2016
Cdd:PRK01156 758 ASQAMTSLTRK 768
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1858-2091 |
6.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 6.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1858 ADLESMHSELENMTRnkslvdeqlyrlqfeKADLLKRIDEDQDDLNELMQKHKDLiaQSAADIGQIQELQLQLEEAKKEK 1937
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1938 HKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAVICDLENKTEfqkvQIKRFEvlvirlrdslikmgEELSQAATSESQQR 2017
Cdd:COG4913 298 EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGD----RLEQLE--------------REIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629690 2018 ESSQYYQRRLEELK----ADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2091
Cdd:COG4913 359 RRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1746-2085 |
6.23e-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: 48.58 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1746 RQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQlllGTMEDGKT 1825
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR---EQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1826 SvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMtrnkslvDEQLYRLQFEKADLLKRIDEDQDDLNEL 1905
Cdd:pfam05557 81 K--KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA-------ELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1906 MQKHKDLIAQ---SAADIGQIQEL--QLQLEEAKKE--KHKLQEQLQVAQMRIEyLEQSTVDRAIVSRQEAVICDLENKT 1978
Cdd:pfam05557 152 EQLRQNLEKQqssLAEAEQRIKELefEIQSQEQDSEivKNSKSELARIPELEKE-LERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1979 EFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYV 2055
Cdd:pfam05557 231 EDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350
....*....|....*....|....*....|
gi 1034629690 2056 EELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1622-2114 |
8.28e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1622 EKGLREKVTQENTSvRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQK 1701
Cdd:TIGR00618 228 LKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1702 IQSQQENTIKQleqlRQRFELEIERMK-QMHQKDREDQEE----------ELEDVRQSCQKRLHQLEmQLEQEYEEKQMV 1770
Cdd:TIGR00618 307 QQAQRIHTELQ----SKMRSRAKLLMKrAAHVKQQSSIEEqrrllqtlhsQEIHIRDAHEVATSIRE-ISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1771 LHEKQDLEGLIGTLcdQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME-DGKTSVSKEELEKVHSQLEQSEAKCEE- 1848
Cdd:TIGR00618 382 HTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKi 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1849 -------ALKTQKVLTADLESMHselENMTRNKSLVDEQLYRLQFEKADLLKRIDEdqddLNELMQKHKDLIAQSAADIG 1921
Cdd:TIGR00618 460 hlqesaqSLKEREQQLQTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIH----PNPARQDIDNPGPLTRRMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1922 QIQELQLQLEEAKKEKHKLQEQLQVAQmriEYLEQSTvdRAIVSRQEAVICDLENKTEFQKVQIKRFEVL-VIRLRDSLI 2000
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRA---SLKEQMQ--EIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2001 KMGEELSQAATSESQ-----------QRESSQYYQRRLEELKADMEELVQ-REAEASRRCMELEkyvEELAAVRQTLQTD 2068
Cdd:TIGR00618 608 DMLACEQHALLRKLQpeqdlqdvrlhLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLP---KELLASRQLALQK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1034629690 2069 LETSIRRIADLqaaLEEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2114
Cdd:TIGR00618 685 MQSEKEQLTYW---KEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1402-1561 |
9.02e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKH 1481
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----------NGGDRLEQLE--REIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEEAQQKIqlndlernPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1561
Cdd:COG4913 355 EERERRRARLEALLAALGLPL--------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1656-2086 |
1.12e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1656 QLKQQVEMLQDHKREllgspslGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIE-RMKQMHQKD 1734
Cdd:TIGR04523 51 NKEKELKNLDKNLNK-------DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKnDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1735 RE--DQEEELEDVRQSCQK---RLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHAL 1809
Cdd:TIGR04523 124 VElnKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK-IKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1810 LSDVQLLlgtMEDGKTSVSK-EELEKVHSQLEQSEAKceealKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQF 1886
Cdd:TIGR04523 203 LSNLKKK---IQKNKSLESQiSELKKQNNQLKDNIEK-----KQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1887 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ---------- 1956
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkkelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1957 ------STVDRAIVSRQEAVIcDLENKTEFQKVQIKRFEVLVIRLRdSLIKMGEELSQAATSESQQRESS-QYYQRRLEE 2029
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQKDEQIKKLQQEkELLEKEIER 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 2030 LKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2086
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1879-2070 |
1.42e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1879 EQLYRLQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQst 1958
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1959 vdraivsRQEAV-----ICDLENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAATSESQQREssqyyqrRLEELKAD 2033
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEA-------ELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034629690 2034 MEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDLE 2070
Cdd:COG1579 140 LEEK---KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1415-1887 |
1.68e-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: 46.77 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1415 RRKLEKSEKLRNELRQNTDLLESKIADLTSDLAderfkgdvacQVLESERAERLqafrEVQELKSKHEQVQKKLGDVNKQ 1494
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRKTLLANRFS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1495 LEEAQQKI--QLNDLERNPTGGDEW--QMRFDCAQMENEFLRKRLQQCEERLDS--EL--TARKELEQKLGELQSAYDga 1566
Cdd:pfam06160 144 YGPAIDELekQLAEIEEEFSQFEELteSGDYLEAREVLEKLEEETDALEELMEDipPLyeELKTELPDQLEELKEGYR-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1567 kkmahQLKRKCHHLT-CDLEDTCVLLENQQSRNHELEKKqkkfdLQLAQAlgesvfEKGLREkvtqentsvrwelgqlqq 1645
Cdd:pfam06160 222 -----EMEEEGYALEhLNVDKEIQQLEEQLEENLALLEN-----LELDEA------EEALEE------------------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1646 qlkqkeqEASQLKQQVEMLQdhkRELLGSPSLGENcVAGLKERLwklessaleqQKIQSQQENTIKQLEQLRQRFELeie 1725
Cdd:pfam06160 268 -------IEERIDQLYDLLE---KEVDAKKYVEKN-LPEIEDYL----------EHAEEQNKELKEELERVQQSYTL--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1726 rmkqmhqkdredQEEELEDVRQScQKRLHQLE---MQLEQEYEEKQMVLHEKQD-LEGLIGTLcDQI--GHRDFDVE-KR 1798
Cdd:pfam06160 324 ------------NENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSELQEeLEEILEQL-EEIeeEQEEFKESlQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1799 LRRDLRRTHALLSDVQLLLGTMedgKTSVSK------------------EELEKVHSQLEQS-------EAKCEEAlktq 1853
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA---- 462
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034629690 1854 kvlTADLESMHSELENMTRNKSLVdEQL------YRLQFE 1887
Cdd:pfam06160 463 ---QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1691-1941 |
1.74e-04 |
|
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: 46.10 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1691 KLESSALEQQKiqsqQENTIKqlEQLRQRFELEIERMKQMHQKDredqeeeledvrqscQKRLHQLEMQLEQEYEEKQMV 1770
Cdd:pfam09728 71 KLEKLCRELQK----QNKKLK--EESKKLAKEEEEKRKELSEKF---------------QSTLKDIQDKMEEKSEKNNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1771 LHEKQDLEGLIGTLCDQIGHRDFDVEKRLR-RDLrrthallsDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1849
Cdd:pfam09728 130 REENEELREKLKSLIEQYELRELHFEKLLKtKEL--------EVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1850 LKTQKVLTADLeSMHS----ELENmTRNKSLVDEQLYRLQFEK-ADLLKRIDEDqddlNELMQKHKDLIAQSAADIGQ-I 1923
Cdd:pfam09728 202 SETEKELREQL-NLYVekfeEFQD-TLNKSNEVFTTFKKEMEKmSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEeR 275
|
250
....*....|....*...
gi 1034629690 1924 QELQLQLEEAKKEKHKLQ 1941
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLE 293
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1707-2044 |
1.90e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1707 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL----HQ-------LEMQLEQ------------- 1762
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrFSfgpaldeLEKQLENleeefsqfvelte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1763 --EYEEKQMVLHEKQDLEGLIGTLCDQI--------------------GHRD----------FDVEKRLRR---DLRRTH 1807
Cdd:PRK04778 190 sgDYVEAREILDQLEEELAALEQIMEEIpellkelqtelpdqlqelkaGYRElveegyhldhLDIEKEIQDlkeQIDENL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1808 ALLSdvQLLLGTMEDGKTSVSkEELEKVHSQLEQS-EAKcEEALKTQKVLTADLEsmHSElenmTRNKSLVDE-----QL 1881
Cdd:PRK04778 270 ALLE--ELDLDEAEEKNEEIQ-ERIDQLYDILEREvKAR-KYVEKNSDTLPDFLE--HAK----EQNKELKEEidrvkQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1882 YRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQ--VAQMRIEylEQSTV 1959
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSemLQGLRKD--ELEAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1960 DRAIVSRQEavicdLENktefqkvqIKRfevLVIRLR---------DSLIKMGEELSQAATSESQQRESSQYYQRRLEEL 2030
Cdd:PRK04778 418 EKLERYRNK-----LHE--------IKR---YLEKSNlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
410
....*....|....
gi 1034629690 2031 KADMEELvQREAEA 2044
Cdd:PRK04778 482 TEDVETL-EEETEE 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1602-1974 |
1.96e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.87 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1602 EKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgENC 1681
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-KKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1682 VAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQKRLHQLEMQLE 1761
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1762 ---QEYEEKQMVLhEKQDLEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQ 1838
Cdd:COG5185 388 stkESLDEIPQNQ-RGYAQEILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1839 LEQSEAKCEEALKTQK-VLTADLESMHSELENMTRNkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1917
Cdd:COG5185 465 LEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 1918 ADIGQIQELQLQLEEakkekHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDL 1974
Cdd:COG5185 542 ENLIPASELIQASNA-----KTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQ 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1800-2100 |
2.04e-04 |
|
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: 46.66 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1800 RRDLRRTHALLSDVQLLLGTME----------DGKTSVSKEELEKVHSQLEQSEAKCEealKTQKVLTADLESMHSELEn 1869
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrarielEKKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1870 MTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDL-NELMQKHKdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQ 1948
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRR-----------QIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1949 MRIEYLEQstvdraivsrqeaVICDLENKTEFQKVQIKRFEVLVIRLR----DSLI--KMGEELSQAATSESQQR----- 2017
Cdd:pfam05557 146 AKASEAEQ-------------LRQNLEKQQSSLAEAEQRIKELEFEIQsqeqDSEIvkNSKSELARIPELEKELErlreh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2018 ---------------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSiRRIADLQ-- 2080
Cdd:pfam05557 213 nkhlnenienklllkEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqr 291
|
330 340
....*....|....*....|..
gi 1034629690 2081 --AALEEVASSDSDTESVQTAV 2100
Cdd:pfam05557 292 eiVLKEENSSLTSSARQLEKAR 313
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1656-2065 |
2.94e-04 |
|
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: 46.22 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1656 QLKQQVEMLQDHKRELLGspslgENcvAGLKERLWKLES------------SALEQQKIQSQQENTikQLEQLRQRFELE 1723
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQ-----EN--KKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENF--RLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1724 IERMK------QMHQKDREDQEEELE------DVRQSCQKRLHQLEMQLE------QEYEE--KQMVLHEKQDLEGLIGT 1783
Cdd:pfam05622 89 CEELEkevlelQHRNEELTSLAEEAQalkdemDILRESSDKVKKLEATVEtykkklEDLGDlrRQVKLLEERNAEYMQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1784 LcdqighrdfdvekRLRRDLRRTHALLSDVQLLlgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1863
Cdd:pfam05622 169 L-------------QLEEELKKANALRGQLETY------------KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1864 HSELENMTRN----KSLVDE----QLYRLQFEKAD-LLKRIDEDQDDLN-ELM------------QKHKDL-IAQSAADI 1920
Cdd:pfam05622 224 QKEKERLIIErdtlRETNEElrcaQLQQAELSQADaLLSPSSDPGDNLAaEIMpaeireklirlqHENKMLrLGQEGSYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1921 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAIVSRQEAvicdlENKTEFQKVQIKRFEVLVIRLRdsli 2000
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ-----GSKAEDSSLLKQKLEEHLEKLH---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2001 KMGEELS--QAATSESQQRESSQyYQRRLEELkadMEELVQREAEAsrRCME--LEKYVEELAAVRQTL 2065
Cdd:pfam05622 374 EAQSELQkkKEQIEELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAMEerYKKYVEKAKSVIKTL 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1408-1794 |
4.36e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1408 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleseraERLQAFREVQELKSKHEQVQKK 1487
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS---------------DHLNLVQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1488 LGDVNKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDseltarkELEQKLGELQSAYDGAK 1567
Cdd:PRK04863 357 LEELEERLEEQNEVVEE-------------------ADEQQEENEARAEAAEEEVD-------ELKSQLADYQQALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1568 KMAHQ------LKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVTQENTSVRW 1638
Cdd:PRK04863 411 TRAIQyqqavqALERAKQL-CGLPD--LTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1639 ELgqlqqqlkqkeqEASQLKQQ-VEMLQDHKRELLGSPSLGencvaGLKERLWKLESSALEQQkiqsQQENTIKQLEQlR 1717
Cdd:PRK04863 488 EV------------SRSEAWDVaRELLRRLREQRHLAEQLQ-----QLRMRLSELEQRLRQQQ----RAERLLAEFCK-R 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1718 QRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIGH 1790
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDaLA----RLREQSGE 621
|
....
gi 1034629690 1791 RDFD 1794
Cdd:PRK04863 622 EFED 625
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
221-513 |
4.40e-04 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 45.76 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 221 LGDPGQGTVAlkkgeEGQSivgKGLGTPKTTEL-KEAEPQGKDRQGTrpQAQGPGEGVRPGKAEKEGAEPTNtvEKGNVS 299
Cdd:TIGR00927 627 LGDLSKGDVA-----EAEH---TGERTGEEGERpTEAEGENGEESGG--EAEQEGETETKGENESEGEIPAE--RKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 300 KDVGSEGKhvRPQIPGRKWGGFLGRRSKWDGPQNKKDKEGVLLSKAEKTG-EPQTQMEKTSQVQGElGDDLRMGEKAGEL 378
Cdd:TIGR00927 695 GEGEIEAK--EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdEGEGEAEGKHEVETE-GDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 379 RSTTGKAGESWDKKEKMGQPQGKSG--NAGEARSQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGA 456
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGEDGEMKGDEGaeGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629690 457 GAlETELEGPSQPALEKDAERPRIRKENQDGPAPQEEGKGGQSRDSDQAPEDRWYEA 513
Cdd:TIGR00927 851 GV-DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1679-2088 |
5.27e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1679 ENCVAGLKERLWKLE---SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ 1755
Cdd:TIGR00606 244 ENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1756 LEMQLEQEYEEKQMVLHEKQDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRL 1799
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1800 RRDLRRTHALLSDVQ------------------LLLGTMEDGKTSVSKE--ELEKVHSQLEQSEAKCEEALKTQKVLTAD 1859
Cdd:TIGR00606 404 EDEAKTAAQLCADLQskerlkqeqadeirdekkGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1860 LESMhSELENMTRNKSLVDEQLYrLQFEKADLLK---RIDEDQDDLN------------------------ELMQKHKDL 1912
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1913 IAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTeFQKVQIKRFEVL 1991
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1992 VIRLRDSLIKMGEELSQAATsesqqreSSQYYQRRLEELkadmeelvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2071
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-------ATAVYSQFITQL-----------TDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
490
....*....|....*..
gi 1034629690 2072 SIRRIADLQAALEEVAS 2088
Cdd:TIGR00606 703 KLRLAPDKLKSTESELK 719
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1691-1945 |
6.39e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 6.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1691 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIermkqmhqKDREDQEEELEDVRQSCQK----RLhQLEMQLE--QEY 1764
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL--------NLRTSAENDLVGLRKDLDEatlaRV-DLEAKIEslKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1765 EEKQMVLHEKQdleglIGTLCDQIGHRDFDVEKRLRRDLRRTHALlSDVQlllgTMEDGKTSVSKEELEkvhsqlEQSEA 1844
Cdd:pfam00038 133 LAFLKKNHEEE-----VRELQAQVSDTQVNVEMDAARKLDLTSAL-AEIR----AQYEEIAAKNREEAE------EWYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1845 KCEEALKTQKVLTADLESMHSELENMTRnkslvdeQLYRLQFEKADLLKRIDEDQDDLNELMQKHkdliaqsAADIGQIQ 1924
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSLKKQKASLERQLAETEERY-------ELQLADYQ 262
|
250 260
....*....|....*....|..
gi 1034629690 1925 ELQLQLEEAKKE-KHKLQEQLQ 1945
Cdd:pfam00038 263 ELISELEAELQEtRQEMARQLR 284
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1873-2095 |
6.40e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1873 NKSLVDEQlyrlqfekADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQ-IQELQLQLEEAKKEKHKLQEQLQVAQMRI 1951
Cdd:PHA02562 172 NKDKIREL--------NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1952 EYLEQSTVDRAivsrqeAVICDLENKTEFQKVQIKRFevlvirlrDSLIKMGEE----------LSQAATSESQQRESSQ 2021
Cdd:PHA02562 244 LNLVMDIEDPS------AALNKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629690 2022 YYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTES 2095
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1879-2085 |
7.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1879 EQLYRL---QFEKA-DLLKRIdedQ-----DDLNELMQKH-------KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQE 1942
Cdd:COG4913 180 ARLRRRlgiGSEKAlRLLHKT---QsfkpiGDLDDFVREYmleepdtFEAADALVEHFDDLERAHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1943 QLQVAQMRIEYLEQSTVDRAIVSRQEAvicdlenktEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRES--- 2019
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRL---------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREElde 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 2020 --SQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:COG4913 328 leAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1402-1781 |
8.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlleskiadltsdladerfkgdvacqvlESERA-ERLQAFREVQELKSK 1480
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQ------------------------------DYQAAsDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEAQQKIQLNDLERnptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1560
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQ-----EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1561 SA----------YDGAKKMAHQLKRKCHHLTCDLEDtcvlLEnQQSRNHELEKKQKKFDLQLAQALGESV--------FE 1622
Cdd:PRK04863 425 RAkqlcglpdltADNAEDWLEEFQAKEQEATEELLS----LE-QKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1623 KGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLESSALEQ 1699
Cdd:PRK04863 500 ELLRRLREQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1700 QKIQSQQENTIKQLEQLRQRFEleiERMKQMHQKD------REDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQmVLHE 1773
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLA---ARAPAWLAAQdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-LAAR 653
|
....*...
gi 1034629690 1774 KQDLEGLI 1781
Cdd:PRK04863 654 KQALDEEI 661
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1828-1937 |
8.64e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.67 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1828 SKEELEKVHSQ---LEQSEAKCEEALKTQKVLTADLE----SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQD 1900
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 1901 DLNELMQK--------------HKDLIAQSaadigqiQELQLQLEEAKKEK 1937
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1402-1664 |
1.02e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1481
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1561
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1562 AYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELG 1641
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260
....*....|....*....|...
gi 1034629690 1642 QLQQQLKQKEQEASQLKQQVEML 1664
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAAL 307
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1703-1918 |
1.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1703 QSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQMVLhekQDLEGLIG 1782
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAEL---AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1783 TLCDQIGHRDFDVEKRLRRDLRrtHALLSDVQLLLGTmEDGKTSVSK---------------EELEKVHSQLEQSEAKCE 1847
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP-EDFLDAVRRlqylkylaparreqaEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 1848 EALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1918
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1837-2107 |
1.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1837 SQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1916
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1917 AADIGQIQELQLQLEeakkekhklQEQLQVAQMRIEYLEQ-STVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlviRL 1995
Cdd:COG3883 96 YRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA-------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1996 RDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR 2075
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1034629690 2076 IADLQAALEEVASSDSDTESVQTAVDCGSSGR 2107
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1614 |
1.21e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLaderfkgdvacQVLESERAErlqAFREVQELKSKH 1481
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1482 EQVQKKLGDVNKQLEE---AQQKIQLNDLER---NPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1555
Cdd:COG4942 93 AELRAELEAQKEELAEllrALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 1556 LGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ 1614
Cdd:COG4942 173 RAELEALLAELEEERAALEA--------------LKAERQKLLARLEKELAELAAELAE 217
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1461-1778 |
1.22e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1461 ESERAERLQAFREVQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTGG---DEWQMRFDCAQMENEFLRKRLQQ 1537
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGQgglDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1538 CEER---LDSELTARKE---LEQKLGELQSAYDGAKkmahQLKRKCHHLTCDLEDTcvllenqqsrnHELEKKQKKFDLQ 1611
Cdd:pfam02029 82 ALERqkeFDPTIADEKEsvaERKENNEEEENSSWEK----EEKRDSRLGRYKEEET-----------EIREKEYQENKWS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1612 LAQALGESVFEKglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL-GSPSLGENCVAGLK---E 1687
Cdd:pfam02029 147 TEVRQAEEEGEE--EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPeVKSQNGEEEVTKLKvttK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1688 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLHQLEMQLEQEY 1764
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 1034629690 1765 EEKQMVLHE-----KQDLE 1778
Cdd:pfam02029 305 AERKLREEEekrrmKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1575 |
1.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkGDVACQVLESERAER-------------L 1468
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALYRLGRqpplalllspedfL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1469 QAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaqmENEFLRKRLQQCEERLDSELTA 1548
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----------------ELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 1034629690 1549 RK----ELEQKLGELQSAYDGAKKMAHQLKR 1575
Cdd:COG4942 197 RQkllaRLEKELAELAAELAELQQEAEELEA 227
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1700-2097 |
1.27e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1700 QKIQSQQENTIKQlEQLRQRFELEIERmKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEG 1779
Cdd:PTZ00440 546 KYYLQSIETLIKD-EKLKRSMKNDIKN-KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQE 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1780 LIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLGTMEDGKTSV----SKEELEKVHSQLEQSEAKCEEalKTQKV 1855
Cdd:PTZ00440 624 KVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLEF--MKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1856 LTADLESMHSELENM-TRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKdliaqsaADIGQIQELQLQLEEAK 1934
Cdd:PTZ00440 686 IDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1935 KE--------KHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQeAVICDlENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL 2006
Cdd:PTZ00440 759 NEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND-INILK-ENKKNNQD-LLNSYNILIQKLEAHTEKNDEEL 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2007 SQaatsesqqreSSQYYQRRLEELKADmeelvqreaeasrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2086
Cdd:PTZ00440 836 KQ----------LLQKFPTEDENLNLK----------------ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAI 889
|
410
....*....|.
gi 1034629690 2087 ASSDSDTESVQ 2097
Cdd:PTZ00440 890 NRSNSNKQLVE 900
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1884-2101 |
1.40e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1884 LQFEKADLLKRIDEDQDDLnelmqkHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmRIEYLEQStvdrai 1963
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1964 VSRQEAVICDLENKTEFQKVQIKRFEVLvirlrdslikmgEELSQAatsesqqRESSQYYQRRLEELKADMEELVQREAE 2043
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY------------QELEAL-------EAELAELPERLEELEERLEELRELEEE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 2044 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA-DLQAALEEVASSDSDTESVQTAVD 2101
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELE 223
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1706-2085 |
1.42e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1706 QENTIKQLEQLRQRFElEIERMkqmhqkdreDQEEELEDVRQscqkrLHqLEMQLEQEYEEKqmvlheKQDLEGLIGTLC 1785
Cdd:PRK04778 24 RKRNYKRIDELEERKQ-ELENL---------PVNDELEKVKK-----LN-LTGQSEEKFEEW------RQKWDEIVTNSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1786 DQIGHRDFDVEKRLRR-DLRRTHALLSDVQLLLGTMEDGKTSVSKE-----ELEKVHSQL-EQSEAKCEEALKT------ 1852
Cdd:PRK04778 82 PDIEEQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEElqellESEEKNREEvEQLKDLYRELRKSllanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1853 -----QKVLTADLESMHSELENMTRNKSLVDEQlyrlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI-GQIQEL 1926
Cdd:PRK04778 162 sfgpaLDELEKQLENLEEEFSQFVELTESGDYV------EAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1927 QL---QLEEAK---------KEKHKLQEQLQVAQMRIEYLEqstVDRAivsrqEAVICDLENKTE-----FQK-VQIKRF 1988
Cdd:PRK04778 236 KAgyrELVEEGyhldhldieKEIQDLKEQIDENLALLEELD---LDEA-----EEKNEEIQERIDqlydiLEReVKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1989 -EVLVIRLRDSLIKMGEELSQ--AATSESQQR--------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEkyvEE 2057
Cdd:PRK04778 308 vEKNSDTLPDFLEHAKEQNKElkEEIDRVKQSytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ---EE 384
|
410 420
....*....|....*....|....*...
gi 1034629690 2058 LAAVRQTLqTDLETSIRRIADLQAALEE 2085
Cdd:PRK04778 385 LEEILKQL-EEIEKEQEKLSEMLQGLRK 411
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1401-1729 |
1.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLEskiadltsdladerfkgdvacqvlesERAERLQAFREVQELKSK 1480
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEaqqkiqlndLERNPTGGDEwqmrfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGELQ 1560
Cdd:COG4913 663 VASAEREIAELEAELER---------LDASSDDLAA--------------LEEQLEELEAELE-------ELEEELDELK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1561 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEkkqkkFDLQLAQALGESVfEKGLREKVTQENTSVRwel 1640
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEA----AEDLARLELRAL-----LEERFAAALGDAV-ERELRENLEERIDALR--- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1641 gqlqqqlkqkeQEASQLKQQVE-MLQDHKRE-----LLGSPSLGENcvAGLKERLWKLESSAL---EQQKIQSQQENTIK 1711
Cdd:COG4913 780 -----------ARLNRAEEELErAMRAFNREwpaetADLDADLESL--PEYLALLDRLEEDGLpeyEERFKELLNENSIE 846
|
330
....*....|....*...
gi 1034629690 1712 QLEQLRQRFELEIERMKQ 1729
Cdd:COG4913 847 FVADLLSKLRRAIREIKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1580 |
1.49e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1378 AVKDWPWWQLLGSLQplLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNtDLLESKIADLTSDLADErfkgdvac 1457
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1458 qvlESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggdewqmrfdcAQMENefLRKRLQQ 1537
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---------------EELEE--LEEELEE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034629690 1538 CEERLDSELTARKELEQKLGELQS--AYDGAKKMAHQLKRKCHHL 1580
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1830-2081 |
1.53e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1830 EELEKVHSQLEQSEAKCEEAlktqkvltadlesmHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQ---------- 1899
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1900 ---DDLNELMQKhKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAI--VSRQEA--V 1970
Cdd:PRK04863 421 qalERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAgeVSRSEAwdV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1971 ICDLENKTEFQKVQIKRFEVLVIRLRDslikMGEELSQAATSESQQRESSQYYQRRLEElkADMEELVQREAEASRRcmE 2050
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE--S 569
|
250 260 270
....*....|....*....|....*....|.
gi 1034629690 2051 LEKYVEELAAVRQTLQTDLETSIRRIADLQA 2081
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1602-1952 |
1.54e-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: 43.51 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1602 EKKQKKFDLQLAQALGESVfEKGLR---EKVT----------QENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1668
Cdd:pfam15742 14 EVQQLRQNLQRLQILCTSA-EKELRyerGKNLdlkqhnsllqEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1669 REllgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQS 1748
Cdd:pfam15742 93 RE---------------------LELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1749 CQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLsdvqlllgTMEDGKTSVS 1828
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNEL--------QQQVRSLQDKEAQL--------EMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtrnkslvdeqlyRLQFEKADLLKRIDEDQDDLNELMQK 1908
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKE--------------ALQEELQQVLKQLDVHVRKYNEKHHH 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034629690 1909 HKdliaqsaADIGQIQELQLQLEEAKKEKHK-LQEQLQVAQMRIE 1952
Cdd:pfam15742 282 HK-------AKLRRAKDRLVHEVEQRDERIKqLENEIGILQQQSE 319
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
324-506 |
1.56e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 324 RRSKWDGPQNKKDKEGVLLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEKAGElrsttGKAGESWDKKEKMGQPQGKSG 403
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEER-----GQGGPSGSGSESVGSPTPSPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 404 NAGEAR----SQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGAGALETELEGPSQPALEKDAERPR 479
Cdd:PHA03169 109 GSAEELasglSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
170 180
....*....|....*....|....*..
gi 1034629690 480 IRKENQDGPAPQEEGKGGQSRDSDQAP 506
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1835 |
1.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1378 AVKDWPWWQLLGSLQpllsatigtEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvac 1457
Cdd:COG4717 124 LLQLLPLYQELEALE---------AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELL------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1458 qvleseRAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlnDLERnptggdewqmrfDCAQMENEFLRKRLQQ 1537
Cdd:COG4717 184 ------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEE------------ELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1538 CEERLDSELTARKELEQKLGELQSAYDGAKKMAhqlkrkchhltcdlEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1617
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------GVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1618 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpSLGENCVAGLKERLWKLESSAL 1697
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1698 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQscqkRLHQLEMQLEQEYEEKQMVLHEKQD 1776
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE----ELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 1777 LEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLGTMEDGKTSVSKEELEKV 1835
Cdd:COG4717 465 LEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREERLPPV 517
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1401-1586 |
1.72e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1401 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSK 1480
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1481 HEQVQKKLGDVNKQLEEAQQKIQlndlernptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1560
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLR------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
170 180
....*....|....*....|....*.
gi 1034629690 1561 SaYDGAKKMAHQLKRKCHHLTCDLED 1586
Cdd:TIGR02169 945 E-IPEEELSLEDVQAELQRVEEEIRA 969
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1887-2079 |
1.77e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1887 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQlqvaqmrieyleqstvdRAIVSR 1966
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-----------------KARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1967 QEAVICDLEnktEFQKVQIKRFEVLViRLRDSLIKMGEElsqaATSESQQRES--SQYYQRRLEELKADMEelvQREAea 2044
Cdd:pfam13851 97 LEKELKDLK---WEHEVLEQRFEKVE-RERDELYDKFEA----AIQDVQQKTGlkNLLLEKKLQALGETLE---KKEA-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034629690 2045 srrcmELEKYV-------EELAAVRQTLQTDLETSIRRIADL 2079
Cdd:pfam13851 164 -----QLNEVLaaanldpDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1843-2100 |
1.92e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1843 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSaadigq 1922
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1923 iQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlENKTEFQKVQIKrfEVLVIRLRDSLIKM 2002
Cdd:pfam07888 104 -KELSASSEELSEEKDALLAQRAAHEARIRELEE------------------DIKTLTQRVLER--ETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2003 GEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVeelaavrQTLQTDLETSIRRIADLQAA 2082
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------TTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*...
gi 1034629690 2083 LEEVASSDSDTESVQTAV 2100
Cdd:pfam07888 236 LEELRSLQERLNASERKV 253
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1656-2101 |
1.92e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1656 QLKQQVEMLQDHKR-----------ELLGSPSLGENCVaglkerlWKLESSALEQQKIQSQQENTIKQLEQLR---QRFE 1721
Cdd:pfam10174 71 HLQLTIQALQDELRaqrdlnqllqqDFTTSPVDGEDKF-------STPELTEENFRRLQSEHERQAKELFLLRktlEEME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1722 LEIERMKQ--------------MHQKD---REDQEEELEDVRQ--SCQKRLHQLEMQLEQEYEEKQMV---LHEK---QD 1776
Cdd:pfam10174 144 LRIETQKQtlgardesikklleMLQSKglpKKSGEEDWERTRRiaEAEMQLGHLEVLLDQKEKENIHLreeLHRRnqlQP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1777 LEGLIGTLCDQIGHRDFDVEKrLRRDLRRthaLLSDVQLL----LGTMEDGKTSVSKEELEKVHS--------QLEQSEA 1844
Cdd:pfam10174 224 DPAKTKALQTVIEMKDTKISS-LERNIRD---LEDEVQMLktngLLHTEDREEEIKQMEVYKSHSkfmknkidQLKQELS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1845 KCEEALKTqkvLTADLESMHSELENMTRNKSLVDEQLYR-------LQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1917
Cdd:pfam10174 300 KKESELLA---LQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1918 ADIGQIQELQ--LQLEEAK-----KEKHKLQEQL-----QVAQM--RIEYLEQ--STVDRAIVSRQEAvICDLENKTEFQ 1981
Cdd:pfam10174 377 TLAGEIRDLKdmLDVKERKinvlqKKIENLQEQLrdkdkQLAGLkeRVKSLQTdsSNTDTALTTLEEA-LSEKERIIERL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1982 KVQIKRFEVLVIRLRDSLIKMGEELSQAATS---ESQQRESSqyyqrrLEELKADMEELVQREAEASRRC----MELEKY 2054
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSAlqpELTEKESS------LIDLKEHASSLASSGLKKDSKLksleIAVEQK 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034629690 2055 VEELAAVRQTLQT-----DLETSIRRIADLQAALE-EVASSDSDTESVQTAVD 2101
Cdd:pfam10174 530 KEECSKLENQLKKahnaeEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVE 582
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1922-2086 |
2.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1922 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdrAIVSRQEAVicdlenktEFQKVQIKRFEVLVIRLRDSLIK 2001
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTEL--------EDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2002 MGEELSQAATsesqQRESsQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR----IA 2077
Cdd:COG1579 78 YEEQLGNVRN----NKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLA 152
|
....*....
gi 1034629690 2078 DLQAALEEV 2086
Cdd:COG1579 153 ELEAELEEL 161
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1549-2125 |
2.11e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1549 RKELEQKLGELQSAYDGAKKmahqLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKkfdlQLAQAlgESVFEKGLREK 1628
Cdd:PRK01156 151 RKKILDEILEINSLERNYDK----LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADD--EKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1629 vtqENTSVrwELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL------LGSPSLGENCVAGLKERLWKLESSALeqqki 1702
Cdd:PRK01156 221 ---ERLSI--EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdLSMELEKNNYYKELEERHMKIINDPV----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1703 qsqqentIKQLEQLRQRFELeiermkqmhQKDREDQEEELEDVRQSCQK--RLHQLEMQLEQEYEEKQMVLHEKQDLegl 1780
Cdd:PRK01156 291 -------YKNRNYINDYFKY---------KNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDL--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1781 igtlcdqighrdfdveKRLRRDLRRTHallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEakceealkTQKVLTADL 1860
Cdd:PRK01156 352 ----------------NNQILELEGYE---MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1861 ESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL--------------MQKHKDLIAQSAADIGQIQEl 1926
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1927 qlQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSrqeavicdlENKTEFQKVQIKRFEVLVIRLRDSLIKmgeel 2006
Cdd:PRK01156 484 --KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADLEDIKIKINELKDKHDK----- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2007 SQAATSESQQRESSQYYQRRLEELKA-------DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD- 2078
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENe 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1034629690 2079 ---LQAALEEVASSDSDTESVQTAVDCGSSGRKEMDnvSILSSQPEGSLQ 2125
Cdd:PRK01156 628 annLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID--SIIPDLKEITSR 675
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1679-1774 |
2.58e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 42.56 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1679 ENCVAGLKERLWKLESSALEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhQLEM 1758
Cdd:cd16269 199 EIEAERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQEA 270
|
90
....*....|....*.
gi 1034629690 1759 QLEQEYEEKQMVLHEK 1774
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1403-1542 |
2.87e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL--------LESKIADLTSDLADerfkgdvacqvLESERAERLQAFREV 1474
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEA-----------LKARWEAEKELIEEI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1475 QELKSKHEQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDE-------W------QMrfdcaqMENEflRKRLQQCEE 1540
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELaELAPLLREEVTEEDiaevvsrWtgipvgKL------LEGE--REKLLNLEE 545
|
..
gi 1034629690 1541 RL 1542
Cdd:COG0542 546 EL 547
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1416-1627 |
2.95e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1416 RKLEKSEKLRNELRQNTDLLeskIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQL 1495
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1496 EEAQQKIQLNDLERNPTggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKR 1575
Cdd:COG4372 83 EELNEQLQAAQAELAQA-----QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034629690 1576 KCHHLTCDLEDTcvlleNQQSRNHELEKKQKKFDLQLAQALGESVFEKGLRE 1627
Cdd:COG4372 158 QLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1829-1971 |
2.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVDEQLYRLQFEKADLLKR----IDEDQDDLN 1903
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEeKKEKLQEEEDKLLEEAEKEAQQAIKEakkeADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629690 1904 ELMQ-KHKDLIAQSAADI-GQIQELQLQLEEAKKEKHKLQEQLQVAQ-MRIEYLEQSTVDRAIVSRQEAVI 1971
Cdd:PRK00409 595 QLQKgGYASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGDeVKYLSLGQKGEVLSIPDDKEAIV 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1691-1933 |
3.13e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1691 KLESSALEQQKIQSQQENTIKQLEQLRQrfelEIERMkqmhQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMV 1770
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA----ELEEL----NEEYNELQAELEALQA-------EID-KLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1771 LHEKQDlegligtlcdqighrdfDVEKRLRrDLRRTHALLSDVQLLLG-----TMEDGKTSVSK---------EELEKVH 1836
Cdd:COG3883 81 IEERRE-----------------ELGERAR-ALYRSGGSVSYLDVLLGsesfsDFLDRLSALSKiadadadllEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1837 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1916
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 1034629690 1917 AADIGQIQELQLQLEEA 1933
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1416-1777 |
3.63e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.59 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1416 RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgDVACQVLESERAERLQAF----REVQELKSKHEQVQKKLGDV 1491
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEK---EALRKEMKKEREELGATMlalsQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1492 NKQLEEAQQKIQLNDLERNPTGGdewQMRF--DCAQMENEFLRKRLQQCEERLDSELTARkelEQKLGELQSAYDGAKKM 1569
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCG---EMRYqlNQTKMKKDEAEKEHREYRTKTGRQLEIK---DQEIEKLGLELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1570 AHQLKRKCHHLTCDLEDTCVLLENQQSRNH----ELEKKQKKFDLQL-AQALGESVFEKGLREKVTQENTSVRWELGQLQ 1644
Cdd:pfam15964 504 LEQAQQDAARAREECLKLTELLGESEHQLHltrlEKESIQQSFSNEAkAQALQAQQREQELTQKMQQMEAQHDKTVNEQY 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1645 QQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFElEI 1724
Cdd:pfam15964 584 SLLTSQNTFIAKLKEECCTLAKKLEEI--------------------TQKSRSEVEQLSQEKEYLQDRLEKLQKRNE-EL 642
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629690 1725 ERMKQMHQKDREDQEEELEDVRQSCQ---KRLHQLEMQLEQEYEEKQMVLHEKQDL 1777
Cdd:pfam15964 643 EEQCVQHGRMHERMKQRLRQLDKHCQataQQLVQLLSKQNQLFKERQNLTEEVQSL 698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1682-2085 |
3.73e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.02 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1682 VAGLKERLWKLESsALEQQKIQSQQENTikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QS 1748
Cdd:COG3096 838 LAALRQRRSELER-ELAQHRAQEQQLRQ--QLDQLKEQLQLLNKLLPQANLLADETLADRLEELReeldaaqeaqafiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1749 CQKRLHQLEM-------------QLEQEYEEKQmvlHEKQDLEGLIGTLCDQIGhrdfdvekrlrrdlRRTHALLSDVQL 1815
Cdd:COG3096 915 HGKALAQLEPlvavlqsdpeqfeQLQADYLQAK---EQQRRLKQQIFALSEVVQ--------------RRPHFSYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1816 LLGTmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkslvdeqlyrlqfekADLLKRI 1895
Cdd:COG3096 978 LLGE--------NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL---------------------ASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1896 DEDQDDLNELMQKHKDLIAQSAADIgqiqelqlqLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLE 1975
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEA---------EERARIRRDELHEELSQNRSRRSQLEKQ------LTRCEAEMDSLQ 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1976 N---KTEfQKVQIKRFEV--------LVIRL-RDSLIKMG---EELsqAATSESQQRESSQYYQRRLEELKADMEEL--V 2038
Cdd:COG3096 1094 KrlrKAE-RDYKQEREQVvqakagwcAVLRLaRDNDVERRlhrREL--AYLSADELRSMSDKALGALRLAVADNEHLrdA 1170
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034629690 2039 QREAEASRRCmelEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:COG3096 1171 LRLSEDPRRP---ERKVQFYIAVYQHLRERIRQDIIRTDDPVEAIEQ 1214
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1805-1913 |
3.91e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 40.29 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1805 RTHALLSDVQLLLGTMEDGKTsvskeELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmTRNKSLVDEQLYRL 1884
Cdd:pfam09744 44 RNQEHNVELEELREDNEQLET-----QYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLE--EENRRLEADHVSRL 116
|
90 100
....*....|....*....|....*....
gi 1034629690 1885 QFEKADLLKRIDEDQDDLNELMQKHKDLI 1913
Cdd:pfam09744 117 EEKEAELKKEYSKLHERETEVLRKLKEVV 145
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
1829-1962 |
3.94e-03 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 40.96 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1829 KEELEKvhSQLEQSEAK-CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1907
Cdd:pfam06785 62 KEKFEK--SFLEEKEAKlTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034629690 1908 KHKDLIAQSAAdigQIQELQLQLEEAKKEKHKLQEQlqvaqmrIEYLEQSTVDRA 1962
Cdd:pfam06785 140 ESEEQLAEKQL---LINEYQQTIEEQRSVLEKRQDQ-------IENLESKVRDLN 184
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1599-2108 |
4.03e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1599 HELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLG 1678
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1679 ENCVAGLKERLWKLESSALEQQKIQSQQENTIK-QLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQKRLHQLE 1757
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGK----HQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1758 MQLEQEYEEKQMVLH-EKQDLEGLIGTLCDQI--GHRDF-DVEKRLRRDLRRTHALLSDVQlllgtmedgktsVSKEELE 1833
Cdd:pfam12128 397 DKLAKIREARDRQLAvAEDDLQALESELREQLeaGKLEFnEEEYRLKSRLGELKLRLNQAT------------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1834 kvhsQLEQSEAKCEEALKTQKVLTADLESMHSELenmTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1913
Cdd:pfam12128 465 ----QLENFDERIERAREEQEAANAEVERLQSEL---RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1914 A---QSAAD----IGQI----QELQLQLEEAKKEKHKLQEQ----LQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 1978
Cdd:pfam12128 538 HflrKEAPDweqsIGKVispeLLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1979 EfqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELV---QREAEASRRCMELEKYV 2055
Cdd:pfam12128 618 E----KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaerKDSANERLNSLEAQLKQ 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034629690 2056 EELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSGRK 2108
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
633-723 |
4.10e-03 |
|
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: 40.41 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKIRATFT 698
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 1034629690 699 VLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1415-1789 |
4.13e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1415 RRKLEKSEKLRNELRQNTDLLESKIADLTsDLADERFKGDVACQVLESE---RAERLQAFREVQELKSKHEQVQKKLGDV 1491
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLV-EMARELEELSARESDLEQDyqaASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1492 NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAyDGAKKMAH 1571
Cdd:COG3096 360 TERLEEQEEVVEE-------------------AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTR-AIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1572 QLKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVtqentsvrWELGQLQQQLK 1648
Cdd:COG3096 420 QALEKARAL-CGLPD--LTPENAEDYLAAFRAKEQQATeevLELEQKLSVADAARRQFEKA--------YELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1649 QKEQEASQLKQQVEMLQDHKrellgspSLGENcVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMK 1728
Cdd:COG3096 489 ERSQAWQTARELLRRYRSQQ-------ALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELL 559
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629690 1729 QMHQKDREDQEEELEDvrqsCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1789
Cdd:COG3096 560 AELEAQLEELEEQAAE----AVEQRSELRQQLEQlrarikELAARAPAWLAAQDaLE----RLREQSG 619
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1402-2076 |
4.13e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------------LESKIADLTSDLADERFKGDVACQVLE------S 1462
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1463 ERAERLQAFR-EVQELKSKHEQVQKKLgDVN-----------KQLEEAQQKIQLNDLErnPTGGDEWQMRFDcAQmENEF 1530
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQAL-DVQqtraiqyqqavQALEKARALCGLPDLT--PENAEDYLAAFR-AK-EQQA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1531 LRKRLQQcEERLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKchhLTCDLEDTCVLLENQQS---RNHELEKK-- 1604
Cdd:COG3096 454 TEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEvERSQAWQTARE---LLRRYRSQQALAQRLQQlraQLAELEQRlr 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1605 --QKKFDL--QLAQALGESVFEKGLREKVTQENTSVRWELgqlQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgen 1680
Cdd:COG3096 530 qqQNAERLleEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKEL--------- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1681 cvaGLKERLWKLESSALEQ------------QKIQSQQENTIK----------QLEQLRQRFELEIERmkqMHQKD-RED 1737
Cdd:COG3096 598 ---AARAPAWLAAQDALERlreqsgealadsQEVTAAMQQLLErereatverdELAARKQALESQIER---LSQPGgAED 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1738 QE--------------EELEDV---------------RQ--------SCQKRLHQLEMQLEQEYeekqMVLHEKQ----- 1775
Cdd:COG3096 672 PRllalaerlggvllsEIYDDVtledapyfsalygpaRHaivvpdlsAVKEQLAGLEDCPEDLY----LIEGDPDsfdds 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1776 --DLEGLIGTLCDQIGHRDFDVEK-----RLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ------- 1841
Cdd:COG3096 748 vfDAEELEDAVVVKLSDRQWRYSRfpevpLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgghla 827
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1842 --SEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVD------EQLYRLQ-----FEKADLLKRIDEDQDDLNEL-- 1905
Cdd:COG3096 828 vaFAPDPEAELAALRQRRSELERELAQHRaQEQQLRQQLDqlkeqlQLLNKLLpqanlLADETLADRLEELREELDAAqe 907
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1906 ----MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTefq 1981
Cdd:COG3096 908 aqafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD--- 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1982 kvqikrfevLVIRLRDSLIKMGEELSQAATS-ESQQRESSQYYQRR-------------LEELKADMEEL-VQREAEASR 2046
Cdd:COG3096 985 ---------LNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQVLaslkssrdakqqtLQELEQELEELgVQADAEAEE 1055
|
810 820 830
....*....|....*....|....*....|
gi 1034629690 2047 RCMELEKYVEELAAVRQTLQTDLETSIRRI 2076
Cdd:COG3096 1056 RARIRRDELHEELSQNRSRRSQLEKQLTRC 1085
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1892-2099 |
4.63e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1892 LKRIDEDQDDLNELmqkhKDLIAQSAAdigQIQELQLQLEEAKKeKHKLQEQLQVAQMRIEYLEqstvDRAIVSRQEAvi 1971
Cdd:COG1196 178 ERKLEATEENLERL----EDILGELER---QLEPLERQAEKAER-YRELKEELKELEAELLLLK----LRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1972 cdLENKTEFQKVQIKRFEvlvirlrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMEL 2051
Cdd:COG1196 244 --LEAELEELEAELEELE--------------AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034629690 2052 EKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2099
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1403-1568 |
5.16e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1403 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvLESERAErlqafREVQELKSKHE 1482
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---------KEIKRLE-----LEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1483 QVQKKLGDV--NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1560
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIES-------------------LKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
....*...
gi 1034629690 1561 SAYDGAKK 1568
Cdd:COG1579 138 AELEEKKA 145
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
261-514 |
6.09e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 261 KDRQGTRPQAQGPGEGVRPGKAEKeGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGGFLGRRSKwDGPQNKKDKEGV 340
Cdd:PHA03169 24 KRHGGTREQAGRRRGTAARAAKPA-PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 341 LLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEkaGELRSTTGKAGESWDKKEKMGQPQGKSGNAGEARSQTEKGCEAPK 420
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 421 EVSTMVESPAA-------PGKGGWPGSRGQEAEEPCSRAGDGA--------GALETELEGPSQPALEKDAERPRIRKENQ 485
Cdd:PHA03169 180 PPTSEPEPDSPgppqsetPTSSPPPQSPPDEPGEPQSPTPQQApspntqqaVEHEDEPTEPEREGPPFPGHRSHSYTVVG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034629690 486 DGPAPQEEG-------KGGQSRDSDQAPEDRWYEAE 514
Cdd:PHA03169 260 WKPSTRPGGvpklclrCTSHPSHRSRLPEGQQSEDK 295
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1654-1958 |
6.62e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1654 ASQLKQQV-EMLQDHKRELLGSPSLGEncvaglkERLWKLESSALEQQKIQsQQENTIKQLEQLRQRFELEIERMKQ--- 1729
Cdd:pfam07888 89 LRQSREKHeELEEKYKELSASSEELSE-------EKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKErak 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1730 ---MHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIG--HRDFDVEKRLRRDLR 1804
Cdd:pfam07888 161 kagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1805 RTHALLSdvqlllgtMEDGKTSVSKEELEKV-----HSQLEQSEAKCEEALKTQKVLTADLE------SMHSELENMTRN 1873
Cdd:pfam07888 241 SLQERLN--------ASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1874 KSLVDEQLYRLQFEKADLLKRIDEDQDDLN----ELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQM 1949
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEERMEREklevELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 1034629690 1950 RIEYLEQST 1958
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1402-1568 |
7.27e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAER-LQAF-REVQELKS 1479
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1480 KHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewQMRFDCAQMENEfLRKRLQQCEERLDSELTARKELEQKLGE- 1558
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAE-LDEELAELEAELEELEAEREELAAKIPPe 175
|
170
....*....|
gi 1034629690 1559 LQSAYDGAKK 1568
Cdd:COG1579 176 LLALYERIRK 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1696-2085 |
7.48e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1696 ALEQQKIQSQQENtiKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QSCQKRLHQLEMQL-- 1760
Cdd:PRK04863 852 ALADHESQEQQQR--SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIReqldeaeeakrfvQQHGNALAQLEPIVsv 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1761 ----EQEYEE-KQMVLHEKQDLegligtlcdqighRDFDVEKRLRRDL--RRTHALLSDVQLLLGtmedgKTSVSKEELE 1833
Cdd:PRK04863 930 lqsdPEQFEQlKQDYQQAQQTQ-------------RDAKQQAFALTEVvqRRAHFSYEDAAEMLA-----KNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1834 KVHSQLEQSEAKCEEALKTQKvltadlesmhselENMTRNKslvdeQLYrlqfekADLLKRIDEDQDDLNELMQKHKDLI 1913
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ-------------AQLAQYN-----QVL------ASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1914 AQsaADIGQIQELQLQLEEakkekhkLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENK-TEFQK--VQIKRFEV 1990
Cdd:PRK04863 1048 VP--ADSGAEERARARRDE-------LHARLSANRSRRNQLEKQ------LTFCEAEMDNLTKKlRKLERdyHEMREQVV 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1991 -------LVIRL-RDSLIK---MGEELsqAATSESQQRESSQYYQRRLEELKADMEEL--VQREAEASRRcmeLEKYVEE 2057
Cdd:PRK04863 1113 nakagwcAVLRLvKDNGVErrlHRREL--AYLSADELRSMSDKALGALRLAVADNEHLrdVLRLSEDPKR---PERKVQF 1187
|
410 420
....*....|....*....|....*...
gi 1034629690 2058 LAAVRQTLQTDLETSIRRIADLQAALEE 2085
Cdd:PRK04863 1188 YIAVYQHLRERIRQDIIRTDDPVEAIEQ 1215
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1402-1503 |
8.42e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1402 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleSERAERLQAFREVQELKSKH 1481
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|..
gi 1034629690 1482 EQVQKKLGDVNKQLEEAQQKIQ 1503
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1371-1507 |
8.46e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1371 KNVAVFLAVKDW-PW-WQLLGSLQPLLSATIGT-----EQLRAKEEELTTLRRKLEKS-----EKLRNELRQNTDLLESK 1438
Cdd:smart00787 123 KTFARLEAKKMWyEWrMKLLEGLKEGLDENLEGlkedyKLLMKELELLNSIKPKLRDRkdaleEELRQLKQLEDELEDCD 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629690 1439 IADLtsDLADERFKGDVACQVLESERAERLQafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDL 1507
Cdd:smart00787 203 PTEL--DRAKEKLKKLLQEIMIKVKKLEELE--EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1400-1516 |
9.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629690 1400 GTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvACQVLESERAERLQAFREVQELK 1478
Cdd:PRK00409 524 SLEELERElEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ---AIKEAKKEADEIIKELRQLQKGG 600
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034629690 1479 SKH------EQVQKKLGDVNKQLEEAQQKIQLNdlERNPTGGDE 1516
Cdd:PRK00409 601 YASvkahelIEARKRLNKANEKKEKKKKKQKEK--QEELKVGDE 642
|
|
| |
