|
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 ... |
627-1364 |
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: 1032.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV---PKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQ 862
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 863 RAVWRVLAAIYHLGAAGACK---VGRKQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRwGLEDEETS 939
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ-ESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 940 SGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGKDRAATFEELCHNYAHERLQL 1019
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1020 LFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQNPsQQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLER 1099
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAP-QQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLER 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1100 LCAAFEKKGAGTeGSSALRTCEQPLQCEIFHQLGWDPVRYDLTGWLHRAKPNLSALDAPQVLHQSKREelrslfqarakl 1179
Cdd:cd01386 479 LFSHYGDKEGGK-GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1180 ppvcravaglegtsqqalqrsrmvrrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRSGQES 1259
Cdd:cd01386 546 -------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTS 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1260 PPPpqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGIDERKA 1339
Cdd:cd01386 595 SPA----------AGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKA 664
|
730 740
....*....|....*....|....*
gi 1034629688 1340 VEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd01386 665 VEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
628-1364 |
3.66e-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: 326.08 E-value: 3.66e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV-----PKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVmekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKIRATFTVLRAFGsvsmaHSRS-----ATRFSMVMSLDFNATG 771
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFG-----NAKTvrndnSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 772 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---HQMADSSSFGMGVWSKPEDKQKAAAAFAQL 848
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 849 QGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKhhlR 918
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 919 QIIqqmtfgpsrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSS--HHLSMASIMVVDSPGFQNPR 995
Cdd:cd00124 309 TIK-----------VGGETITKPLTVEQaEDARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 996 HQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVVDQNPSqqvrlpagggaqd 1074
Cdd:cd00124 378 VNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKPL------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1075 arGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSa 1154
Cdd:cd00124 437 --GILSLLDEECLFPKGTDATFLEKLYSAHGSH-----PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFLEKNKDTLP- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1155 ldapqvlhqskrEELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMI 1234
Cdd:cd00124 507 ------------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTL 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1235 KRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRR 1314
Cdd:cd00124 531 NSTQPHFVRCIKPND----------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1315 QFQVLDAPLLKKLMSTSEgiderKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd00124 589 RYRILAPGATEKASDSKK-----AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
608-1376 |
4.76e-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: 312.56 E-value: 4.76e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 608 NPPELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKvpkGRRDG-LPAHIGS 680
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPykqlpiYTDEVIKKYR---GKSRGeLPPHVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 681 MAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRF 759
Cdd:smart00242 78 IADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEdQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 760 SMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQmadSSSFG---MGVWSK-- 834
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS---PEDYRylnQGGCLTvd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 835 -PEDKqkaaAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFmrfewaNYAAEALGC 903
Cdd:smart00242 235 gIDDA----EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEEL------SNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 904 EYEELNTA-TFKhhlrqiiqQMTFGpsrwgleDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMA 981
Cdd:smart00242 305 DPEELEKAlTKR--------KIKTG-------GEVITKPLNVEQAlDARDALAKALYSRLFDWLVKRINQSLSFKDGSTY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 982 SIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ----FDLpdpspGTTVAVVD 1057
Cdd:smart00242 370 FIGVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTfidfFDN-----QDCIDLIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1058 QNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCeqplqceiF---HQLGw 1134
Cdd:smart00242 439 KKP---------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTE--------FiikHYAG- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1135 dPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravaglegtSQQALQRSRMVRRTFASslaav 1214
Cdd:smart00242 495 -DVTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLF-------------------PSGVSNAGSKKRFQTVG----- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1215 rrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILE 1294
Cdd:smart00242 549 ------SQFKEQLNELMDTLNSTNPHFIRCIKPNE--EKKPGD--------------------FDSSLVLHQLRYLGVLE 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1295 ALRLHRTGYADHMGLTRFRRQFQVLDAPLLKklmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQ 1374
Cdd:smart00242 601 NIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 1034629688 1375 RE 1376
Cdd:smart00242 676 RE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
552-2128 |
2.18e-75 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 278.88 E-value: 2.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 552 WYEA-EKVWLA---QKDGFTLATVlkpdEGTADLPAGRVrlwIDADKTITEVDEEhvhraNPPELDQVEDLASLISVNES 627
Cdd:COG5022 13 WIPDeEKGWIWaeiIKEAFNKGKV----TEEGKKEDGES---VSVKKKVLGNDRI-----KLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGpsVPSAG-----KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:COG5022 81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPyRD--LGIYTddiiqSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQ 779
Cdd:COG5022 159 GESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 780 TMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISE 859
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 860 SEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQqmtfgpsrwGLEDEE 937
Cdd:COG5022 318 EEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVK---RQIKT---------GGEWIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 938 TSSGLKMTgVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 1017
Cdd:COG5022 386 VPLNLEQA-LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNS------FEQLCINYTNEKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1018 QLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVV 1096
Cdd:COG5022 459 QQFFNQHMFKLEQEEYVKEGIEWSFiDYFDNQP-CIDLIEKKNPL---------------GILSLLDEECVMPHATDESF 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1097 LERLCAAFEKKgagtegSSALRTCEQPLQCEIF--HQLGwDpVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQ 1174
Cdd:COG5022 523 TSKLAQRLNKN------SNPKFKKSRFRDNKFVvkHYAG-D-VEYDVEGFLDKNKDPLN-DDLLELLKASTNEFVSTLFD 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1175 ARaklppvcravaglegtsQQALQRSRmvRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESR 1254
Cdd:COG5022 594 DE-----------------ENIESKGR--FPTLG------------SRFKESLNSLMSTLNSTQPHYIRCIKPN---EEK 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1255 SgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGi 1334
Cdd:COG5022 640 S-------------------PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKE- 699
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1335 DERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQK 1414
Cdd:COG5022 700 DTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH 779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1415 NVAVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEK----SEKLRNELRQNTDLLESKIADltSDLA 1490
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKA 857
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1491 DERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQkKLGDVNKQLE----EAQQKIQLNDLERNptggdewqmrfdc 1566
Cdd:COG5022 858 KKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELEseiiELKKSLSSDLIENL------------- 923
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1567 aQMENEFLrKRLQQCEERLDSELTARKELEQK--LGELQSAydgakkmahqlkrkchhlTCDLEDTCVLLENqqsrnhEL 1644
Cdd:COG5022 924 -EFKTELI-ARLKKLLNNIDLEEGPSIEYVKLpeLNKLHEV------------------ESKLKETSEEYED------LL 977
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1645 EKKqkkfdlqlaqalgesvfEKGLREKVTQENTSVRW--ELGQLQQQLKQKEQEASQLKQQVEMLQDHKREllgspslge 1722
Cdd:COG5022 978 KKS-----------------TILVREGNKANSELKNFkkELAELSKQYGALQESTKQLKELPVEVAELQSA--------- 1031
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1723 ncvaglkERLWKLESSALEQQK-IQSQQENTIKQLEQLRQRFE---LEIERmkqmhQKDREDQEEELEDVRqscqkrlhq 1798
Cdd:COG5022 1032 -------SKIISSESTELSILKpLQKLKGLLLLENNQLQARYKalkLRREN-----SLLDDKQLYQLESTE--------- 1090
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1799 lemQLEQEYEEKQMVLhEKQDLEGLIGTLcdqighrDFDVEKRLRRDL-RRTHALLSdvqLLLGTMEDGKTSVSKEELE- 1876
Cdd:COG5022 1091 ---NLLKTINVKDLEV-TNRNLVKPANVL-------QFIVAQMIKLNLlQEISKFLS---QLVNTLEPVFQKLSVLQLEl 1156
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1877 ---KVHSQLEQSEAKCEEALKTQKVLTADleSMHSEL--ENMTRNKSLVDE--QLYRLQFE---KADLLKRIDEDQDDLN 1946
Cdd:COG5022 1157 dglFWEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSSSEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPT 1234
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1947 ELMQKHKDliAQSAADIGQiqelqlqlEEAKKEKHKLQEQL-QVAQMRIEYLEQSTVDRAIVsrqeavicdlenKTEFQK 2025
Cdd:COG5022 1235 EYSTSLKG--FNNLNKKFD--------TPASMSNEKLLSLLnSIDNLLSSYKLEEEVLPATI------------NSLLQY 1292
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2026 VQIKRFEVLVIRLRDSLIKMGEELSQaatseSQQRESSQYYQRRLEELKADMEELVQReaeasRRCMELEKY-VEELAAV 2104
Cdd:COG5022 1293 INVGLFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQA-----VKVLQLLKDdLNKLDEL 1362
|
1610 1620
....*....|....*....|....*
gi 1034629688 2105 RQTLQTDLETSIRRI-ADLQAALEE 2128
Cdd:COG5022 1363 LDACYSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
615-1364 |
5.72e-71 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 253.36 E-value: 5.72e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 615 VEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAY 686
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiYSEDMIKAyrGK----RRGELPPHIFAIADEAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 687 WALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMV 762
Cdd:pfam00063 77 RSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 763 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGM-GVWSKP 835
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyHYLSQSGCYTIdGIDDSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 836 EDKqkaaaafaQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANYAAEALGCEYEEL 908
Cdd:pfam00063 236 EFK--------ITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 909 NTATFKhhlRQIiqqmtfgpsrwgledeETSSGLKMTGVDC------VEGMASGLYQELFAAVVSLINRSFSSHHLSMAS 982
Cdd:pfam00063 304 EKALCK---RRI----------------KTGRETVSKPQNVeqanyaRDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 983 -IMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVV 1056
Cdd:pfam00063 365 fIGVLDIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFiDFGDNQP--CIDLI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1057 DQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEK----KGAGTEGSSALRtceqplqceIFHQL 1132
Cdd:pfam00063 433 EKKP---------------LGILSLLDEECLFPKATDQTFLDKLYSTFSKhphfQKPRLQGETHFI---------IKHYA 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1133 GwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKlppvcRAVAGLEGTSQQALQRSRMVRRTFASsla 1212
Cdd:pfam00063 489 G--DVEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITVG--- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1213 avrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHI 1292
Cdd:pfam00063 558 --------SQFKESLGELMKTLNSTNPHYIRCIKPNE--KKRAGV--------------------FDNSLVLHQLRCNGV 607
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 1293 LEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMStsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:pfam00063 608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-----DAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
627-1364 |
6.16e-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: 199.62 E-value: 6.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVP---KGRRDGLPAHIGSMAQRAYWALLN----QRRDQS 697
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsiPDLYSEERMLlyhGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 698 IVALGWSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSV----EKIRATFTVLRAFGSVSMAHSRSATRFS 760
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLgsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 761 MVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEDKq 839
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 840 kaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRkQFMRFewanyAAEALGCEYEELN 909
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfesendtTVLEDATTL-QSLKL-----AAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 910 TATFKHHL----RQIIQQMTFGPSRwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMV 985
Cdd:cd14890 312 KALLTRQLfvggKTIVQPQNVEQAR-----------------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 986 VDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSqqVR 1065
Cdd:cd14890 375 LDIYGFEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFNDNQAC--LE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1066 LPAGGGAQDArGLFWVLDEEVHVEGS-SDSVVLERLCAAFekkGAGTEGSSALRTCEQ------P-----LQCEIFHQLG 1133
Cdd:cd14890 437 LIEGKVNGKP-GIFITLDDCWRFKGEeANKKFVSQLHASF---GRKSGSGGTRRGSSQhphfvhPkfdadKQFGIKHYAG 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1134 wdPVRYDLTGWLHRAKPNLSAldapqvlhqskreELRSLfqaraklppvcravaglegtsqqalqrsrmvrrtFASSLAA 1213
Cdd:cd14890 513 --DVIYDASGFNEKNNETLNA-------------EMKEL----------------------------------IKQSRRS 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1214 VRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHIL 1293
Cdd:cd14890 544 IREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA----------------------PGKFDGLDCLRQLKYSGMM 601
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 1294 EALRLHRTGYA---DHmglTRFRRQFQVLDapllkklmSTSEGIDErkAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14890 602 EAIQIRQQGFAlreEH---DSFFYDFQVLL--------PTAENIEQ--LVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1364 |
5.58e-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: 190.61 E-value: 5.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP----SAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPY-KNLPiyseNIIEMYRGKkRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRI 773
Cdd:cd14920 80 GESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 774 TAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFgMGVWSKPEDKQKAAAAFAQLQGAME 853
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRF-LSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 854 MLGISESEQRAVWRVLAAIYHLGAAGACKvGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsRWGL 933
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 934 EDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNY 1012
Cdd:cd14920 311 QKAQTKEQADFA----VEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1013 AHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVE 1089
Cdd:cd14920 381 TNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP---------------GVLALLDEECWFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1090 GSSDSVVLERLcaafekkgAGTEGS-SALRTCEQP---LQCEIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQ 1163
Cdd:cd14920 445 KATDKTFVEKL--------VQEQGShSKFQKPRQLkdkADFCIIHYAG--KVDYKADEWLMK---NMDPLndNVATLLHQ 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1164 SKREELRSLFQARAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIH 1243
Cdd:cd14920 512 SSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVG------------QLYKESLTKLMATLRNTNPNFVR 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1244 CLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPL 1323
Cdd:cd14920 580 CIIPNH--EKRAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 637
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1034629688 1324 LKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14920 638 IPKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
628-1319 |
2.46e-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: 188.29 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAgkvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPfkdvplYGNEFITA----YRQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 780
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG---IEnEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 781 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 861 EQRAVWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKHHLRqiiqqmtfgpsrwg 932
Cdd:cd01383 234 DQEHIFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQ-------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 933 LEDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSF-SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd01383 295 AGGDKIVKKLTLQqAIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlpdpspgTTVAVVDQNPSQQV--RLPAgggaqdarGLFWVLDEEVHV 1088
Cdd:cd01383 369 NYANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFEDNQECLDLieKKPL--------GLISLLDEESNF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1089 EGSSDSVVLERL--------CAAFEKKGAGTegssalrtceqplqceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQV 1160
Cdd:cd01383 431 PKATDLTFANKLkqhlksnsCFKGERGGAFT----------------IRHYAG--EVTYDTSGFLEKNRDLLHS-DLIQL 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1161 LHQSKreelRSLFQARAklppvcravAGLEGTSQQALQRSRMvrrtfasSLAAVRRKAPCSQIKLQMDALTSMIKRSRLH 1240
Cdd:cd01383 492 LSSCS----CQLPQLFA---------SKMLDASRKALPLTKA-------SGSDSQKQSVATKFKGQLFKLMQRLENTTPH 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1241 FIHCLVPNPV-VESRSGQEsppppqpgrdkpgaggpLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1319
Cdd:cd01383 552 FIRCIKPNNKqLPGVFDQD-----------------LVLQ------QLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFL 608
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
628-1321 |
6.77e-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: 182.07 E-value: 6.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALL-------NQRRD 695
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPF-KHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRrrlhepgASKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 696 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDF 767
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 768 -----NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--DSSSFGMGVWSKPEDKQK 840
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQRNDGVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 841 AAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANYAAE 899
Cdd:cd14895 241 DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 900 ALGCEYEELNTATFKhhlRQIiqqmtfgpsrwGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLIN-----RSF 973
Cdd:cd14895 321 LFAVDQDELVSALTT---RKI-----------SVGGETFHANLSLAQCgDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 974 SSHHLSMAS------IMVVDSPGFQnprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPD 1046
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1047 PSpgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagteGSSALRTCEQPLQC 1126
Cdd:cd14895 461 NS--VCLEMLEQRPS---------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS----NFSASRTDQADVAF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1127 EIFHQLGwdPVRYDLTGWL--HRAKPNLSALDapqVLHQSKREELRSLfqaraklppvCRAVAGLEgTSQQALQRSRMVR 1204
Cdd:cd14895 520 QIHHYAG--AVRYQAEGFCekNKDQPNAELFS---VLGKTSDAHLREL----------FEFFKASE-SAELSLGQPKLRR 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1205 RTfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALR 1284
Cdd:cd14895 584 RS--SVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND--ESASDQ--------------------FDMAKVS 636
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629688 1285 VQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1321
Cdd:cd14895 637 SQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
628-1249 |
1.40e-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: 177.19 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSV-----------PSAGKVPkgrrdglpaHIGSMAQRAYWALLNQRR 694
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfkTIPGLysdemllkfiqPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 695 DQSIVALGWSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT- 770
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 771 --------GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-------------DLDLRTELNLHQMA-DSSSFG 828
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeenDEKLAKGADAKPISiDMSSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 829 MGVWSKPEDKQKAAAAFA--------QLQGAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 894
Cdd:cd14888 232 PHLKFRYLTKSSCHELPDvddleefeSTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 895 NYAAEALGCEYEEL-NTATFkhhlRQIIQQmtfgpsrwgleDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRS 972
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA-----------HEFYTKPLRVDeAEDVRDALARALYSCLFDKVVERTNES 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 973 FS-SHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFdl 1044
Cdd:cd14888 377 IGySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIswnPLDF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1045 pdPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTceQPL 1124
Cdd:cd14888 445 --PDNQDCVDLLQEKPL---------------GIFCMLDEECFVPGGKD----QGLCNKLCQKHKGHKRFDVVKT--DPN 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1125 QCEIFHQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglegtsqqalqrsrMVR 1204
Cdd:cd14888 502 SFVIVHFAG--PVKYCSDGFLEKNKDQLS-VDAQEVIKNSKNPFISNLFSA--------------------------YLR 552
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1034629688 1205 RTFASSLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNP 1249
Cdd:cd14888 553 RGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
627-1364 |
2.35e-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: 176.36 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP---------SAGKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQS 697
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPY-KELPiytqdivkqYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 698 IVALGWSGAGKTTCCEQVLEHLVgmagSVDGRVS-VE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14883 76 VIISGESGAGKTETTKLILQYLC----AVTNNHSwVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAG--LDLDLRTELNLHQMAD------SSSFGMGVWSKPEDkqkaaaaFAQ 847
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDyhylnqSGCIRIDNINDKKD-------FDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 848 LQGAMEMLGISESEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEA--LGCEYEELNTA-TFKHhlRQIIQ 922
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 923 QMTFGPsrwgledeetssgLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 1001
Cdd:cd14883 303 NVTEIP-------------LKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1002 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQF-------DLPDPSPgttvavvdqnpsqqvrlpaggg 1071
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP---------------------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1072 aqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQceifHQLGwdPVRYDLTGWLHRAKPN 1151
Cdd:cd14883 422 ----LGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK----HYAG--EVTYTVQGFLDKNKDT 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1152 LSaLDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEGTSQqalqrsrmvRRTfasslaavRRKAP--CSQIKLQMDA 1229
Cdd:cd14883 492 QQ-DDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS---------RGT--------SKGKPtvGDTFKHQLQS 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1230 LTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGL 1309
Cdd:cd14883 554 LVDVLSATQPWYVRCIKPNSLKE----------------------PNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTF 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1034629688 1310 TRFRRQFQVLDapllkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14883 612 KEFVDRYLCLD-----PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
627-1364 |
2.60e-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: 176.71 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPedKQKAAAAF 845
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP--GVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 846 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEyeelNTATFK--HHLRQIIQQ 923
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 924 MT--FGPSRWGL-EDEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgK 999
Cdd:cd14911 303 MTraFLTPRIKVgRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE------I 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1000 DRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqqvrlpagggaqdAR 1076
Cdd:cd14911 377 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGL-DLQP--TIDLIDK----------------PG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1077 GLFWVLDEEVHVEGSSDSVVLERLCAA------FEKkgAGTEGSSALrtceqplqcEIFHQLGwdPVRYDLTGWLHRakp 1150
Cdd:cd14911 438 GIMALLDEECWFPKATDKTFVDKLVSAhsmhpkFMK--TDFRGVADF---------AIVHYAG--RVDYSAAKWLMK--- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1151 NLSALDapqvlhqskrEELRSLFQArAKLPPVCR--AVAGLEGTSQQALQRSRMVRRTFASSLAAVrrkapcSQI-KLQM 1227
Cdd:cd14911 502 NMDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTV------SHLyKEQL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1228 DALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgAGGPLALDipalrvQLAGFHILEALRLHRTGYADHM 1307
Cdd:cd14911 565 AKLMDTLRNTNPNFVRCIIPNH--EKRAGK--------------IDAPLVLD------QLRCNGVLEGIRICRQGFPNRI 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 1308 GLTRFRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14911 623 PFQEFRQRYELLTPNVIPKGF-----MDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
628-1361 |
2.76e-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: 176.12 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPS--AGKVPKGrrdgLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 700 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQL 778
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 779 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNlhqmaDSSSFGMGVWSKPEDKQKAAAAF--AQLQGAMEMLG 856
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG-----SSAAYGYLSLSGCIEVEGVDDVAdfEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 857 ISESEQRAVWRVLAAIYHLG------AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTAtFKHHLRQIIQQmtfGPSR 930
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 931 WGLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQ----NprhqgkdraaTF 1005
Cdd:cd14872 306 IPLTPAQ--------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ-FDLPDPSPgttvaVVDQNPSQQvrlpagggaqdaRGLFWVLDE 1084
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEhIDFIDNQP-----VLDLIEKKQ------------PGLMLALDD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1085 EVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1164
Cdd:cd14872 431 QVKIPKGSD----ATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAG--DVTYDITGFLEKNKDTLQK-DLYVLLSSS 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1165 KREELRSLFqaraklPPvcraVAGLEGTSQQALqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIKRSRLHFIHC 1244
Cdd:cd14872 504 KNKLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRC 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1245 LVPNpvvesrsgqesppppQPGRDKPGAGgplALDIPALRvqLAGfhILEALRLHRTGYAdhmgltrFR---RQFQVLDA 1321
Cdd:cd14872 552 VKPN---------------QEKRARLFDG---FMSLEQLR--YAG--VFEAVKIRKTGYP-------FRyshERFLKRYR 602
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629688 1322 PLLKKlMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQV 1361
Cdd:cd14872 603 FLVKT-IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
627-1320 |
1.14e-44 |
|
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: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAG---KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQwlPELYTEEqhsKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ---------------MADSSSFgmgvwskpedkqkaaaafA 846
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANecaytganktikiegMSDRKHF------------------A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANYAAEALGCEYEELNTATFKH 915
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 916 HLRQIIQQMTFgpsrwGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPR 995
Cdd:cd14903 296 TMRAAGDVYTV-----PLKKDQAE--------DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 996 HQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVdqnpsqqvrlpagggaQD 1074
Cdd:cd14903 363 HN------SFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRwAHIDFADNQ--DVLAVI----------------ED 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1075 ARGLFWVLDEEV-HVEGSSDSVVLeRLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAK---- 1149
Cdd:cd14903 419 RLGIISLLNDEVmRPKGNEESFVS-KLSSIHKDEQDVIEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdall 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1150 PNLSALdapqvLHQSKREELRSLFQARaklppvcravAGLEGTSQQALQRSRMVRRTFASSLAAVRrkapcSQIKLQMDA 1229
Cdd:cd14903 491 PDLSDL-----MRGSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNE 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1230 LTSMIKRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGL 1309
Cdd:cd14903 551 LMTTIRSTNVHYVRCIKPNS----------------------IKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLH 608
|
730
....*....|.
gi 1034629688 1310 TRFRRQFQVLD 1320
Cdd:cd14903 609 EEFLDKFWLFL 619
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
627-1364 |
2.43e-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: 173.66 E-value: 2.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKkRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 774
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 775 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQGAMEM 854
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQ--DDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 855 LGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglE 934
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSI--LTPRIKVG------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 935 DEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYA 1013
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1014 HERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEG 1090
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP---------------GVLALLDEECWFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1091 SSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREE 1168
Cdd:cd14921 446 ATDKSFVEKLC---TEQGNHPKFQKPKQLKDKTEFS-IIHYAG--KVDYNASAWLTK---NMDPLndNVTSLLNASSDKF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1169 LRSLFQARAKlppvcraVAGLEgtsqqalQRSRMVRRTFASslAAVRRKAPCSQI----KLQMDALTSMIKRSRLHFIHC 1244
Cdd:cd14921 517 VADLWKDVDR-------IVGLD-------QMAKMTESSLPS--ASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1245 LVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1324
Cdd:cd14921 581 IIPNH--EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629688 1325 KKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14921 639 PKGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
624-1363 |
2.98e-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: 172.73 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 624 VNESSVLNTLLQRYKAQLLHTCTGPD-LIVLQP--RGPSV--PSAGK-------VPKGRRDGLPAHIGSMAQRAYWALLN 691
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPykYLSSNsdASLGEygseyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 692 QRRDQSIVALGWSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHqmaDSSSFGMGvWS--------KP--EDkqk 840
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYALL-ASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 841 aAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVgrkqfmrfewANY-----AAEALGCEY 905
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnleftydhegGEESAVV----------KNTdvldiVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 906 EELNTA-TFKhhlrqiiqqmtfgpsrwgledeetssgLKMTGVDCVEGM-------------ASGLYQELFAAVVSLINR 971
Cdd:cd14879 303 EDLETSlTYK---------------------------TKLVRKELCTVFldpegaaaqrdelARTLYSLLFAWVVETINQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 972 SFSSHHLSMAS-IMVVDSPGFQNprhQGKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSPG 1050
Cdd:cd14879 356 KLCAPEDDFATfISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSV----PATSYF 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1051 TTVAVvdqnpsqqVRLPAGGGAqdarGLFWVLDEEV-HVEGSSDSVVLERLCAAFEKK-------GAGTEGSSALRTceq 1122
Cdd:cd14879 429 DNSDC--------VRLLRGKPG----GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHssfiavgNFATRSGSASFT--- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1123 plqceIFHQLGwdPVRYDLTGWLHRakpNLSALDApqvlhqskreELRSLfqaraklppvcravagLEGTSQqalqrsrm 1202
Cdd:cd14879 494 -----VNHYAG--EVTYSVEGFLER---NGDVLSP----------DFVNL----------------LRGATQ-------- 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1203 vrrtFASSLaavrrkapcsqiklqmDALTSMIKRSRLHFIHCLVPNPvvesrsgqeSPPPPQPGRDKpgaggplaldipa 1282
Cdd:cd14879 530 ----LNAAL----------------SELLDTLDRTRLWSVFCIRPND---------SQLPNSFDKRR------------- 567
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1283 LRVQLAGFHILEALRLHRTGYADHMGLTRFrrqfqvldaplLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVF 1362
Cdd:cd14879 568 VKAQIRSLGLPELAARLRVEYVVSLEHAEF-----------CERYKSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVF 636
|
.
gi 1034629688 1363 L 1363
Cdd:cd14879 637 L 637
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
628-1173 |
1.00e-43 |
|
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: 171.03 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR------RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKP-LPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-----HQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLG 856
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 857 ISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFE---WANYAAEALGCEYEELNTAtfkhhlrqIIQQMTFgpsrwgL 933
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAdeyPLHAVAKLLGIDEVELTEA--------LISNVNT------I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 934 EDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHL-----SMASIMVVDSPGFQNPRHQGkdraatFEE 1007
Cdd:cd14897 306 RGERIQSWKSLrQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1008 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVH 1087
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL---------------GILPLLDEEST 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1088 VEGSSDSVVLERLcaafEKKGagteGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSK 1165
Cdd:cd14897 444 FPQSTDSSLVQKL----NKYC----GESPRYVASPGNRVAfgIRHYAE--QVTYDADGFLEKNRDNLSS-DIVGCLLNSN 512
|
....*...
gi 1034629688 1166 REELRSLF 1173
Cdd:cd14897 513 NEFISDLF 520
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
628-1364 |
1.34e-43 |
|
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: 171.11 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 700 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATF--------TVLRAFGSVSMAHSRSATRFSMVMSLDFNATG 771
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 772 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGM-------GVWSKPEDKqkaaaa 844
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltidGVDDAEEFK------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 845 faQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELNTATFKHHL---R 918
Cdd:cd01377 232 --LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 919 QIIQQmtfgpsrwgledeetssGLKMTGVDC-VEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----N 993
Cdd:cd01377 310 EWVTK-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 994 prhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVD--QNPSQqvrl 1066
Cdd:cd01377 373 ----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfglDLQ--------PTIDliEKPNM---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1067 pagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegsSALRTCEQPLQCE----IFHQLGwdPVRYDLT 1142
Cdd:cd01377 431 ----------GILSILDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEahfiLKHYAG--DVEYNID 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1143 GWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQ 1222
Cdd:cd01377 492 GWLEKNKDPLNE-NVVALLKKSSDPLVASLF-----------KDYEESGGGGGKKKKKGGSFRTVS------------QL 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1223 IKLQMDALTSMIKRSRLHFIHCLVPNpvvESRsgqesppppQPGR-DKpgaggPLALDipalrvQLA--GfhILEALRLH 1299
Cdd:cd01377 548 HKEQLNKLMTTLRSTHPHFVRCIIPN---EEK---------KPGKiDA-----PLVLH------QLRcnG--VLEGIRIC 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 1300 RTGYADHMGLTRFRRQFQVLDAPLLKKlmstseGIDERKAVEELLETLDLEKKAV-AVGHSQVFLK 1364
Cdd:cd01377 603 RKGFPNRIIFAEFKQRYSILAPNAIPK------GFDDGKAACEKILKALQLDPELyRIGNTKVFFK 662
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
630-1364 |
5.61e-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: 169.17 E-value: 5.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 630 LNTLLQRYKAQLLHTCTGPDLIVLQPRG--------PSVPSAGKVPKGRRDGLPaHIGSMAQRAYWAL----LNQRRDQS 697
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKsipllydvPGFDSQRKEEATASSPPP-HVFSIAERAYRAMkgvgKGQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 698 IVALGWSGAGKTTCCEQVLEHLV-------GMAGSVDGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLD 766
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLAtasklakGASTSKGAANAHESIEECVllsnLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 767 FNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFA 846
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgackvgrkqfmRFEwANYAAEALGCEYEELNTATFKHHLRQIIQQMTF 926
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNV-----------RFE-ENADDEDVFAQSADGVNVAKAAGLLGVDAAELM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 927 GPSRWgledEETSSG------LKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSSH----HLSMAS------IMVVD 987
Cdd:cd14892 310 FKLVT----QTTSTArgsvleIKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 988 SPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFDlpDPSPgtTVAVVDQNPSqq 1063
Cdd:cd14892 386 IFGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ--DNQD--CLDLIQKKPL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1064 vrlpagggaqdarGLFWVLDEEVHV-EGSSDSVVLERLCAAFEKKGAgtegssalrTCEQP-LQCEIF---HQLGwdPVR 1138
Cdd:cd14892 453 -------------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHP---------HYAKPrFECDEFvlrHYAG--DVT 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1139 YDLTGWLhrAKPNLSaldapqvLHqskrEELRSLfqaraklppvcravaglegtsqqaLQRSRMVRRtfasslaavrrka 1218
Cdd:cd14892 509 YDVHGFL--AKNNDN-------LH----DDLRDL------------------------LRSSSKFRT------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1219 pcsqiklQMDALTSMIKRSRLHFIHCLVPNPVvesrsgqespppPQPGrdkpGAGGPLALDipalrvQLAGFHILEALRL 1298
Cdd:cd14892 539 -------QLAELMEVLWSTTPSYIKCIKPNNL------------KFPG----GFSCELVRD------QLIYSGVLEVVRI 589
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 1299 HRTGYADHMGLTRFRRQFQVLDAPLLKKLMS--TSEGIDERKAVeELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNKAGVAASpdACDATTARKKC-EEIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
674-1364 |
2.29e-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: 167.34 E-value: 2.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 674 LPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKIR----ATFTVLRAFGSVS 749
Cdd:cd01378 52 VPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIA--AVSGGSESEVERVKdmllASNPLLEAFGNAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 750 MAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ--------- 820
Cdd:cd01378 130 TLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpeqyyyysk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 821 --------MADSSSFgmgvwskpedkqkaaaafAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGR 885
Cdd:cd01378 210 sgcfdvdgIDDAADF------------------KEVLNAMKVIGFTEEEQDSIFRILAAILHLGniqfaedEEGNAAISD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 886 KQFMRFewanyAAEALGCEYEELNTA-TFkhhlRQIIqqmtfgpSRWGlEDEETSSGLKMTGVDCV-EGMASGLYQELFA 963
Cdd:cd01378 272 TSVLDF-----VAYLLGVDPDQLEKAlTH----RTIE-------TGGG-GRSVYEVPLNVEQAAYArDALAKAIYSRLFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 964 AVVSLINRSFSSHHLSMASIM-VVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---P 1039
Cdd:cd01378 335 WIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS------FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1040 VQF-------DLpdpspgttvavVDQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEG-SSDSVVLERLCAAFEKKGAGT 1111
Cdd:cd01378 409 IKYfnnkiicDL-----------IEEKP---------------PGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1112 EGSSALrtcEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravagLE 1190
Cdd:cd01378 463 CPSGHF---ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDLLFK-DLKELMQSSSNPFLRSLF---------------PE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1191 GTSQQALQRSrmvrrTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgrdkp 1270
Cdd:cd01378 522 GVDLDSKKRP-----PTAG-----------TKFKNSANALVETLMKKQPSYIRCIKPN---DNKS--------------- 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1271 gaggPLALDIPALRVQLAGFHILEALRLHRTGYAdhmgltrFRRQFqvlDAPLLK-KLMS--TS---EGIDeRKAVEELL 1344
Cdd:cd01378 568 ----PGEFDEELVLHQVKYLGLLENVRVRRAGFA-------YRQTY---EKFLERyKLLSpkTWpawDGTW-QGGVESIL 632
|
730 740
....*....|....*....|
gi 1034629688 1345 ETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd01378 633 KDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
628-1248 |
3.19e-42 |
|
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: 166.68 E-value: 3.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 703
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 704 SGAGKTTCCEQVLEHLVGMaGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLL 783
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 784 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTE---LNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 861 EQRAVWRVLAAIYHLG-------AAGACKVGRKQFMRFEWANYAAEALGCEYEElntatfkhhlrqiiqqmtfgpsrwgL 933
Cdd:cd01379 241 EVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADE-------------------------L 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 934 EDEETSSGLKMTG------------VDCVEGMASGLYQELFAAVVSLINR--SFSSHHLSMA-SIMVVDSPGFQNPRHQg 998
Cdd:cd01379 296 QEALTSHSVVTRGetiirnntveeaTDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 999 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQQVRLpagggaQDARGL 1078
Cdd:cd01379 375 -----SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVD----------LIEYEDNRPLLDMFL------QKPMGL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1079 FWVLDEEVHVEGSSDSVVLERlcaaFEKkgaGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAP 1158
Cdd:cd01379 434 LALLDEESRFPKATDQTLVEK----FHN---NIKSKYYWRPKSNALSFGIHHYAG--KVLYDASGFLEKNRDTLPP-DVV 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1159 QVLHQSKreelrslfqaraklppvcravaglegtsqqalqrSRMVRRTFAS----SLaavrrkapcsqiklqMDALTSMI 1234
Cdd:cd01379 504 QLLRSSE----------------------------------NPLVRQTVATyfrySL---------------MDLLSKMV 534
|
650
....*....|....
gi 1034629688 1235 KrSRLHFIHCLVPN 1248
Cdd:cd01379 535 V-GQPHFVRCIKPN 547
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
627-1248 |
4.74e-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: 163.19 E-value: 4.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-SVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQIlPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 780
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 781 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwSKPEDKQKAAAAFAQLQGAMEMLGISES 860
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGN-CLTCEGRDDAAEFADIRSAMKVLMFTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 861 EQRAVWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANYAAEALGCEYEELNTATFKHHLrqiiqqMTFGpsr 930
Cdd:cd01381 236 EIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTI------FTRG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 931 wgledEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSF---SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd01381 302 -----ETVVSPLSAEQaLDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSQQVRlpagggAQDARGLFWVLDEEV 1086
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQH----------IEFVDNQDVLDLI------ALKPMNIMSLIDEES 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1087 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1166
Cdd:cd01381 435 KFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT-----SFGINHFAG--VVFYDTRGFLEKNRDTFSA-DLLQLVQSSKN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1167 EELRSLFQAraklppvCRAvAGLEGtsqqalqrsrmvrrtfasslaavRRKAP--CSQIKLQMDALTSMIKRSRLHFIHC 1244
Cdd:cd01381 507 KFLKQLFNE-------DIS-MGSET-----------------------RKKSPtlSSQFRKSLDQLMKTLSACQPFFVRC 555
|
....
gi 1034629688 1245 LVPN 1248
Cdd:cd01381 556 IKPN 559
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
628-1364 |
5.30e-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: 163.30 E-value: 5.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvyNPEVVEGYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAAFAQLQ 849
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEilvASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 929
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKALCF--P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 RWGLEDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14913 305 RVKVGNEYVTKGQTVDQVHhAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLpdpspGTTVAVVdqnpsqqVRLpagggAQDARGLFWVLDEEVH 1087
Cdd:cd14913 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC-------IEL-----IEKPMGIFSILEEECM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1088 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKRE 1167
Cdd:cd14913 442 FPKATDTSFKNKLYDQHLGKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKSSNR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1168 ELRSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCL 1245
Cdd:cd14913 518 LLAHLYAtfATADADSGKKKVAKKKGSSFQ--------------TVSALFRE--------NLNKLMSNLRTTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1246 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1325
Cdd:cd14913 576 IPN---ETKT-------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629688 1326 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14913 634 E----GQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
627-1364 |
1.22e-40 |
|
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: 162.50 E-value: 1.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKYLPIYSEEIVNmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQL 848
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPgqQDK----ELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 849 QGAMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFG 927
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNM-SFKKERNSDQASMPDDTAAQKV-CHLLGMNVTDFT---RAILSpRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 928 psRWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFE 1006
Cdd:cd14932 311 --RDYVQKAQTQEQAEFA----VEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqqvrlPAGggaqdARGLFWVLD 1083
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQP--CIELIEK--------PNG-----PPGILALLD 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1084 EEVHVEGSSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSALD--APQVL 1161
Cdd:cd14932 443 EECWFPKATDKSFVEKVV---QEQGNNPKFQKPKKLKDDADFC-IIHYAG--KVDYKANEWLMK---NMDPLNenVATLL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1162 HQSKREELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHF 1241
Cdd:cd14932 514 NQSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVG------------QLYKEQLMNLMTTLRNTNPNF 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1242 IHCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1321
Cdd:cd14932 581 VRCIIPNH--EKKAGKLAH--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 638
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 1034629688 1322 PLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14932 639 NAIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
628-1316 |
1.52e-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: 162.75 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP--SVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALL-NQR 693
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPlpDLYSESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 694 RDQSIVALGWSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADS---SSFGMGVWSKPEDKQKAA 842
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 843 AAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANyAAEALGCEYEELNTATFKH 915
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 916 HLRQIIQQMTFGPSRWGLEDEETSsglkmtgvdcvegMASGLYQELFAAVVSLIN---------RSFSSHHLSMASIMVV 986
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGS-------------LAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 987 DSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqqvrl 1066
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWK-NISYPSNAACLALFDDKSN----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1067 pagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagtegssalrtceqplQCEIFHQLGwdPVRYDLTGWLH 1146
Cdd:cd14902 456 ----------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAG--RVCYNVEQFVE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1147 RAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEgtsqqalQRSRMVRrtfASSLAAvrrkapcsQIKLQ 1226
Cdd:cd14902 508 KNTDALPA-DASDILSSSSNEVVVAIGADENRDSPGADNGAAGR-------RRYSMLR---APSVSA--------QFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1227 MDALTSMIKRSRLHFIHCLVPNPVvesrsgqesppppqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADH 1306
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEV----------------------KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVR 626
|
730
....*....|
gi 1034629688 1307 MGLTRFRRQF 1316
Cdd:cd14902 627 LAHASFIELF 636
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
627-1364 |
2.05e-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: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPS-AGKVPKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPykRYPVYTNrCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-HQMADSSSFGMGVWSKPedKQKAAAAFAQLQGAMEM 854
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVP--NVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 855 LGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMR---FEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRw 931
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 932 gleDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHN 1011
Cdd:cd14909 318 ---QQVTNS---------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1012 YAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLpdpspgttVAVVDQnpsqqvrlpagggAQDARGLFWVLDEEV 1086
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL-------------IEKPMGILSILEEES 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1087 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldaPQVLHQSKR 1166
Cdd:cd14909 439 MFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAG--CVSYNITGWLEKNKDPLN----DTVVDQFKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1167 EELRSLFQARAKLPPVCRAVAGLEGTsqqalqrsrmvRRTFASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLV 1246
Cdd:cd14909 513 SQNKLLIEIFADHAGQSGGGEQAKGG-----------RGKKGGGFATVS-----SAYKEQLNSLMTTLRSTQPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1247 PNPVvesrsgqespppPQPGrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1326
Cdd:cd14909 577 PNEM------------KQPG----------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQG 634
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629688 1327 LMstsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14909 635 EE------DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
628-1303 |
2.37e-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: 161.26 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKGRrDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESE 861
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 862 QRAVWRVLAAIYHLGAAGACKVGRK--QFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQQmtfgpsrwgledeETS 939
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEALCN---RSVVTR-------------NES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 940 SGLKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSS-HHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHE 1015
Cdd:cd14904 304 VTVPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1016 RLQLLFYQRTFVSTLQRYQEEGvpVQFD-LPDPSPGTTVAVVDQNpsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDS 1094
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREG--LQWDhIEYQDNQGIVEVIDGK----------------MGIIALMNDHLRQPRGTEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1095 VVLERLCAAFEKKGAGT--EGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSL 1172
Cdd:cd14904 440 ALVNKIRTNHQTKKDNEsiDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTEL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1173 FQAraklppvcravagLEGTSQQALQRSRmvRRTFAsslaavrRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvE 1252
Cdd:cd14904 512 FGS-------------SEAPSETKEGKSG--KGTKA-------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPN---A 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 1253 SRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGY 1303
Cdd:cd14904 567 NKS-------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
627-1364 |
3.37e-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: 160.96 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAG----KVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPY-KWLPIYGarvaNMYKGKkRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 776
Cdd:cd14934 80 GESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 777 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSF-----GMGVWSKPEDkqkaAAAFAQLQGA 851
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYhwvsqGVTVVDNMDD----GEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 852 MEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELntatfkhhlrqiiqQMTFGP 928
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGEL--------------QKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 929 SRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEE 1007
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCnNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1008 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEVH 1087
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVF-------------IDFGLDLQACIDL---LEKPMGIFSILEEQCV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1088 VEGSSDSVV--------LERLCAAFEKKGAGTEGSSAlrtceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapq 1159
Cdd:cd14934 438 FPKATDATFkaalydnhLGKSSNFLKPKGGKGKGPEA--------HFELVHYAG--TVGYNITGWLEKNKDPLN------ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1160 vlhqskrEELRSLFQARAKLppVC----RAVAGLEGTSQQALQRSRMVRRTFasslaavrrkapcsqIKLQMDALTSMIK 1235
Cdd:cd14934 502 -------ETVVGLFQKSSLG--LLallfKEEEAPAGSKKQKRGSSFMTVSNF---------------YREQLNKLMTTLH 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1236 RSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1315
Cdd:cd14934 558 STAPHFVRCIVPNEFKQSG----------------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 1034629688 1316 FQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14934 616 YQVLNPNVIPQGF-----VDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
627-1364 |
4.18e-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: 160.53 E-value: 4.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 700
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKwlpvyqKEVMAAYK--GKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 701 LGWSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 776
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 777 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGldldlrtELNLHQM----ADSSSFGM---GVWSKpeDKQKAAAAFAQLQ 849
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSG-------KKELRDLllvsANPSDFHFcscGAVAV--ESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 929
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFG-----NMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKGLIH--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14929 299 RIKVGNEYVTRSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEG---VPVQFDLpdpspgTTVAVVDQnpsqqvrlpagggAQDARGLFWVLDEE 1085
Cdd:cd14929 373 CINFTNEKLQQFFNQHMFVLEQEEYRKEGidwVSIDFGL------DLQACIDL-------------IEKPMGIFSILEEE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1086 VHVEGSSDSVVLERLC-AAFEKKGAGTEGSSALRTCEqpLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSAlDAPQVLHQS 1164
Cdd:cd14929 434 CMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNKDLLNE-TVVAVFQKS 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1165 KREELRSLFQARAklppvcravaglegTSQQALQRSRMVRRTFASSlaavrrKAPCSQIKLQMDALTSMIKRSRLHFIHC 1244
Cdd:cd14929 509 SNRLLASLFENYI--------------STDSAIQFGEKKRKKGASF------QTVASLHKENLNKLMTNLKSTAPHFVRC 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1245 LVPNPvvesrsgqesppppqpgRDKPGAGGP-LALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDApl 1323
Cdd:cd14929 569 INPNV-----------------NKIPGVLDPyLVLQ------QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP-- 623
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1034629688 1324 lkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14929 624 --RTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1364 |
4.81e-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: 160.64 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQLQGAMEML 855
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPgqQDK----DMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 856 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALGcEYEELNTATFKHHLrqIIQQMTFGpsrwglED 935
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNI-VFKKERNTDQASMPDNTAAQKVS-HLLGINVTDFTRGI--LTPRIKVG------RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 936 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNYAH 1014
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1015 ERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPdpspgttvavVDQNPS-QQVRLPAGggaqdARGLFWVLDEEVHVEGSS 1092
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEWNFiDFG----------LDLQPCiDLIEKPAG-----PPGILALLDEECWFPKAT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1093 DSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELR 1170
Cdd:cd14919 445 DKSFVEKV---VQEQGTHPKFQKPKQLKDKADFC-IIHYAG--KVDYKADEWLMK---NMDPLndNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1171 SLFQARAKlppvcraVAGLE---GTSQQALQRSRMVRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1247
Cdd:cd14919 516 ELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1248 NPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1327
Cdd:cd14919 581 NH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629688 1328 MstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14919 639 F-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
629-1364 |
2.91e-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: 157.97 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 629 VLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 851
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 852 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 931
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 932 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd14918 307 KVGNEYVTKGQTVQQVyNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEVHVEG 1090
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK----------------PLGIFSILEEECMFPK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1091 SSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQ-SKREEL 1169
Cdd:cd14918 445 ATDTSFKNKLYDQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLN--DTVVGLYQkSAMKTL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1170 RSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1247
Cdd:cd14918 520 ASLFStyASAEADSGAKKGAKKKGSSFQ--------------TVSALFRE--------NLNKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1248 NpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKl 1327
Cdd:cd14918 578 N---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE- 634
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629688 1328 mstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14918 635 ---GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
628-1248 |
3.05e-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: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP----RGPSVPSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyfdiPKLYSSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLH--QMADSSSFGmgvwskpedkqkaaaafaQLQGAMEMLGISES 860
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKdpLLDDVGDFI------------------RMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 861 EQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanYAAEALGCEYEELntatfKHHLRQIIQQMTFGPS- 929
Cdd:cd01382 222 EKLDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 ----RWGLEDEETSSGLkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSShhlSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd01382 294 gtviKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVD-QNPSQQVRLPAGggaqdarGLFWVL 1082
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVDnQDCIDLIEAKLV-------GILDLL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1083 DEEVHVEGSSD----SVVLE------RLCAAFEKKGAGTEgssALRTCEQPLqceIFHQLGwdPVRYDLTGWLHRakpNL 1152
Cdd:cd01382 420 DEESKLPKPSDqhftSAVHQkhknhfRLSIPRKSKLKIHR---NLRDDEGFL---IRHFAG--AVCYETAQFIEK---NN 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1153 SALDAP--QVLHQSKREELRSLFQARAKLPPVCRAVAGlegtsqqalqrsrmvRRTFASslaaVRRKapcsqIKLQMDAL 1230
Cdd:cd01382 489 DALHASleSLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FKTQLNLL 544
|
650
....*....|....*...
gi 1034629688 1231 TSMIKRSRLHFIHCLVPN 1248
Cdd:cd01382 545 MDKLRSTGTSFIRCIKPN 562
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
627-1364 |
3.07e-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: 157.95 E-value: 3.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSA-GKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPykQLPIYTEAiVEMYRGKkRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFT---VLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRkepgVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkaAAAFAQLQGAMEML 855
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE---RELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 856 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglED 935
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRAL--LTPRIKVG------RD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 936 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYAH 1014
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1015 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGS 1091
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPwtfLDFGL-DLQPCIDLIERPANPP---------------GLLALLDEECWFPKA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1092 SDSVVLERLCaafEKKGAGTEGSSAlRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKReelrs 1171
Cdd:cd14930 446 TDKSFVEKVA---QEQGGHPKFQRP-RHLRDQADFSVLHYAG--KVDYKANEWLMKNMDPLND-NVAALLHQSTD----- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1172 lfQARAKLPPVCRAVAGLEGTSQQAL-QRSRMVRRTFASSLAAVRRKApcsqiklqMDALTSMIKRSRLHFIHCLVPNPv 1250
Cdd:cd14930 514 --RLTAEIWKDVEGIVGLEQVSSLGDgPPGGRPRRGMFRTVGQLYKES--------LSRLMATLSNTNPSFVRCIVPNH- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1251 vESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMst 1330
Cdd:cd14930 583 -EKRAGKLEP--------------RLVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-- 639
|
730 740 750
....*....|....*....|....*....|....
gi 1034629688 1331 segIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14930 640 ---MDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
628-1364 |
1.00e-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: 156.42 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpvynAEVVAAYRGKK--RSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFAQLQ 849
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPS 929
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGN-----------MKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14917 305 RVKVGNEYVTKGQNVQQVIYATGaLAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEVHV 1088
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLQACIDL---IEKPMGIMSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1089 EGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1168
Cdd:cd14917 443 PKATDMTFKAKLFDNHLGKSNNFQKPRNIKG-KPEAHFSLIHYAGT--VDYNIIGWLQKNKDPLNE-TVVGLYQKSSLKL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1169 LRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMvrrtfaSSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14917 519 LSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHFVRCIIPN 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1249 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1328
Cdd:cd14917 579 ---ETKS-------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE-- 634
|
730 740 750
....*....|....*....|....*....|....*.
gi 1034629688 1329 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14917 635 --GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
629-1319 |
1.55e-38 |
|
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: 155.83 E-value: 1.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 629 VLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR-----RDGLPAHIGSMAQRAYWALLNQ----RRDQSIV 699
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKY-LHIYEKEVSQKykcekKSSLPPHIFAVADRAYQSMLGRlargPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 700 ALGWSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQL 778
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 779 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKpEDKQKAAAAFAQLQGAMEMLGIS 858
Cdd:cd14889 158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 859 ESEQRAVWRVLAAIYHLGA-------AGACKVGRKQfmrFEWANYAAEALGCEYEEL-----NTATF-------KHHLRQ 919
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNitfemddDEALKVENDS---NGWLKAAAGQFGVSEEDLlktltCTVTFtrgeqiqRHHTKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 920 IIQqmtfgpsrwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFS---SHHLSMASIMVVDSPGFQnprH 996
Cdd:cd14889 314 QAE-------------------------DARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---N 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 997 QGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQQVRLpagggaQDAR 1076
Cdd:cd14889 366 FAVNR---FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWK----------EITYKDNKPILDLFL------NKPI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1077 GLFWVLDEEVHVEGSSDSVVLERLCAAFekKGAGTEGSSALRTceqPLqCEIFHQLGwdPVRYDLTGWLHRAKPNLSAld 1156
Cdd:cd14889 427 GILSLLDEQSHFPQATDESFVDKLNIHF--KGNSYYGKSRSKS---PK-FTVNHYAG--KVTYNASGFLEKNRDTIPA-- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1157 apqvlhqSKREE-LRSLFQARAKLPPVCRAVAGLEGTSQQALQRSrmvrrtfASSLAAVRRKAPCSQIKLQMDALTSMIK 1235
Cdd:cd14889 497 -------SIRTLfINSATPLLSVLFTATRSRTGTLMPRAKLPQAG-------SDNFNSTRKQSVGAQFKHSLGVLMEKMF 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1236 RSRLHFIHCLVPNPVvesrsgqespppPQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1315
Cdd:cd14889 563 AASPHFVRCIKPNHV------------KVPGQ----------LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAER 620
|
....
gi 1034629688 1316 FQVL 1319
Cdd:cd14889 621 YKIL 624
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
629-1058 |
2.63e-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: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 703
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfkRLPHLYDAHMMEqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 704 SGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGMGVWSKPEDkqkaaaaFAQLQGAMEML 855
Cdd:cd01384 163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 856 GISESEQRAVWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANyAAEALGCEYEELNTATFKhhlRQIIqqmtfg 927
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVIV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 928 psrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQnprhQGKDRaaTFE 1006
Cdd:cd01384 305 -----TPDGIITKPLDPDAaTLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKTN--SFE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-------DLPDPSPGTTVAVVDQ 1058
Cdd:cd01384 374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKPGGIIALLDE 435
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
627-1364 |
2.80e-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: 155.11 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 700
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYK--GKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 701 LGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT-------------VLRAFGSVSMAHSRSATRFSMVMSLDF 767
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 768 NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAA 844
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVttvDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 845 FAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQfmRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQM 924
Cdd:cd14927 235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNM---KFKQKQ--REE----QAEADGTESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 925 TFGPSRWGleDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVyAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqqvrlpagggAQDARGL 1078
Cdd:cd14927 378 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL-------------IEKPLGI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1079 FWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSALDAP 1158
Cdd:cd14927 437 LSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVP--YNIVGWLDKNKDPLNETVVA 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1159 qVLHQSKREELRSLFQARAKLPPVCRAVAGLEGtsqqalqrsrmvRRTFASSLAAVrrkapcSQI-KLQMDALTSMIKRS 1237
Cdd:cd14927 515 -IFQKSQNKLLATLYENYVGSDSTEDPKSGVKE------------KRKKAASFQTV------SQLhKENLNKLMTNLRAT 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1238 RLHFIHCLVPNpvvESRSgqesppppqpgrdkPGAGGPLaLDIPALRVQlagfHILEALRLHRTGYADHMGLTRFRRQFQ 1317
Cdd:cd14927 576 QPHFVRCIIPN---ETKT--------------PGVMDPF-LVLHQLRCN----GVLEGIRICRKGFPNRILYADFKQRYR 633
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1034629688 1318 VLDAPLLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14927 634 ILNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
628-1364 |
3.15e-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: 154.89 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFA 846
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEitvPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTF 926
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKALCY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 927 gpSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 1005
Cdd:cd14915 306 --PRVKVGNEYVTKGQTVQQVyNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEE 1085
Cdd:cd14915 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1086 VHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqsk 1165
Cdd:cd14915 442 CMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN------------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1166 rEELRSLFQaRAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAS--SLAAVRRKapcsqiklQMDALTSMIKRSRLHFIH 1243
Cdd:cd14915 507 -ETVVGLYQ-KSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSfqTVSALFRE--------NLNKLMTNLRSTHPHFVR 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1244 CLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPL 1323
Cdd:cd14915 577 CLIPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1034629688 1324 LKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14915 635 IPE----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
628-1364 |
3.28e-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: 154.57 E-value: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEqySRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 775
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 776 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL------NLHQMADSssfgmGVWSkpEDKQKAAAAFAQLQ 849
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVE--DKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNYAAEALGCEYEELNTAtfkhhlrqIIQQM 924
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDA--------LTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 925 TFgpsrwgLEDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHlSMASIMVVDSPGFQNPRHQgkdraa 1003
Cdd:cd14873 302 MF------LRGEEILTPLNVqQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1004 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPSPGTTVAVVDQNpsqqvrlpagggaqdaRGLFWVLD 1083
Cdd:cd14873 369 HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGL-VWEDIDWIDNGECLDLIEKK----------------LGLLALIN 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1084 EEVHVEGSSDSVVLERLcaafekKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQ 1163
Cdd:cd14873 432 EESHFPQATDSTLLEKL------HSQHANNHFYVKPRVAVNNFGVKHYAG--EVQYDVRGILEKNRDTFRD-DLLNLLRE 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1164 SKREELRSLFQARAKlppvcravAGLEGTSQQALQRsrmvrrtfasslaavRRKAPCSQIKLQMDALTSMIKRSRLHFIH 1243
Cdd:cd14873 503 SRFDFIYDLFEHVSS--------RNNQDTLKCGSKH---------------RRPTVSSQFKDSLHSLMATLSSSNPFFVR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1244 CLVPNpvVESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYAdhmgltrFRRQFQvldaPL 1323
Cdd:cd14873 560 CIKPN--MQKMPDQFDQ--------------AVVLN------QLRYSGMLETVRIRKAGYA-------VRRPFQ----DF 606
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1034629688 1324 LKKLMSTSEGI----DERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14873 607 YKRYKVLMRNLalpeDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
628-1364 |
8.52e-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: 153.73 E-value: 8.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFA 846
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYDYPFVSQGEISVASiddQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 847 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEElnTATFKHHLRQIIQQMTF 926
Cdd:cd14912 235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREE----QAEPDGTEVAD--KAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 927 GPSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 1005
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVtNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1006 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEE 1085
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK----------------PMGIFSILEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1086 VHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAldapQVLHQSK 1165
Cdd:cd14912 442 CMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE----TVVGLYQ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1166 REELRSLfqarAKLPPVCRAVAGlEGTSQQALQRSRMVRRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCL 1245
Cdd:cd14912 515 KSAMKTL----AYLFSGAQTAEG-ASAGGGAKKGGKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCI 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1246 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1325
Cdd:cd14912 581 IPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 638
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629688 1326 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14912 639 E----GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
628-1364 |
1.07e-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: 153.29 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 703
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVAAYRgkkRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 704 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAG-----LDLDLRTElNLHQMADSSSFGMGVWSKPEDKqkaaaAFAQ 847
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNkkpelLDMLLVTN-NPYDYAFVSQGEVSVASIDDSE-----ELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 848 LQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFG 927
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGN-----------MKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 928 PSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd14916 304 HPRVKVGNEYVTKGQSVQQVyYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEV 1086
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLQACIDL---IEKPMGIMSILEEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1087 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1166
Cdd:cd14916 442 MFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVVGLYQKSSL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1167 EELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMVRrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1246
Cdd:cd14916 518 KLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTHPHFVRCII 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1247 PNPvvesrsgqesppppqpgRDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1326
Cdd:cd14916 579 PNE-----------------RKAPG-----VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 636
|
730 740 750
....*....|....*....|....*....|....*...
gi 1034629688 1327 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14916 637 ----GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
628-1036 |
2.74e-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: 2.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRY-KAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvPKGRRDglPaHIGSMAQRAYWALLNQRRDQSI 698
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPyedlpiYGEDIIQAysGQ-NMGELD--P-HIFAIAEEAYRQMARDEKNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 699 VALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd01380 78 IVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqmADSSSF---GMGvwSKPE-DKQKAAAAFAQLQGAME 853
Cdd:cd01380 158 MRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL---GSAEDFfytNQG--GSPViDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 854 MLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFEWA---NYAAEALGCEYEElntatFKHHL-RQIIQQMTfgps 929
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDehlQIACELLGIDESQ-----LAKWLcKRKIVTRS---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 rwgledEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MASIMVVDSPGFQ----Nprhqgkdra 1002
Cdd:cd01380 304 ------EVIVKPLTLQqAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN--------- 368
|
410 420 430
....*....|....*....|....*....|....
gi 1034629688 1003 aTFEELCHNYAHERLQLLFYQRTFvstlQRYQEE 1036
Cdd:cd01380 369 -SFEQFCINYANEKLQQQFNQHVF----KLEQEE 397
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
628-1364 |
3.30e-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: 151.81 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 703
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVTAYRgkkRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 704 SGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 772
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 851
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 852 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 931
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 932 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 1010
Cdd:cd14910 309 KVGNEYVTKGQTVQQVyNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1011 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEVHVEG 1090
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEECMFPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1091 SSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1168
Cdd:cd14910 447 ATDTSFKNKL---YEQHLGKSNNFQKPKPAKGKVEAHfsLIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1169 LRSLFQARAKLPpvCRAVAGLEGTSQQAlqrsrmvrRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14910 521 LALLFSGAAAAE--AEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPN 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1249 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1328
Cdd:cd14910 582 ---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE-- 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 1034629688 1329 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14910 638 --GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
627-1364 |
5.12e-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: 151.37 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQG 850
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQ--DKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 851 AMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFGps 929
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNM-SFKKERHTDQASMPDNTAAQKV-CHLMGMNVTDFT---RAILSpRIKVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 930 RWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEEL 1008
Cdd:cd15896 311 RDYVQKAQTQEQAEFA----VEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFEQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPdpspgttvavVDQNPS-QQVRLPAgggaqDARGLFWVLDEEV 1086
Cdd:cd15896 381 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFiDFG----------LDLQPCiDLIEKPA-----SPPGILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1087 HVEGSSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1166
Cdd:cd15896 446 WFPKATDKSFVEKV---LQEQGTHPKFFKPKKLKDEADFC-IIHYAG--KVDYKADEWLMKNMDPLND-NVATLLNQSTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1167 EELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTfasslaavrrkapcSQI-KLQMDALTSMIKRSRLHFIHCL 1245
Cdd:cd15896 519 KFVSELWKDVDRIVGLDK-VSGMSEMPGAFKTRKGMFRTV--------------GQLyKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1246 VPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1325
Cdd:cd15896 584 IPNH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP 641
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629688 1326 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd15896 642 KGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
628-1364 |
4.06e-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: 148.29 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMA-----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 770
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 771 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFAQ 847
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEvtvASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 848 LQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFg 927
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGLCC- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 928 pSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 1006
Cdd:cd14923 305 -PRVKVGNEYVTKGQNVQQVtNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1007 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEV 1086
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1087 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQSKR 1166
Cdd:cd14923 442 MFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN--ETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1167 EELRS-LFQARAKlppvcrAVAGLEGTSQQALQRsrmvRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCL 1245
Cdd:cd14923 517 LKLLSfLFSNYAG------AEAGDSGGSKKGGKK----KGSSFQTVSAVFRE--------NLNKLMTNLRSTHPHFVRCL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1246 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1325
Cdd:cd14923 579 IPN---ETKT-------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
730 740 750
....*....|....*....|....*....|....*....
gi 1034629688 1326 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14923 637 E----GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
593-1401 |
1.02e-35 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 148.64 E-value: 1.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 593 DKTITEVDEEHVHRANPP-ELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR 670
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 671 R----DGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV-GMAGSVDGRVSvEKIRATFTVLRAF 745
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQ-NAIMAANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 746 GSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--- 822
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEeyk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 823 -------------DSSSFGMGVWSkpedkqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLGAA----------- 878
Cdd:PTZ00014 314 yinpkcldvpgidDVKDFEEVMES------------------FDSMGLSESQIEDIFSILSGVLLLGNVeiegkeegglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 879 -GACKVGRKQfmrfEWANYAAEALGCEYEELntatfKHHLrqIIQQMTFGP----SRWGLEDEETSsglkmtgvdcVEGM 953
Cdd:PTZ00014 376 dAAAISDESL----EVFNEACELLFLDYESL-----KKEL--TVKVTYAGNqkieGPWSKDESEML----------KDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 954 ASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVST 1029
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1030 LQRYQEEGVPvqfdlpdpspgtTVAVVDQNPSQQVRLPAGGGaqdaRGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKga 1109
Cdd:PTZ00014 505 SKLYKDEGIS------------TEELEYTSNESVIDLLCGKG----KSVLSILEDQCLAPGGTD----EKFVSSCNTN-- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1110 gTEGSSALRTCE--QPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrava 1187
Cdd:PTZ00014 563 -LKNNPKYKPAKvdSNKNFVIKHTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF-------------- 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1188 glEGtsqQALQRSRMVRRTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgr 1267
Cdd:PTZ00014 625 --EG---VEVEKGKLAKGQLIG-----------SQFLNQLDSLMSLINSTEPHFIRCIKPN---ENKK------------ 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1268 dkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLlkklmSTSEGIDERKAVEELLETL 1347
Cdd:PTZ00014 674 -------PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-----SNDSSLDPKEKAEKLLERS 741
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 1348 DLEKKAVAVGHSQVFLKAGVISRL-EKQREKLVS-QSIV-LFQAACKGFLSRQEFKK 1401
Cdd:PTZ00014 742 GLPKDSYAIGKTMVFLKKDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
628-1363 |
1.10e-35 |
|
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: 146.86 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-----------RGPSVPSAGKVPKGRRDgLPAHIGSMAQRAYWALLNQRR-- 694
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 695 --DQSIVALGWSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 766 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAF 845
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 846 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfMRFEWANYAAEALGCEYEELNTATFKHHL--RQIIQQ 923
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 924 MTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSSHHLSMASIMVVDSPGF----QNprhq 997
Cdd:cd14901 320 GEYITMPLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 998 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarG 1077
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF-VEYPNNDACVAMFEARPT---------------G 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1078 LFWVLDEEVHVEGSSDsvvlERLCAAFekkgagtegssalrtceqplqceifhqlgwdpvrYDLTGwlhrAKPNLSAlda 1157
Cdd:cd14901 444 LFSLLDEQCLLPRGND----EKLANKY----------------------------------YDLLA----KHASFSV--- 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1158 pqvlhqSKREELRSLFQARAKLPPVCRAVAGL-----EGTSQQALQRSRMVRRTFASSLAAvrrkapcSQIKLQMDALTS 1232
Cdd:cd14901 479 ------SKLQQGKRQFVIHHYAGAVCYATDGFcdknkDHVHSEALALLRTSSNAFLSSTVV-------AKFKVQLSSLLE 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1233 MIKRSRLHFIHCLVPNPVVESRSgqesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRF 1312
Cdd:cd14901 546 VLNATEPHFIRCIKPNDVLSPSE----------------------FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 1313 RRQFQVLDAPLLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1363
Cdd:cd14901 604 VHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
627-1248 |
1.61e-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: 146.33 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALLNQR 693
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykQIDNLFSEEVMqmykeqiiqngEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 694 RDQSIVALGWSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRS 755
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 756 ATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSFGMGVWSK 834
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL--KNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 835 PE----DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRfewanYAAEA 900
Cdd:cd14907 239 SNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ-----IIAKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 901 LGCEYEELNTA-TFKhhLRQIIQQMTFGPsrwgledeetssglkMTGVDCV---EGMASGLYQELFAAVVSLINRSFSSH 976
Cdd:cd14907 314 LGIDEEELKEAlTTK--IRKVGNQVITSP---------------LSKKECInnrDSLSKELYDRLFNWLVERLNDTIMPK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 977 HLS--------MASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLP 1045
Cdd:cd14907 377 DEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylNQLSYT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1046 DPSPgtTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAafekkgagTEGSSALRTCEQPLQ 1125
Cdd:cd14907 451 DNQD--VIDLLDKPPI---------------GIFNLLDDSCKLATGTDEKLLNKIKK--------QHKNNSKLIFPNKIN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1126 CEIF---HQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglEGTSQQALQRSRM 1202
Cdd:cd14907 506 KDTFtirHTAK--EVEYNIEGFREKNKDEIS-QSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQSKQK 568
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1034629688 1203 VRRtfasslaaVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14907 569 KSQ--------KKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPN 606
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
628-1364 |
9.85e-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: 144.44 E-value: 9.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSV-PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 703
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKflPIYnPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 704 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 781
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 782 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGmgvwskpEDKQKAAAAFAQLQGAMEML 855
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 856 GISESEQRAVWRVLAAIYHLgaagackvGRKQFMRfeWANYAAEALGCEYEE-LNTATfkhHLRQIIQQMtfgpsrwgLE 934
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIIS---ELLRVKEET--------LL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 935 DEETSSGLKMTGVDCV------------EGMASGLYQELFAAVV-----SLINRSFSSHHlSMASIMVVDSPGFQNPRHQ 997
Cdd:cd01385 292 EALTTKKTVTVGETLIlpyklpeaiatrDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 998 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVDQNPSqqvrlpagggaqdar 1076
Cdd:cd01385 371 ------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISwHNIEYTDNT--GCLQLISKKPT--------------- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1077 GLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegssalRTCEQPLQCE----IFHQLGwdPVRYDLTGWLHRAKPNL 1152
Cdd:cd01385 428 GLLCLLDEESNFPGATNQTLLAKFKQQHKDN----------KYYEKPQVMEpafiIAHYAG--KVKYQIKDFREKNLDLM 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1153 SAlDAPQVLHQSK----RE-------------ELRSLFQARAKLPPVCRA----VAGLEGTSQQALQRSRMVRRTfassl 1211
Cdd:cd01385 496 RP-DIVAVLRSSSsafvREligidpvavfrwaVLRAFFRAMAAFREAGRRraqrTAGHSLTLHDRTTKSLLHLHK----- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1212 aavRRKAPCSQIKLQ--MDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAG 1289
Cdd:cd01385 570 ---KKKPPSVSAQFQtsLSKLMETLGQAEPFFIRCIKSN------------------AEK----KPLRFDDELVLRQLRY 624
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629688 1290 FHILEALRLHRTGYADHMGLTRFRRQFQVLdapLLKKLMSTSEGIderkavEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVL---LPKGLISSKEDI------KDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
627-1303 |
4.47e-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: 138.73 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAtGRITAAQLQTML 782
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVT-EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---------HQMADSSSFGMGvwskpedkqkAAAAFAQLQGAME 853
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLqeaekyfylNQGGNCEIAGKS----------DADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 854 MLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMRfewanYAAEALGCEYEELNTA-TFKhhLRQII 921
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGnvyfhkrqlrhGQEGVSVGSDAEIQ-----WVAHLLQISPEGLQKAlTFK--VTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 922 QQMTFGPsrwgLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 1001
Cdd:cd01387 302 RERIFTP----LTIDQ--------ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1002 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGTTVAVVDQNPSQQVRlpagggAQDARGLFWV 1081
Cdd:cd01387 366 --SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPVINLI------SKKPVGILHI 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1082 LDEEVHVEGSSDSVVLERlCaafEKKGAGTEGSSALRTCEQPLQceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVL 1161
Cdd:cd01387 428 LDDECNFPQATDHSFLEK-C---HYHHALNELYSKPRMPLPEFT--IKHYAG--QVWYQVHGFLDKNRDQLRQ-DVLELL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1162 HQSKREELRSLF-----QARAKLPpvcravAGLEGTSQQALQRSRMVRRTFASSLaavrrkapcsqiklqMDALTSMikr 1236
Cdd:cd01387 499 VSSRTRVVAHLFsshraQTDKAPP------RLGKGRFVTMKPRTPTVAARFQDSL---------------LQLLEKM--- 554
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 1237 SRLH--FIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAGFHILEALRLHRTGY 1303
Cdd:cd01387 555 ERCNpwFVRCLKPN------------------HKK----EPMLFDMDVVMAQLRYSGMLETIRIRKEGY 601
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
627-1319 |
1.84e-31 |
|
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: 133.75 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP----SVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSlplfSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQTML 782
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 783 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSF----GMGVWSKPEDKqkaaAAFAQLQGAMEMLGIS 858
Cdd:cd14896 159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDA----QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 859 ESEQRAVWRVLAAIYHLGaaGACkvgrkqFMRFEWANYAAEALGCEYEELNTATFKH----HLRQII-QQMTFGPSRWgl 933
Cdd:cd14896 234 AEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARLLQvppeRLEGAVtHRVTETPYGR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 934 edeeTSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFS--SHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCH 1010
Cdd:cd14896 304 ----VSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1011 NYAHERLQLLFYQRTFVSTLQRYQEE---GVPVqfdlPDPSPGTTVAVVDQNPsqqvrlpagggaqdaRGLFWVLDEEVH 1087
Cdd:cd14896 374 NLASERLQLFSSQTLLAQEEEECQREllpWVPI----PQPPRESCLDLLVDQP---------------HSLLSILDDQTW 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1088 VEGSSDSVVLErlcaafekKGAGTEGSSALRTCEQpLQCEIF---HQLGwdPVRYDLTGWLHRakpNLSALDaPQVLH-- 1162
Cdd:cd14896 435 LSQATDHTFLQ--------KCHYHHGDHPSYAKPQ-LPLPVFtvrHYAG--TVTYQVHKFLNR---NRDQLD-PAVVEml 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1163 -QSKREELRSLFQaraklppvcravaglEGTSQQALQRSRmvrrtfaSSLAavrrkapcSQIKLQMDALTSMIKRSRLHF 1241
Cdd:cd14896 500 aQSQLQLVGSLFQ---------------EAEPQYGLGQGK-------PTLA--------SRFQQSLGDLTARLGRSHVYF 549
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 1242 IHCLVPNPVvesrsgqesppppqpgrDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1319
Cdd:cd14896 550 IHCLNPNPG-----------------KLPG-----LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
628-1252 |
1.53e-30 |
|
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: 131.26 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALLNQRRDQSIVAL 701
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 702 GWSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT-G 771
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 772 RITAAQLQTMLLEKSRVARQPEGES-NFLVFSQMLAGLDLDLRTELNLHQMADS-----------SSF---GMGVWSKPE 836
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKyryldarddviSSFksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 837 DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEwanyaAEALGCEYEELnTATFKHH 916
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFE-----EDSDFSKYAYQ-KDKVTAS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 917 LRQIIQQMTFGPSRWglEDEETSSGLKMTGVDCV--------------EGMASGLYQELFAAVVSLINRSF----SSHHL 978
Cdd:cd14906 305 LESVSKLLGYIESVF--KQALLNRNLKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSNDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 979 SMAS-------IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGT 1051
Cdd:cd14906 383 AGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PWS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1052 TVAVVDQNPSQQVRlpagggAQDARGLFWVLDEEVHVEGSSDSVVLERlcaaFEKKGAGTEgSSALRTCEQpLQCEIFHQ 1131
Cdd:cd14906 447 NSNFIDNKECIELI------EKKSDGILSLLDDECIMPKGSEQSLLEK----YNKQYHNTN-QYYQRTLAK-GTLGIKHF 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1132 LGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPvcravaglegTSQQalqrsrmvRRTFASSL 1211
Cdd:cd14906 515 AG--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTK--------KQTQSNTV 573
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1034629688 1212 AavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVE 1252
Cdd:cd14906 574 S--------GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
675-1040 |
2.18e-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: 130.16 E-value: 2.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 675 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV--GMAGSVDGRVSVEKIRATFT------------ 740
Cdd:cd14891 55 PYAIAEMAYQQMCLGSGRMQNQSIVISGESGAGKTETSKIILRFLTtrAVGGKKASGQDIEQSSKKRKlsvtslderlmd 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 741 ---VLRAFGSVSMAHSRSATRFSMVMSLDFNATG-RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL 816
Cdd:cd14891 135 tnpILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 817 NLhqmadsssfgmgvwSKPEDKQKAAAAF-------------AQLQGAMEMLGISESEQRAVWRVLAAIYHLG------- 876
Cdd:cd14891 215 LL--------------LSPEDFIYLNQSGcvsddniddaanfDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdee 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 877 --AAGACKVGRKQFMrfEWANYAAEALGCEYEELntatfkhhLRQIIQQ--MTFGPSRWGLEDEETSSGLKmtgvdcvEG 952
Cdd:cd14891 281 dtSEGEAEIASESDK--EALATAAELLGVDEEAL--------EKVITQReiVTRGETFTIKRNAREAVYSR-------DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 953 MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQR 1032
Cdd:cd14891 344 IAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES-----FETKNDFEQLLINYANEALQATFNQQVFIAEQEL 418
|
....*...
gi 1034629688 1033 YQEEGVPV 1040
Cdd:cd14891 419 YKSEGIDV 426
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
677-1254 |
2.83e-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: 130.54 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 677 HIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKIRATFTVLRAFGSVSMAHS 753
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 754 RSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLdlrtelnlhqmadSSSFGMGVWS 833
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA-------------AATQKSSAGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 834 K-PEdkqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfmRFEWANYAAEALGC--------- 903
Cdd:cd14887 210 GdPE-----STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPE--TSKKRKLTSVSVGCeetaadrsh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 904 --EYEELN-----TATFKHHLRQIIQQMTFGPSRWGLED----------EETSSGLKMTGVDCVEGMAS-GLYQELFAAV 965
Cdd:cd14887 283 ssEVKCLSsglkvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 966 VSLINRSFSSHHLSMAS--------------IMVVDSPGFQNPRHQGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQ 1031
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1032 RYQEEGV---------PVQFDLPDPSPGTTVAVVDQNPSQQVRlpAGGGAQDARGLFWVLDEEVHVEGSSDSVVLERLCA 1102
Cdd:cd14887 440 LYTQEGVfqnqdcsafPFSFPLASTLTSSPSSTSPFSPTPSFR--SSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNS 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1103 --AFEKKGAGTEGSSALRTCEQPLQCE-----IFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskrEELRSLFQA 1175
Cdd:cd14887 518 dlFYEKLNKNIINSAKYKNITPALSREnleftVSHFAC--DVTYDARDFCRANREATS-------------DELERLFLA 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 1176 raklppvCRAVaglegTSQQALQRSRMVRrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESR 1254
Cdd:cd14887 583 -------CSTY-----TRLVGSKKNSGVR------AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
627-1332 |
1.08e-29 |
|
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: 128.01 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKVPKGRR-DGLPAHIGSMAQRAYWALLNQRRDQSIV 699
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPykelpiYSTMVSQLYLSSSGQLcSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 700 ALGWSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDF-NATGRITAAQ 777
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwskPEDKQKAAAAFAQLQ-----GAM 852
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM---REDVSTAERSLNREKlavlkQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 853 EMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNtatfkhhlrQIIQQMTFGPsrwg 932
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGD-----------IRFTALTEADSAFVSDLQLLE---------QVAGMLQVST---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 933 ledEETSSGLkMTGVDCVEG------------------MASGLYQELFAAVVSLINRSFSSHH----LSMASIMVVDSPG 990
Cdd:cd14878 292 ---DELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKSLYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 991 FQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLpdpSPGTTVAVVD---QNPSqqvrlp 1067
Cdd:cd14878 368 FEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAY---SPGNQTGVLDfffQKPS------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1068 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGT------EGSSALRTCEQPLQCEIFHQLGwdPVRYDL 1141
Cdd:cd14878 433 ---------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAvyspmkDGNGNVALKDQGTAFTVMHYAG--RVMYEI 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1142 TGWLHRAKPNLSaldapQVLhqskreelrsLFQARaklppvcravaglegTSQQALqrsrmVRRTFASSLAAVrrkapCS 1221
Cdd:cd14878 502 VGAIEKNKDSLS-----QNL----------LFVMK---------------TSENVV-----INHLFQSKLVTI-----AS 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1222 QIKLQMDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgrdkpGAGGPLALDIPALRVQLAGFHILEALRLHRT 1301
Cdd:cd14878 542 QLRKSLADIIGKLQKCTPHFIHCIKPN----------------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 599
|
730 740 750
....*....|....*....|....*....|...
gi 1034629688 1302 GYADHMGLTRFRRQFQVLDAPLL--KKLMSTSE 1332
Cdd:cd14878 600 GYPVRLSFSDFLSRYKPLADTLLgeKKKQSAEE 632
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
673-1316 |
3.35e-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: 126.85 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 673 GLPAHIGSMAQRAYWALLNQ-RRDQSIVALGWSGAGKTTCCEQVLEHLVGMA----GSVDGRVSVEKIRATFT----VLR 743
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDENLKwsnpVME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 744 AFGSVSMAHSRSATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL-NLHQM 821
Cdd:cd14875 133 SFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 822 AD------SSSF-GMGVWSKPEDKqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFE-- 892
Cdd:cd14875 213 QDykclngGNTFvRRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLME-----------VEFEsd 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 893 ------WANYAAEALGCEYEELNTATfkhhLRQIIqqmtfgpsrwgLEDEETSSGLKMTGVDCVEGM----ASGLYQELF 962
Cdd:cd14875 279 qndkaqIADETPFLTACRLLQLDPAK----LRECF-----------LVKSKTSLVTILANKTEAEGFrnafCKAIYVGLF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 963 AAVVSLINRSFSSHH--LSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPV 1040
Cdd:cd14875 344 DRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1041 -QFDLPDPSpgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRT 1119
Cdd:cd14875 418 pKIEFPDNS--ECVNMFDQKRT---------------GIFSMLDEECNFKGGTT----ERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1120 CEQPLQCEIFHQLGWdpVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELRSLFQARAKLPpvcravaglegtsqqal 1197
Cdd:cd14875 477 STIPNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA----------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1198 QRSRMVRRTFASSLAAVRrkapcsqiklqmdaltSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLA 1277
Cdd:cd14875 535 RRKQTVAIRFQRQLTDLR----------------TELESTETQFIRCIKPNMEAS----------------------PSF 576
|
650 660 670
....*....|....*....|....*....|....*....
gi 1034629688 1278 LDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1316
Cdd:cd14875 577 LDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
628-1038 |
1.15e-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: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGK--VPKGRRDGLPaHIGSMAQRAYWALLNQRrDQSIVALGWSG 705
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMkaYLKNYSHVEP-HVYDVAEASVQDLLVHG-NQTIVISGESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 706 AGKTTCCEQVLEHLV-GMAGSVdgrvSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNatGRITAAQLQTMLL 783
Cdd:cd14898 80 SGKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 784 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqmADSSSFGmgvwSKPEDKQKAAAAFAQLQGAMEMLGISESeqR 863
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCASKRLNIKNDF-----IDTSSTA----GNKESIVQLSEKYKMTCSAMKSLGIANF--K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 864 AVWRVLAAIYHLGAAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlrqiiqqmtfGPSRWGLEDEETSSGLK 943
Cdd:cd14898 223 SIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVK------------FSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 944 mTGVDCVEGMASGLYQELFAAVVSLINRSFSSHhlSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQ 1023
Cdd:cd14898 291 -QARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDFIK 361
|
410
....*....|....*
gi 1034629688 1024 RTFVSTLQRYQEEGV 1038
Cdd:cd14898 362 KMFRAKQGMYKEEGI 376
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
628-1248 |
1.21e-27 |
|
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: 121.57 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPK--------------GRRDGLPAHIGSMAQRAYWALLN 691
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqKLPGLYSSDTMAKyllsfearssstrnKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 692 QRR----DQSIVALGWSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKIRATFTVLRAFGSVSMAHSRSAT 757
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 758 RFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSssfgmgvwskped 837
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMDA------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 838 kqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NYAAEALGCEYEE 907
Cdd:cd14900 228 --------------MDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 908 LNTATfkhHLRQIIQQMTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRSF-----SSHHLSMAS 982
Cdd:cd14900 294 LEKAL---SVRRIRAGTDFVSMKLSAAQANNAR----------DALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 983 IMVVDSPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-DLPDpspgtTVAVVD 1057
Cdd:cd14900 361 IGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFcDNQD-----CVNLIS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1058 QNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtEGSSALRTCEQPLQCEIFHQLGwdPV 1137
Cdd:cd14900 429 QRPT---------------GILSLIDEECVMPKGSDTTLASKLYRACGSH----PRFSASRIQRARGLFTIVHYAG--HV 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1138 RYDLTGWLHRAKpnlsaldapQVLHQskreELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrk 1217
Cdd:cd14900 488 EYSTDGFLEKNK---------DVLHQ----EAVDLFVY------------------------------------------ 512
|
650 660 670
....*....|....*....|....*....|.
gi 1034629688 1218 apCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14900 513 --GLQFKEQLTTLLETLQQTNPHYVRCLKPN 541
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
627-1248 |
2.50e-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: 120.73 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAgKVPKGRRD--------GLPAHIGSMAQRAYWALLNQRR--DQ 696
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKP-VPQL-YSPELMREyhaapqpqKLKPHIFTVGEQTYRNVKSLIEpvNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 697 SIVALGWSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLDFNA 769
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 770 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSsfgmgvWSKPEDKQKAAAAFAQLQ 849
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLG---------AAGACKV--GRKQFMRFewanyAAEALGCEYEELNTATFKHHLR 918
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGniqfadsedEAQPCQPmdDTKESVRT-----SALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 919 QIIQQMTF-GPSRWGLEDeetssglkmTGVDCvegMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQNPRH 996
Cdd:cd14880 308 AGKQQQVFkKPCSRAECD---------TRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 997 QgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSpgTTVAVVDQNPSQqvrlpagggaqda 1075
Cdd:cd14880 376 N------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFiNYQDNQ--TCLDLIEGSPIS------------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1076 rgLFWVLDEEVHVEGSSDSVVLErlcAAFEKKGAGTEGSSALRTCEQPlQCEIFHQLGwdPVRYDLTGWLHRAK----PN 1151
Cdd:cd14880 435 --ICSLINEECRLNRPSSAAQLQ---TRIESALAGNPCLGHNKLSREP-SFIVVHYAG--PVRYHTAGLVEKNKdpvpPE 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1152 LSaldapQVLHQSKREELRSLFQARAKlppvcravaglEGTSQQALQRSRmvrrtfASSLAAVrrkapcSQIKLQMDALT 1231
Cdd:cd14880 507 LT-----RLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SKFKASLEQLL 558
|
650
....*....|....*..
gi 1034629688 1232 SMIKRSRLHFIHCLVPN 1248
Cdd:cd14880 559 QVLHSTTPHYIRCIKPN 575
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
629-1364 |
7.03e-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: 116.24 E-value: 7.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP-------------RGPSVPSAGKvpkgrrdgLPAHIGSMAQRAYWALLNQRRD 695
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirKYRDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 696 QSIVALGWSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 774
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 775 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMAD-----SSSFGMGVWSKPEDkqkaaaaFAQLQ 849
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEykflnPKCLDVPGIDDVAD-------FEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 850 GAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQFMRFEwanYAAEALGCEYEELNTATFKHHL------RQIIQQ 923
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 924 MTF-GP----SRWGLEDEETssgLKMTgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQg 998
Cdd:cd14876 301 VTKaGGqeieGRWTKDDAEM---LKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 999 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSPGTTVAVVDqnpsqqvrLPAGGGaqdaRGL 1078
Cdd:cd14876 370 -----SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPT----AELEYTSNAEVID--------VLCGKG----KSV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1079 FWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAP 1158
Cdd:cd14876 429 LSILEDQCLAPGGSD----EKFVSACVSKLKSNGKFKPAKV-DSNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1159 QVLHQSKREELRSLFqaraklppvcravaglEGtsqQALQRSRMVRrtfaSSLAAvrrkapcSQIKLQMDALTSMIKRSR 1238
Cdd:cd14876 501 EVVQASTNPVVKALF----------------EG---VVVEKGKIAK----GSLIG-------SQFLKQLESLMGLINSTE 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1239 LHFIHCLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQV 1318
Cdd:cd14876 551 PHFIRCIKPN---ETKK-------------------PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKF 608
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1034629688 1319 LDAPLlkklmSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1364
Cdd:cd14876 609 LDLGI-----ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
628-1326 |
2.53e-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: 114.62 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGK--VPKGRRDG------------LPAHIGSMAQRAYWALLN-Q 692
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPF-QRLPLYGKeiLESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 693 RRDQSIVALGWSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMV 762
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 763 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFG------MGVWSKPE 836
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLpnefhyTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 837 -DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNYAAEALGCE 904
Cdd:cd14908 241 lREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 905 YEELNTAtfkhhLRQIIQQMTFGPSRWGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MAS 982
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKAY--------DARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 983 IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDpspgttvavvDQNPS 1061
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD----------NQDCL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1062 QQVRLPagggaqdARGLFWVLDEEvhvegssdsvvlerlCAAFEKkgaGTEGSSALRTCEQPLQceifhqlgwdpvrydl 1141
Cdd:cd14908 447 DTIQAK-------KKGILTMLDDE---------------CRLGIR---GSDANYASRLYETYLP---------------- 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1142 tgwlhrakpnlsalDAPQVLHQSKREELRSLfqARAKLppvCRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRKAPCS 1221
Cdd:cd14908 486 --------------EKNQTHSENTRFEATSI--QKTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQ 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1222 QIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRT 1301
Cdd:cd14908 547 QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAK----------------------PDLVTRKRVTEQLRYGGVLEAVRVARS 604
|
730 740
....*....|....*....|....*
gi 1034629688 1302 GYADHMGLTRFRRQFQVLdAPLLKK 1326
Cdd:cd14908 605 GYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
627-1317 |
1.63e-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: 108.91 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP---SVPSAGKVPKGRRDGL-----------PAHIGSMAQRAYWALLNQ 692
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPlpiYTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 693 RRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KIRATFTVLRAFGSVSMAHSRSATRFSM 761
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 762 VMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLD--LRTELNLHQMADssSFGMGVWSKPE--D 837
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVN--EFVMLKQADPLatN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 838 KQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfewANYAAEALGCEYEELNT 910
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 911 ATFKHHLRQ---IIQQMTFGPSRWGLED-EETSSGLKMTGV----DCVEGMASGLYQELFAAVVSLIN-------RSFSS 975
Cdd:cd14893 313 ILLAAKLLEvepVVLDNYFRTRQFFSKDgNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 976 HHLSMAS--IMVVDSPGFQN--PRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDpspGT 1051
Cdd:cd14893 393 SNIVINSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTV---NS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1052 TVAVV-DQNPSQQVRlpagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK--------KGAGTEGSSALRTCEQ 1122
Cdd:cd14893 464 NVDITsEQEKCLQLF------EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSKDW 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1123 PLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSALDApQVLHQSKREELRSLFQARAklppvcrAVAGLEGTSQQALQRSRm 1202
Cdd:cd14893 538 RLLFIVQHHCG--KVTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1203 VRRTFASSLAAVRR-----KAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplA 1277
Cdd:cd14893 607 TSSKFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEG----------------------V 664
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1034629688 1278 LDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1317
Cdd:cd14893 665 FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
629-1038 |
4.05e-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: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 629 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPKGRR--------DGLPAHIGSMAQRAYWALLNQRRDQSI 698
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 699 VALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 777
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSlILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 778 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMaDSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLgI 857
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 858 SESEQRAVWRVLAAIYHLGAAGACKVGRkqfMRFEwaNYAAEALGCEYEEL------NTATFKHHLRQ---IIQQMTFgp 928
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAAQAIITkvvVINNETI-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 929 srwgledeeTSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 1008
Cdd:cd14886 312 ---------ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQL 376
|
410 420 430
....*....|....*....|....*....|
gi 1034629688 1009 CHNYAHERLQLLFYQRTFVSTLQRYQEEGV 1038
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1444-2128 |
4.44e-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: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1444 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1523
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIqlndlernptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1603
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEEL------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1604 SAYDGAKKMAHQLKRKchhltcdledtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVfEKGLREKVTQENT------ 1677
Cdd:TIGR02168 400 NEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERleeale 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1678 SVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGspsLGENCVAGLKERLWKlessaleqqkiqSQQENTIKQLE 1757
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGL------------SGILGVLSELI 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1758 QLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDqig 1832
Cdd:TIGR02168 530 SVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD--- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1833 HRDFDVEKRL------------------RRDLRRTHALLSDVQL---LLG-----TMEDGKTSVS----KEELEKVHSQL 1882
Cdd:TIGR02168 607 LVKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdLVRpggviTGGSAKTNSSilerRREIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1883 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAAD 1962
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1963 IGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDS 2041
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2042 LIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2121
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
....*..
gi 1034629688 2122 LQAALEE 2128
Cdd:TIGR02168 927 LELRLEG 933
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
627-1319 |
1.60e-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: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKgrrdglPAHIGSMAQRAYWALL-NQRRDQSIVALGWSG 705
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIK------KCHISGVAENALDRIKsMSSNAESIVFGGESG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 706 AGKTTCCEQVLEHLVGMAGSvdgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQ-TMLLE 784
Cdd:cd14874 75 SGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKyTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 785 KSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMadSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRA 864
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 865 VWRVLAAIYHLGaagackvgrKQFMRFEWANYAAEALGcEYEELNTATFKHHLRQI-IQQMtfgpSRWGLEDEETSSGLK 943
Cdd:cd14874 229 IYKIISTILHIG---------NIYFRTKRNPNVEQDVV-EIGNMSEVKWVAFLLEVdFDQL----VNFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 944 M-TGVDCVEGMASGLYQELFAAVVSLINRSFSShHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFY 1022
Cdd:cd14874 295 LnAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1023 QRTFVSTLQRYQEEGVPVQFDLPDP-SPGTTVAVVDQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLC 1101
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKP---------------YGLLPLLTDECKFPKGSHESYLEHCN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1102 AAFEKKGAGTEGSSALRtceqpLQCEIFHQLG--WdpvrYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQARAKl 1179
Cdd:cd14874 433 LNHTDRSSYGKARNKER-----LEFGVRHCIGttW----YNVTDFFSRNKRIIS-LSAVQLLRSSKNPIIGLLFESYSS- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1180 ppvcravagleGTSQQALQRSRMVRRTfASSLAavrrkapcsqiklqmdaltSMIKRSRLHFIHCLvpnpvvesRSGQES 1259
Cdd:cd14874 502 -----------NTSDMIVSQAQFILRG-AQEIA-------------------DKINGSHAHFVRCI--------KSNNER 542
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1260 ppppQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1319
Cdd:cd14874 543 ----QPKK----------FDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1369-2137 |
9.06e-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: 100.53 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1369 SRLEKQREKL--VSQSIVLFQAACKgfLSRQEFKKLKIRRLAAQCIQknvAVFLAVKDWPWWQLLGSLQPLLsatigtEQ 1446
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALE------RQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1447 LRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKHEQ 1526
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----------LGEEEQLRVK--EKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1527 VQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQmenefLRKRLQQCEERLDSELTARKELEQKLGELQSAY 1606
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-----ERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1607 DGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALgesvfeKGLREKVTQ---ENTSVRWEL 1683
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAI------AGIEAKINEleeEKEDKALEI 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1684 gqlqqqlKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLES--SALEQQKIQSQQE----------- 1750
Cdd:TIGR02169 451 -------KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRelAEAEAQARASEERvrggraveevl 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1751 --------NTIKQLEQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQL---EMQLEQEYEEkqmVL 1814
Cdd:TIGR02169 517 kasiqgvhGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLS---IL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1815 HEkqdlEGLIGTLCDQIghrDFDVEKR-----------LRRDLRRTHALLSDVQLLL---------GTM------EDGKT 1868
Cdd:TIGR02169 594 SE----DGVIGFAVDLV---EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMVTlegelfeksGAMtggsraPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1869 SVSKEELEKVHS------QLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLvdeQLYRLQFEKADLLKRIDEDQ 1942
Cdd:TIGR02169 667 LFSRSEPAELQRlrerleGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKERLEELE 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1943 DDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLqvAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKt 2021
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKlEEEVSRIEARLREIEQK- 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2022 efqkvqIKRFEVLVIRLRDsliKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2101
Cdd:TIGR02169 821 ------LNRLTLEKEYLEK---EIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGDL 887
|
810 820 830
....*....|....*....|....*....|....*.
gi 1034629688 2102 AAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTE 2137
Cdd:TIGR02169 888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
628-1096 |
2.60e-20 |
|
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: 98.26 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgpsvpsagkvpkgRRDGLPAHIGSMAQRA-YWALLN-------QRRD---- 695
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY-------------RDVGNPLTLTSTRSSPlAPQLLKvvqeavrQQSEtgyp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 696 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATR---FSMVMSLDfnatGR 772
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRighFIEVQVTD----GA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 773 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL--HQMADSS--SFGMGVWSKPEDKqkaaAAFAQL 848
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRylSHGDTRQNEAEDA----ARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 849 QGAMEMLGISESEqraVWRVLAAIYHLG--------AAGACKVGRKQFmrfewaNYAAEALGCE----YEELNTATfkHH 916
Cdd:cd14881 221 KACLGILGIPFLD---VVRVLAAVLLLGnvqfidggGLEVDVKGETEL------KSVAALLGVSgaalFRGLTTRT--HN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 917 LR-QIIQQmtfgpsrwgLEDEETSSGLKmtgvDCvegMASGLYQELFAAVVSLINR-----SFSSHHLSMASIMVVDSPG 990
Cdd:cd14881 290 ARgQLVKS---------VCDANMSNMTR----DA---LAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 991 FQNPrhqgkdRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP--VQFDLPDPSPgttvaVVDQNPSQQVrlpa 1068
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQceVEVDYVDNVP-----CIDLISSLRT---- 418
|
490 500
....*....|....*....|....*...
gi 1034629688 1069 gggaqdarGLFWVLDEEVHVEGSSDSVV 1096
Cdd:cd14881 419 --------GLLSMLDVECSPRGTAESYV 438
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
627-1248 |
5.56e-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: 97.47 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPS--AGKVPKG--------------RRDGLPAHIGSMAQRAYWALL 690
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPF-QDLPQlyGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 691 NQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KIRATFTVLRAFGSVSMAHSR 754
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 755 SATRFSMVMSLDFNATGR-ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELN--LHQMADSSSFGM-- 829
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKqvLALSGGPQSFRLln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 830 -GVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGA---------------AGACKVGRKQFMRFEW 893
Cdd:cd14899 240 qSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 894 ANYAAEALGCEYEELNTATFKhhlrqiiqqmtfgpsRWGLEDEETSsglkMTGVDCVEG------MASGLYQELFAAVVS 967
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTK---------------RWLHASNETL----VVGVDVAHArntrnaLTMECYRLLFEWLVA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 968 LINRSFSSH---------------HLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQR 1032
Cdd:cd14899 381 RVNNKLQRQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1033 YQEEGVPVQFdLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTE 1112
Cdd:cd14899 455 YRDEGIRWSF-VDFPNNRACLELFEHRPI---------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPH 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1113 GSSAlRTCEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLfqARAKLPPVCRAVAGLEGT 1192
Cdd:cd14899 519 FRSA-PLIQRTTQFVVAHYAGC--VTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQAL--AAGSNDEDANGDSELDGF 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 1193 SQQALQRSRmvrrtfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14899 593 GGRTRRRAK-------SAIAAV---SVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1429-2113 |
3.31e-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: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1429 QLLGSLQPLLSATIGTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvaCQVLESER 1507
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1508 AERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDS 1587
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ-EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEA 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1588 ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfEKG 1667
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EKA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1668 LREKVTQENTSVRWElgqlqqqLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESS--------- 1738
Cdd:pfam01576 616 ISARYAEERDRAEAE-------AREKETRALSLARALEEALEAKEEL-------ERTNKQLRAEMEDLVSSkddvgknvh 681
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1739 -------ALEQQ----KIQSQQ-ENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQE 1806
Cdd:pfam01576 682 elerskrALEQQveemKTQLEElEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDE 761
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1807 YEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQlllgtmedgktsvskEELEKVHSQLEQSE 1886
Cdd:pfam01576 762 RKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQ---------------RELEEARASRDEIL 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1887 AKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMqkhkdliaqsaadiGQI 1966
Cdd:pfam01576 826 AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE--------------ARI 891
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1967 QELQLQLEEAKKEKHKLQEQLQVAQMRIEYL------EQSTVDRAIVSRQEAVICDLENKTEFQKV--QIK-RFEVLVIR 2037
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQLttelaaERSTSQKSESARQQLERQNKELKAKLQEMegTVKsKFKSSIAA 971
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2038 LRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL--------------KADMEELVQREAEASRRCMELEKYVEELAA 2103
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqvederrhadqyKDQAEKGNSRMKQLKRQLEEAEEEASRANA 1051
|
730
....*....|
gi 1034629688 2104 VRQTLQTDLE 2113
Cdd:pfam01576 1052 ARRKLQRELD 1061
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1445-2110 |
1.09e-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: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1524
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEEAqqKIQLNDLERNPTGGDEWQ---------MRFDCAQMENEFLRKRLQQCEERLDSELTARKEL 1595
Cdd:TIGR02168 389 AQLELQIASLNNEIERL--EARLERLEDRRERLQQEIeellkkleeAELKELQAELEELEEELEELQEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1596 EQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE------DTCVLLENQQSRNH-------ELEKKQKKFDLQLAQALGES 1662
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDSLERLQEnlegfsEGVKALLKNQSGLSgilgvlsELISVDEGYEAAIEAALGGR 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1663 VfekglrEKVTQENTSVRW---------ELGQLQQQLKQKEQEASQLKQQVEMLQDHKR------ELLGSPSLGENCVAG 1727
Cdd:TIGR02168 547 L------QAVVVENLNAAKkaiaflkqnELGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1728 LKERLWKLES--SALEQQKIQS-------------------------------QQENTIKQLEQLRQRFELEIERMKQ-- 1772
Cdd:TIGR02168 621 LLGGVLVVDDldNALELAKKLRpgyrivtldgdlvrpggvitggsaktnssilERRREIEELEEKIEELEEKIAELEKal 700
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1773 -MHQKDREDQEEELEDVR---QSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRR 1848
Cdd:TIGR02168 701 aELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1849 THALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQ 1928
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1929 FEKADLLKRIDEDQDDLNEL----------MQKHKDLIAQSAADI----GQIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1994
Cdd:TIGR02168 859 AEIEELEELIEELESELEALlnerasleeaLALLRSELEELSEELreleSKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1995 EYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlVIRLRDSLIKMGeELSQAATSESQQressqyYQRRLEELK 2074
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-----LKRLENKIKELG-PVNLAAIEEYEE------LKERYDFLT 1006
|
730 740 750
....*....|....*....|....*....|....*..
gi 1034629688 2075 ADMEELVqrEAEASrrcmeLEKYVEEL-AAVRQTLQT 2110
Cdd:TIGR02168 1007 AQKEDLT--EAKET-----LEEAIEEIdREARERFKD 1036
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
628-1248 |
1.66e-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: 89.58 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-------------------SVPSAGKVPkgrrdglPAHIGSMAQRAYWA 688
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPlkelydqdvmnvylhkksnSAASAAPFP-------KAHIYDIANMAYKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 689 LLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFN 768
Cdd:cd14884 75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 769 A---------TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-DLDL---RTELNLH----------QMADSS 825
Cdd:cd14884 155 EventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvygllnpdesHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 826 SFGMGVWSK-----PEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGackvgrkqfmrfewANYAAEA 900
Cdd:cd14884 235 KGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRA--------------YKAAAEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 901 LGCEYEELNTaTFKHHLRQIIQQMTFGPSRwglEDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINR--------- 971
Cdd:cd14884 301 LQIEEEDLEN-VIKYKNIRVSHEVIRTERR---KENATST---------RDTLIKFIYKKLFNKIIEDINRnvlkckekd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 972 SFSSHHLSM---ASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPS 1048
Cdd:cd14884 368 ESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1049 PGTTVAVVDQ---NPSQQVRLPAgGGAQDARGLFW---------VLDEEVHVEGSsdsvVLERLCAAFEKKGAGTEGSSA 1116
Cdd:cd14884 441 YSDTLIFIAKifrRLDDITKLKN-QGQKKTDDHFFryllnnerqQQLEGKVSYGF----VLNHDADGTAKKQNIKKNIFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1117 LRtceqplqceifHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSlfqaraklppvcravAGLEGTSQQA 1196
Cdd:cd14884 516 IR-----------HYAG--LVTYRINNWIDKNSDKIET-SIETLISCSSNRFLRE---------------ANNGGNKGNF 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 1197 LQRSRMVrrtfasslaavrrkapcsqIKlQMDALTSMIKRSRLHFIHCLVPN 1248
Cdd:cd14884 567 LSVSKKY-------------------IK-ELDNLFTQLQSTDMYYIRCFLPN 598
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
628-1041 |
2.25e-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: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVP-----SAGKVPKGRRDGLPaHIGSMAQRAYWALLNQRRDQSIVALG 702
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEypqefHAKYRCKSRSDNAP-HIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 703 WSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 782
Cdd:cd14882 81 ESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 783 LEKSRVARQPEGESNFLVFSQMLAGL-------DLDLRTELNLHQM----ADSSSFGMGVWSKPEDKQKAAAAFAQLQGA 851
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFIeaqnrlkEYNLKAGRNYRYLrippEVPPSKLKYRRDDPEGNVERYKEFEEILKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 852 MEMlgiSESEQRAVWRVLAAIYHLGAAGACKV-GRKQFMRFEWANYAAEALGceyeeLNTATFKHHLRQIIQQMTFGPSR 930
Cdd:cd14882 239 LDF---NEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 931 WGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINrsfssHHLSMA--------SIMVVDSPGFQNPRHQGkdra 1002
Cdd:cd14882 311 RKHTTEEAR--------DARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR---- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 1034629688 1003 atFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ 1041
Cdd:cd14882 374 --LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIPTI 410
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
627-1041 |
2.38e-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: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 627 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGA 706
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 707 GKTTCCEQVLE-HLVGMagSVDGRVSVEKIRATFtVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEK 785
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 786 SRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPE-DKQKAAAAFAQLQGAMEMLGISESeqra 864
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNMHDMKDD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 865 VWRVLAAIYHLG--------AAGACKVGRKQFMRFEWANYAAEALGCEYEEL-NTATFKHhlRQIIQQMTFGPsrwgLED 935
Cdd:cd14937 234 LFLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 936 EETSSGLKMTGVDcvegmasgLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHE 1015
Cdd:cd14937 308 EESVSICKSISKD--------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANE 373
|
410 420
....*....|....*....|....*.
gi 1034629688 1016 RLQLLFYQRTFVSTLQRYQEEGVPVQ 1041
Cdd:cd14937 374 EIHSIYLYIVYEKETELYKAEDILIE 399
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1446-2132 |
2.48e-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: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1446 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVA----------CQVLESERAERLQAFR 1515
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDTLDTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1516 EVQELKSKHEQvqkKLGDVNKQLEEAQQ--KIQLNDL-ERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEE--------- 1583
Cdd:pfam01576 317 AQQELRSKREQ---EVTELKKALEEETRshEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1584 ------RLDSElTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQL-- 1655
Cdd:pfam01576 394 rtlqqaKQDSE-HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1656 AQALG--ESVFEKGLREKVTQ---ENTSVRWELGQLQQQLKQKEQEASQLKQQvemLQDHKREllgspslgencvagLKE 1730
Cdd:pfam01576 473 TQELLqeETRQKLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQ---LSDMKKK--------------LEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1731 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSC------QKRLHQL---EM 1801
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkQKKFDQMlaeEK 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1802 QLEQEY-EEKQMVLHEKQDLEGLIGTLCdqighRDFDVEKRLRRDLRRTHALL-SDVQLLLGTMEDGKTSVskEELEKVH 1879
Cdd:pfam01576 615 AISARYaEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTNKQLrAEMEDLVSSKDDVGKNV--HELERSK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1880 SQLEQSeakcEEALKTQkvltadLESMHSELEnMTRNKSL---VDEQLYRLQFE-------------KADLLKRIDEDQD 1943
Cdd:pfam01576 688 RALEQQ----VEEMKTQ------LEELEDELQ-ATEDAKLrleVNMQALKAQFErdlqardeqgeekRRQLVKQVRELEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1944 DLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLeQSTVDRAIVSRQEAVICDLENKTef 2023
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2024 qkvQIKRFEVLVIRLRDSLI--------------KMGEELSQAATSESQQRESsqyyQRRLEELKADMEELVQREAEAS- 2088
Cdd:pfam01576 834 ---KLKNLEAELLQLQEDLAaserarrqaqqerdELADEIASGASGKSALQDE----KRRLEARIAQLEEELEEEQSNTe 906
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 2089 -------RRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASS 2132
Cdd:pfam01576 907 llndrlrKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGT 960
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1445-1999 |
3.48e-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: 88.54 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLAD---ERFKGDVACQVLES--ERAERLQAfrEVQE 1519
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKkiQKNKSLES--QISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1520 LKSKH-------EQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLdSELT 1590
Cdd:TIGR04523 223 LKKQNnqlkdniEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-SDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1591 ARKE-------------LEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQ-QSRNHELEKKQKKfdLQLA 1656
Cdd:TIGR04523 302 NQKEqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----SESEnSEKQRELEEKQNE--IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1657 QALGESVFEKglREKVTQENTSVRWELgqlqqqlKQKEQEASQLKQQVEMLQDHKRELLGspslgencvaglkerlwkle 1736
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1737 ssalEQQKIQSQ---QENTIKQLEQLRQRFELEIERMKQMhqkdREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQ-- 1811
Cdd:TIGR04523 427 ----EIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNT----RESLETQLKVLSRSINKIKQNLE-QKQKELKSKEke 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1812 --MVLHEKQDLEGLIGTLCDQIghrdfdvekrlrrdlrrthallsdvqlllgtmedgktSVSKEELEKVHSQLEQSEAKC 1889
Cdd:TIGR04523 498 lkKLNEEKKELEEKVKDLTKKI-------------------------------------SSLKEKIEKLESEKKEKESKI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1890 EEalktqkvLTADLESMHSEL--ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQ 1967
Cdd:TIGR04523 541 SD-------LEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590
....*....|....*....|....*....|..
gi 1034629688 1968 ELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1999
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1451-2128 |
1.59e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 86.65 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1451 EEELTTLRRKLEKSEKLRnELRQntDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1530
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYK-ELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1531 LGDVNKQLEEAQQK-----IQLNDLERNPTGGDEwqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1605
Cdd:TIGR02168 276 VSELEEEIEELQKElyalaNEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1606 YDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfekgLREKVTQentsvrwelgq 1685
Cdd:TIGR02168 353 LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLER----------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1686 lqqqlkqkeqeasqLKQQVEMLQDHKRELLGSPSLGEncvagLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL 1765
Cdd:TIGR02168 412 --------------LEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1766 EIERMKQmhqkdREDQEEELedvrQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfDVEKRLRRD 1845
Cdd:TIGR02168 473 AEQALDA-----AERELAQL----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEAA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1846 LRRthALLSDVQLLLgtMEDgktsvsKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVD 1921
Cdd:TIGR02168 539 IEA--ALGGRLQAVV--VEN------LNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1922 EqlYRLQFEKA--DLLKR--IDEDQDDLNELMQKHK----------DLIA-------QSAADIGQIQELQLQLEEAKKEK 1980
Cdd:TIGR02168 609 K--FDPKLRKAlsYLLGGvlVVDDLDNALELAKKLRpgyrivtldgDLVRpggvitgGSAKTNSSILERRREIEELEEKI 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1981 HKLQEQLQVAQMRIEYLEQSTVDraivsrqeavicdLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQr 2060
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL- 752
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 2061 essqyyQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:TIGR02168 753 ------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
628-1100 |
2.31e-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: 85.53 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 628 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVPK-GRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWS 704
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRylPFLHSQELVRNyNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 705 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLE 784
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 785 KSRVARQPEGESNFLVFSQMLAGLDLDlrtELNLHQMADSSSF-------GMGVWSKPEDKqkaaaAFAQLQGAMEMLGI 857
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDE---EKAAYQLGDINSYhylnqggSISVESIDDNR-----VFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 858 SESEQRAVWRVLAAIYHLGAAgackvgrkQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRWGLEDEE 937
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 938 TssglkmtgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMaSIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 1017
Cdd:cd14905 305 S--------------LARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1018 QLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgTTVAVVDQNPSQQVrlpagggaqdARGLFWVLDEEVHVEGSSDSVVL 1097
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWM---------TPISFKDNEESVEM----------MEKIINLLDQESKNINSSDQIFL 424
|
...
gi 1034629688 1098 ERL 1100
Cdd:cd14905 425 EKL 427
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1445-2113 |
1.51e-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: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNEL-RQNTDLLESKIA---------DLTSDLADERFKGDVACQVLES---ERAERL 1511
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNAlqeqlqaetELCAEAEEMRARLAARKQELEEilhELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1512 QAFRE-VQELKSKHEQVQKKLGDVNKQLEE---AQQKIQlndLERNPTGGDEWQMRFDCAQME--NEFLRKRLQQCEERL 1585
Cdd:pfam01576 85 EEEEErSQQLQNEKKKMQQHIQDLEEQLDEeeaARQKLQ---LEKVTTEAKIKKLEEDILLLEdqNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1586 DSELTARKELEQKLgelqsaydgakKMAHQLKRKCHHLTCDLEDTcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFE 1665
Cdd:pfam01576 162 SEFTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1666 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL---------------GSPSLGENCVAgLKE 1730
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraarnkaekQRRDLGEELEA-LKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1731 RLWKLESSALEQQKIQSQQENTI----KQLEQLRQRFELEIERMKQMHQKDREDQEEELED---VRQSCQKRLHQLEMQL 1803
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQEVtelkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrNKANLEKAKQALESEN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1804 EQEYEEKQMVLHEKQDLEgligtlcdqigHRdfdvEKRLRRDLRRTHALLSDVQLLLGTMEDgKTSVSKEELEKVHSQLE 1883
Cdd:pfam01576 387 AELQAELRTLQQAKQDSE-----------HK----RKKLEGQLQELQARLSESERQRAELAE-KLSKLQSELESVSSLLN 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1884 QSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI 1963
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1964 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY------------------LEQSTVDraiVSRQEAVICDLENKTefqk 2025
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrlqqeLDDLLVD---LDHQRQLVSNLEKKQ---- 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2026 vqiKRFEVLVIRLRDSLIKMGEELSQA----------ATSESQQRESSQYYQRRLEE----LKADMEELVQREAEASRRC 2091
Cdd:pfam01576 604 ---KKFDQMLAEEKAISARYAEERDRAeaeareketrALSLARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKNV 680
|
730 740
....*....|....*....|..
gi 1034629688 2092 MELEKYVEELAAVRQTLQTDLE 2113
Cdd:pfam01576 681 HELERSKRALEQQVEEMKTQLE 702
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1515-2144 |
3.66e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 3.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1515 REVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENefLRKRLQQCEERLDSELTARKE 1594
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE--LKEEIEELEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1595 LEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdledtcvllenqqsrnhELEKKQKKFdlqlaQALGEsvfekgLREKVTQ 1674
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELK------------------ELKEKAEEY-----IKLSE------FYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1675 ENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvAGLKERLWKLESSALEQQKIQSQQENtik 1754
Cdd:PRK03918 308 ELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKKEE--- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1755 qLEQLRQRFE-LEIERMKQMHQKDREDQEEELEDVRQSCQKRlhqleMQLEQEYEEKQMVLHEkqdLEGLIGTlCDQIGh 1833
Cdd:PRK03918 374 -LERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARI-----GELKKEIKELKKAIEE---LKKAKGK-CPVCG- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1834 RDFDVEKRLRRdLRRTHALLSDVqlllgtmedgktSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTAdLESMHSELENm 1913
Cdd:PRK03918 443 RELTEEHRKEL-LEEYTAELKRI------------EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKE- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1914 trnkslVDEQLYRLQFEKadlLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMR 1993
Cdd:PRK03918 508 ------LEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1994 IEYLEQSTVDraivsrqeavicDLENKTEFQKVQIKRFevlvIRLRDSLIKMGEELSQAATSESQQRESSQYYQR---RL 2070
Cdd:PRK03918 579 LEELGFESVE------------ELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAEtekRL 642
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2071 EELKADMEEL-----VQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVD 2144
Cdd:PRK03918 643 EELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1427-2064 |
3.73e-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: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1427 WW--QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdllESKIADLTSDLADERFKGDVACQVLE 1504
Cdd:TIGR00618 243 AYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1505 SERAERLQAFREVQELKSKHEQVQKKLGDVNKQLeeaQQKIQLNDLERNPTGgdeWQMRFDCAQMENEFLRKRLQQCEER 1584
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH---SQEIHIRDAHEVATS---IREISCQQHTLTQHIHTLQQQKTTL 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1585 LDSELTARKELEQKLGEL-QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGES 1662
Cdd:TIGR00618 392 TQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQeSAQSLKER 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1663 VFEKGLREKVTQENTSVRWELGQLQQQLKQKEQE--ASQLKQQVEMLQDHKRELLGSPSL-GENCVAGLKERLWKLE--- 1736
Cdd:TIGR00618 472 EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYhql 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1737 SSALEQQKIQSQQENTIKQ----LEQLRQRFELEIERMKQMHQKDREDQEEELEDvRQSCQKRLHQLEMQLEQEYEEKQM 1812
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQsfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-EDMLACEQHALLRKLQPEQDLQDV 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1813 VLHEKQ----------DLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVS--KEELEKVHS 1880
Cdd:TIGR00618 631 RLHLQQcsqelalkltALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQT 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1881 QLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1960
Cdd:TIGR00618 705 LLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1961 ADIGQIQELQLQLEEAKKEKHKLQEQLQvaQMRIEYLEQSTV-DRAIVSRQEAVICDLENKTEfqkvqikrfevLVIRLR 2039
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLqCETLVQEEEQFLSRLEEKSA-----------TLGEIT 848
|
650 660
....*....|....*....|....*
gi 1034629688 2040 DSLIKMGEELSQAATSESQQRESSQ 2064
Cdd:TIGR00618 849 HQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1451-2131 |
1.58e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.98 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1451 EEELTTLRRKLEKSEKLRNELRQNTDLLE--SKIA----DLTSDLadERFKGDVACQVLESERAERLQAFREVQELKSKH 1524
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLErqAEKAeryrELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENE--FLRKRLQQCEERLDSELTARKELEQKLGEL 1602
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiaRLEERRRELEERLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1603 QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWE 1682
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1683 LGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpslgencVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQR 1762
Cdd:COG1196 416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEE-------EAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1763 FELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ---LEMQLEQEYEEkqmvlhekqDLEGLIGTLCDQIGHRDFDVE 1839
Cdd:COG1196 489 AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavaVLIGVEAAYEA---------ALEAALAAALQNIVVEDDEVA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1840 KRLRRDLRRtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSL 1919
Cdd:COG1196 560 AAAIEYLKA-AKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1920 VDEQLYRLQFEKADLlkridedqddlnelmqkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1999
Cdd:COG1196 639 AVTLAGRLREVTLEG-------------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2000 STVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDsLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEE 2079
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 2080 L------VQREAEasrrcmELEKYVEELAAVRQTLQ---TDLETSIRRI-----ADLQAALEEVAS 2131
Cdd:COG1196 779 LgpvnllAIEEYE------ELEERYDFLSEQREDLEearETLEEAIEEIdretrERFLETFDAVNE 838
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1872-2140 |
2.39e-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: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1951
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1952 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENKTEFQKVQIKRF 2031
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2032 EVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2111
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....*....
gi 1034629688 2112 LETSIRRIADLQAALEEVASSDSDTESVQ 2140
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 ... |
1729-2165 |
2.58e-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: 2.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1729 KERLWKLESSALEQQKIQSQ--QENTIKQlEQLRQRFEL--EIERMKQMhqkdREDQEEELEDVrqscqkrLHQLEMQLE 1804
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMRAR----LAARKQELEEI-------LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1805 QEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEE--LEKVHSQL 1882
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEE-AARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERklLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1883 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNkslvdEQLYRLQFEKADllKRIDEDQDDLNElmqkhkdliaqsaad 1962
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-----EEKGRQELEKAK--RKLEGESTDLQE--------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1963 igQIQELQLQLEEAKKEKHKLQEQLQVAQMRieyLEQSTVDRAIVSRQ----EAVICDLE----------NKTEFQKVQI 2028
Cdd:pfam01576 223 --QIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKirelEAQISELQedleseraarNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2029 -KRFEVLVIRLRDSL----------IKMGEELSQ--------AATSESQQRESSQYYQRRLEELKADMEELVQREAEASR 2089
Cdd:pfam01576 298 gEELEALKTELEDTLdttaaqqelrSKREQEVTElkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 2090 RCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQT-AVDCGSSGRKEMDNVSILSSQPEG 2165
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAeLAEKLSKLQSELESVSSLLNEAEG 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1445-1985 |
1.26e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.03 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvleseraERLQAFRE-VQELKSK 1523
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLE---------------EKIRELEErIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggDEWQMRFDCAQMENEFLRKRLQQCEERLD--SELTAR-KELEQKLG 1600
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFY------EEYLDELREIEKRLSRLEEEINGIEERIKelEEKEERlEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1601 ELQSAYDGAKKmAHQLkrkchhltcdLEDTCVLLENQQsrnhELEKKQKKFDLQLAQALGESVFEKglREKVTQENTSVR 1680
Cdd:PRK03918 349 ELEKRLEELEE-RHEL----------YEEAKAKKEELE----RLKKRLTGLTPEKLEKELEELEKA--KEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1681 WELGQLQQQLKQKEQEASQLKQ--------QVEMLQDHKRELLGSPSLG----ENCVAGLKERLWKLESSALEQQKIQSQ 1748
Cdd:PRK03918 412 ARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1749 QENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLHQLEMQLEQEYE---EKQMVLHEKQDLEG 1822
Cdd:PRK03918 492 ESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEE 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1823 LIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGtmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTAD 1902
Cdd:PRK03918 571 ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1903 LESMHSELENMTRNKSLVD-EQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKH 1981
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
....
gi 1034629688 1982 KLQE 1985
Cdd:PRK03918 722 RVEE 725
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1476-2140 |
2.03e-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: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1476 DLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREvQELKSKHEQVQKkLGDVNKQLEEAQQKIQLNDlernpt 1555
Cdd:TIGR00618 171 NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQV-LEKELKHLREALQQTQQSH------ 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1556 ggdEWQMRFDCAQMENEFLRKRLQQCEERLDsELTArkeLEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLE 1635
Cdd:TIGR00618 243 ---AYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA---QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1636 nQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEA-----SQLKQQVEMLQDH 1710
Cdd:TIGR00618 316 -LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1711 KRELLGSPSLGENCVAGLKERLwkLESSALEQQKI--QSQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEELE 1786
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRT--SAFRDLQGQLAhaKKQQELQQRYAELCAAAITctAQCEKLEKIHLQESAQSLKERE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1787 dvrqscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfdvekrlrrdlrrTHALLSDvqlllgtmEDG 1866
Cdd:TIGR00618 473 -------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-------------PARQDID--------NPG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1867 KTSVSKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID--- 1939
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkls 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1940 EDQDDLNELMQKHKDLIAQSAADIGQIQEL-QLQLEEAKKEKHKLQEQLQVAQMRI-EYLEQSTVDRA-IVSRQEAVICD 2016
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKeLLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2017 LENKTEF---------QKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESS------QYYQRRLEELKADMEELV 2081
Cdd:TIGR00618 685 MQSEKEQltywkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAHF 764
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2082 QREAEASRRCMELEKYvEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQ 2140
Cdd:TIGR00618 765 NNNEEVTAALQTGAEL-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1445-2128 |
2.64e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.25 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRnELRQNTDLLESKIADLTSDL--ADERFKGDVACQVLESERAERLQAFREVQ--EL 1520
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVrkAEELRKAEDARKAEAARKAEEERKAEEARkaED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1521 KSKHEQVqKKLGDVNKQLEEAQQKiqlnDLERNptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLG 1600
Cdd:PTZ00121 1223 AKKAEAV-KKAEEAKKDAEEAKKA----EEERN----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1601 ELQSAYDgaKKMAHQLKRKChhltcdledtcvllenQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ-ENTSV 1679
Cdd:PTZ00121 1294 EAKKAEE--KKKADEAKKKA----------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEAA 1355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1680 RWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK--ERLWKLESSALEQQKIQSQQENtIKQLE 1757
Cdd:PTZ00121 1356 ADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEE-KKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1758 QLRQRFEleiERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEmqLEQEYEEKQMVLHEKQDLEgligtlcdqighrdfd 1837
Cdd:PTZ00121 1435 EAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAE---------------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1838 vEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSvskEELEKVHSQLEQSEA-KCEEALKTQKVLTADLESMHSELENMTRN 1916
Cdd:PTZ00121 1494 -EAKKKADEAKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEEA 1569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1917 KSlvDEQLYRLQFEKADLLKRIDEDQddLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKhklQEQLQVAQMRIEY 1996
Cdd:PTZ00121 1570 KK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKKE 1642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1997 LEQstVDRAIVSRQEavicdlENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAatsESQQRESSQYYQRRLEElKAD 2076
Cdd:PTZ00121 1643 AEE--KKKAEELKKA------EEENKIKAAEEAKKA-------EEDKKKAEEAKKA---EEDEKKAAEALKKEAEE-AKK 1703
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 2077 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1444-1988 |
3.01e-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: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1444 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSK 1523
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfDCAQMENEFLRKRLQQcEERLDSELTARKELEQKLGELQ 1603
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA-----------EAEEALLEAEAELAEA-EEELEELAEELLEALRAAAELA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1604 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWEL 1683
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1684 GQLQQQLKQKEQEASQLKQQVEMLQDH------KRELLGSPSLGENCVAGLKERLWKLESSALEQqkiqsqqentikqle 1757
Cdd:COG1196 477 AALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE--------------- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1758 qlrqrfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDF- 1836
Cdd:COG1196 542 ------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARy 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1837 -----------DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLES 1905
Cdd:COG1196 616 yvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1906 MHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELqLQLEEAKKEKHKLQE 1985
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLER 774
|
...
gi 1034629688 1986 QLQ 1988
Cdd:COG1196 775 EIE 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1446-2100 |
8.44e-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: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1446 QLRAKEEELTTLRRKLEKSEKLRNELR-QNTDL---LESKIADlTSDLADERFKGDVACQVLESERAerlQAFREVQELK 1521
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQfENEKVslkLEEEIQE-NKDLIKENNATRHLCNLLKETCA---RSAEKTKKYE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1522 SKHEQVQKKLGDVNkqleeaqqkiqlNDLERNPTGGDEWQMRFDCAQMENEFLRK----RLQQCEERLDSELTARK---- 1593
Cdd:pfam05483 176 YEREETRQVYMDLN------------NNIEKMILAFEELRVQAENARLEMHFKLKedheKIQHLEEEYKKEINDKEkqvs 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1594 -------ELEQKLGELQSAYDGAKKMAHQLKRKC--------------HHLTCDLEDTCVLLENQQSRNHELEKkqkkfD 1652
Cdd:pfam05483 244 llliqitEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKELEDIKMSLQRSMSTQKALEE-----D 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1653 LQLAQalgESVFEkglrekVTQENTSVRWELGqlqQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERL 1732
Cdd:pfam05483 319 LQIAT---KTICQ------LTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMEL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1733 WKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKRLHQLEMQLEQEYEEK 1810
Cdd:pfam05483 387 QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1811 QMVLHEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALL---SDVQLLLGTMEDGKTSVSKEElEKVHSQLEQSEa 1887
Cdd:pfam05483 467 EHYLKEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTqeaSDMTLELKKHQEDIINCKKQE-ERMLKQIENLE- 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1888 kceealKTQKVLTADLESMHSEL---------------ENMTRNKSLV---DEQLYRLQFEKADLLKRIDEDQDDLNELM 1949
Cdd:pfam05483 541 ------EKEMNLRDELESVREEFiqkgdevkckldkseENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELH 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1950 QKHKDLIAQSAADIGQ-------IQELQLQLEEAKKekhKLQEQLQVAQMRIEYLEQS------TVDRAIVSRQEAVICD 2016
Cdd:pfam05483 615 QENKALKKKGSAENKQlnayeikVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAVKLQ 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2017 LENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL-SQAATSESQQRESSQyyqrrleeLKADME-ELVQREAE--ASRRCM 2092
Cdd:pfam05483 692 KEIDKRCQH-KIAEMVALMEKHKHQYDKIIEERdSELGLYKNKEQEQSS--------AKAALEiELSNIKAEllSLKKQL 762
|
....*...
gi 1034629688 2093 ELEKYVEE 2100
Cdd:pfam05483 763 EIEKEEKE 770
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1865-2130 |
1.99e-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: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1865 DGKTSVSKEELEKVHSQLEQSEAKCEE-------------------ALKTQK------VLTADLESMHSELENMTRNKSL 1919
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrerekaeryqALLKEKreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1920 VDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI--------GQIQELQLQLEEAKKEKHKLQEQLQVAQ 1991
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1992 MRIEyleqstvdraivsRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLE 2071
Cdd:TIGR02169 329 AEID-------------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2072 ELKADMEELvqrEAEASRRCMELEKYVEELAAVRQtlqtDLETSIRRIADLQAALEEVA 2130
Cdd:TIGR02169 396 KLKREINEL---KRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA 447
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1445-2128 |
2.20e-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: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTS-DLADERFKGDVACQVLE-----SERAERLQAF--RE 1516
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSrKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNhqRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1517 VQELKSKHEQVQKKLGDVNKQLEEAQQKIQ--LNDLERNPTGGDEWQ---MRFDCAQMENEfLRKRLQQCEERLDSELTA 1591
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLLNQEKTelLVEQGRLQLQADRHQehiRARDSLIQSLA-TRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1592 R--------------KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSrnhelEKKQKKFDLQLAQ 1657
Cdd:TIGR00606 393 KnfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1658 ALGESVFEKglrekvTQENTSVRWELgqlqqQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGL---KERLWK 1734
Cdd:TIGR00606 468 GSSDRILEL------DQELRKAEREL-----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1735 LESSALEQ----QKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLHQLEMQLEQEYE 1808
Cdd:TIGR00606 537 MEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1809 EKQMVLHEKQDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSdvqlllgtMEDGKTSVSKEELEKVHSQLEQSEA 1887
Cdd:TIGR00606 616 SKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRA--------MLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1888 KCEEALKTQKVL---TADLESM-------HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIA 1957
Cdd:TIGR00606 682 VCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1958 QSAADIGQiQELQLQLEEAKKEKHKLQeQLQVAQMRIEYLEQSTVDRAI---VSRQEAVICDLENKTEFQKVQIKRFEVl 2034
Cdd:TIGR00606 762 RLKNDIEE-QETLLGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIaqqAAKLQGSDLDRTVQQVNQEKQEKQHEL- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2035 virlrDSLIKMGEELSQAAtseSQQRESSQYYQRRLEELKADMEELvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2114
Cdd:TIGR00606 839 -----DTVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
730
....*....|....
gi 1034629688 2115 SIRRIADLQAALEE 2128
Cdd:TIGR00606 907 AKEQDSPLETFLEK 920
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1522-2128 |
3.38e-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: 65.81 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1522 SKHEQVQKKLGDVNKQLEEAQQKIQlnDLERNPTGGDEwqmrfDCAQMENEFlrKRLQQCEERLDSELTARKeleQKLGE 1601
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELK--NLDKNLNKDEE-----KINNSNNKI--KILEQQIKDLNDKLKKNK---DKINK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1602 LQSaydGAKKMAHQLKRKchhltcdlEDTCVLLENQQSRnheLEKKQKKFDLQLAQALGESVFEKGLREKVTQENtsvrw 1681
Cdd:TIGR04523 101 LNS---DLSKINSEIKND--------KEQKNKLEVELNK---LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY----- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1682 elgqlqqqlkqkeqeaSQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQ 1761
Cdd:TIGR04523 162 ----------------NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1762 RFElEIERMKQMHQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMVLHEKQ-DLE---GLIGTLCDQIghrdfd 1837
Cdd:TIGR04523 226 QNN-QLKDNIEKKQQEINEKTTEISNTQT-------QLN-QLKDEQNKIKKQLSEKQkELEqnnKKIKELEKQL------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1838 vekrlrrdlrrtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNK 1917
Cdd:TIGR04523 291 ------------NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1918 SLVDEQLYrlqfEKADLLKRIDEDQDDLNELMQKHKDliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL 1997
Cdd:TIGR04523 359 SEKQRELE----EKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1998 EQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSqyyQRRLEELKAD 2076
Cdd:TIGR04523 425 EKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKE 497
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 2077 MEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:TIGR04523 498 LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1445-1933 |
3.70e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.93 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELttlrRKLEKSEKLRNELRQNTDllESKIADLTSDLADERFKGDVACQVLESER-AERL----QAFREVQE 1519
Cdd:PTZ00121 1401 EEDKKKADEL----KKAAAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKADEAKKKAEEAKkAEEAkkkaEEAKKADE 1474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1520 LKSKHEQvQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDEWQmrfdcaQMENEFLRKRLQQCEERLDSELTARKELEQK 1598
Cdd:PTZ00121 1475 AKKKAEE-AKKADEAKKKAEEAKKKAdEAKKAAEAKKKADEAK------KAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1599 LGELQSAYDGAK----KMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ 1674
Cdd:PTZ00121 1548 ADELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1675 ENtSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK----------ERLWKLESSALEQQK 1744
Cdd:PTZ00121 1628 AE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALKKEAEEAKKAEE 1706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1745 IQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE--EEL---EDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQD 1819
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAkkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD 1786
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1820 LE-------------------------GLIGTLCDQIGHRDFDVEKR---LRRDLRRTHALLSDVQLLLGTMEDGKTSVS 1871
Cdd:PTZ00121 1787 EEdekrrmevdkkikdifdnfaniiegGKEGNLVINDSKEMEDSAIKevaDSKNMQLEEADAFEKHKFNKNNENGEDGNK 1866
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKAD 1933
Cdd:PTZ00121 1867 EADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1739-2135 |
3.97e-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: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1739 ALEQQKIQSQQENTIKQLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQ----KRLHQLEMQLEQEYEEKQMVL 1814
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELER----LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1815 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVqlllgtmedgktsvsKEELEKVHSQLEQSEAKceealk 1894
Cdd:COG4913 359 RRRARLE----ALLAALGLPLPASAEEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAA------ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1895 tQKVLTADLESMHSELENMTRNKSLVDEQLYRLqfeKADLLKRIDEDQDDLN---ELMQ-KHKDLIAQSAAdigqiqELQ 1970
Cdd:COG4913 414 -LRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAELPfvgELIEvRPEEERWRGAI------ERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1971 L------------QLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD---------------------RAIVSRQEAVIC 2015
Cdd:COG4913 484 LggfaltllvppeHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfrawlEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2016 dLENKTEFQKVqikRFEVlvirLRDSLIKMGEELSQAATsesQQRESSQYY-----QRRLEELKADMEELVQREAEASRR 2090
Cdd:COG4913 564 -VDSPEELRRH---PRAI----TRAGQVKGNGTRHEKDD---RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 2091 CMELEKYVEELAAVRQTLQT---------DLETSIRRIADLQAALEEVASSDSD 2135
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDD 686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1725-2145 |
4.96e-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: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1725 VAGLKERlwKLESsaleQQKIQSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRLH 1797
Cdd:TIGR02168 167 ISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1798 QLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLGTMEdGKTSVSKEELE 1876
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLE-QQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1877 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1956
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1957 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAvicdLENKTEfqkvqikRFEVLVI 2036
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQE-------ELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2037 RLrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSi 2116
Cdd:TIGR02168 462 AL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD- 532
|
410 420 430
....*....|....*....|....*....|..
gi 1034629688 2117 rriADLQAALEEVASSDSD---TESVQTAVDC 2145
Cdd:TIGR02168 533 ---EGYEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1441-1901 |
1.58e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1441 TIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvlesERAERLQAFREVQEL 1520
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELR------------EELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1521 KSKHEQVQKKLGDVNKQLEEAQQKIQ-LNDLERnptggdewqmrfDCAQMENEFLRKRLQQCEERLDSELTARKELEQ-- 1597
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEeLRELEE------------ELEELEAELAELQEELEELLEQLSLATEEELQDla 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1598 -KLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQEN 1676
Cdd:COG4717 199 eELEELQQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1677 -----------TSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK-RELLGSPSLGENcvaGLKERLWKLESSALEQQK 1744
Cdd:COG4717 275 iagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAALGLPPD---LSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1745 IQSQQENTIKQLEQlrQRFELEIER-MKQMHQKDREDQEEELEDVRQSCQ--KRLHQLEMQLEQEYEEKQMVL--HEKQD 1819
Cdd:COG4717 352 LLREAEELEEELQL--EELEQEIAAlLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLeaLDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1820 LEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGktsvskEELEKVHSQLEQSEAKCEEALKTQKVL 1899
Cdd:COG4717 430 LEEELEELEEEL--------EELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAAL 495
|
..
gi 1034629688 1900 TA 1901
Cdd:COG4717 496 KL 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1697-2139 |
1.66e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1697 ASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES------SALEQQKIQSQQENtiKQLEQLRQRFELEIERM 1770
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrDRLEECRVAAQAHN--EEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1771 KQMHQK----------------DREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghr 1834
Cdd:PRK02224 359 EELREEaaeleseleeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1835 dfdveKRLRRDLRRTHALLsdvqlllgtmEDGKTSVSKEELEKvhSQLEQSEAKCEEALKTQKVLTADLESMHSELEN-M 1913
Cdd:PRK02224 436 -----RTARERVEEAEALL----------EAGKCPECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEErL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1914 TRNKSLV--DEQLYRLQfEKADLLK--------RIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKL 1983
Cdd:PRK02224 499 ERAEDLVeaEDRIERLE-ERREDLEeliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1984 QEQLQVAQMRIEYLEqstvdraivsRQEAVICDLENktefqkvqikrfevlvirLRDSLIKMGEELSQAATSESQQRESS 2063
Cdd:PRK02224 578 NSKLAELKERIESLE----------RIRTLLAAIAD------------------AEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2064 QYYQRRLEELKAD-----MEELVQREAEASRRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASSDSD 2135
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
....
gi 1034629688 2136 TESV 2139
Cdd:PRK02224 710 LEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1632-2127 |
1.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1632 VLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1711
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1712 R--ELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR 1789
Cdd:COG4717 126 QllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1790 QSCQkrlhqlemQLEQEYEEKQMVLHE-KQDLEGLigtlcdQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLGTMEDGKT 1868
Cdd:COG4717 206 QRLA--------ELEEELEEAQEELEElEEELEQL------ENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1869 SVskeelekvhsqleqseakceeaLKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQfekaDLLKRIDEDQDDLNEL 1948
Cdd:COG4717 271 LI----------------------LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----ALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1949 MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEylEQSTVDRAIVSRQEAVICDLENKTEFQKVQi 2028
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2029 KRFEVLVIRLRDSLIKMGEELsqAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEK--YVEELAAVRQ 2106
Cdd:COG4717 402 EELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELE 479
|
490 500
....*....|....*....|.
gi 1034629688 2107 TLQTDLETSIRRIADLQAALE 2127
Cdd:COG4717 480 ELKAELRELAEEWAALKLALE 500
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1582-2128 |
2.20e-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: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1582 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdLEDTCVLLENQ--QSRNHELEKKQKKFDLQLAQAL 1659
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKlnEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1660 GESVFEKglrEKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspSLGENCVAGLKERLWKLESSA 1739
Cdd:pfam02463 258 QEIEKEE---EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1740 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRLHQLEMQLEQEYEEKQMV--L 1814
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAAKLKEEELELKSEEEKEAqlL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1815 HEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKT-SVSKEELEKVHSQLEQSEAKCEEAL 1893
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1894 KTQKVLTAD-LESMHSELENMtrNKSLVDEQLYRLQFEKADLLKRIDE-DQDDLNELMQKHKDLIAQSAADIGQIQELQL 1971
Cdd:pfam02463 491 SRQKLEERSqKESKARSGLKV--LLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1972 QLEEAKKEKHKLQEQLQVAQMRIeyleqstVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ 2051
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL-------KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 2052 AATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1453-2139 |
2.35e-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: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1453 ELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADErfKGDVACQVLESERAE-RLQAFRE--VQELKSKHEQ--- 1526
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAA--DAAVAKDRSELEALEdQHGAFLDadIETAAADQEQlps 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1527 VQKKLGDVNKQ---LEEAQQKIQ-------LNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELtaRKELE 1596
Cdd:pfam12128 352 WQSELENLEERlkaLTGKHQDVTakynrrrSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1597 QKLGELQSAYDGAKKMAHQLKRKCHHLTCDlEDTCVLLENQQSRNHELEKKQKK-----FDLQLAQALGESVFEKGLrEK 1671
Cdd:pfam12128 430 AGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAanaevERLQSELRQARKRRDQAS-EA 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1672 VTQENTSVRWELGQLQQQLKQKEQEASQL----KQQVEMLQDH-----KRELLG----SPSLGENCVAG----------- 1727
Cdd:pfam12128 508 LRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSigkviSPELLHrtdlDPEVWDGSVGGelnlygvkldl 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1728 --------------LKERLWKLESSALEQQKIQSQQEntiKQLEQLRQRFE---LEIERMKQMHQKDREDQeEELEDVRQ 1790
Cdd:pfam12128 588 kridvpewaaseeeLRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFARTALKNARLDL-RRLFDEKQ 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1791 SCQKRLHQlemqleQEYEEKQMVLHEKQDLEGLIGTLcdQIGHRDFDVEKRlRRDLRRTHALLSDVQLLLGTMEDGKTSV 1870
Cdd:pfam12128 664 SEKDKKNK------ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQLALL 734
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1871 sKEELEKVHSQLEQSEAKCEEALKT---------QKV--LTADLESMHSELENMTRNKSLVDE--QLYRLQF--EKADLL 1935
Cdd:pfam12128 735 -KAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERIAVRRQEVLRyfDWYQETWlqRRPRLA 813
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1936 KRIDEDQDDLNELMQkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL----EQSTVDRAIVSRQE 2011
Cdd:pfam12128 814 TQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGSIGE 890
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2012 AVIC--DLENKTEFQKVQIKRFevlvIRLRDSLI--KMGEELsqAATSESqQRESSQYYQRRLEELKADMEELVQREAEA 2087
Cdd:pfam12128 891 RLAQleDLKLKRDYLSESVKKY----VEHFKNVIadHSGSGL--AETWES-LREEDHYQNDKGIRLLDYRKLVPYLEQWF 963
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 2088 SRRCMELEKYVEELAAVRQTLQTD----LETSIRRIADLQAALEEVASSDSDTESV 2139
Cdd:pfam12128 964 DVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1445-2111 |
2.68e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEE--ELTTLRRKLEKSEKlRNELRQNTDLLESKiADLTSDLADERFKGDVACQVLESERAERLQAFREVQEL-K 1521
Cdd:PTZ00121 1293 DEAKKAEEkkKADEAKKKAEEAKK-ADEAKKKAEEAKKK-ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAaE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1522 SKHEQVQKKLGDVNKQLEEAQQKIQL-NDLERNPTGGDEWQMRfDCAQMENEFLRKRLQqcEERLDSELTARKELEQKLG 1600
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAkKKAEEDKKKADELKKA-AAAKKKADEAKKKAE--EKKKADEAKKKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1601 ELQSAYDGAKKmAHQLKRKCHhltcdledtcvllenQQSRNHELEKK-QKKFDLQLAQALGESVFEKGLREKVTQENTSV 1679
Cdd:PTZ00121 1448 EAKKKAEEAKK-AEEAKKKAE---------------EAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKK 1511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1680 RWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGEncvaglKERLWKLES--SALEQQKIQSQQENTIKQLE 1757
Cdd:PTZ00121 1512 ADEAKKAEEAKKADEAKKAEEAKKADEAKK-AEEKKKADELKK------AEELKKAEEkkKAEEAKKAEEDKNMALRKAE 1584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1758 QLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhqlEMQLEQEYEEKQMVLHEKQDLEGligtlcdqighrdfd 1837
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQLKKKEAE--------------- 1644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1838 vEKRLRRDLRRthallsdvqlllgtmEDGKTSVSKEELEKvhsQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNk 1917
Cdd:PTZ00121 1645 -EKKKAEELKK---------------AEEENKIKAAEEAK---KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA- 1704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1918 slvdEQLYRLQFE---KADLLKRIDEDQDDLNELMQKhkdliaQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQmRI 1994
Cdd:PTZ00121 1705 ----EELKKKEAEekkKAEELKKAEEENKIKAEEAKK------EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE-EI 1773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1995 EYLEQSTVDRAIVSRQEAVICDLENKTefqKVQIKRFEVLV-------IRLRDSLIKMGEELSQAATSESQQRESSQYYQ 2067
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVDKKI---KDIFDNFANIIeggkegnLVINDSKEMEDSAIKEVADSKNMQLEEADAFE 1850
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1034629688 2068 RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2111
Cdd:PTZ00121 1851 KHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1445-2329 |
2.73e-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: 62.83 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKS-EKLRNELRQNTDLLESKIADLTSDLAderfkgdVACQVLESERAERLQAFREVQELKsk 1523
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQFSQESGNLD-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 hEQVQKKLGDVNKQ-----LEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEflrkRLQQCEERLDSEltARKELEQK 1598
Cdd:pfam15921 377 -DQLQKLLADLHKRekelsLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE--CQGQMERQ 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1599 LGELQSAYDGAKKMAhqlkrkchHLTCDLEDTCVLL----ENQQSRNHELEKKQKKFDlQLAQALGESvfEKGLrEKVTQ 1674
Cdd:pfam15921 450 MAAIQGKNESLEKVS--------SLTAQLESTKEMLrkvvEELTAKKMTLESSERTVS-DLTASLQEK--ERAI-EATNA 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1675 ENTSVRwelgqlqqqlkqkeqeaSQLKQQVEMLQDHKREllgspslGENcvaglkerlwkLESSALEQQKIQSQQENTIK 1754
Cdd:pfam15921 518 EITKLR-----------------SRVDLKLQELQHLKNE-------GDH-----------LRNVQTECEALKLQMAEKDK 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1755 QLEQLRQrfelEIERMKQM-HQKDREDQEEELEdvrqscqkrlhqlEMQLEQEYEEKQMVLHEKQDLEgligtlcdqigh 1833
Cdd:pfam15921 563 VIEILRQ----QIENMTQLvGQHGRTAGAMQVE-------------KAQLEKEINDRRLELQEFKILK------------ 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1834 rdfdvEKRLRRdLRRTHALLSDVQL----LLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMH 1907
Cdd:pfam15921 614 -----DKKDAK-IRELEARVSDLELekvkLVNAGSERLRAVKdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1908 SELEnMTRNKslvdeqlYRLQFEKADllkridedqddlNELMQKHKDLIAQSAADiGQIQELQLQLEEAKKEKhklQEQL 1987
Cdd:pfam15921 688 EEME-TTTNK-------LKMQLKSAQ------------SELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAK---RGQI 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1988 QVAQMRIEYLEQSTVDraivsrqeavicdlENKTefqkvqiKRFevlvirLRDSLIKMGEELSQAATSESQ---QRESSQ 2064
Cdd:pfam15921 744 DALQSKIQFLEEAMTN--------------ANKE-------KHF------LKEEKNKLSQELSTVATEKNKmagELEVLR 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2065 YYQRRLEELKADMEELVQREAEASRRCMELEKYvEELAAVRQTLQTDLETS------IRRIADLQAALEEVASSDSDTES 2138
Cdd:pfam15921 797 SQERRLKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKelqgpgYTSNSSMKPRLLQPASFTRTHSN 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2139 VQTAVDCGSSGRKEMDNVSILSSQPEGSLQSWLSCTLSL-----ATDTMRTPSRQSATSSRILSPRINEEAgdterTQSA 2213
Cdd:pfam15921 876 VPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCI-----IESS 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2214 LALSRARSTNVHSKTSGDKpVSPHFVRRQKYCHFGDGEVLAVQRKSTERLEPASSPLASRSTNTSPlsrEKLPSPSaALS 2293
Cdd:pfam15921 951 LRSDICHSSSNSLQTEGSK-SSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSP---KKSPVHS-LLT 1025
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1034629688 2294 EFVEGLRRKRAQRGQGSTL----GLEDWPTLPIyQTTGAS 2329
Cdd:pfam15921 1026 SSAEGSIGSSSQYRSAKTIhspdSVKDSQSLPI-ETTGKT 1064
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1448-1914 |
4.64e-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: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1448 RAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDladerfKGDVACQVLESERAERLqAFREVQELKSKHEQV 1527
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1528 QKKLG---------DVNKQLEEAQqkiqlndLERnptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSE-------LTA 1591
Cdd:pfam01576 705 EDELQatedaklrlEVNMQALKAQ-------FER------DLQARDEQGEEKRRQLVKQVRELEAELEDErkqraqaVAA 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1592 RKELEQKLGELQSAYDGA-----------KKMAHQLKrkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1660
Cdd:pfam01576 772 KKKLELDLKELEAQIDAAnkgreeavkqlKKLQAQMK----DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQE 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1661 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgencvagLKERLWKLESSAL 1740
Cdd:pfam01576 848 DLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-------LNDRLRKSTLQVE 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1741 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQkdredqeeELEDVRQSCQK--------RLHQLEMQLEQEYEEKQM 1812
Cdd:pfam01576 921 QLTTELAAERSTSQKSESARQQLERQNKELKAKLQ--------EMEGTVKSKFKssiaaleaKIAQLEEQLEQESRERQA 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1813 VlhekqdlegligtlcdqighrdfdvekrlRRDLRRTHALLSDVqLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1892
Cdd:pfam01576 993 A-----------------------------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEA 1042
|
490 500
....*....|....*....|..
gi 1034629688 1893 LKTQKVLTADLESMHSELENMT 1914
Cdd:pfam01576 1043 EEEASRANAARRKLQRELDDAT 1064
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1445-2122 |
5.38e-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: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1524
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEEAQQKiqLNDLERnptggdewqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ------- 1597
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEE--YDRVEK----------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvhg 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1598 ---KLGELQSAYDGAKKMAhqLKRKCHHLTCDLEDTCV-----LLENQQSRNHEL---EKKQKKFDLQLAQALGESVFEK 1666
Cdd:TIGR02169 526 tvaQLGSVGERYATAIEVA--AGNRLNNVVVEDDAVAKeaielLKRRKAGRATFLplnKMRDERRDLSILSEDGVIGFAV 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1667 GLREKVTQENTSVRWELGQLQQqlkqkeqeasqlkqqVEMLqDHKRELLGspslgencvaglKERLWKLESSALEQQKIQ 1746
Cdd:TIGR02169 604 DLVEFDPKYEPAFKYVFGDTLV---------------VEDI-EAARRLMG------------KYRMVTLEGELFEKSGAM 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1747 SQQENTIKQLEQLRQRFELEIERMKqmhqkdreDQEEELEDVRQSCQKRLHQLEMQLEQeyeekqmVLHEKQDLEGLIGT 1826
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLR--------ERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIGE 720
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1827 LCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGKTSV--SKEELEKVHSQLEQSEAKCEEALktqkvltADLE 1904
Cdd:TIGR02169 721 IEKEI--------EQLEQEEEKLKERLEELEEDLSSLEQEIENVksELKELEARIEELEEDLHKLEEAL-------NDLE 785
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1905 SM--HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHK 1982
Cdd:TIGR02169 786 ARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1983 LQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ------AATS 2055
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgEDEE 945
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 2056 ESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADL 2122
Cdd:TIGR02169 946 IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1926-2128 |
6.46e-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: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1926 RLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdra 2005
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2006 ivsrqeavicDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREA 2085
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034629688 2086 EASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1725-2231 |
1.59e-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: 60.52 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1725 VAGLKERLwkLESSAL-EQQKIQSQQenTIKQLEQLRQRFELEIERMKQMHQKDREDQEeeleDVRQSCQKRLHQLEmql 1803
Cdd:pfam15921 87 VKDLQRRL--NESNELhEKQKFYLRQ--SVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQNTVHELE--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1804 eqeyEEKQMvlheKQDLEGLIGTLCDQighrdfdvekrLRRDLRRTHALLSDVQLLLGTMEDGKTsvskeelEKVHSQLE 1883
Cdd:pfam15921 156 ----AAKCL----KEDMLEDSNTQIEQ-----------LRKMMLSHEGVLQEIRSILVDFEEASG-------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1884 QSeakceealktqkvlTADLESMHSELENMTRNkslVDEQLYRLQ---FEKADLLKRI-DEDQDDLNELMQKHKDLIAQ- 1958
Cdd:pfam15921 210 MS--------------TMHFRSLGSAISKILRE---LDTEISYLKgriFPVEDQLEALkSESQNKIELLLQQHQDRIEQl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1959 -SAADIgQIQELQLQLEEAKKEKHKLQEQLQVAQmrieylEQSTVDRAIVSRQeavICDLEN-----KTEFQKVQiKRFE 2032
Cdd:pfam15921 273 iSEHEV-EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQ---LSDLEStvsqlRSELREAK-RMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2033 VLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEelvQREAEASrrcmeLEKYVEELAAVRQT----- 2107
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELS-----LEKEQNKRLWDRDTgnsit 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2108 ---LQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSgrKEMDNVSILSSQPEGSLQSWLSCTLSLATDTMRT 2184
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 2185 PSRQSATSSriLSPRINEEAGDTERTQSALALSRAR-----STNVHSKTSGD 2231
Cdd:pfam15921 492 ESSERTVSD--LTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGD 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1872-2128 |
2.03e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1951
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1952 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKR- 2030
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2031 FEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQT 2110
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|....*...
gi 1034629688 2111 DLETSIRRIADLQAALEE 2128
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1446-1993 |
3.36e-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: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1446 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSdladerfKGDVACQVLESERAErLQafREVQELKSKHE 1525
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE-------KKDHLTKELEDIKMS-LQ--RSMSTQKALEE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1526 QVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMEnEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1605
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEM 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1606 ydgaKKMAHQLKRKCHHLTCDL-EDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGESVFEkgLREKVTQENTSVRWel 1683
Cdd:pfam05483 397 ----TKFKNNKEVELEELKKILaEDEKLLDEKKQFEKIAEELKGKEQELIfLLQAREKEIHD--LEIQLTAIKTSEEH-- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1684 gqlqqqlkqkeqeasQLKQQVEMLQDHKRELLGSPSLGENCvaglkeRLWKLESSALEQQ------KIQSQQENTIKQLE 1757
Cdd:pfam05483 469 ---------------YLKEVEDLKTELEKEKLKNIELTAHC------DKLLLENKELTQEasdmtlELKKHQEDIINCKK 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1758 QlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFD 1837
Cdd:pfam05483 528 Q-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1838 VEKRLR--RDLRRTHALLSDVqlllGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTADLESMHSELENMT 1914
Cdd:pfam05483 603 IENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEEKLLEEVE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1915 RNKSLVDEQLyRLQFEkadLLKRIDEDQDDLNELMQKHK---DLIA----------------QSAADIGQIQEL------ 1969
Cdd:pfam05483 679 KAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAALEIELsnikae 754
|
570 580 590
....*....|....*....|....*....|
gi 1034629688 1970 ------QLQLEEAKKEKHKLQEQLQVAQMR 1993
Cdd:pfam05483 755 llslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1839-2129 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1839 EKRLRRDLRRTHALlsdvqlllgtmedGKTSVSK-EELEKVHSQLEQSEAKCEEALKTQKVLTADLE---SMHSELENMT 1914
Cdd:COG4913 591 EKDDRRRIRSRYVL-------------GFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQerrEALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1915 RNKSLVDEQLYRLQfEKADLLKRIDEDQDDLNELMQKHKDLIAQsaadigqIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1994
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1995 EYLeQSTVDRAIVSRQEAVICDLENKteFQKVQI-KRFEVLVIRLRDSLIKMGEELSQAATS-ESQQR------------ 2060
Cdd:COG4913 730 DEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEElERAMRafnrewpaetad 806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 2061 -----ESSQYYQRRLEELKADmeELVQREAEASRRCMELEKyvEELAAVRQTLQTDLETSIRRIADLQAALEEV 2129
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 ... |
1445-1951 |
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 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSD---LADERFKGDVACQVLESERAERLQafrEVQELK 1521
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQ---EIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1522 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaQMENEFlrKRLQQCEERLDSELtarKELEQKLGE 1601
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKE--------------LLEKEI--ERLKETIIKNNSEI---KDLTNQDSV 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1602 LQSAYDGAKKMAHQLKRKchhltcdLEDtcvlLENQ-QSRNHELEKKQKKFDLQlaqalgesvfekglrekvtqentsvr 1680
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQ-------LKV----LSRSiNKIKQNLEQKQKELKSK-------------------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1681 welgqlqqqlkqkeqeasqlKQQVEMLQDHKRELlgspslgENCVAGLKErlwKLESSALEQQKIqsqqENTIKQLEQLR 1760
Cdd:TIGR04523 495 --------------------EKELKKLNEEKKEL-------EEKVKDLTK---KISSLKEKIEKL----ESEKKEKESKI 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1761 QRFELEIERMKQMHQKdredqeEELEDVRQSCQKRLHQLEMQ---LEQEYEEKQMVLHEKQDlegLIGTLCDQIGHRDFD 1837
Cdd:TIGR04523 541 SDLEDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEK---EKKDLIKEIEEKEKK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1838 VEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE------------- 1904
Cdd:TIGR04523 612 ISS-LEKELEKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiielmkdwlkel 689
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1034629688 1905 SMHSE--LENMTRNKSLvdEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1951
Cdd:TIGR04523 690 SLHYKkyITRMIRIKDL--PKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1754-2133 |
1.61e-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: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1754 KQLEQLRqRFELEIE-RMKQMHQKDREDQE--EELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEK---QDLEGLIGTL 1827
Cdd:pfam05483 85 KEAEKIK-KWKVSIEaELKQKENKLQENRKiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1828 CDQIGHRDFDVEKRlRRDLRRTHA-LLSDVQLLLGTMEDGKTSVSKEELEkVHSQLEQSEAKCEEALktqkvltadlESM 1906
Cdd:pfam05483 164 CARSAEKTKKYEYE-REETRQVYMdLNNNIEKMILAFEELRVQAENARLE-MHFKLKEDHEKIQHLE----------EEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1907 HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK-------DLIAQSAADIGQIQELQLQLEEAKKE 1979
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1980 KHKLQEQLQVAQMRIEYL--------EQSTVDRA----IVSRQEAVICDLEnktEFQKVQIKRFEvlviRLRDSLIKMGE 2047
Cdd:pfam05483 312 QKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLE---ELLRTEQQRLE----KNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2048 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALE 2127
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
....*.
gi 1034629688 2128 EVASSD 2133
Cdd:pfam05483 461 AIKTSE 466
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1429-2102 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1429 QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKlrnelRQNTDLLESKIADLTSDLADerfkgdvacqVLESERA 1508
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKSLQNEKAD----------LDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1509 ErlqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNdlernptggdEWQMRFDCAQMENEFLRKRlqQCEERLDSE 1588
Cdd:TIGR00606 520 L-----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI----------KSRHSDELTSLLGYFPNKK--QLEDWLHSK 582
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1589 LTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE-------DTCVlLENQQSRNHELEKKQKKFDLQLAQALGE 1661
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfDVCG-SQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1662 SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESSALE 1741
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAPG 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1742 QQKIQSQQENTIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDVR------QSCQKRLHQLEMQLEQEYEEKQMVLH 1815
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKN----DIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQ 810
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1816 EKQDLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVskEELEKVHSQLEQSEAKCEEALKT 1895
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQR 882
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1896 QKVLTADLESMHSELENM------TRNKSLVDEQ-LYRLQFEKADLLKRIDED----QDDLNELMQKHKDLIAQSAADIG 1964
Cdd:TIGR00606 883 RQQFEEQLVELSTEVQSLireikdAKEQDSPLETfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIEN 962
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1965 QIQE---------------LQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTV---DRAIVSRQEAVICDLENKTEFQKV 2026
Cdd:TIGR00606 963 KIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKQHLK 1042
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 2027 QIKRFEVLviRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELA 2102
Cdd:TIGR00606 1043 EMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1870-2129 |
2.72e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1870 VSKEELEKVHSQLEQSEaKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL- 1948
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1949 --MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraivsrqeavICDLENKTEFQKv 2026
Cdd:PRK03918 221 eeLEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-------------IEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2027 QIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL---KADMEELVQREAEASRRCMELEKYVEELAA 2103
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270
....*....|....*....|....*....|.
gi 1034629688 2104 VRQtLQTDLET-----SIRRIADLQAALEEV 2129
Cdd:PRK03918 367 AKA-KKEELERlkkrlTGLTPEKLEKELEEL 396
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1745-2126 |
3.22e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1745 IQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQEEELEDVRQSCQkRLHQLEMQLEQEYEEKQMVLHEKQDLE 1821
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1822 GLIGTLCDQIGHRDFDVEKRLRRdlrrthaLLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVL 1899
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELErmKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1900 TADLESMHSELENMTRNKSLVDEQLYRLQfekadllkridedqDDLNELMQKhkdliaqsaadIGQIQELQLQLEEAKKE 1979
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQ--------------DTITTLTQK-----------LTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1980 KHKLQEQLQVAQMRIEYLEQSTvdRAIVSRQEAVICDLeNKTEFQKVQikrfevLVIRLRDSLIKMGEELSQAATSESQQ 2059
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2060 RESSQYYQRRLEELKAD---MEELVQREAeasrrcMELEKYVEELAAVRQTLQTDLETSIRRIADLQAAL 2126
Cdd:pfam07888 310 QQSAEADKDRIEKLSAElqrLEERLQEER------MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1966-2220 |
3.89e-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: 3.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1966 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIV----------SRQEAVICDLEN-KTEFQKVQiKRFEVL 2034
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2035 VIRlRDSLIKMGEElsqaATSESQQREssqyyqRRLEELKAD----MEEL-----VQREAEASRRC-------------- 2091
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGaalareqdklnwek 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2092 ------MELEKYVEELAAVRQtLQTDLETSIRRIADLQA--------ALEEVASSDSDTE----SVQTAVDcgsSGRKEM 2153
Cdd:pfam05701 227 elkqaeEELQRLNQQLLSAKD-LKSKLETASALLLDLKAelaaymesKLKEEADGEGNEKktstSIQAALA---SAKKEL 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 2154 DNV--SILSSQPE--------GSLQSWLSCTLS-LATdtmrtpSRQSATSSRILSPRINEEagdTERTQSALALSRAR 2220
Cdd:pfam05701 303 EEVkaNIEKAKDEvnclrvaaASLRSELEKEKAeLAS------LRQREGMASIAVSSLEAE---LNRTKSEIALVQAK 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1923-2142 |
4.18e-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: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1923 QLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstv 2002
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2003 draivsrqeavicdlenktefqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQREssqyyqrRLEELKADMEELvq 2082
Cdd:COG1196 303 ------------------------DIARLEERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEA-- 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2083 rEAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2142
Cdd:COG1196 350 -EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1725-2214 |
4.27e-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: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1725 VAGLKERLWKLESSaLEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLE 1804
Cdd:pfam15921 233 ISYLKGRIFPVEDQ-LEALKSESQN-----KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1805 QEYEEKQMVLHEKQDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLSDvqlllgtmedgktsvSKEELEK--VHSQL 1882
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---------------SQLRSELREAKRMYED---------------KIEELEKqlVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1883 EQSEAKCEEALKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQFEKA------DLLKRideDQDDLNELMQKHKD 1954
Cdd:pfam15921 357 ELTEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1955 LIA------------QSAADIG------QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAvicd 2016
Cdd:pfam15921 434 LLKamksecqgqmerQMAAIQGknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEK---- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2017 lENKTEFQKVQIKRFEVLV-IRLRD--SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADME--------------- 2078
Cdd:pfam15921 509 -ERAIEATNAEITKLRSRVdLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtaga 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2079 ---ELVQREAEASRRCMELEKYveelaavrQTLQTDLETSIR----RIADLQaaLEEVASSDSDTESVQTAVDCgssgRK 2151
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRVSDLE--LEKVKLVNAGSERLRAVKDI----KQ 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034629688 2152 EMDNVSILSSQPEGSLQSwLSCTLSLATDTMRTPSRQSATSSRILSPRINEEAGDTERTQSAL 2214
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1942-2130 |
4.87e-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: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1942 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAIVSRQEAvicdLEN 2019
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2020 KTEFQKVQIKRFEVLvirlrdSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVE 2099
Cdd:COG3883 91 RARALYRSGGSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|.
gi 1034629688 2100 ELAAVRQTLQTDLETSIRRIADLQAALEEVA 2130
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1890-2125 |
7.88e-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: 7.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1890 EEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAqsaadigQIQEL 1969
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1970 QLQLEEAKKEkhkLQEQLQVAQM--RIEYLE----QSTVDRAIVSRQ--EAVICDLENKTEFQKVQIKRfevlVIRLRDS 2041
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRlgRQPPLAlllsPEDFLDAVRRLQylKYLAPARREQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2042 LIKMGEELSQAATSESQQRessqyyqRRLEELKADMEELVqreAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2121
Cdd:COG4942 169 LEAERAELEALLAELEEER-------AALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 1034629688 2122 LQAA 2125
Cdd:COG4942 239 AAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1854-2128 |
9.44e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1854 SDVQLLLGTMEDGKtsvsKEELEKVHSQLEQSEAKceEALKTQKVLTADLESMHSELENMTRNKSLVDEQLyrlqfEKAD 1933
Cdd:PRK02224 172 SDARLGVERVLSDQ----RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-----DEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1934 L-LKRIDEDQDDLNELMQkhkdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLE--------QSTVDR 2004
Cdd:PRK02224 241 EvLEEHEERREELETLEA--------------EIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2005 AIVSRQEAVICDLENKTEF-------QKVQIKRFEVLVIRLRDSLIKMGEEL----SQAATSESQ---QRESSQYYQRRL 2070
Cdd:PRK02224 307 ADAEAVEARREELEDRDEElrdrleeCRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESEleeAREAVEDRREEI 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629688 2071 EELKADMEELVQREAEASRRCMELEKYVEELAAVRQ-------TLQTDLETSIRRIADLQAALEE 2128
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereaELEATLRTARERVEEAEALLEA 451
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1911-2140 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1911 ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK--DLIAQSAADIGQIQELQLQLEEAkkekhklQEQLQ 1988
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-------RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1989 VAQMRIEYLEQ---STVDRAIVSRQEAVICDLenKTEFQKVQIKRFEVLViRLRDSLIKMGEELSQAATSESQQRESSqy 2065
Cdd:COG3206 237 EAEARLAALRAqlgSGPDALPELLQSPVIQQL--RAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALRAQLQQEA-- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2066 yQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQT---LQTDLETSIRRIADLQAALEEV-ASSDSDTESVQ 2140
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1507-2157 |
1.78e-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: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1507 RAERLQAfrEVQELKSKHEQVQK-KLGDVNKQLEEA-QQKIQ---LNDLE-RNPTGGDEWQMRFDCAQMENEFLRKRLQQ 1580
Cdd:pfam12128 242 EFTKLQQ--EFNTLESAELRLSHlHFGYKSDETLIAsRQEERqetSAELNqLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1581 CEERLDSeLTARKELEQKLGELQSAYDgaKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKFDLQLAQALg 1660
Cdd:pfam12128 320 DRSELEA-LEDQHGAFLDADIETAAAD--QEQLPSWQSELENLEERLK---ALTGKHQDVTAKYNRRRSKIKEQNNRDI- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1661 eSVFEKGLREkvtQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLES 1737
Cdd:pfam12128 393 -AGIKDKLAK---IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLksrLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1738 SALEQQKIQSQQENTIKQLE-------QLRQRFELEIERMKQMHQKdredqeeeLEDVRQSCQKRLHQLEMQleqeyeeK 1810
Cdd:pfam12128 469 FDERIERAREEQEAANAEVErlqselrQARKRRDQASEALRQASRR--------LEERQSALDELELQLFPQ-------A 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1811 QMVLH----EKQDLEGLIGTLCD--QIGHRDFDVEKrlrrdlrrTHALLSDVQLLLGTMEDGKtSVSKEELEKVHSQLEQ 1884
Cdd:pfam12128 534 GTLLHflrkEAPDWEQSIGKVISpeLLHRTDLDPEV--------WDGSVGGELNLYGVKLDLK-RIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1885 SEAKCEEALKTQKVLTADLESMHSELenmtrNKSLvDEQLYRLQFEKADlLKRIDEDQDDLNELMQKHKDLIAQSAADIG 1964
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQA-----NGEL-EKASREETFARTA-LKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1965 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQST-------------------VDRAIVSRQEAV-----ICDLENK 2020
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywqvvegaldaqlalLKAAIAARRSGAkaelkALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2021 TEFQKVQIKrfEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQR-----------RLEELKADMEEL------VQR 2083
Cdd:pfam12128 758 RDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprlatQLSNIERAISELqqqlarLIA 835
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034629688 2084 EAEASRRCMELEKYVEELAAVRQT-LQTDLETSIRRIADLQaaleEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2157
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSeNLRGLRCEMSKLATLK----EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1639-1920 |
2.65e-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: 52.82 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1639 SRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQ--DHKRELlg 1716
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeERKREL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1717 sPSLGENCVAGLKERLWKLESSALEQQ----KIQSQQENTIKQ--LEQLRQR------FELEIERMKQMHQKDR------ 1778
Cdd:pfam17380 363 -ERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVkiLEEERQRkiqqqkVEMEQIRAEQEEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1779 EDQEEELEDVRQSCQKRLHQLEM--QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDv 1856
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 1857 qlllgTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRNKSLV 1920
Cdd:pfam17380 521 -----EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1734-1999 |
2.78e-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: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1734 KLESSALEQQKIQSQQENTIKQLEQLRQR----------FELEIERMKQM--HQKDREDQEE--ELEDVRQSCQKRLHQL 1799
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARieeleedlhkLEEALNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1800 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKE------ 1873
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdelea 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1874 ELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkSLVDEQLYRLQFEKADLLKrIDEDQDDLNELMQKHK 1953
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIR 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034629688 1954 DLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1999
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1445-1878 |
2.96e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLeSKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSKH 1524
Cdd:PRK03918 276 EELEEKVKELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEI-------NGIEERIKELEEKEERLEELKKKL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVN---KQLEEAQQKI-QLNDLERNPTGgdewqMRFDCAQMENEFLRKRLQQCEERLdSELTARK-ELEQKL 1599
Cdd:PRK03918 348 KELEKRLEELEerhELYEEAKAKKeELERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEI-SKITARIgELKKEI 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1600 GELQSAYDGAKKMahqlKRKC---------HH-------LTCDLED-----------------------TCVLLENQQSR 1640
Cdd:PRK03918 422 KELKKAIEELKKA----KGKCpvcgrelteEHrkelleeYTAELKRiekelkeieekerklrkelreleKVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1641 NH-------ELEKKQKKFDLQLAQALGESvFEKGLRE--KVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1711
Cdd:PRK03918 498 LKelaeqlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1712 RELLgspSLGENCVAGLKERLWKLES------------SALE-----QQKIQSQQENTIKQLEQLRQRFELEIERMKQMH 1774
Cdd:PRK03918 577 KELE---ELGFESVEELEERLKELEPfyneylelkdaeKELEreekeLKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1775 QKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVlheKQDLEGLigtlcdqigHRDFDVEKRLRRDLRRTHALLS 1854
Cdd:PRK03918 654 KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKL---------KEELEEREKAKKELEKLEKALE 721
|
490 500
....*....|....*....|....
gi 1034629688 1855 DVQLLLGTMEDGKTSVSKEELEKV 1878
Cdd:PRK03918 722 RVEELREKVKKYKALLKERALSKV 745
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1728-2134 |
5.93e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1728 LKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQE-EELEDVRQSCQKRLHQLEMQL 1803
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1804 eQEYEEKQmvlHEKQDLEGLIGTLCDQI----GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDgktsvSKEELEKVH 1879
Cdd:COG4717 156 -EELRELE---EELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1880 SQLEQSEAKCEEALKTQK---------------------------------VLTADLESMHSELENMTRNKSLVDEQLYR 1926
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1927 LQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmrIEYLEQstvdrai 2006
Cdd:COG4717 307 LQ----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQ------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2007 vsrqeavicdlENKTEFQKVQIKrfevlvirLRDSLIKMGEELSQAAtsesQQRESSQYYQRRLEELKADMEELVQREAE 2086
Cdd:COG4717 371 -----------EIAALLAEAGVE--------DEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1034629688 2087 AsrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2134
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1516-2004 |
7.25e-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: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1516 EVQELKSK-HEQVQKKLGDVNKQLEEAQQkiqLNDlernptggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKE 1594
Cdd:pfam06160 46 KFEEWRKKwDDIVTKSLPDIEELLFEAEE---LND-----------KYRFKKAKKALDEIEELLDDIEEDIKQILEELDE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1595 LEQKLGELQSAYDGAKKMAHQLKRKchhltcdledtcvLLENqqsrNHELEKKQKKFDLQLAQAlgESVFEKglrekVTQ 1674
Cdd:pfam06160 112 LLESEEKNREEVEELKDKYRELRKT-------------LLAN----RFSYGPAIDELEKQLAEI--EEEFSQ-----FEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1675 ENTSvrwelgqlqqqlkQKEQEASQLKQQVEMLQDHKRELLGS-PSLGENCVAGLKERLWKLES--SALEQQKIQSQQEN 1751
Cdd:pfam06160 168 LTES-------------GDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyREMEEEGYALEHLN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1752 TIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDvrqscqkRLHQLEMQLEQEYEEKQMVLHEKQDLEgligtlcDQI 1831
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEKNLPEIE-------DYL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1832 GHRDfDVEKRLRRDLRRT---------------------HALLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAK 1888
Cdd:pfam06160 301 EHAE-EQNKELKEELERVqqsytlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSelQEELEEILEQLEEIEEE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1889 CEEALKTQKVLTAD-------LESMHSELENM-----TRNKSLVDEQlYRLQFEKA-DLLKRIDED-------------- 1941
Cdd:pfam06160 380 QEEFKESLQSLRKDelearekLDEFKLELREIkrlveKSNLPGLPES-YLDYFFDVsDEIEDLADElnevplnmdevnrl 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1942 ----QDDLNELMQKHKDLIaQSAADIGQ-IQ----------ELQLQLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVDR 2004
Cdd:pfam06160 459 ldeaQDDVDTLYEKTEELI-DNATLAEQlIQyanryrssnpEVAEALTEAELlfRNYDYEKALEIAATALEKVEPGAYER 537
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1737-2129 |
7.62e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 51.76 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1737 SSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----HQLEMQLEQ--EYEE 1809
Cdd:PTZ00440 891 RSNSNKQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYD 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1810 KQmvlheKQDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAK 1888
Cdd:PTZ00440 970 KS-----KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKE 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1889 CEEalKTQKVLTAdLESMHSELENMTRNK-------SLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS-- 1959
Cdd:PTZ00440 1040 IEE--KVDQYISL-LEKMKTKLSSFHFNIdikkyknPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdk 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1960 ------------AADIG----QIQELQLQLEEAKKEKHKLQEqlqVAQMRIEYleqstvDRAIVSRQEAVICDLENKTEF 2023
Cdd:PTZ00440 1117 eknkqtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILIDHIVEQINNEAKKSKT 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2024 QKVQIKRFEVLVIRLRDSLIKmgEELSQAATSESQQressqyYQRRLEELKADMEELVQrEAEASRRCMELEKYVEELAA 2103
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNMSK--ERNDHLTTFEYNA------YYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKE 1258
|
410 420
....*....|....*....|....*.
gi 1034629688 2104 VRQTLQTDLETSIRRIADLQAALEEV 2129
Cdd:PTZ00440 1259 IKLQVFSYLQQVIKENNKMENALHEI 1284
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1431-1802 |
7.97e-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: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1431 LGSLQPLLSATigTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAER 1510
Cdd:pfam15921 463 VSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1511 lqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERL--DSE 1588
Cdd:pfam15921 541 ----DHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1589 LTARKELEQKLGELQ--------------SAYDGAKKMAHQLKRKCHHLTCDL----EDTCVLLENQQSRNHELEKKQKK 1650
Cdd:pfam15921 617 DAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTNK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1651 FDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGENcvaglKE 1730
Cdd:pfam15921 697 LKMQLKSAQSE-------LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNAN-----KE 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1731 R-LWKLESSALEQQ--KIQSQQENTIKQLEQLR---QRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKRL 1796
Cdd:pfam15921 764 KhFLKEEKNKLSQElsTVATEKNKMAGELEVLRsqeRRLKEKVANMEvaldkaslQFAECQDIIQRQEQESVRLKLQHTL 843
|
....*.
gi 1034629688 1797 HQLEMQ 1802
Cdd:pfam15921 844 DVKELQ 849
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1745-2070 |
1.33e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1745 IQSQQENTIKQLEQLrqrfeleiERMKQMHQKDrEDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLI 1824
Cdd:PLN02939 102 MQRDEAIAAIDNEQQ--------TNSKDGEQLS-DFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1825 GTLcdqighrdfdvEKRLRRdlrrthallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---SEAKCEEA-------LK 1894
Cdd:PLN02939 173 NIL-----------EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVHSlskeldvLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1895 TQKV-LTADLESMHSELENMT----------RNKSLVDEQLYRLQFE----KADLLK----RID---EDQDDLNELMQKH 1952
Cdd:PLN02939 233 EENMlLKDDIQFLKAELIEVAeteervfkleKERSLLDASLRELESKfivaQEDVSKlsplQYDcwwEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1953 KDLIAQSAADIGQ-------IQELQLQLEEAKKEKHKLqEQLQVAQMRIEYLEqstvdraivSRQEAviCDLENKTefqk 2025
Cdd:PLN02939 313 TNQVEKAALVLDQnqdlrdkVDKLEASLKEANVSKFSS-YKVELLQQKLKLLE---------ERLQA--SDHEIHS---- 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034629688 2026 vQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRL 2070
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1740-2144 |
1.61e-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: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1740 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE-DQEEELEDVRQSCQKRLH--------QLEM--------- 1801
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAeaeealreQAELnrlkkkyle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1802 ---QLEQEYEEKQMVLHEKQD-LEGLIGTLCDQIGHRDFDVE------KRLRRDLRRTHALLSDVQLLLGTMEdGKTSVS 1871
Cdd:pfam05557 87 alnKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQstnselEELQERLDLLKAKASEAEQLRQNLE-KQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVhSQLE---QSEAKCEEALKTQKVLTADLESMHSELE----------NMTRNKSLVDEQLYRLQFEkadlLKRI 1938
Cdd:pfam05557 166 AEAEQRI-KELEfeiQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRK----LERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1939 DEDQDDLNELMQKHKDLIA--QSAADIGQIQEL-------------QLQLEEA--KKEKHKLQEQLQVAQMRIEYLEQSt 2001
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQelQSWVKLAQDTGLnlrspedlsrrieQLQQREIvlKEENSSLTSSARQLEKARRELEQE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2002 vdraiVSRQEAVICDLENKTEFQKVQIKRFE---VLVIRLRDSLIKMGEELSqaatSESQQRESSQYYQRRLEELkADME 2078
Cdd:pfam05557 320 -----LAQYLKKIEDLNKKLKRHKALVRRLQrrvLLLTKERDGYRAILESYD----KELTMSNYSPQLLERIEEA-EDMT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 2079 ELVQREAEASRrcMELEKYVEELAAVRQTLQTD-LETSIRRiadLQAALEEVASSDSDTESVQTAVD 2144
Cdd:pfam05557 390 QKMQAHNEEME--AQLSVAEEELGGYKQQAQTLeRELQALR---QQESLADPSYSKEEVDSLRRKLE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1445-1805 |
2.16e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKL-EKSEKLRNELRQNT-------DLLESKIADLTSDLadERFkgdvacqVLESERAERLQAFRE 1516
Cdd:PRK04778 129 QELLESEEKNREEVEQLkDLYRELRKSLLANRfsfgpalDELEKQLENLEEEF--SQF-------VELTESGDYVEAREI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1517 VQELKSKHEQVQKKLGDVNKQLEEAQQKI--QLNDLErnpTGGDEWQM---RFDCAQMENEF--LRKRLQQC-------- 1581
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELpdQLQELK---AGYRELVEegyHLDHLDIEKEIqdLKEQIDENlalleeld 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1582 -----------EERLDS-------ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLtcdledtcvllenQQSR--N 1641
Cdd:PRK04778 277 ldeaeekneeiQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV-------------KQSYtlN 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1642 HELEKKQKKFDLQLAQAlgESVFEKgLREKVTQENTSvrwelgqlqqqlkqkeqeASQLKQQVEMLQDHkrellgspslg 1721
Cdd:PRK04778 344 ESELESVRQLEKQLESL--EKQYDE-ITERIAEQEIA------------------YSELQEELEEILKQ----------- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1722 encvaglkerlwklessaLEQqkIQSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEELE 1786
Cdd:PRK04778 392 ------------------LEE--IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMFF 451
|
410
....*....|....*....
gi 1034629688 1787 DVrqscQKRLHQLEMQLEQ 1805
Cdd:PRK04778 452 EV----SDEIEALAEELEE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1872-2088 |
2.74e-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: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRnkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1951
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1952 HKDLIAQSAAD--IGQIQELQLQLEEAKK---EKH----KLQEQLQVAQmrieyleqstvdRAIVSRQEAVICDLENKTE 2022
Cdd:COG3206 256 LPELLQSPVIQqlRAQLAELEAELAELSArytPNHpdviALRAQIAALR------------AQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 2023 FQKVQIKrfevlviRLRDSLIKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEAS 2088
Cdd:COG3206 324 ALQAREA-------SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1873-2101 |
3.49e-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: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1873 EELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKH 1952
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1953 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAI--VSRQEAVICDLENKTEFQKVQIKR 2030
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVELEEELKVVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 2031 FEVlvirlrdslikmgeelsqaATSESQQRESSqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2101
Cdd:pfam00261 160 LEA-------------------SEEKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1444-1611 |
4.49e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1444 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1523
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE-------AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIQlndlERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERldsELTAR-KELEQKLGEL 1602
Cdd:COG1340 80 RDELNEKLNELREELDELRKELA----ELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK---ELVEKiKELEKELEKA 152
|
....*....
gi 1034629688 1603 QSAYDGAKK 1611
Cdd:COG1340 153 KKALEKNEK 161
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1451-2059 |
5.04e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1451 EEELTTLRRKLEKSEKLRNELRQNTDLLES---KIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQV 1527
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1528 QKklgdVNKQLEEAQQKIQLNDLERNP-TGGDEWQMRF--DCAQMENEFLRK---------RLQQCEERLDSELTARKEL 1595
Cdd:PRK01156 252 NR----YESEIKTAESDLSMELEKNNYyKELEERHMKIinDPVYKNRNYINDyfkykndieNKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1596 EQKLGELQSAYDGAKKMAHQ---LKRKCHHLTCDLEDTCVLLENQQSRN---HELEKKQKKFDLQLAQALGESVFE---- 1665
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDpdai 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1666 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGE----NCVAGLKERLWKLESSALE 1741
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEeksnHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1742 QQKIQSQQENTIKQLEQLRQRFEL-EIERMKQMHQKdREDQEEELEDVRQScQKRLHQLEMQLEQEYEE-KQMVLhekQD 1819
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNK-IESARADLEDIKIK-INELKDKHDKYEEIKNRyKSLKL---ED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1820 LEGLIGTLCDQIGHRD-FDVEK-RLRRDlrrthallsDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTqk 1897
Cdd:PRK01156 563 LDSKRTSWLNALAVISlIDIETnRSRSN---------EIKKQLNDLESRLQEI-EIGFPDDKSYIDKSIREIENEANN-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1898 vltadLESMHSELENmtrNKSLVDEqlyrLQFEKADLLKRI---DEDQDDLNELMQKhkdlIAQSAADIGQIQElqlQLE 1974
Cdd:PRK01156 631 -----LNNKYNEIQE---NKILIEK----LRGKIDNYKKQIaeiDSIIPDLKEITSR----INDIEDNLKKSRK---ALD 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1975 EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavicdleNKTEFQKVQIKRFEVLVIRLRDSLIKMG------EE 2048
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDI--------------NETLESMKKIKKAIGDLKRLREAFDKSGvpamirKS 757
|
650
....*....|.
gi 1034629688 2049 LSQAATSESQQ 2059
Cdd:PRK01156 758 ASQAMTSLTRK 768
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1901-2134 |
6.34e-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: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1901 ADLESMHSELENMTRnkslvdeqlyrlqfeKADLLKRIDEDQDDLNELMQKHKDLiaQSAADIGQIQELQLQLEEAKKEK 1980
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1981 HKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAVICDLENKTEfqkvQIKRFEvlvirlrdslikmgEELSQAATSESQQR 2060
Cdd:COG4913 298 EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGD----RLEQLE--------------REIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 2061 ESSQYYQRRLEELK----ADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2134
Cdd:COG4913 359 RRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1789-2128 |
6.45e-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: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1789 RQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQlllGTMEDGKT 1868
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR---EQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1869 SvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMtrnkslvDEQLYRLQFEKADLLKRIDEDQDDLNEL 1948
Cdd:pfam05557 81 K--KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA-------ELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1949 MQKHKDLIAQ---SAADIGQIQEL--QLQLEEAKKE--KHKLQEQLQVAQMRIEyLEQSTVDRAIVSRQEAVICDLENKT 2021
Cdd:pfam05557 152 EQLRQNLEKQqssLAEAEQRIKELefEIQSQEQDSEivKNSKSELARIPELEKE-LERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2022 EFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYV 2098
Cdd:pfam05557 231 EDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350
....*....|....*....|....*....|
gi 1034629688 2099 EELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1665-2157 |
9.33e-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: 48.04 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1665 EKGLREKVTQENTSvRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQK 1744
Cdd:TIGR00618 228 LKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1745 IQSQQENTIKQleqlRQRFELEIERMK-QMHQKDREDQEE----------ELEDVRQSCQKRLHQLEmQLEQEYEEKQMV 1813
Cdd:TIGR00618 307 QQAQRIHTELQ----SKMRSRAKLLMKrAAHVKQQSSIEEqrrllqtlhsQEIHIRDAHEVATSIRE-ISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1814 LHEKQDLEGLIGTLcdQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME-DGKTSVSKEELEKVHSQLEQSEAKCEE- 1891
Cdd:TIGR00618 382 HTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKi 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1892 -------ALKTQKVLTADLESMHselENMTRNKSLVDEQLYRLQFEKADLLKRIDEdqddLNELMQKHKDLIAQSAADIG 1964
Cdd:TIGR00618 460 hlqesaqSLKEREQQLQTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIH----PNPARQDIDNPGPLTRRMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1965 QIQELQLQLEEAKKEKHKLQEQLQVAQmriEYLEQSTvdRAIVSRQEAVICDLENKTEFQKVQIKRFEVL-VIRLRDSLI 2043
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRA---SLKEQMQ--EIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2044 KMGEELSQAATSESQ-----------QRESSQYYQRRLEELKADMEELVQ-REAEASRRCMELEkyvEELAAVRQTLQTD 2111
Cdd:TIGR00618 608 DMLACEQHALLRKLQpeqdlqdvrlhLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLP---KELLASRQLALQK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1034629688 2112 LETSIRRIADLqaaLEEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2157
Cdd:TIGR00618 685 MQSEKEQLTYW---KEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1445-1604 |
9.66e-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: 9.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKH 1524
Cdd:COG4913 288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----------NGGDRLEQLE--REIERLEREL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEEAQQKIqlndlernPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1604
Cdd:COG4913 355 EERERRRARLEALLAALGLPL--------PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1699-2129 |
1.07e-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: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1699 QLKQQVEMLQDHKREllgspslGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIE-RMKQMHQKD 1777
Cdd:TIGR04523 51 NKEKELKNLDKNLNK-------DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKnDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1778 RE--DQEEELEDVRQSCQK---RLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHAL 1852
Cdd:TIGR04523 124 VElnKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK-IKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1853 LSDVQLLlgtMEDGKTSVSK-EELEKVHSQLEQSEAKceealKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQF 1929
Cdd:TIGR04523 203 LSNLKKK---IQKNKSLESQiSELKKQNNQLKDNIEK-----KQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1930 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ---------- 1999
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkkelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2000 ------STVDRAIVSRQEAVIcDLENKTEFQKVQIKRFEVLVIRLRdSLIKMGEELSQAATSESQQRESS-QYYQRRLEE 2072
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQKDEQIKKLQQEkELLEKEIER 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 2073 LKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2129
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1922-2113 |
1.50e-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: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1922 EQLYRLQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQst 2001
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2002 vdraivsRQEAV-----ICDLENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAATSESQQREssqyyqrRLEELKAD 2076
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEA-------ELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034629688 2077 MEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDLE 2113
Cdd:COG1579 140 LEEK---KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1734-1984 |
1.72e-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: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1734 KLESSALEQQKiqsqQENTIKqlEQLRQRFELEIERMKQMHQKDredqeeeledvrqscQKRLHQLEMQLEQEYEEKQMV 1813
Cdd:pfam09728 71 KLEKLCRELQK----QNKKLK--EESKKLAKEEEEKRKELSEKF---------------QSTLKDIQDKMEEKSEKNNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1814 LHEKQDLEGLIGTLCDQIGHRDFDVEKRLR-RDLrrthallsDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1892
Cdd:pfam09728 130 REENEELREKLKSLIEQYELRELHFEKLLKtKEL--------EVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1893 LKTQKVLTADLeSMHS----ELENmTRNKSLVDEQLYRLQFEK-ADLLKRIDEDqddlNELMQKHKDLIAQSAADIGQ-I 1966
Cdd:pfam09728 202 SETEKELREQL-NLYVekfeEFQD-TLNKSNEVFTTFKKEMEKmSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEeR 275
|
250
....*....|....*...
gi 1034629688 1967 QELQLQLEEAKKEKHKLQ 1984
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLE 293
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1458-1930 |
1.74e-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: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1458 RRKLEKSEKLRNELRQNTDLLESKIADLTSDLAderfkgdvacQVLESERAERLqafrEVQELKSKHEQVQKKLGDVNKQ 1537
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRKTLLANRFS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1538 LEEAQQKI--QLNDLERNPTGGDEW--QMRFDCAQMENEFLRKRLQQCEERLDS--EL--TARKELEQKLGELQSAYDga 1609
Cdd:pfam06160 144 YGPAIDELekQLAEIEEEFSQFEELteSGDYLEAREVLEKLEEETDALEELMEDipPLyeELKTELPDQLEELKEGYR-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1610 kkmahQLKRKCHHLT-CDLEDTCVLLENQQSRNHELEKKqkkfdLQLAQAlgesvfEKGLREkvtqentsvrwelgqlqq 1688
Cdd:pfam06160 222 -----EMEEEGYALEhLNVDKEIQQLEEQLEENLALLEN-----LELDEA------EEALEE------------------ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1689 qlkqkeqEASQLKQQVEMLQdhkRELLGSPSLGENcVAGLKERLwklessaleqQKIQSQQENTIKQLEQLRQRFELeie 1768
Cdd:pfam06160 268 -------IEERIDQLYDLLE---KEVDAKKYVEKN-LPEIEDYL----------EHAEEQNKELKEELERVQQSYTL--- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1769 rmkqmhqkdredQEEELEDVRQScQKRLHQLE---MQLEQEYEEKQMVLHEKQD-LEGLIGTLcDQI--GHRDFDVE-KR 1841
Cdd:pfam06160 324 ------------NENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSELQEeLEEILEQL-EEIeeEQEEFKESlQS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1842 LRRDLRRTHALLSDVQLLLGTMedgKTSVSK------------------EELEKVHSQLEQS-------EAKCEEAlktq 1896
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA---- 462
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1034629688 1897 kvlTADLESMHSELENMTRNKSLVdEQL------YRLQFE 1930
Cdd:pfam06160 463 ---QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1750-2087 |
1.93e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1750 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL----HQ-------LEMQLEQ------------- 1805
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrFSfgpaldeLEKQLENleeefsqfvelte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1806 --EYEEKQMVLHEKQDLEGLIGTLCDQI--------------------GHRD----------FDVEKRLRR---DLRRTH 1850
Cdd:PRK04778 190 sgDYVEAREILDQLEEELAALEQIMEEIpellkelqtelpdqlqelkaGYRElveegyhldhLDIEKEIQDlkeQIDENL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1851 ALLSdvQLLLGTMEDGKTSVSkEELEKVHSQLEQS-EAKcEEALKTQKVLTADLEsmHSElenmTRNKSLVDE-----QL 1924
Cdd:PRK04778 270 ALLE--ELDLDEAEEKNEEIQ-ERIDQLYDILEREvKAR-KYVEKNSDTLPDFLE--HAK----EQNKELKEEidrvkQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1925 YRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQ--VAQMRIEylEQSTV 2002
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSemLQGLRKD--ELEAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2003 DRAIVSRQEavicdLENktefqkvqIKRfevLVIRLR---------DSLIKMGEELSQAATSESQQRESSQYYQRRLEEL 2073
Cdd:PRK04778 418 EKLERYRNK-----LHE--------IKR---YLEKSNlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
410
....*....|....
gi 1034629688 2074 KADMEELvQREAEA 2087
Cdd:PRK04778 482 TEDVETL-EEETEE 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1645-2017 |
2.10e-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: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1645 EKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgENC 1724
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-KKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1725 VAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQKRLHQLEMQLE 1804
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1805 ---QEYEEKQMVLhEKQDLEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQ 1881
Cdd:COG5185 388 stkESLDEIPQNQ-RGYAQEILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1882 LEQSEAKCEEALKTQK-VLTADLESMHSELENMTRNkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1960
Cdd:COG5185 465 LEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 1961 ADIGQIQELQLQLEEakkekHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDL 2017
Cdd:COG5185 542 ENLIPASELIQASNA-----KTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQ 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1843-2143 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1843 RRDLRRTHALLSDVQLLLGTME----------DGKTSVSKEELEKVHSQLEQSEAKCEealKTQKVLTADLESMHSELEn 1912
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrarielEKKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1913 MTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDL-NELMQKHKdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQ 1991
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRR-----------QIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1992 MRIEYLEQstvdraivsrqeaVICDLENKTEFQKVQIKRFEVLVIRLR----DSLI--KMGEELSQAATSESQQR----- 2060
Cdd:pfam05557 146 AKASEAEQ-------------LRQNLEKQQSSLAEAEQRIKELEFEIQsqeqDSEIvkNSKSELARIPELEKELErlreh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2061 ---------------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSiRRIADLQ-- 2123
Cdd:pfam05557 213 nkhlnenienklllkEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqr 291
|
330 340
....*....|....*....|..
gi 1034629688 2124 --AALEEVASSDSDTESVQTAV 2143
Cdd:pfam05557 292 eiVLKEENSSLTSSARQLEKAR 313
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1699-2108 |
2.99e-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: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1699 QLKQQVEMLQDHKRELLGspslgENcvAGLKERLWKLES------------SALEQQKIQSQQENTikQLEQLRQRFELE 1766
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQ-----EN--KKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENF--RLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1767 IERMK------QMHQKDREDQEEELE------DVRQSCQKRLHQLEMQLE------QEYEE--KQMVLHEKQDLEGLIGT 1826
Cdd:pfam05622 89 CEELEkevlelQHRNEELTSLAEEAQalkdemDILRESSDKVKKLEATVEtykkklEDLGDlrRQVKLLEERNAEYMQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1827 LcdqighrdfdvekRLRRDLRRTHALLSDVQLLlgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1906
Cdd:pfam05622 169 L-------------QLEEELKKANALRGQLETY------------KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1907 HSELENMTRN----KSLVDE----QLYRLQFEKAD-LLKRIDEDQDDLN-ELM------------QKHKDL-IAQSAADI 1963
Cdd:pfam05622 224 QKEKERLIIErdtlRETNEElrcaQLQQAELSQADaLLSPSSDPGDNLAaEIMpaeireklirlqHENKMLrLGQEGSYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1964 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAIVSRQEAvicdlENKTEFQKVQIKRFEVLVIRLRdsli 2043
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ-----GSKAEDSSLLKQKLEEHLEKLH---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2044 KMGEELS--QAATSESQQRESSQyYQRRLEELkadMEELVQREAEAsrRCME--LEKYVEELAAVRQTL 2108
Cdd:pfam05622 374 EAQSELQkkKEQIEELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAMEerYKKYVEKAKSVIKTL 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1451-1837 |
4.51e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1451 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleseraERLQAFREVQELKSKHEQVQKK 1530
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS---------------DHLNLVQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1531 LGDVNKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDseltarkELEQKLGELQSAYDGAK 1610
Cdd:PRK04863 357 LEELEERLEEQNEVVEE-------------------ADEQQEENEARAEAAEEEVD-------ELKSQLADYQQALDVQQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1611 KMAHQ------LKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVTQENTSVRW 1681
Cdd:PRK04863 411 TRAIQyqqavqALERAKQL-CGLPD--LTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1682 ELgqlqqqlkqkeqEASQLKQQ-VEMLQDHKRELLGSPSLGencvaGLKERLWKLESSALEQQkiqsQQENTIKQLEQlR 1760
Cdd:PRK04863 488 EV------------SRSEAWDVaRELLRRLREQRHLAEQLQ-----QLRMRLSELEQRLRQQQ----RAERLLAEFCK-R 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1761 QRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIGH 1833
Cdd:PRK04863 546 LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDaLA----RLREQSGE 621
|
....
gi 1034629688 1834 RDFD 1837
Cdd:PRK04863 622 EFED 625
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
263-555 |
4.63e-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: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 263 LGDPGQGTVAlkkgeEGQSivgKGLGTPKTTEL-KEAEPQGKDRQGTrpQAQGPGEGVRPGKAEKEGAEPTNtvEKGNVS 341
Cdd:TIGR00927 627 LGDLSKGDVA-----EAEH---TGERTGEEGERpTEAEGENGEESGG--EAEQEGETETKGENESEGEIPAE--RKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 342 KDVGSEGKhvRPQIPGRKWGGFLGRRSKWDGPQNKKDKEGVLLSKAEKTG-EPQTQMEKTSQVQGElGDDLRMGEKAGEL 420
Cdd:TIGR00927 695 GEGEIEAK--EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdEGEGEAEGKHEVETE-GDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 421 RSTTGKAGESWDKKEKMGQPQGKSG--NAGEARSQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGA 498
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGEDGEMKGDEGaeGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034629688 499 GAlETELEGPSQPALEKDAERPRIRKENQDGPAPQEEGKGGQSRDSDQAPEDRWYEA 555
Cdd:TIGR00927 851 GV-DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1722-2131 |
5.28e-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: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1722 ENCVAGLKERLWKLE---SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ 1798
Cdd:TIGR00606 244 ENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1799 LEMQLEQEYEEKQMVLHEKQDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRL 1842
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1843 RRDLRRTHALLSDVQ------------------LLLGTMEDGKTSVSKE--ELEKVHSQLEQSEAKCEEALKTQKVLTAD 1902
Cdd:TIGR00606 404 EDEAKTAAQLCADLQskerlkqeqadeirdekkGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1903 LESMhSELENMTRNKSLVDEQLYrLQFEKADLLK---RIDEDQDDLN------------------------ELMQKHKDL 1955
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1956 IAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTeFQKVQIKRFEVL 2034
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2035 VIRLRDSLIKMGEELSQAATsesqqreSSQYYQRRLEELkadmeelvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2114
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-------ATAVYSQFITQL-----------TDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
490
....*....|....*..
gi 1034629688 2115 SIRRIADLQAALEEVAS 2131
Cdd:TIGR00606 703 KLRLAPDKLKSTESELK 719
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1916-2138 |
6.69e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1916 NKSLVDEQlyrlqfekADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQ-IQELQLQLEEAKKEKHKLQEQLQVAQMRI 1994
Cdd:PHA02562 172 NKDKIREL--------NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1995 EYLEQSTVDRAivsrqeAVICDLENKTEFQKVQIKRFevlvirlrDSLIKMGEE----------LSQAATSESQQRESSQ 2064
Cdd:PHA02562 244 LNLVMDIEDPS------AALNKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034629688 2065 YYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTES 2138
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1734-1988 |
6.97e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1734 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIermkqmhqKDREDQEEELEDVRQSCQK----RLhQLEMQLE--QEY 1807
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL--------NLRTSAENDLVGLRKDLDEatlaRV-DLEAKIEslKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1808 EEKQMVLHEKQdleglIGTLCDQIGHRDFDVEKRLRRDLRRTHALlSDVQlllgTMEDGKTSVSKEELEkvhsqlEQSEA 1887
Cdd:pfam00038 133 LAFLKKNHEEE-----VRELQAQVSDTQVNVEMDAARKLDLTSAL-AEIR----AQYEEIAAKNREEAE------EWYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1888 KCEEALKTQKVLTADLESMHSELENMTRnkslvdeQLYRLQFEKADLLKRIDEDQDDLNELMQKHkdliaqsAADIGQIQ 1967
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSLKKQKASLERQLAETEERY-------ELQLADYQ 262
|
250 260
....*....|....*....|..
gi 1034629688 1968 ELQLQLEEAKKE-KHKLQEQLQ 1988
Cdd:pfam00038 263 ELISELEAELQEtRQEMARQLR 284
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1922-2128 |
8.02e-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: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1922 EQLYRL---QFEKA-DLLKRIdedQ-----DDLNELMQKH-------KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQE 1985
Cdd:COG4913 180 ARLRRRlgiGSEKAlRLLHKT---QsfkpiGDLDDFVREYmleepdtFEAADALVEHFDDLERAHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1986 QLQVAQMRIEYLEQSTVDRAIVSRQEAvicdlenktEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRES--- 2062
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRL---------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREElde 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 2063 --SQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:COG4913 328 leAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1445-1824 |
8.62e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlleskiadltsdladerfkgdvacqvlESERA-ERLQAFREVQELKSK 1523
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQ------------------------------DYQAAsDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIQLNDLERnptggDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1603
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEADEQQ-----EENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1604 SA----------YDGAKKMAHQLKRKCHHLTCDLEDtcvlLEnQQSRNHELEKKQKKFDLQLAQALGESV--------FE 1665
Cdd:PRK04863 425 RAkqlcglpdltADNAEDWLEEFQAKEQEATEELLS----LE-QKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1666 KGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLESSALEQ 1742
Cdd:PRK04863 500 ELLRRLREQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSEA 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1743 QKIQSQQENTIKQLEQLRQRFEleiERMKQMHQKD------REDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQmVLHE 1816
Cdd:PRK04863 578 RERRMALRQQLEQLQARIQRLA---ARAPAWLAAQdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-LAAR 653
|
....*...
gi 1034629688 1817 KQDLEGLI 1824
Cdd:PRK04863 654 KQALDEEI 661
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1871-1980 |
8.80e-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: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1871 SKEELEKVHSQ---LEQSEAKCEEALKTQKVLTADLE----SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQD 1943
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 1944 DLNELMQK--------------HKDLIAQSaadigqiQELQLQLEEAKKEK 1980
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1445-1707 |
1.07e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1524
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1604
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1605 AYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELG 1684
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260
....*....|....*....|...
gi 1034629688 1685 QLQQQLKQKEQEASQLKQQVEML 1707
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAAL 307
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1743-2140 |
1.11e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1743 QKIQSQQENTIKQlEQLRQRFELEIERmKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEG 1822
Cdd:PTZ00440 546 KYYLQSIETLIKD-EKLKRSMKNDIKN-KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQE 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1823 LIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLGTMEDGKTSV----SKEELEKVHSQLEQSEAKCEEalKTQKV 1898
Cdd:PTZ00440 624 KVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLEF--MKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1899 LTADLESMHSELENM-TRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKdliaqsaADIGQIQELQLQLEEAK 1977
Cdd:PTZ00440 686 IDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1978 KE--------KHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQeAVICDlENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL 2049
Cdd:PTZ00440 759 NEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND-INILK-ENKKNNQD-LLNSYNILIQKLEAHTEKNDEEL 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2050 SQaatsesqqreSSQYYQRRLEELKADmeelvqreaeasrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2129
Cdd:PTZ00440 836 KQ----------LLQKFPTEDENLNLK----------------ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAI 889
|
410
....*....|.
gi 1034629688 2130 ASSDSDTESVQ 2140
Cdd:PTZ00440 890 NRSNSNKQLVE 900
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1746-1961 |
1.17e-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: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1746 QSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQMVLhekQDLEGLIG 1825
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAEL---AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1826 TLCDQIGHRDFDVEKRLRRDLRrtHALLSDVQLLLGTmEDGKTSVSK---------------EELEKVHSQLEQSEAKCE 1890
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP-EDFLDAVRRlqylkylaparreqaEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 1891 EALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1961
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1445-1657 |
1.23e-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: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLaderfkgdvacQVLESERAErlqAFREVQELKSKH 1524
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1525 EQVQKKLGDVNKQLEE---AQQKIQLNDLER---NPTGGDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1598
Cdd:COG4942 93 AELRAELEAQKEELAEllrALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 1599 LGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ 1657
Cdd:COG4942 173 RAELEALLAELEEERAALEA--------------LKAERQKLLARLEKELAELAAELAE 217
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1880-2150 |
1.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1880 SQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1959
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1960 AADIGQIQELQLQLEeakkekhklQEQLQVAQMRIEYLEQ-STVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlviRL 2038
Cdd:COG3883 96 YRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA-------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2039 RDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR 2118
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 1034629688 2119 IADLQAALEEVASSDSDTESVQTAVDCGSSGR 2150
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1445-1618 |
1.29e-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: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkGDVACQVLESERAER-------------L 1511
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALYRLGRqpplalllspedfL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1512 QAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewqmrfdcaqmENEFLRKRLQQCEERLDSELTA 1591
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA----------------ELEALLAELEEERAALEALKAE 196
|
170 180 190
....*....|....*....|....*....|.
gi 1034629688 1592 RK----ELEQKLGELQSAYDGAKKMAHQLKR 1618
Cdd:COG4942 197 RQkllaRLEKELAELAAELAELQQEAEELEA 227
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1504-1821 |
1.37e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1504 ESERAERLQAFREVQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTGG---DEWQMRFDCAQMENEFLRKRLQQ 1580
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGQgglDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1581 CEER---LDSELTARKE---LEQKLGELQSAYDGAKkmahQLKRKCHHLTCDLEDTcvllenqqsrnHELEKKQKKFDLQ 1654
Cdd:pfam02029 82 ALERqkeFDPTIADEKEsvaERKENNEEEENSSWEK----EEKRDSRLGRYKEEET-----------EIREKEYQENKWS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1655 LAQALGESVFEKglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL-GSPSLGENCVAGLK---E 1730
Cdd:pfam02029 147 TEVRQAEEEGEE--EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPeVKSQNGEEEVTKLKvttK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1731 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLHQLEMQLEQEY 1807
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 1034629688 1808 EEKQMVLHE-----KQDLE 1821
Cdd:pfam02029 305 AERKLREEEekrrmKEEIE 323
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1749-2128 |
1.44e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1749 QENTIKQLEQLRQRFElEIERMkqmhqkdreDQEEELEDVRQscqkrLHqLEMQLEQEYEEKqmvlheKQDLEGLIGTLC 1828
Cdd:PRK04778 24 RKRNYKRIDELEERKQ-ELENL---------PVNDELEKVKK-----LN-LTGQSEEKFEEW------RQKWDEIVTNSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1829 DQIGHRDFDVEKRLRR-DLRRTHALLSDVQLLLGTMEDGKTSVSKE-----ELEKVHSQL-EQSEAKCEEALKT------ 1895
Cdd:PRK04778 82 PDIEEQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEElqellESEEKNREEvEQLKDLYRELRKSllanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1896 -----QKVLTADLESMHSELENMTRNKSLVDEQlyrlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI-GQIQEL 1969
Cdd:PRK04778 162 sfgpaLDELEKQLENLEEEFSQFVELTESGDYV------EAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1970 QL---QLEEAK---------KEKHKLQEQLQVAQMRIEYLEqstVDRAivsrqEAVICDLENKTE-----FQK-VQIKRF 2031
Cdd:PRK04778 236 KAgyrELVEEGyhldhldieKEIQDLKEQIDENLALLEELD---LDEA-----EEKNEEIQERIDqlydiLEReVKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2032 -EVLVIRLRDSLIKMGEELSQ--AATSESQQR--------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEkyvEE 2100
Cdd:PRK04778 308 vEKNSDTLPDFLEHAKEQNKElkEEIDRVKQSytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ---EE 384
|
410 420
....*....|....*....|....*...
gi 1034629688 2101 LAAVRQTLqTDLETSIRRIADLQAALEE 2128
Cdd:PRK04778 385 LEEILKQL-EEIEKEQEKLSEMLQGLRK 411
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1421-1623 |
1.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1421 AVKDWPWWQLLGSLQplLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNtDLLESKIADLTSDLADErfkgdvac 1500
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1501 qvlESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggdewqmrfdcAQMENefLRKRLQQ 1580
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE---------------EELEE--LEEELEE 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034629688 1581 CEERLDSELTARKELEQKLGELQS--AYDGAKKMAHQLKRKCHHL 1623
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1444-1772 |
1.52e-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: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1444 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLEskiadltsdladerfkgdvacqvlesERAERLQAFREVQELKSK 1523
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEaqqkiqlndLERNPTGGDEwqmrfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGELQ 1603
Cdd:COG4913 663 VASAEREIAELEAELER---------LDASSDDLAA--------------LEEQLEELEAELE-------ELEEELDELK 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1604 SAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEkkqkkFDLQLAQALGESVfEKGLREKVTQENTSVRwel 1683
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEA----AEDLARLELRAL-----LEERFAAALGDAV-ERELRENLEERIDALR--- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1684 gqlqqqlkqkeQEASQLKQQVE-MLQDHKRE-----LLGSPSLGENcvAGLKERLWKLESSAL---EQQKIQSQQENTIK 1754
Cdd:COG4913 780 -----------ARLNRAEEELErAMRAFNREwpaetADLDADLESL--PEYLALLDRLEEDGLpeyEERFKELLNENSIE 846
|
330
....*....|....*...
gi 1034629688 1755 QLEQLRQRFELEIERMKQ 1772
Cdd:COG4913 847 FVADLLSKLRRAIREIKE 864
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1927-2144 |
1.53e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1927 LQFEKADLLKRIDEDQDDLnelmqkHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmRIEYLEQStvdrai 2006
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2007 VSRQEAVICDLENKTEFQKVQIKRFEVLvirlrdslikmgEELSQAatsesqqRESSQYYQRRLEELKADMEELVQREAE 2086
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY------------QELEAL-------EAELAELPERLEELEERLEELRELEEE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 2087 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA-DLQAALEEVASSDSDTESVQTAVD 2144
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELE 223
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1645-1995 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1645 EKKQKKFDLQLAQALGESVfEKGLR---EKVT----------QENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1711
Cdd:pfam15742 14 EVQQLRQNLQRLQILCTSA-EKELRyerGKNLdlkqhnsllqEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1712 REllgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQS 1791
Cdd:pfam15742 93 RE---------------------LELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1792 CQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLsdvqlllgTMEDGKTSVS 1871
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNEL--------QQQVRSLQDKEAQL--------EMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtrnkslvdeqlyRLQFEKADLLKRIDEDQDDLNELMQK 1951
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKE--------------ALQEELQQVLKQLDVHVRKYNEKHHH 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1034629688 1952 HKdliaqsaADIGQIQELQLQLEEAKKEKHK-LQEQLQVAQMRIE 1995
Cdd:pfam15742 282 HK-------AKLRRAKDRLVHEVEQRDERIKqLENEIGILQQQSE 319
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1873-2124 |
1.62e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1873 EELEKVHSQLEQSEAKCEEAlktqkvltadlesmHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQ---------- 1942
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1943 ---DDLNELMQKhKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAI--VSRQEA--V 2013
Cdd:PRK04863 421 qalERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAgeVSRSEAwdV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2014 ICDLENKTEFQKVQIKRFEVLVIRLRDslikMGEELSQAATSESQQRESSQYYQRRLEElkADMEELVQREAEASRRcmE 2093
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE--S 569
|
250 260 270
....*....|....*....|....*....|.
gi 1034629688 2094 LEKYVEELAAVRQTLQTDLETSIRRIADLQA 2124
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1421-1878 |
1.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1421 AVKDWPWWQLLGSLQpllsatigtEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvac 1500
Cdd:COG4717 124 LLQLLPLYQELEALE---------AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELL------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1501 qvleseRAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlnDLERnptggdewqmrfDCAQMENEFLRKRLQQ 1580
Cdd:COG4717 184 ------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEE------------ELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1581 CEERLDSELTARKELEQKLGELQSAYDGAKKMAhqlkrkchhltcdlEDTCVLLENQQSRNHELEKKQKKFDLQLAQALG 1660
Cdd:COG4717 244 RLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------GVLFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1661 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpSLGENCVAGLKERLWKLESSAL 1740
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1741 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQscqkRLHQLEMQLEQEYEEKQMVLHEKQD 1819
Cdd:COG4717 389 AALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE----ELEELEEELEELREELAELEAELEQ 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 1820 LEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLGTMEDGKTSVSKEELEKV 1878
Cdd:COG4717 465 LEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREERLPPV 517
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
366-548 |
1.66e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 366 RRSKWDGPQNKKDKEGVLLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEKAGElrsttGKAGESWDKKEKMGQPQGKSG 445
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEER-----GQGGPSGSGSESVGSPTPSPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 446 NAGEAR----SQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGAGALETELEGPSQPALEKDAERPR 521
Cdd:PHA03169 109 GSAEELasglSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
170 180
....*....|....*....|....*..
gi 1034629688 522 IRKENQDGPAPQEEGKGGQSRDSDQAP 548
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1930-2122 |
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 1034629688 1930 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQlqvaqmrieyleqstvdRAIVSR 2009
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-----------------KARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2010 QEAVICDLEnktEFQKVQIKRFEVLViRLRDSLIKMGEElsqaATSESQQRES--SQYYQRRLEELKADMEelvQREAea 2087
Cdd:pfam13851 97 LEKELKDLK---WEHEVLEQRFEKVE-RERDELYDKFEA----AIQDVQQKTGlkNLLLEKKLQALGETLE---KKEA-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034629688 2088 srrcmELEKYV-------EELAAVRQTLQTDLETSIRRIADL 2122
Cdd:pfam13851 164 -----QLNEVLaaanldpDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1444-1629 |
1.85e-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: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1444 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSK 1523
Cdd:TIGR02169 797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1524 HEQVQKKLGDVNKQLEEAQQKIQlndlernptggdEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1603
Cdd:TIGR02169 877 LRDLESRLGDLKKERDELEAQLR------------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
170 180
....*....|....*....|....*.
gi 1034629688 1604 SaYDGAKKMAHQLKRKCHHLTCDLED 1629
Cdd:TIGR02169 945 E-IPEEELSLEDVQAELQRVEEEIRA 969
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1699-2144 |
1.97e-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: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1699 QLKQQVEMLQDHKR-----------ELLGSPSLGENCVaglkerlWKLESSALEQQKIQSQQENTIKQLEQLR---QRFE 1764
Cdd:pfam10174 71 HLQLTIQALQDELRaqrdlnqllqqDFTTSPVDGEDKF-------STPELTEENFRRLQSEHERQAKELFLLRktlEEME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1765 LEIERMKQ--------------MHQKD---REDQEEELEDVRQ--SCQKRLHQLEMQLEQEYEEKQMV---LHEK---QD 1819
Cdd:pfam10174 144 LRIETQKQtlgardesikklleMLQSKglpKKSGEEDWERTRRiaEAEMQLGHLEVLLDQKEKENIHLreeLHRRnqlQP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1820 LEGLIGTLCDQIGHRDFDVEKrLRRDLRRthaLLSDVQLL----LGTMEDGKTSVSKEELEKVHS--------QLEQSEA 1887
Cdd:pfam10174 224 DPAKTKALQTVIEMKDTKISS-LERNIRD---LEDEVQMLktngLLHTEDREEEIKQMEVYKSHSkfmknkidQLKQELS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1888 KCEEALKTqkvLTADLESMHSELENMTRNKSLVDEQLYR-------LQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1960
Cdd:pfam10174 300 KKESELLA---LQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1961 ADIGQIQELQ--LQLEEAK-----KEKHKLQEQL-----QVAQM--RIEYLEQ--STVDRAIVSRQEAvICDLENKTEFQ 2024
Cdd:pfam10174 377 TLAGEIRDLKdmLDVKERKinvlqKKIENLQEQLrdkdkQLAGLkeRVKSLQTdsSNTDTALTTLEEA-LSEKERIIERL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2025 KVQIKRFEVLVIRLRDSLIKMGEELSQAATS---ESQQRESSqyyqrrLEELKADMEELVQREAEASRRC----MELEKY 2097
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSAlqpELTEKESS------LIDLKEHASSLASSGLKKDSKLksleIAVEQK 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034629688 2098 VEELAAVRQTLQT-----DLETSIRRIADLQAALE-EVASSDSDTESVQTAVD 2144
Cdd:pfam10174 530 KEECSKLENQLKKahnaeEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVE 582
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1592-2168 |
2.15e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1592 RKELEQKLGELQSAYDGAKKmahqLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKkfdlQLAQAlgESVFEKGLREK 1671
Cdd:PRK01156 151 RKKILDEILEINSLERNYDK----LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADD--EKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1672 vtqENTSVrwELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL------LGSPSLGENCVAGLKERLWKLESSALeqqki 1745
Cdd:PRK01156 221 ---ERLSI--EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdLSMELEKNNYYKELEERHMKIINDPV----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1746 qsqqentIKQLEQLRQRFELeiermkqmhQKDREDQEEELEDVRQSCQK--RLHQLEMQLEQEYEEKQMVLHEKQDLegl 1823
Cdd:PRK01156 291 -------YKNRNYINDYFKY---------KNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDL--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1824 igtlcdqighrdfdveKRLRRDLRRTHallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEakceealkTQKVLTADL 1903
Cdd:PRK01156 352 ----------------NNQILELEGYE---MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1904 ESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL--------------MQKHKDLIAQSAADIGQIQEl 1969
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1970 qlQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSrqeavicdlENKTEFQKVQIKRFEVLVIRLRDSLIKmgeel 2049
Cdd:PRK01156 484 --KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADLEDIKIKINELKDKHDK----- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2050 SQAATSESQQRESSQYYQRRLEELKA-------DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD- 2121
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENe 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2122 ---LQAALEEVASSDSDTESVQTAVDCGSSGRKEMDnvSILSSQPEGSLQ 2168
Cdd:PRK01156 628 annLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID--SIIPDLKEITSR 675
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1965-2129 |
2.19e-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: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1965 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdrAIVSRQEAVicdlenktEFQKVQIKRFEVLVIRLRDSLIK 2044
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTEL--------EDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2045 MGEELSQAATsesqQRESsQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR----IA 2120
Cdd:COG1579 78 YEEQLGNVRN----NKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLA 152
|
....*....
gi 1034629688 2121 DLQAALEEV 2129
Cdd:COG1579 153 ELEAELEEL 161
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1886-2143 |
2.20e-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: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1886 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSaadigq 1965
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1966 iQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlENKTEFQKVQIKrfEVLVIRLRDSLIKM 2045
Cdd:pfam07888 104 -KELSASSEELSEEKDALLAQRAAHEARIRELEE------------------DIKTLTQRVLER--ETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2046 GEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVeelaavrQTLQTDLETSIRRIADLQAA 2125
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------TTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*...
gi 1034629688 2126 LEEVASSDSDTESVQTAV 2143
Cdd:pfam07888 236 LEELRSLQERLNASERKV 253
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1722-1817 |
2.62e-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: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1722 ENCVAGLKERLWKLESSALEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhQLEM 1801
Cdd:cd16269 199 EIEAERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQEA 270
|
90
....*....|....*.
gi 1034629688 1802 QLEQEYEEKQMVLHEK 1817
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1446-1585 |
2.92e-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: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1446 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL--------LESKIADLTSDLADerfkgdvacqvLESERAERLQAFREV 1517
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEA-----------LKARWEAEKELIEEI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1518 QELKSKHEQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGDE-------W------QMrfdcaqMENEflRKRLQQCEE 1583
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELaELAPLLREEVTEEDiaevvsrWtgipvgKL------LEGE--REKLLNLEE 545
|
..
gi 1034629688 1584 RL 1585
Cdd:COG0542 546 EL 547
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1872-2014 |
2.93e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVDEQLYRLQFEKADLLKR----IDEDQDDLN 1946
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEeKKEKLQEEEDKLLEEAEKEAQQAIKEakkeADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034629688 1947 ELMQ-KHKDLIAQSAADI-GQIQELQLQLEEAKKEKHKLQEQLQVAQ-MRIEYLEQSTVDRAIVSRQEAVI 2014
Cdd:PRK00409 595 QLQKgGYASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGDeVKYLSLGQKGEVLSIPDDKEAIV 665
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1459-1670 |
3.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1459 RKLEKSEKLRNELRQNTDLLeskIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQL 1538
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1539 EEAQQKIQLNDLERNPTggdewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKR 1618
Cdd:COG4372 83 EELNEQLQAAQAELAQA-----QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1034629688 1619 KCHHLTCDLEDTcvlleNQQSRNHELEKKQKKFDLQLAQALGESVFEKGLRE 1670
Cdd:COG4372 158 QLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1734-1976 |
3.38e-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: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1734 KLESSALEQQKIQSQQENTIKQLEQLRQrfelEIERMkqmhQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMV 1813
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA----ELEEL----NEEYNELQAELEALQA-------EID-KLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1814 LHEKQDlegligtlcdqighrdfDVEKRLRrDLRRTHALLSDVQLLLG-----TMEDGKTSVSK---------EELEKVH 1879
Cdd:COG3883 81 IEERRE-----------------ELGERAR-ALYRSGGSVSYLDVLLGsesfsDFLDRLSALSKiadadadllEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1880 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1959
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 1034629688 1960 AADIGQIQELQLQLEEA 1976
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1725-2128 |
3.76e-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: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1725 VAGLKERLWKLESsALEQQKIQSQQENTikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QS 1791
Cdd:COG3096 838 LAALRQRRSELER-ELAQHRAQEQQLRQ--QLDQLKEQLQLLNKLLPQANLLADETLADRLEELReeldaaqeaqafiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1792 CQKRLHQLEM-------------QLEQEYEEKQmvlHEKQDLEGLIGTLCDQIGhrdfdvekrlrrdlRRTHALLSDVQL 1858
Cdd:COG3096 915 HGKALAQLEPlvavlqsdpeqfeQLQADYLQAK---EQQRRLKQQIFALSEVVQ--------------RRPHFSYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1859 LLGTmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkslvdeqlyrlqfekADLLKRI 1938
Cdd:COG3096 978 LLGE--------NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL---------------------ASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1939 DEDQDDLNELMQKHKDLIAQSAADIgqiqelqlqLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLE 2018
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEA---------EERARIRRDELHEELSQNRSRRSQLEKQ------LTRCEAEMDSLQ 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2019 N---KTEfQKVQIKRFEV--------LVIRL-RDSLIKMG---EELsqAATSESQQRESSQYYQRRLEELKADMEEL--V 2081
Cdd:COG3096 1094 KrlrKAE-RDYKQEREQVvqakagwcAVLRLaRDNDVERRlhrREL--AYLSADELRSMSDKALGALRLAVADNEHLrdA 1170
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1034629688 2082 QREAEASRRCmelEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:COG3096 1171 LRLSEDPRRP---ERKVQFYIAVYQHLRERIRQDIIRTDDPVEAIEQ 1214
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1459-1820 |
3.82e-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: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1459 RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgDVACQVLESERAERLQAF----REVQELKSKHEQVQKKLGDV 1534
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEK---EALRKEMKKEREELGATMlalsQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1535 NKQLEEAQQKIQLNDLERNPTGGdewQMRF--DCAQMENEFLRKRLQQCEERLDSELTARkelEQKLGELQSAYDGAKKM 1612
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCG---EMRYqlNQTKMKKDEAEKEHREYRTKTGRQLEIK---DQEIEKLGLELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1613 AHQLKRKCHHLTCDLEDTCVLLENQQSRNH----ELEKKQKKFDLQL-AQALGESVFEKGLREKVTQENTSVRWELGQLQ 1687
Cdd:pfam15964 504 LEQAQQDAARAREECLKLTELLGESEHQLHltrlEKESIQQSFSNEAkAQALQAQQREQELTQKMQQMEAQHDKTVNEQY 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1688 QQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFElEI 1767
Cdd:pfam15964 584 SLLTSQNTFIAKLKEECCTLAKKLEEI--------------------TQKSRSEVEQLSQEKEYLQDRLEKLQKRNE-EL 642
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034629688 1768 ERMKQMHQKDREDQEEELEDVRQSCQ---KRLHQLEMQLEQEYEEKQMVLHEKQDL 1820
Cdd:pfam15964 643 EEQCVQHGRMHERMKQRLRQLDKHCQataQQLVQLLSKQNQLFKERQNLTEEVQSL 698
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
1872-2005 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1872 KEELEKvhSQLEQSEAK-CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1950
Cdd:pfam06785 62 KEKFEK--SFLEEKEAKlTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034629688 1951 KHKDLIAQSAAdigQIQELQLQLEEAKKEKHKLQEQlqvaqmrIEYLEQSTVDRA 2005
Cdd:pfam06785 140 ESEEQLAEKQL---LINEYQQTIEEQRSVLEKRQDQ-------IENLESKVRDLN 184
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1848-1956 |
4.05e-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: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1848 RTHALLSDVQLLLGTMEDGKTsvskeELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmTRNKSLVDEQLYRL 1927
Cdd:pfam09744 44 RNQEHNVELEELREDNEQLET-----QYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLE--EENRRLEADHVSRL 116
|
90 100
....*....|....*....|....*....
gi 1034629688 1928 QFEKADLLKRIDEDQDDLNELMQKHKDLI 1956
Cdd:pfam09744 117 EEKEAELKKEYSKLHERETEVLRKLKEVV 145
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1642-2151 |
4.07e-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: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1642 HELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLG 1721
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1722 ENCVAGLKERLWKLESSALEQQKIQSQQENTIK-QLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQKRLHQLE 1800
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGK----HQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1801 MQLEQEYEEKQMVLH-EKQDLEGLIGTLCDQI--GHRDF-DVEKRLRRDLRRTHALLSDVQlllgtmedgktsVSKEELE 1876
Cdd:pfam12128 397 DKLAKIREARDRQLAvAEDDLQALESELREQLeaGKLEFnEEEYRLKSRLGELKLRLNQAT------------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1877 kvhsQLEQSEAKCEEALKTQKVLTADLESMHSELenmTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1956
Cdd:pfam12128 465 ----QLENFDERIERAREEQEAANAEVERLQSEL---RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1957 A---QSAAD----IGQI----QELQLQLEEAKKEKHKLQEQ----LQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 2021
Cdd:pfam12128 538 HflrKEAPDweqsIGKVispeLLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2022 EfqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELV---QREAEASRRCMELEKYV 2098
Cdd:pfam12128 618 E----KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaerKDSANERLNSLEAQLKQ 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1034629688 2099 EELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSGRK 2151
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
675-765 |
4.17e-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: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 675 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKIRATFT 740
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 1034629688 741 VLRAFGSVSMAHSRSATRFSMVMSL 765
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1458-1832 |
4.42e-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: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1458 RRKLEKSEKLRNELRQNTDLLESKIADLTsDLADERFKGDVACQVLESE---RAERLQAFREVQELKSKHEQVQKKLGDV 1534
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLV-EMARELEELSARESDLEQDyqaASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1535 NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAyDGAKKMAH 1614
Cdd:COG3096 360 TERLEEQEEVVEE-------------------AAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTR-AIQYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1615 QLKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVtqentsvrWELGQLQQQLK 1691
Cdd:COG3096 420 QALEKARAL-CGLPD--LTPENAEDYLAAFRAKEQQATeevLELEQKLSVADAARRQFEKA--------YELVCKIAGEV 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1692 QKEQEASQLKQQVEMLQDHKrellgspSLGENcVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMK 1771
Cdd:COG3096 489 ERSQAWQTARELLRRYRSQQ-------ALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEELL 559
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034629688 1772 QMHQKDREDQEEELEDvrqsCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1832
Cdd:COG3096 560 AELEAQLEELEEQAAE----AVEQRSELRQQLEQlrarikELAARAPAWLAAQDaLE----RLREQSG 619
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1445-2119 |
4.45e-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: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------------LESKIADLTSDLADERFKGDVACQVLE------S 1505
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1506 ERAERLQAFR-EVQELKSKHEQVQKKLgDVN-----------KQLEEAQQKIQLNDLErnPTGGDEWQMRFDcAQmENEF 1573
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQAL-DVQqtraiqyqqavQALEKARALCGLPDLT--PENAEDYLAAFR-AK-EQQA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1574 LRKRLQQcEERLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKchhLTCDLEDTCVLLENQQS---RNHELEKK-- 1647
Cdd:COG3096 454 TEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEvERSQAWQTARE---LLRRYRSQQALAQRLQQlraQLAELEQRlr 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1648 --QKKFDL--QLAQALGESVFEKGLREKVTQENTSVRWELgqlQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgen 1723
Cdd:COG3096 530 qqQNAERLleEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKEL--------- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1724 cvaGLKERLWKLESSALEQ------------QKIQSQQENTIK----------QLEQLRQRFELEIERmkqMHQKD-RED 1780
Cdd:COG3096 598 ---AARAPAWLAAQDALERlreqsgealadsQEVTAAMQQLLErereatverdELAARKQALESQIER---LSQPGgAED 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1781 QE--------------EELEDV---------------RQ--------SCQKRLHQLEMQLE---------QEYEEKqmvL 1814
Cdd:COG3096 672 PRllalaerlggvllsEIYDDVtledapyfsalygpaRHaivvpdlsAVKEQLAGLEDCPEdlyliegdpDSFDDS---V 748
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1815 HEKQDLEgliGTLCDQIGHRDFDVEK-----RLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ----- 1884
Cdd:COG3096 749 FDAEELE---DAVVVKLSDRQWRYSRfpevpLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvggh 825
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1885 ----SEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVD------EQLYRLQ-----FEKADLLKRIDEDQDDLNEL 1948
Cdd:COG3096 826 lavaFAPDPEAELAALRQRRSELERELAQHRaQEQQLRQQLDqlkeqlQLLNKLLpqanlLADETLADRLEELREELDAA 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1949 ------MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTe 2022
Cdd:COG3096 906 qeaqafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD- 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2023 fqkvqikrfevLVIRLRDSLIKMGEELSQAATS-ESQQRESSQYYQRR-------------LEELKADMEEL-VQREAEA 2087
Cdd:COG3096 985 -----------LNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQVLaslkssrdakqqtLQELEQELEELgVQADAEA 1053
|
810 820 830
....*....|....*....|....*....|..
gi 1034629688 2088 SRRCMELEKYVEELAAVRQTLQTDLETSIRRI 2119
Cdd:COG3096 1054 EERARIRRDELHEELSQNRSRRSQLEKQLTRC 1085
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1935-2142 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1935 LKRIDEDQDDLNELmqkhKDLIAQSAAdigQIQELQLQLEEAKKeKHKLQEQLQVAQMRIEYLEqstvDRAIVSRQEAvi 2014
Cdd:COG1196 178 ERKLEATEENLERL----EDILGELER---QLEPLERQAEKAER-YRELKEELKELEAELLLLK----LRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2015 cdLENKTEFQKVQIKRFEvlvirlrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMEL 2094
Cdd:COG1196 244 --LEAELEELEAELEELE--------------AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1034629688 2095 EKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2142
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1446-1611 |
5.35e-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: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1446 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvLESERAErlqafREVQELKSKHE 1525
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---------KEIKRLE-----LEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1526 QVQKKLGDV--NKQLEEAQQKIQLndlernptggdewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQ 1603
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIES-------------------LKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
....*...
gi 1034629688 1604 SAYDGAKK 1611
Cdd:COG1579 138 AELEEKKA 145
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
303-556 |
6.70e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 303 KDRQGTRPQAQGPGEGVRPGKAEKeGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGGFLGRRSKwDGPQNKKDKEGV 382
Cdd:PHA03169 24 KRHGGTREQAGRRRGTAARAAKPA-PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 383 LLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEkaGELRSTTGKAGESWDKKEKMGQPQGKSGNAGEARSQTEKGCEAPK 462
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 463 EVSTMVESPAA-------PGKGGWPGSRGQEAEEPCSRAGDGA--------GALETELEGPSQPALEKDAERPRIRKENQ 527
Cdd:PHA03169 180 PPTSEPEPDSPgppqsetPTSSPPPQSPPDEPGEPQSPTPQQApspntqqaVEHEDEPTEPEREGPPFPGHRSHSYTVVG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034629688 528 DGPAPQEEG-------KGGQSRDSDQAPEDRWYEAE 556
Cdd:PHA03169 260 WKPSTRPGGvpklclrCTSHPSHRSRLPEGQQSEDK 295
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1697-2001 |
7.03e-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: 41.42 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1697 ASQLKQQV-EMLQDHKRELLGSPSLGEncvaglkERLWKLESSALEQQKIQsQQENTIKQLEQLRQRFELEIERMKQ--- 1772
Cdd:pfam07888 89 LRQSREKHeELEEKYKELSASSEELSE-------EKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKErak 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1773 ---MHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIG--HRDFDVEKRLRRDLR 1847
Cdd:pfam07888 161 kagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1848 RTHALLSdvqlllgtMEDGKTSVSKEELEKV-----HSQLEQSEAKCEEALKTQKVLTADLE------SMHSELENMTRN 1916
Cdd:pfam07888 241 SLQERLN--------ASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1917 KSLVDEQLYRLQFEKADLLKRIDEDQDDLN----ELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQM 1992
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEERMEREklevELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 1034629688 1993 RIEYLEQST 2001
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1445-1611 |
7.40e-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: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAER-LQAF-REVQELKS 1522
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1523 KHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggdewQMRFDCAQMENEfLRKRLQQCEERLDSELTARKELEQKLGE- 1601
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAE-LDEELAELEAELEELEAEREELAAKIPPe 175
|
170
....*....|
gi 1034629688 1602 LQSAYDGAKK 1611
Cdd:COG1579 176 LLALYERIRK 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1739-2128 |
7.62e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1739 ALEQQKIQSQQENtiKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QSCQKRLHQLEMQL-- 1803
Cdd:PRK04863 852 ALADHESQEQQQR--SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIReqldeaeeakrfvQQHGNALAQLEPIVsv 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1804 ----EQEYEE-KQMVLHEKQDLegligtlcdqighRDFDVEKRLRRDL--RRTHALLSDVQLLLGtmedgKTSVSKEELE 1876
Cdd:PRK04863 930 lqsdPEQFEQlKQDYQQAQQTQ-------------RDAKQQAFALTEVvqRRAHFSYEDAAEMLA-----KNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1877 KVHSQLEQSEAKCEEALKTQKvltadlesmhselENMTRNKslvdeQLYrlqfekADLLKRIDEDQDDLNELMQKHKDLI 1956
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ-------------AQLAQYN-----QVL------ASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1957 AQsaADIGQIQELQLQLEEakkekhkLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENK-TEFQK--VQIKRFEV 2033
Cdd:PRK04863 1048 VP--ADSGAEERARARRDE-------LHARLSANRSRRNQLEKQ------LTFCEAEMDNLTKKlRKLERdyHEMREQVV 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 2034 -------LVIRL-RDSLIK---MGEELsqAATSESQQRESSQYYQRRLEELKADMEEL--VQREAEASRRcmeLEKYVEE 2100
Cdd:PRK04863 1113 nakagwcAVLRLvKDNGVErrlHRREL--AYLSADELRSMSDKALGALRLAVADNEHLrdVLRLSEDPKR---PERKVQF 1187
|
410 420
....*....|....*....|....*...
gi 1034629688 2101 LAAVRQTLQTDLETSIRRIADLQAALEE 2128
Cdd:PRK04863 1188 YIAVYQHLRERIRQDIIRTDDPVEAIEQ 1215
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1414-1550 |
8.53e-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: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1414 KNVAVFLAVKDW-PW-WQLLGSLQPLLSATIGT-----EQLRAKEEELTTLRRKLEKS-----EKLRNELRQNTDLLESK 1481
Cdd:smart00787 123 KTFARLEAKKMWyEWrMKLLEGLKEGLDENLEGlkedyKLLMKELELLNSIKPKLRDRkdaleEELRQLKQLEDELEDCD 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034629688 1482 IADLtsDLADERFKGDVACQVLESERAERLQafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDL 1550
Cdd:smart00787 203 PTEL--DRAKEKLKKLLQEIMIKVKKLEELE--EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1445-1546 |
8.57e-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: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1445 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleSERAERLQAFREVQELKSKH 1524
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|..
gi 1034629688 1525 EQVQKKLGDVNKQLEEAQQKIQ 1546
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1443-1559 |
9.74e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034629688 1443 GTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvACQVLESERAERLQAFREVQELK 1521
Cdd:PRK00409 524 SLEELERElEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ---AIKEAKKEADEIIKELRQLQKGG 600
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1034629688 1522 SKH------EQVQKKLGDVNKQLEEAQQKIQLNdlERNPTGGDE 1559
Cdd:PRK00409 601 YASvkahelIEARKRLNKANEKKEKKKKKQKEK--QEELKVGDE 642
|
|
| |
