|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
585-1322 |
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: 1031.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV---PKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVakmFKGcRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQ 820
Cdd:cd01386 161 LERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 821 RAVWRVLAAIYHLGAAGACK---VGRKQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRwGLEDEETS 897
Cdd:cd01386 241 RAIWSILAAIYHLGAAGATKaasAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ-ESPARSSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 898 SGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGKDRAATFEELCHNYAHERLQL 977
Cdd:cd01386 320 GGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQERLQL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 978 LFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQNPsQQVRLPAGGGAQDARGLFWVLDEEVHVEGSSDSVVLER 1057
Cdd:cd01386 400 LFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAP-QQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFLER 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1058 LCAAFEKKGAGTeGSSALRTCEQPLQCEIFHQLGWDPVRYDLTGWLHRAKPNLSALDAPQVLHQSKREelrslfqarakl 1137
Cdd:cd01386 479 LFSHYGDKEGGK-GHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE------------ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1138 ppvcravaglegtsqqalqrsrmvrrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRSGQES 1217
Cdd:cd01386 546 -------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDERSTS 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1218 PPPpqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGIDERKA 1297
Cdd:cd01386 595 SPA----------AGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGLNSEVADERKA 664
|
730 740
....*....|....*....|....*
gi 970949420 1298 VEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd01386 665 VEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
586-1322 |
3.59e-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: 3.59e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKV-----PKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVmekyrGKGRSADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVS------VEKIRATFTVLRAFGsvsmaHSRS-----ATRFSMVMSLDFNATG 729
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSssassiEQQILQSNPILEAFG-----NAKTvrndnSSRFGKFIELQFDPTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---HQMADSSSFGMGVWSKPEDKQKAAAAFAQL 806
Cdd:cd00124 157 RLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLellLSYYYLNDYLNSSGCDRIDGVDDAEEFQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 807 QGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKhhlR 876
Cdd:cd00124 237 LDALDVLGFSDEEQDSIFRILAAILHLGniefeedeedEDSSAEVADD-----ESLKAAAKLLGVDAEDLEEALTT---R 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 877 QIIqqmtfgpsrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSS--HHLSMASIMVVDSPGFQNPR 953
Cdd:cd00124 309 TIK-----------VGGETITKPLTVEQaEDARDALAKALYSRLFDWLVNRINAALSPtdAAESTSFIGILDIFGFENFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 954 HQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVVDQNPSqqvrlpagggaqd 1032
Cdd:cd00124 378 VNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFiDFPDNQD--CLDLIEGKPL------------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1033 arGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagteGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSa 1112
Cdd:cd00124 437 --GILSLLDEECLFPKGTDATFLEKLYSAHGSH-----PRFFSKKRKAKLEFGIKHYAG--DVTYDADGFLEKNKDTLP- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1113 ldapqvlhqskrEELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMI 1192
Cdd:cd00124 507 ------------PDLVDLLRS--------------------------------------------GSQFRSQLDALMDTL 530
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1193 KRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRR 1272
Cdd:cd00124 531 NSTQPHFVRCIKPND----------------------EKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLK 588
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 970949420 1273 QFQVLDAPLLKKLMSTSEgiderKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd00124 589 RYRILAPGATEKASDSKK-----AAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
566-1334 |
4.53e-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: 4.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 566 NPPELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKvpkGRRDG-LPAHIGS 638
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPykqlpiYTDEVIKKYR---GKSRGeLPPHVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 639 MAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRF 717
Cdd:smart00242 78 IADNAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGSVEdQILESNPILEAFGNAKTLRNNNSSRF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 718 SMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQmadSSSFG---MGVWSK-- 792
Cdd:smart00242 158 GKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS---PEDYRylnQGGCLTvd 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 793 -PEDKqkaaAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFmrfewaNYAAEALGC 861
Cdd:smart00242 235 gIDDA----EEFKETLNAMRVLGFSEEEQESIFKILAAILHLGniefeegrndNAASTVKDKEEL------SNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 862 EYEELNTA-TFKhhlrqiiqQMTFGpsrwgleDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMA 939
Cdd:smart00242 305 DPEELEKAlTKR--------KIKTG-------GEVITKPLNVEQAlDARDALAKALYSRLFDWLVKRINQSLSFKDGSTY 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 940 SIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ----FDLpdpspGTTVAVVD 1015
Cdd:smart00242 370 FIGVLDIYGFEIFEVNS------FEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTfidfFDN-----QDCIDLIE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1016 QNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCeqplqceiF---HQLGw 1092
Cdd:smart00242 439 KKP---------------PGILSLLDEECRFPKGTDQTFLEKLNQHHKKHPHFSKPKKKGRTE--------FiikHYAG- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1093 dPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravaglegtSQQALQRSRMVRRTFASslaav 1172
Cdd:smart00242 495 -DVTYDVTGFLEKNKDTLSD-DLIELLQSSKNPLIASLF-------------------PSGVSNAGSKKRFQTVG----- 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1173 rrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILE 1252
Cdd:smart00242 549 ------SQFKEQLNELMDTLNSTNPHFIRCIKPNE--EKKPGD--------------------FDSSLVLHQLRYLGVLE 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1253 ALRLHRTGYADHMGLTRFRRQFQVLDAPLLKklmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQ 1332
Cdd:smart00242 601 NIRIRRAGFPYRLPFDEFLQRYRVLLPDTWP-----PWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEEL 675
|
..
gi 970949420 1333 RE 1334
Cdd:smart00242 676 RE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
510-2087 |
2.80e-75 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 278.50 E-value: 2.80e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 510 WYEA-EKVWLA---QKDGFTLATVlkpdEGTADLPAGRVrlwIDADKTITEVDEEhvhraNPPELDQVEDLASLISVNES 585
Cdd:COG5022 13 WIPDeEKGWIWaeiIKEAFNKGKV----TEEGKKEDGES---VSVKKKVLGNDRI-----KLPKFDGVDDLTELSYLNEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGpsVPSAG-----KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:COG5022 81 AVLHNLEKRYNNGQIYTYSGLVLIAVNPyRD--LGIYTddiiqSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIIS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSV-DGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQ 737
Cdd:COG5022 159 GESGAGKTENAKRIMQYLASVTSSStVEISSIEkQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 738 TMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISE 817
Cdd:COG5022 239 TYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLL-LLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLDALKTIGIDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 818 SEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQqmtfgpsrwGLEDEE 895
Cdd:COG5022 318 EEQDQIFKILAAILHIGniEFKEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVK---RQIKT---------GGEWIV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 896 TSSGLKMTgVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:COG5022 386 VPLNLEQA-LAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKNS------FEQLCINYTNEKL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 976 QLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVV 1054
Cdd:COG5022 459 QQFFNQHMFKLEQEEYVKEGIEWSFiDYFDNQP-CIDLIEKKNPL---------------GILSLLDEECVMPHATDESF 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1055 LERLCAAFEKKgagtegSSALRTCEQPLQCEIF--HQLGwDpVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQ 1132
Cdd:COG5022 523 TSKLAQRLNKN------SNPKFKKSRFRDNKFVvkHYAG-D-VEYDVEGFLDKNKDPLN-DDLLELLKASTNEFVSTLFD 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1133 ARaklppvcravaglegtsQQALQRSRmvRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESR 1212
Cdd:COG5022 594 DE-----------------ENIESKGR--FPTLG------------SRFKESLNSLMSTLNSTQPHYIRCIKPN---EEK 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1213 SgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMSTSEGi 1292
Cdd:COG5022 640 S-------------------PWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKSWTGEYTWKE- 699
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1293 DERKAVEELLETLDLEKKAVAVGHSQVFLKAGVISRLEKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQK 1372
Cdd:COG5022 700 DTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQH 779
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1373 NVAVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEK----SEKLRNELRQNTDLLESKIADltSDLA 1448
Cdd:COG5022 780 GFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKA 857
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1449 DERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQkKLGDVNKQLEeaqQKIqlndLERNPTGGADewqMRFDCaQM 1528
Cdd:COG5022 858 KKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS-SLKLVNLELE---SEI----IELKKSLSSD---LIENL-EF 925
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1529 ENEFLrKRLQQCEERLDSELTARKELEQK--LGELQSAydgakkmahqlkrkchhlTCDLEDTCVLLENqqsrnhELEKK 1606
Cdd:COG5022 926 KTELI-ARLKKLLNNIDLEEGPSIEYVKLpeLNKLHEV------------------ESKLKETSEEYED------LLKKS 980
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1607 qkkfdlqlaqalgesvfEKGLREKVTQENTSVRW--ELGQLQQQLKQKEQEASQLKQQVEMLQDHKREllgspslgencv 1684
Cdd:COG5022 981 -----------------TILVREGNKANSELKNFkkELAELSKQYGALQESTKQLKELPVEVAELQSA------------ 1031
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1685 aglkERLWKLESSALEQQK-IQSQQENTIKQLEQLRQRFE---LEIERmkqmhQKDREDQEEELEDVRqscqkrlhqlem 1760
Cdd:COG5022 1032 ----SKIISSESTELSILKpLQKLKGLLLLENNQLQARYKalkLRREN-----SLLDDKQLYQLESTE------------ 1090
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1761 QLEQEYEEKQMVLhEKQDLEGLIGTLcdqighrDFDVEKRLRRDL-RRTHALLSdvqLLLGTMEDGKTSVSKEELE---- 1835
Cdd:COG5022 1091 NLLKTINVKDLEV-TNRNLVKPANVL-------QFIVAQMIKLNLlQEISKFLS---QLVNTLEPVFQKLSVLQLEldgl 1159
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1836 KVHSQLEQSEAKCEEALKTQKVLTADleSMHSEL--ENMTRNKSLVDE--QLYRLQFE---KADLLKRIDEDQDDLNELM 1908
Cdd:COG5022 1160 FWEANLEALPSPPPFAALSEKRLYQS--ALYDEKskLSSSEVNDLKNEliALFSKIFSgwpRGDKLKKLISEGWVPTEYS 1237
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1909 QKHKDliAQSAADIGQiqelqlqlEEAKKEKHKLQEQL-QVAQMRIEYLEQSTVDRAIVsrqeavicdlenKTEFQKVQI 1987
Cdd:COG5022 1238 TSLKG--FNNLNKKFD--------TPASMSNEKLLSLLnSIDNLLSSYKLEEEVLPATI------------NSLLQYINV 1295
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1988 KRFEVLVIRLRDSLIKMGEELSQaatseSQQRESSQYYQRRLEELKADMEELVQReaeasRRCMELEKY-VEELAAVRQT 2066
Cdd:COG5022 1296 GLFNALRTKASSLRWKSATEVNY-----NSEELDDWCREFEISDVDEELEELIQA-----VKVLQLLKDdLNKLDELLDA 1365
|
1610 1620
....*....|....*....|..
gi 970949420 2067 LQTDLETSIRRI-ADLQAALEE 2087
Cdd:COG5022 1366 CYSLNPAEIQNLkSRYDPADKE 1387
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
573-1322 |
5.50e-71 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 253.36 E-value: 5.50e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 573 VEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAY 644
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPykqlpiYSEDMIKAyrGK----RRGELPPHIFAIADEAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 645 WALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVD----GRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:pfam00063 77 RSMLQDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSagnvGRLE-EQILQSNPILEAFGNAKTVRNNNSSRFGKY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGM-GVWSKP 793
Cdd:pfam00063 156 IEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyHYLSQSGCYTIdGIDDSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 794 EDKqkaaaafaQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfEWANYAAEALGCEYEEL 866
Cdd:pfam00063 236 EFK--------ITDKAMDILGFSDEEQMGIFRIVAAILHLGniefkkeRNDEQAVPDDT----ENLQKAASLLGIDSTEL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 867 NTATFKhhlRQIiqqmtfgpsrwgledeETSSGLKMTGVDC------VEGMASGLYQELFAAVVSLINRSFSSHHLSMAS 940
Cdd:pfam00063 304 EKALCK---RRI----------------KTGRETVSKPQNVeqanyaRDALAKAIYSRLFDWLVDRINKSLDVKTIEKAS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 941 -IMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSPgtTVAVV 1014
Cdd:pfam00063 365 fIGVLDIYGFEifekN----------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFiDFGDNQP--CIDLI 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1015 DQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEK----KGAGTEGSSALRtceqplqceIFHQL 1090
Cdd:pfam00063 433 EKKP---------------LGILSLLDEECLFPKATDQTFLDKLYSTFSKhphfQKPRLQGETHFI---------IKHYA 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1091 GwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKlppvcRAVAGLEGTSQQALQRSRMVRRTFASsla 1170
Cdd:pfam00063 489 G--DVEYNVEGFLEKNKDPLND-DLVSLLKSSSDPLLAELFPDYET-----AESAAANESGKSTPKRTKKKRFITVG--- 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1171 avrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHI 1250
Cdd:pfam00063 558 --------SQFKESLGELMKTLNSTNPHYIRCIKPNE--KKRAGV--------------------FDNSLVLHQLRCNGV 607
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970949420 1251 LEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMStsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:pfam00063 608 LEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKG-----DAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
585-1322 |
6.04e-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: 6.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVP---KGRRDGLPAHIGSMAQRAYWALLN----QRRDQS 655
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKsiPDLYSEERMLlyhGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 656 IVALGWSGAGKT-------------TCCEQVLEHLVGMAGSVDGRVSV----EKIRATFTVLRAFGSVSMAHSRSATRFS 718
Cdd:cd14890 81 IIISGESGAGKTeatkiimqylariTSGFAQGASGEGEAASEAIEQTLgsleDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 719 MVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEDKq 797
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLrGECSSIPSCDD- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 798 kaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRkQFMRFewanyAAEALGCEYEELN 867
Cdd:cd14890 240 --AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGnvdfesendtTVLEDATTL-QSLKL-----AAELLGVNEDALE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 868 TATFKHHL----RQIIQQMTFGPSRwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMV 943
Cdd:cd14890 312 KALLTRQLfvggKTIVQPQNVEQAR-----------------DKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 944 VDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSqqVR 1023
Cdd:cd14890 375 LDIYGFEKFEWN------TFEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQY----------ITFNDNQAC--LE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1024 LPAGGGAQDArGLFWVLDEEVHVEGS-SDSVVLERLCAAFekkGAGTEGSSALRTCEQ------P-----LQCEIFHQLG 1091
Cdd:cd14890 437 LIEGKVNGKP-GIFITLDDCWRFKGEeANKKFVSQLHASF---GRKSGSGGTRRGSSQhphfvhPkfdadKQFGIKHYAG 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1092 wdPVRYDLTGWLHRAKPNLSAldapqvlhqskreELRSLfqaraklppvcravaglegtsqqalqrsrmvrrtFASSLAA 1171
Cdd:cd14890 513 --DVIYDASGFNEKNNETLNA-------------EMKEL----------------------------------IKQSRRS 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1172 VRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHIL 1251
Cdd:cd14890 544 IREVSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKA----------------------PGKFDGLDCLRQLKYSGMM 601
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 1252 EALRLHRTGYA---DHmglTRFRRQFQVLDapllkklmSTSEGIDErkAVEELLETLDLEKKAVAVGHSQVFLK 1322
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 ... |
585-1322 |
5.52e-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: 5.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP----SAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPY-KNLPiyseNIIEMYRGKkRHEMPPHIYAISESAYRCMLQDREDQSILCT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMA--------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRI 731
Cdd:cd14920 80 GESGAGKTENTKKVIQYLAHVAsshkgrkdHNIPGELERQLLQAN-PILESFGNAKTVKNDNSSRFGKFIRINFDVTGYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 732 TAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLHQMADSSSFgMGVWSKPEDKQKAAAAFAQLQGAME 811
Cdd:cd14920 159 VGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRF-LSNGYIPIPGQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 812 MLGISESEQRAVWRVLAAIYHLGAAGACKvGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsRWGL 891
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKL-CHLLGMNVMEFTRAI--LTPRIKVG--RDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 892 EDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNY 970
Cdd:cd14920 311 QKAQTKEQADFA----VEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFE------IFELNSFEQLCINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 971 AHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVE 1047
Cdd:cd14920 381 TNEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIDLIERPANPP---------------GVLALLDEECWFP 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1048 GSSDSVVLERLcaafekkgAGTEGS-SALRTCEQP---LQCEIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQ 1121
Cdd:cd14920 445 KATDKTFVEKL--------VQEQGShSKFQKPRQLkdkADFCIIHYAG--KVDYKADEWLMK---NMDPLndNVATLLHQ 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1122 SKREELRSLFQARAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHFIH 1201
Cdd:cd14920 512 SSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKGMFRTVG------------QLYKESLTKLMATLRNTNPNFVR 579
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1202 CLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPL 1281
Cdd:cd14920 580 CIIPNH--EKRAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 637
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 970949420 1282 LKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14920 638 IPKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
586-1277 |
2.55e-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: 2.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAgkvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPfkdvplYGNEFITA----YRQKLLDSPHVYAVADTAYREMMRDEINQSIIIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01383 78 GESGAGKTETAKIAMQYLAALGGGSSG---IEnEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNL-KSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 819 EQRAVWRVLAAIYHLG--------AAGACKVGRKqfmrfEWANYAAEALGCEYEELNTATFKHHLRqiiqqmtfgpsrwg 890
Cdd:cd01383 234 DQEHIFQMLAAVLWLGnisfqvidNENHVEVVAD-----EAVSTAASLLGCNANDLMLALSTRKIQ-------------- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 891 LEDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSF-SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd01383 295 AGGDKIVKKLTLQqAIDARDALAKAIYASLFDWLVEQINKSLeVGKRRTGRSISILDIYGFESFQKN------SFEQLCI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlpdpspgTTVAVVDQNPSQQV--RLPAgggaqdarGLFWVLDEEVHV 1046
Cdd:cd01383 369 NYANERLQQHFNRHLFKLEQEEYELDGIDW----------TKVDFEDNQECLDLieKKPL--------GLISLLDEESNF 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1047 EGSSDSVVLERL--------CAAFEKKGAGTegssalrtceqplqceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQV 1118
Cdd:cd01383 431 PKATDLTFANKLkqhlksnsCFKGERGGAFT----------------IRHYAG--EVTYDTSGFLEKNRDLLHS-DLIQL 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1119 LHQSKreelRSLFQARAklppvcravAGLEGTSQQALQRSRMvrrtfasSLAAVRRKAPCSQIKLQMDALTSMIKRSRLH 1198
Cdd:cd01383 492 LSSCS----CQLPQLFA---------SKMLDASRKALPLTKA-------SGSDSQKQSVATKFKGQLFKLMQRLENTTPH 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1199 FIHCLVPNPV-VESRSGQEsppppqpgrdkpgaggpLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1277
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 ... |
586-1279 |
7.01e-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: 7.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALL-------NQRRD 653
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPF-KHIPGLYDLHKYREEmpgwtALPPHVFSIAEGAYRSLRrrlhepgASKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAISGsellsanpILESFGNARTLRNDNSSRFGKFVRMFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 726 -----NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--DSSSFGMGVWSKPEDKQK 798
Cdd:cd14895 161 eghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGQCYQRNDGVR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 799 AAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG------------------AAGACKVGR---KQFMRFEWANYAAE 857
Cdd:cd14895 241 DDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngaASAPCRLASaspSSLTVQQHLDIVSK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 858 ALGCEYEELNTATFKhhlRQIiqqmtfgpsrwGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLIN-----RSF 931
Cdd:cd14895 321 LFAVDQDELVSALTT---RKI-----------SVGGETFHANLSLAQCgDARDAMARSLYAFLFQFLVSKVNsaspqRQF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 932 SSHHLSMAS------IMVVDSPGFQnprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPD 1004
Cdd:cd14895 387 ALNPNKAANkdttpcIAVLDIFGFE------EFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKwNAVDYED 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1005 PSpgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagteGSSALRTCEQPLQC 1084
Cdd:cd14895 461 NS--VCLEMLEQRPS---------------GIFSLLDEECVVPKGSDAGFARKLYQRLQEHS----NFSASRTDQADVAF 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1085 EIFHQLGwdPVRYDLTGWL--HRAKPNLSALDapqVLHQSKREELRSLfqaraklppvCRAVAGLEgTSQQALQRSRMVR 1162
Cdd:cd14895 520 QIHHYAG--AVRYQAEGFCekNKDQPNAELFS---VLGKTSDAHLREL----------FEFFKASE-SAELSLGQPKLRR 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1163 RTfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALR 1242
Cdd:cd14895 584 RS--SVLSSV---GIGSQFKQQLASLLDVVQQTQTHYIRCIKPND--ESASDQ--------------------FDMAKVS 636
|
730 740 750
....*....|....*....|....*....|....*..
gi 970949420 1243 VQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1279
Cdd:cd14895 637 SQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA 673
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
586-1207 |
1.38e-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: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSV-----------PSAGKVPkgrrdglpaHIGSMAQRAYWALLNQRR 652
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfkTIPGLysdemllkfiqPSISKSP---------HVFSTASSAYQGMCNNKK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 653 DQSIVALGWSGAGKTTCCEQVLEHLVgMAGSVD--GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT- 728
Cdd:cd14888 73 SQTILISGESGAGKTESTKYVMKFLA-CAGSEDikKRSLVEaQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLk 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 729 --------GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-------------DLDLRTELNLHQMA-DSSSFG 786
Cdd:cd14888 152 skrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAreakntglsyeenDEKLAKGADAKPISiDMSSFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 787 MGVWSKPEDKQKAAAAFA--------QLQGAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRK-QFMRFEWA 852
Cdd:cd14888 232 PHLKFRYLTKSSCHELPDvddleefeSTLYAMQTVGISPEEQNQIFSIVAAILYLGnilfeNNEACSEGAVvSASCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 853 NYAAEALGCEYEEL-NTATFkhhlRQIIQQmtfgpsrwgleDEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRS 930
Cdd:cd14888 312 EKVASLLGVDAEDLlNALCY----RTIKTA-----------HEFYTKPLRVDeAEDVRDALARALYSCLFDKVVERTNES 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 931 FS-SHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFdl 1002
Cdd:cd14888 377 IGySKDNSLLFCGVLDIFGFEcfqlN----------SFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIswnPLDF-- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1003 pdPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTceQPL 1082
Cdd:cd14888 445 --PDNQDCVDLLQEKPL---------------GIFCMLDEECFVPGGKD----QGLCNKLCQKHKGHKRFDVVKT--DPN 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1083 QCEIFHQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglegtsqqalqrsrMVR 1162
Cdd:cd14888 502 SFVIVHFAG--PVKYCSDGFLEKNKDQLS-VDAQEVIKNSKNPFISNLFSA--------------------------YLR 552
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 970949420 1163 RTFASSLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNP 1207
Cdd:cd14888 553 RGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNS 597
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
585-1322 |
2.50e-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: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMeryKGiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGS-----------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkpkgsgavphpavnpavLIGELEQQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPedKQKAAAAF 803
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP--GVDDYAEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEyeelNTATFK--HHLRQIIQQ 881
Cdd:cd14911 238 QATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-----------MKFRQERNNDQATLPD----NTVAQKiaHLLGLSVTD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 882 MT--FGPSRWGL-EDEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgK 957
Cdd:cd14911 303 MTraFLTPRIKVgRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFE------I 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 958 DRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqqvrlpagggaqdAR 1034
Cdd:cd14911 377 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGL-DLQP--TIDLIDK----------------PG 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1035 GLFWVLDEEVHVEGSSDSVVLERLCAA------FEKkgAGTEGSSALrtceqplqcEIFHQLGwdPVRYDLTGWLHRakp 1108
Cdd:cd14911 438 GIMALLDEECWFPKATDKTFVDKLVSAhsmhpkFMK--TDFRGVADF---------AIVHYAG--RVDYSAAKWLMK--- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1109 NLSALDapqvlhqskrEELRSLFQArAKLPPVCR--AVAGLEGTSQQALQRSRMVRRTFASSLAAVrrkapcSQI-KLQM 1185
Cdd:cd14911 502 NMDPLN----------ENIVSLLQG-SQDPFVVNiwKDAEIVGMAQQALTDTQFGARTRKGMFRTV------SHLyKEQL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1186 DALTSMIKRSRLHFIHCLVPNPvvESRSGQesppppqpgrdkpgAGGPLALDipalrvQLAGFHILEALRLHRTGYADHM 1265
Cdd:cd14911 565 AKLMDTLRNTNPNFVRCIIPNH--EKRAGK--------------IDAPLVLD------QLRCNGVLEGIRICRQGFPNRI 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1266 GLTRFRRQFQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14911 623 PFQEFRQRYELLTPNVIPKGF-----MDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
585-1322 |
2.52e-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: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVP---------SAGKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQS 655
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPY-KELPiytqdivkqYFGK----RMGALPPHIFALAEAAYTNMQEDGKNQS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 656 IVALGWSGAGKTTCCEQVLEHLVgmagSVDGRVS-VE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14883 76 VIISGESGAGKTETTKLILQYLC----AVTNNHSwVEqQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAG--LDLDLRTELNLHQMAD------SSSFGMGVWSKPEDkqkaaaaFAQ 805
Cdd:cd14883 152 AIIQDYLLEQSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDyhylnqSGCIRIDNINDKKD-------FDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 806 LQGAMEMLGISESEQRAVWRVLAAIYHLG--AAGACKVGRKQFMRFEWANYAAEA--LGCEYEELNTA-TFKHhlRQIIQ 880
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGnlTFEDIDGETGALTVEDKEILKIVAklLGVDPDKLKKAlTIRQ--INVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 881 QMTFGPsrwgledeetssgLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd14883 303 NVTEIP-------------LKVQeARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQF-------DLPDPSPgttvavvdqnpsqqvrlpaggg 1029
Cdd:cd14883 366 --SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGInwsHIVFtdnqeclDLIEKPP---------------------- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1030 aqdaRGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQceifHQLGwdPVRYDLTGWLHRAKPN 1109
Cdd:cd14883 422 ----LGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEFGVK----HYAG--EVTYTVQGFLDKNKDT 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1110 LSaLDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEGTSQqalqrsrmvRRTfasslaavRRKAP--CSQIKLQMDA 1187
Cdd:cd14883 492 QQ-DDLFDLMSRSKNKFVKELFTYPDLLALTGLSISLGGDTTS---------RGT--------SKGKPtvGDTFKHQLQS 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1188 LTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGL 1267
Cdd:cd14883 554 LVDVLSATQPWYVRCIKPNSLKE----------------------PNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTF 611
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 970949420 1268 TRFRRQFQVLDapllkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14883 612 KEFVDRYLCLD-----PRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
586-1319 |
2.83e-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: 2.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPS--AGKVPKGrrdgLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPfkrlplYTPTVMDqyMHKGPKE----MPPHTYNIADDAYRAMIVDAMNQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGrvsVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQL 736
Cdd:cd14872 78 ISGESGAGKTEATKQCLSFFAEVAGSTNG---VEqRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNlhqmaDSSSFGMGVWSKPEDKQKAAAAF--AQLQGAMEMLG 814
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWG-----SSAAYGYLSLSGCIEVEGVDDVAdfEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 815 ISESEQRAVWRVLAAIYHLG------AAGACKVGRKQFMRFEWANYAAEALGCEYEELNTAtFKHHLRQIIQQmtfGPSR 888
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGniefasGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEA-LTSRLMEIKGC---DPTR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 889 WGLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQ----NprhqgkdraaTF 963
Cdd:cd14872 306 IPLTPAQ--------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTfIGVLDIFGFEifekN----------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ-FDLPDPSPgttvaVVDQNPSQQvrlpagggaqdaRGLFWVLDE 1042
Cdd:cd14872 368 EQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKFEhIDFIDNQP-----VLDLIEKKQ------------PGLMLALDD 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1043 EVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQS 1122
Cdd:cd14872 431 QVKIPKGSD----ATFMIAANQTHAAKSTFVYAEVRTSRTEFIVKHYAG--DVTYDITGFLEKNKDTLQK-DLYVLLSSS 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1123 KREELRSLFqaraklPPvcraVAGLEGTSQQALqrsrmvrrtfasslaavrrkapCSQIKLQMDALTSMIKRSRLHFIHC 1202
Cdd:cd14872 504 KNKLIAVLF------PP----SEGDQKTSKVTL----------------------GGQFRKQLSALMTALNATEPHYIRC 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1203 LVPNpvvesrsgqesppppQPGRDKPGAGgplALDIPALRvqLAGfhILEALRLHRTGYAdhmgltrFR---RQFQVLDA 1279
Cdd:cd14872 552 VKPN---------------QEKRARLFDG---FMSLEQLR--YAG--VFEAVKIRKTGYP-------FRyshERFLKRYR 602
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 970949420 1280 PLLKKlMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQV 1319
Cdd:cd14872 603 FLVKT-IAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRV 641
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
585-1278 |
1.24e-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: 174.19 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAG---KVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQwlPELYTEEqhsKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLN-DSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ---------------MADSSSFgmgvwskpedkqkaaaafA 804
Cdd:cd14903 160 LLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANecaytganktikiegMSDRKHF------------------A 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAA-----------GACKVGRkqfmrfEWANYAAEALGCEYEELNTATFKH 873
Cdd:cd14903 222 RTKEALSLIGVSEEKQEVLFEVLAGILHLGQLqiqskpnddekSAIAPGD------QGAVYATKLLGLSPEALEKALCSR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 874 HLRQIIQQMTFgpsrwGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPR 953
Cdd:cd14903 296 TMRAAGDVYTV-----PLKKDQAE--------DCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 954 HQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVdqnpsqqvrlpagggaQD 1032
Cdd:cd14903 363 HN------SFEQFCINYANEKLQQKFTQDVFKTVQIEYEEEGIRwAHIDFADNQ--DVLAVI----------------ED 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1033 ARGLFWVLDEEV-HVEGSSDSVVLeRLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAK---- 1107
Cdd:cd14903 419 RLGIISLLNDEVmRPKGNEESFVS-KLSSIHKDEQDVIEFPRTSRT-----QFTIKHYAG--PVTYESLGFLEKHKdall 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1108 PNLSALdapqvLHQSKREELRSLFQARaklppvcravAGLEGTSQQALQRSRMVRRTFASSLAAVRrkapcSQIKLQMDA 1187
Cdd:cd14903 491 PDLSDL-----MRGSSKPFLRMLFKEK----------VESPAAASTSLARGARRRRGGALTTTTVG-----TQFKDSLNE 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1188 LTSMIKRSRLHFIHCLVPNPvvesrsgqesppppqpgrdkpgAGGPLALDIPALRVQLAGFHILEALRLHRTGYADHMGL 1267
Cdd:cd14903 551 LMTTIRSTNVHYVRCIKPNS----------------------IKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLH 608
|
730
....*....|.
gi 970949420 1268 TRFRRQFQVLD 1278
Cdd:cd14903 609 EEFLDKFWLFL 619
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
585-1322 |
2.39e-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: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVP---KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVdmyKGKkRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGS--------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASShkgkkdtsITGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQGAMEM 812
Cdd:cd14921 160 GANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQ--DDEMFQETLEAMSI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 813 LGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglE 892
Cdd:cd14921 238 MGFSEEEQLSILKVVSSVLQLGNI-VFKKERNTDQASMPDNTAAQKV-CHLMGINVTDFTRSI--LTPRIKVG------R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 893 DEETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYA 971
Cdd:cd14921 308 DVVQKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFE------IFEVNSFEQLCINYT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 972 HERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEG 1048
Cdd:cd14921 382 NEKLQQLFNHTMFILEQEEYQREGIEwnfIDFGL-DLQPCIELIERPNNPP---------------GVLALLDEECWFPK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1049 SSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREE 1126
Cdd:cd14921 446 ATDKSFVEKLC---TEQGNHPKFQKPKQLKDKTEFS-IIHYAG--KVDYNASAWLTK---NMDPLndNVTSLLNASSDKF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1127 LRSLFQARAKlppvcraVAGLEgtsqqalQRSRMVRRTFASslAAVRRKAPCSQI----KLQMDALTSMIKRSRLHFIHC 1202
Cdd:cd14921 517 VADLWKDVDR-------IVGLD-------QMAKMTESSLPS--ASKTKKGMFRTVgqlyKEQLGKLMTTLRNTTPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1203 LVPNPvvESRSGQesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLL 1282
Cdd:cd14921 581 IIPNH--EKRSGK--------------------LDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAI 638
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 970949420 1283 KKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14921 639 PKGF-----MDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
582-1321 |
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 970949420 582 VNESSVLNTLLQRYKAQLLHTCTGPD-LIVLQP--RGPSV--PSAGK-------VPKGRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPykYLSSNsdASLGEygseyydTTSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 650 QRRDQSIVALGWSGAGKTTCCEQVLEHLVGM-AGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTKLSSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFNER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHqmaDSSSFGMGvWS--------KP--EDkqk 798
Cdd:cd14879 161 GRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLD---DPSDYALL-ASygchplplGPgsDD--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 799 aAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVgrkqfmrfewANY-----AAEALGCEY 863
Cdd:cd14879 234 -AEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGnleftydhegGEESAVV----------KNTdvldiVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 864 EELNTA-TFKhhlrqiiqqmtfgpsrwgledeetssgLKMTGVDCVEGM-------------ASGLYQELFAAVVSLINR 929
Cdd:cd14879 303 EDLETSlTYK---------------------------TKLVRKELCTVFldpegaaaqrdelARTLYSLLFAWVVETINQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 930 SFSSHHLSMAS-IMVVDSPGFQNprhQGKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSPG 1008
Cdd:cd14879 356 KLCAPEDDFATfISLLDFPGFQN---RSSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSV----PATSYF 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1009 TTVAVvdqnpsqqVRLPAGGGAqdarGLFWVLDEEV-HVEGSSDSVVLERLCAAFEKK-------GAGTEGSSALRTceq 1080
Cdd:cd14879 429 DNSDC--------VRLLRGKPG----GLLGILDDQTrRMPKKTDEQMLEALRKRFGNHssfiavgNFATRSGSASFT--- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1081 plqceIFHQLGwdPVRYDLTGWLHRakpNLSALDApqvlhqskreELRSLfqaraklppvcravagLEGTSQqalqrsrm 1160
Cdd:cd14879 494 -----VNHYAG--EVTYSVEGFLER---NGDVLSP----------DFVNL----------------LRGATQ-------- 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1161 vrrtFASSLaavrrkapcsqiklqmDALTSMIKRSRLHFIHCLVPNPvvesrsgqeSPPPPQPGRDKpgaggplaldipa 1240
Cdd:cd14879 530 ----LNAAL----------------SELLDTLDRTRLWSVFCIRPND---------SQLPNSFDKRR------------- 567
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1241 LRVQLAGFHILEALRLHRTGYADHMGLTRFrrqfqvldaplLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVF 1320
Cdd:cd14879 568 VKAQIRSLGLPELAARLRVEYVVSLEHAEF-----------CERYKSTLRGSAAERIRQCARANGWWEGRDYVLGNTKVF 636
|
.
gi 970949420 1321 L 1321
Cdd:cd14879 637 L 637
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
586-1131 |
9.73e-44 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 171.03 E-value: 9.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR------RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKP-LPIFDKKHHEEysnlsvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRVsVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSDL-LDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-----HQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLG 814
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLedpdcHRILRDDNRNRPVFNDSEELEYYRQMFHDLTNIMKLIG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 815 ISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFE---WANYAAEALGCEYEELNTAtfkhhlrqIIQQMTFgpsrwgL 891
Cdd:cd14897 240 FSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVAdeyPLHAVAKLLGIDEVELTEA--------LISNVNT------I 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 892 EDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHL-----SMASIMVVDSPGFQNPRHQGkdraatFEE 965
Cdd:cd14897 306 RGERIQSWKSLrQANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDfqimtRGPSIGILDMSGFENFKINS------FDQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVH 1045
Cdd:cd14897 380 LCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR-DIEYHDNDDVLELFFKKPL---------------GILPLLDEEST 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1046 VEGSSDSVVLERLcaafEKKGagteGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSK 1123
Cdd:cd14897 444 FPQSTDSSLVQKL----NKYC----GESPRYVASPGNRVAfgIRHYAE--QVTYDADGFLEKNRDNLSS-DIVGCLLNSN 512
|
....*...
gi 970949420 1124 REELRSLF 1131
Cdd:cd14897 513 NEFISDLF 520
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
586-1322 |
1.32e-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: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvpkgRRDGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPykrlpiYTEEVIDKykGK----RREEMPPHIFAIADNAYRNMLQDRENQSIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 658 ALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATF--------TVLRAFGSVSMAHSRSATRFSMVMSLDFNATG 729
Cdd:cd01377 78 ITGESGAGKTENTKKVIQYLASVAASSKKKKESGKKKGTLedqilqanPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 730 RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGM-------GVWSKPEDKqkaaaa 802
Cdd:cd01377 158 KIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSqgeltidGVDDAEEFK------ 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 803 faQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELNTATFKHHL---R 876
Cdd:cd01377 232 --LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELdgtEEADKAAHLLGVNSSDLLKALLKPRIkvgR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 877 QIIQQmtfgpsrwgledeetssGLKMTGVDC-VEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----N 951
Cdd:cd01377 310 EWVTK-----------------GQNKEQVVFsVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 952 prhqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVD--QNPSQqvrl 1024
Cdd:cd01377 373 ----------SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfglDLQ--------PTIDliEKPNM---- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1025 pagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegsSALRTCEQPLQCE----IFHQLGwdPVRYDLT 1100
Cdd:cd01377 431 ----------GILSILDEECVFPKATDKTFVEKLYSNHLGK-------SKNFKKPKPKKSEahfiLKHYAG--DVEYNID 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1101 GWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrAVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQ 1180
Cdd:cd01377 492 GWLEKNKDPLNE-NVVALLKKSSDPLVASLF-----------KDYEESGGGGGKKKKKGGSFRTVS------------QL 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1181 IKLQMDALTSMIKRSRLHFIHCLVPNpvvESRsgqesppppQPGR-DKpgaggPLALDipalrvQLA--GfhILEALRLH 1257
Cdd:cd01377 548 HKEQLNKLMTTLRSTHPHFVRCIIPN---EEK---------KPGKiDA-----PLVLH------QLRcnG--VLEGIRIC 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970949420 1258 RTGYADHMGLTRFRRQFQVLDAPLLKKlmstseGIDERKAVEELLETLDLEKKAV-AVGHSQVFLK 1322
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 ... |
588-1322 |
5.76e-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: 5.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 588 LNTLLQRYKAQLLHTCTGPDLIVLQPRG--------PSVPSAGKVPKGRRDGLPaHIGSMAQRAYWAL----LNQRRDQS 655
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPYKsipllydvPGFDSQRKEEATASSPPP-HVFSIAERAYRAMkgvgKGQGTPQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 656 IVALGWSGAGKTTCCEQVLEHLV-------GMAGSVDGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLD 724
Cdd:cd14892 83 IVVSGESGAGKTEASKYIMKYLAtasklakGASTSKGAANAHESIEECVllsnLILEAFGNAKTIRNDNSSRFGKYIQIH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 725 FNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSFGMGVWSKPEDKQKAAAAFA 804
Cdd:cd14892 163 YNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALEL-TPAESFLFLNQGNCVEVDGVDDATEFK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgackvgrkqfmRFEwANYAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14892 242 QLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNV-----------RFE-ENADDEDVFAQSADGVNVAKAAGLLGVDAAELM 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 885 GPSRWgledEETSSG------LKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSSH----HLSMAS------IMVVD 945
Cdd:cd14892 310 FKLVT----QTTSTArgsvleIKLTAREAKNaldALCKYLYGELFDWLISRINACHKQQtsgvTGGAASptfspfIGILD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 946 SPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---PVQFDlpDPSPgtTVAVVDQNPSqq 1021
Cdd:cd14892 386 IFGFEImPTN-------SFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIdvsAIEFQ--DNQD--CLDLIQKKPL-- 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1022 vrlpagggaqdarGLFWVLDEEVHV-EGSSDSVVLERLCAAFEKKGAgtegssalrTCEQP-LQCEIF---HQLGwdPVR 1096
Cdd:cd14892 453 -------------GLLPLLEEQMLLkRKTTDKQLLTIYHQTHLDKHP---------HYAKPrFECDEFvlrHYAG--DVT 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1097 YDLTGWLhrAKPNLSaldapqvLHqskrEELRSLfqaraklppvcravaglegtsqqaLQRSRMVRRtfasslaavrrka 1176
Cdd:cd14892 509 YDVHGFL--AKNNDN-------LH----DDLRDL------------------------LRSSSKFRT------------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1177 pcsqiklQMDALTSMIKRSRLHFIHCLVPNPVvesrsgqespppPQPGrdkpGAGGPLALDipalrvQLAGFHILEALRL 1256
Cdd:cd14892 539 -------QLAELMEVLWSTTPSYIKCIKPNNL------------KFPG----GFSCELVRD------QLIYSGVLEVVRI 589
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 1257 HRTGYADHMGLTRFRRQFQVLDAPLLKKLMS--TSEGIDERKAVeELLETLDLEKKAVAVGHSQVFLK 1322
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, ... |
632-1322 |
2.23e-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: 2.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 632 LPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEKIR----ATFTVLRAFGSVS 707
Cdd:cd01378 52 VPPHVFALADSAYRNMKSEKENQCVIISGESGAGKTEASKRIMQYIA--AVSGGSESEVERVKdmllASNPLLEAFGNAK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 708 MAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQ--------- 778
Cdd:cd01378 130 TLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRpeqyyyysk 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 779 --------MADSSSFgmgvwskpedkqkaaaafAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGR 843
Cdd:cd01378 210 sgcfdvdgIDDAADF------------------KEVLNAMKVIGFTEEEQDSIFRILAAILHLGniqfaedEEGNAAISD 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 844 KQFMRFewanyAAEALGCEYEELNTA-TFkhhlRQIIqqmtfgpSRWGlEDEETSSGLKMTGVDCV-EGMASGLYQELFA 921
Cdd:cd01378 272 TSVLDF-----VAYLLGVDPDQLEKAlTH----RTIE-------TGGG-GRSVYEVPLNVEQAAYArDALAKAIYSRLFD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 922 AVVSLINRSFSSHHLSMASIM-VVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGV---P 997
Cdd:cd01378 335 WIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKNS------FEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIewtP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 998 VQF-------DLpdpspgttvavVDQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEG-SSDSVVLERLCAAFEKKGAGT 1069
Cdd:cd01378 409 IKYfnnkiicDL-----------IEEKP---------------PGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1070 EGSSALrtcEQPLQC-EIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcravagLE 1148
Cdd:cd01378 463 CPSGHF---ELRRGEfRIKHYAG--DVTYNVEGFLDKNKDLLFK-DLKELMQSSSNPFLRSLF---------------PE 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1149 GTSQQALQRSrmvrrTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgrdkp 1228
Cdd:cd01378 522 GVDLDSKKRP-----PTAG-----------TKFKNSANALVETLMKKQPSYIRCIKPN---DNKS--------------- 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1229 gaggPLALDIPALRVQLAGFHILEALRLHRTGYAdhmgltrFRRQFqvlDAPLLK-KLMS--TS---EGIDeRKAVEELL 1302
Cdd:cd01378 568 ----PGEFDEELVLHQVKYLGLLENVRVRRAGFA-------YRQTY---EKFLERyKLLSpkTWpawDGTW-QGGVESIL 632
|
730 740
....*....|....*....|
gi 970949420 1303 ETLDLEKKAVAVGHSQVFLK 1322
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 ... |
586-1206 |
3.10e-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: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGiytEEHSRLYRGAkRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 662 SGAGKTTCCEQVLEHLVGMaGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLL 741
Cdd:cd01379 82 SGAGKTESANLLVQQLTVL-GKANNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTE---LNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01379 161 EKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkykLPENKPPRYLQNDGLTVQDIVNNSGNREKFEEIEQCFKVIGFTKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 819 EQRAVWRVLAAIYHLG-------AAGACKVGRKQFMRFEWANYAAEALGCEYEElntatfkhhlrqiiqqmtfgpsrwgL 891
Cdd:cd01379 241 EVDSVYSILAAILHIGdieftevESNHQTDKSSRISNPEALNNVAKLLGIEADE-------------------------L 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 892 EDEETSSGLKMTG------------VDCVEGMASGLYQELFAAVVSLINR--SFSSHHLSMA-SIMVVDSPGFQNPRHQg 956
Cdd:cd01379 296 QEALTSHSVVTRGetiirnntveeaTDARDAMAKALYGRLFSWIVNRINSllKPDRSASDEPlSIGILDIFGFENFQKN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQQVRLpagggaQDARGL 1036
Cdd:cd01379 375 -----SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVD----------LIEYEDNRPLLDMFL------QKPMGL 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1037 FWVLDEEVHVEGSSDSVVLERlcaaFEKkgaGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAP 1116
Cdd:cd01379 434 LALLDEESRFPKATDQTLVEK----FHN---NIKSKYYWRPKSNALSFGIHHYAG--KVLYDASGFLEKNRDTLPP-DVV 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1117 QVLHQSKreelrslfqaraklppvcravaglegtsqqalqrSRMVRRTFAS----SLaavrrkapcsqiklqMDALTSMI 1192
Cdd:cd01379 504 QLLRSSE----------------------------------NPLVRQTVATyfrySL---------------MDLLSKMV 534
|
650
....*....|....
gi 970949420 1193 KrSRLHFIHCLVPN 1206
Cdd:cd01379 535 V-GQPHFVRCIKPN 547
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
585-1206 |
4.65e-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: 4.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-SVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQIlPIYTAEQIRlyRNKKIGeLPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLvgmaGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQT 738
Cdd:cd01381 81 ESGAGKTESTKLILQYL----AAISGQHSwIEQqILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 739 MLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwSKPEDKQKAAAAFAQLQGAMEMLGISES 818
Cdd:cd01381 157 YLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGN-CLTCEGRDDAAEFADIRSAMKVLMFTDE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 819 EQRAVWRVLAAIYHLGAAG----------ACKVGRKQFmrfewANYAAEALGCEYEELNTATFKHHLrqiiqqMTFGpsr 888
Cdd:cd01381 236 EIWDIFKLLAAILHLGNIKfeatvvdnldASEVRDPPN-----LERAAKLLEVPKQDLVDALTTRTI------FTRG--- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 889 wgledEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSF---SSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd01381 302 -----ETVVSPLSAEQaLDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENFEVN------SFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttVAVVDQNPSQQVRlpagggAQDARGLFWVLDEEV 1044
Cdd:cd01381 371 QLCINFANENLQQFFVRHIFKLEQEEYDKEGINWQH----------IEFVDNQDVLDLI------ALKPMNIMSLIDEES 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1045 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1124
Cdd:cd01381 435 KFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNT-----SFGINHFAG--VVFYDTRGFLEKNRDTFSA-DLLQLVQSSKN 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1125 EELRSLFQAraklppvCRAvAGLEGtsqqalqrsrmvrrtfasslaavRRKAP--CSQIKLQMDALTSMIKRSRLHFIHC 1202
Cdd:cd01381 507 KFLKQLFNE-------DIS-MGSET-----------------------RKKSPtlSSQFRKSLDQLMKTLSACQPFFVRC 555
|
....
gi 970949420 1203 LVPN 1206
Cdd:cd01381 556 IKPN 559
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
586-1322 |
5.20e-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: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYkwlpvyNPEVVEGYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVD-GRVSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14913 80 GESGAGKTVNTKRVIQYFATIAATGDlAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAAFAQLQ 807
Cdd:cd14913 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELL----LITTNPYDYPFISQGEilvASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKTAYLMGLNSSDLLKALCF--P 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 RWGLEDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14913 305 RVKVGNEYVTKGQTVDQVHhAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN------SLEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLpdpspGTTVAVVdqnpsqqVRLpagggAQDARGLFWVLDEEVH 1045
Cdd:cd14913 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFiDF-----GMDLAAC-------IEL-----IEKPMGIFSILEEECM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1046 VEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKRE 1125
Cdd:cd14913 442 FPKATDTSFKNKLYDQHLGKSNNFQKPKVVKG-RAEAHFSLIHYAG--TVDYSVSGWLEKNKDPLNE-TVVGLYQKSSNR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1126 ELRSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCL 1203
Cdd:cd14913 518 LLAHLYAtfATADADSGKKKVAKKKGSSFQ--------------TVSALFRE--------NLNKLMSNLRTTHPHFVRCI 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1204 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1283
Cdd:cd14913 576 IPN---ETKT-------------------PGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
|
730 740 750
....*....|....*....|....*....|....*....
gi 970949420 1284 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
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 ... |
585-1322 |
1.12e-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: 1.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKYLPIYSEEIVNmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVD------------GRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKtkkdqssialshGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQL 806
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPgqQDK----ELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 807 QGAMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFG 885
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNM-SFKKERNSDQASMPDDTAAQKV-CHLLGMNVTDFT---RAILSpRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 886 psRWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFE 964
Cdd:cd14932 311 --RDYVQKAQTQEQAEFA----VEALAKASYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPgtTVAVVDQnpsqqvrlPAGggaqdARGLFWVLD 1041
Cdd:cd14932 379 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwsfIDFGL-DLQP--CIELIEK--------PNG-----PPGILALLD 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1042 EEVHVEGSSDSVVLERLCaafEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSALD--APQVL 1119
Cdd:cd14932 443 EECWFPKATDKSFVEKVV---QEQGNNPKFQKPKKLKDDADFC-IIHYAG--KVDYKANEWLMK---NMDPLNenVATLL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1120 HQSKREELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTFAsslaavrrkapcSQIKLQMDALTSMIKRSRLHF 1199
Cdd:cd14932 514 NQSTDKFVSELWKDVDRIVGLDK-VAGMGESLHGAFKTRKGMFRTVG------------QLYKEQLMNLMTTLRNTNPNF 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1200 IHCLVPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDA 1279
Cdd:cd14932 581 VRCIIPNH--EKKAGKLAH--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 638
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 970949420 1280 PLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14932 639 NAIPKGF-----MDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
586-1274 |
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 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP--SVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALL-NQR 651
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPLKPlpDLYSESQLnaykasmtstsPVSQLSELPPHVFAIGGKAFGGLLkPER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 652 RDQSIVALGWSGAGKTTCCEQVLEHL--VG-----MAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLtsVGrdqssTEQEGSDAVEIGKrILQTNPILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADS---SSFGMGVWSKPEDKQKAA 800
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYellNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 801 AAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFM-------RFEWANyAAEALGCEYEELNTATFKH 873
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDAtavtaasRFHLAK-CAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 874 HLRQIIQQMTFGPSRWGLEDEETSsglkmtgvdcvegMASGLYQELFAAVVSLIN---------RSFSSHHLSMASIMVV 944
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGS-------------LAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 945 DSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfDLPDPSPGTTVAVVDQNPSqqvrl 1024
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWK-NISYPSNAACLALFDDKSN----- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1025 pagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGagtegssalrtceqplQCEIFHQLGwdPVRYDLTGWLH 1104
Cdd:cd14902 456 ----------GLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAG--RVCYNVEQFVE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1105 RAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPVCRAVAGLEgtsqqalQRSRMVRrtfASSLAAvrrkapcsQIKLQ 1184
Cdd:cd14902 508 KNTDALPA-DASDILSSSSNEVVVAIGADENRDSPGADNGAAGR-------RRYSMLR---APSVSA--------QFKSQ 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1185 MDALTSMIKRSRLHFIHCLVPNPVvesrsgqesppppqpgrdkpgaGGPLALDIPALRVQLAGFHILEALRLHRTGYADH 1264
Cdd:cd14902 569 LDRLIVQIGRTEAHYVRCLKPNEV----------------------KKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVR 626
|
730
....*....|
gi 970949420 1265 MGLTRFRRQF 1274
Cdd:cd14902 627 LAHASFIELF 636
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
586-1261 |
2.36e-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: 2.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKGRrDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPYKwidnlyGDHLHEQYLKKPR-DKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVDGRvSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDK-TIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESE 819
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 820 QRAVWRVLAAIYHLGAAGACKVGRK--QFMRFEWANYAAEALGCEYEELNTATFKhhlRQIIQQmtfgpsrwgledeETS 897
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENgsRISNGSQLSQVAKMLGLPTTRIEEALCN---RSVVTR-------------NES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 898 SGLKMTGVDCVE---GMASGLYQELFAAVVSLINRSFSS-HHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHE 973
Cdd:cd14904 304 VTVPLAPVEAEEnrdALAKAIYSKLFDWMVVKINAAISTdDDRIKGQIGVLDIFGFEDFAHNG------FEQFCINYANE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 974 RLQLLFYQRTFVSTLQRYQEEGvpVQFD-LPDPSPGTTVAVVDQNpsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDS 1052
Cdd:cd14904 378 KLQQKFTTDVFKTVEEEYIREG--LQWDhIEYQDNQGIVEVIDGK----------------MGIIALMNDHLRQPRGTEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1053 VVLERLCAAFEKKGAGT--EGSSALRTceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSL 1130
Cdd:cd14904 440 ALVNKIRTNHQTKKDNEsiDFPKVKRT-----QFIINHYAG--PVTYETVGFMEKHRDTLQN-DLLDLVLLSSLDLLTEL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1131 FQAraklppvcravagLEGTSQQALQRSRmvRRTFAsslaavrRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvE 1210
Cdd:cd14904 512 FGS-------------SEAPSETKEGKSG--KGTKA-------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPN---A 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1211 SRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGY 1261
Cdd:cd14904 567 NKS-------------------PTEFDKRMVVEQLRSAGVIEAIRITRSGY 598
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
585-1322 |
2.43e-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: 161.16 E-value: 2.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPS-AGKVPKG-RRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPykRYPVYTNrCAKMYRGkRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSkgsledqVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL-HQMADSSSFGMGVWSKPedKQKAAAAFAQLQGAMEM 812
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVP--NVDDGEEFSLTDQAFDI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 813 LGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMR---FEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRw 889
Cdd:cd14909 239 LGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEqdgEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 890 gleDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHN 969
Cdd:cd14909 318 ---QQVTNS---------IGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG------FEQLCIN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 970 YAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLpdpspgttVAVVDQnpsqqvrlpagggAQDARGLFWVLDEEV 1044
Cdd:cd14909 380 FTNEKLQQFFNHHMFVLEQEEYKREGIDWAFidfgmDL--------LACIDL-------------IEKPMGILSILEEES 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1045 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldaPQVLHQSKR 1124
Cdd:cd14909 439 MFPKATDQTFSEKLTNTHLGKSAPFQKPKPPKPGQQAAHFAIAHYAG--CVSYNITGWLEKNKDPLN----DTVVDQFKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1125 EELRSLFQARAKLPPVCRAVAGLEGTsqqalqrsrmvRRTFASSLAAVRrkapcSQIKLQMDALTSMIKRSRLHFIHCLV 1204
Cdd:cd14909 513 SQNKLLIEIFADHAGQSGGGEQAKGG-----------RGKKGGGFATVS-----SAYKEQLNSLMTTLRSTQPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1205 PNPVvesrsgqespppPQPGrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1284
Cdd:cd14909 577 PNEM------------KQPG----------VVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGIQG 634
|
730 740 750
....*....|....*....|....*....|....*...
gi 970949420 1285 LMstsegiDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14909 635 EE------DPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
585-1322 |
3.52e-40 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 160.58 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAG----KVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPY-KWLPIYGarvaNMYKGKkRTEMPPHLFSISDNAYHDMLMDRENQSMLIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAG----SVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14934 80 GESGAGKTENTKKVIQYFANIGGtgkqSSDGKGSLEdQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSF-----GMGVWSKPEDkqkaAAAFAQLQGA 809
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL--VPNPKEYhwvsqGVTVVDNMDD----GEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 810 MEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRF---EWANYAAEALGCEYEELntatfkhhlrqiiqQMTFGP 886
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVdttEVADKVAHLMGLNSGEL--------------QKGITR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 887 SRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEE 965
Cdd:cd14934 300 PRVKVGNEFVQKGQNMEQCnNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN------SFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 966 LCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEVH 1045
Cdd:cd14934 374 LCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVF-------------IDFGLDLQACIDL---LEKPMGIFSILEEQCV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1046 VEGSSDSVV--------LERLCAAFEKKGAGTEGSSAlrtceqplQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapq 1117
Cdd:cd14934 438 FPKATDATFkaalydnhLGKSSNFLKPKGGKGKGPEA--------HFELVHYAG--TVGYNITGWLEKNKDPLN------ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1118 vlhqskrEELRSLFQARAKLppVC----RAVAGLEGTSQQALQRSRMVRRTFasslaavrrkapcsqIKLQMDALTSMIK 1193
Cdd:cd14934 502 -------ETVVGLFQKSSLG--LLallfKEEEAPAGSKKQKRGSSFMTVSNF---------------YREQLNKLMTTLH 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1194 RSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1273
Cdd:cd14934 558 STAPHFVRCIVPNEFKQSG----------------------VVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 970949420 1274 FQVLDAPLLKKLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
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 ... |
585-1322 |
4.09e-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: 4.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKwlpvyqKEVMAAYK--GKRRSEAPPHIFAVANNAFQDMLHNRENQSILF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAA 734
Cdd:cd14929 79 TGESGAGKTVNTKHIIQYFATIAAMIESKkklgALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 735 QLQTMLLEKSRVARQPEGESNFLVFSQMLAGldldlrtELNLHQM----ADSSSFGM---GVWSKpeDKQKAAAAFAQLQ 807
Cdd:cd14929 159 DIDIYLLEKSRVIFQQPGERNYHIFYQILSG-------KKELRDLllvsANPSDFHFcscGAVAV--ESLDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFgpS 887
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFG-----NMKFKQKPREE----QLEADGTENADKAAFLMGINSSELVKGLIH--P 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14929 299 RIKVGNEYVTRSQNIEQVTYAVGaLSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN------SLEQL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEG---VPVQFDLpdpspgTTVAVVDQnpsqqvrlpagggAQDARGLFWVLDEE 1043
Cdd:cd14929 373 CINFTNEKLQQFFNQHMFVLEQEEYRKEGidwVSIDFGL------DLQACIDL-------------IEKPMGIFSILEEE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1044 VHVEGSSDSVVLERLC-AAFEKKGAGTEGSSALRTCEqpLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSAlDAPQVLHQS 1122
Cdd:cd14929 434 CMFPKATDLTFKTKLFdNHFGKSVHFQKPKPDKKKFE--AHFELVHYAGVVP--YNISGWLEKNKDLLNE-TVVAVFQKS 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1123 KREELRSLFQARAklppvcravaglegTSQQALQRSRMVRRTFASSlaavrrKAPCSQIKLQMDALTSMIKRSRLHFIHC 1202
Cdd:cd14929 509 SNRLLASLFENYI--------------STDSAIQFGEKKRKKGASF------QTVASLHKENLNKLMTNLKSTAPHFVRC 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1203 LVPNPvvesrsgqesppppqpgRDKPGAGGP-LALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDApl 1281
Cdd:cd14929 569 INPNV-----------------NKIPGVLDPyLVLQ------QLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP-- 623
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 970949420 1282 lkKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14929 624 --RTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
585-1322 |
4.67e-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: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSV-----DGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHkskkdQGELERQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGAN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKP--EDKqkaaAAFAQLQGAMEML 813
Cdd:cd14919 160 IETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPgqQDK----DMFQETMEAMRIM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALGcEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14919 236 GIPEEEQMGLLRVISGVLQLGNI-VFKKERNTDQASMPDNTAAQKVS-HLLGINVTDFTRGI--LTPRIKVG------RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14919 306 YVQKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASfIGILDIAGFE------IFDLNSFEQLCINYTN 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 973 ERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPdpspgttvavVDQNPS-QQVRLPAGggaqdARGLFWVLDEEVHVEGSS 1050
Cdd:cd14919 380 EKLQQLFNHTMFILEQEEYQREGIEWNFiDFG----------LDLQPCiDLIEKPAG-----PPGILALLDEECWFPKAT 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1051 DSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELR 1128
Cdd:cd14919 445 DKSFVEKV---VQEQGTHPKFQKPKQLKDKADFC-IIHYAG--KVDYKADEWLMK---NMDPLndNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1129 SLFQARAKlppvcraVAGLE---GTSQQALQRSRMVRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1205
Cdd:cd14919 516 ELWKDVDR-------IIGLDqvaGMSETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIP 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1206 NPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKL 1285
Cdd:cd14919 581 NH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPKG 638
|
730 740 750
....*....|....*....|....*....|....*..
gi 970949420 1286 MstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14919 639 F-----MDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
587-1322 |
2.88e-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: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMA----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14918 81 ESGAGKTVNTKRVIQYFATIAvtgekkkeesGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14918 238 IDILGFTPEEKVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14918 307 KVGNEYVTKGQTVQQVyNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEVHVEG 1048
Cdd:cd14918 381 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK----------------PLGIFSILEEECMFPK 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1049 SSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQ-SKREEL 1127
Cdd:cd14918 445 ATDTSFKNKLYDQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--TVDYNITGWLDKNKDPLN--DTVVGLYQkSAMKTL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1128 RSLFQ--ARAKLPPVCRAVAGLEGTSQQalqrsrmvrrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVP 1205
Cdd:cd14918 520 ASLFStyASAEADSGAKKGAKKKGSSFQ--------------TVSALFRE--------NLNKLMTNLRSTHPHFVRCIIP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1206 NpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKl 1285
Cdd:cd14918 578 N---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASAIPE- 634
|
730 740 750
....*....|....*....|....*....|....*..
gi 970949420 1286 mstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14918 635 ---GQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
586-1206 |
2.99e-39 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 157.80 E-value: 2.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP----RGPSVPSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyfdiPKLYSSETIKSYQGKSLGtLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIE-QRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnLH--QMADSSSFGmgvwskpedkqkaaaafaQLQGAMEMLGISES 818
Cdd:cd01382 161 LEKSRICVQSKEERNYHIFYRLCAGAPEDLREKL-LKdpLLDDVGDFI------------------RMDKAMKKIGLSDE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 819 EQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRFEwanYAAEALGCEYEELntatfKHHLRQIIQQMTFGPS- 887
Cdd:cd01382 222 EKLDIFRVVAAVLHLGniefeengsdSGGGCNVKPKSEQSLE---YAAELLGLDQDEL-----RVSLTTRVMQTTRGGAk 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 ----RWGLEDEETSSGLkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSShhlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd01382 294 gtviKVPLKVEEANNAR--------DALAKAIYSKLFDHIVNRINQCipFET---SSYFIGVLDIAGFEYFEVN------ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVD-QNPSQQVRLPAGggaqdarGLFWVL 1040
Cdd:cd01382 357 SFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVK----------EVEYVDnQDCIDLIEAKLV-------GILDLL 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1041 DEEVHVEGSSD----SVVLE------RLCAAFEKKGAGTEgssALRTCEQPLqceIFHQLGwdPVRYDLTGWLHRakpNL 1110
Cdd:cd01382 420 DEESKLPKPSDqhftSAVHQkhknhfRLSIPRKSKLKIHR---NLRDDEGFL---IRHFAG--AVCYETAQFIEK---NN 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1111 SALDAP--QVLHQSKREELRSLFQARAKLPPVCRAVAGlegtsqqalqrsrmvRRTFASslaaVRRKapcsqIKLQMDAL 1188
Cdd:cd01382 489 DALHASleSLICESKDKFIRSLFESSTNNNKDSKQKAG---------------KLSFIS----VGNK-----FKTQLNLL 544
|
650
....*....|....*...
gi 970949420 1189 TSMIKRSRLHFIHCLVPN 1206
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 ... |
585-1322 |
3.01e-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: 3.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSA-GKVPKGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPykQLPIYTEAiVEMYRGKkRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGR----VSVEKIRATFT---VLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRkepgVPGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkaAAAFAQLQGAMEML 813
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE---RELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 814 GISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKHHLrqIIQQMTFGpsrwglED 893
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNI-VLKRERNTDQATMPDNTAAQKL-CRLLGLGVTDFSRAL--LTPRIKVG------RD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 894 EETSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIM-VVDSPGFQnprhqgKDRAATFEELCHNYAH 972
Cdd:cd14930 308 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFE------IFQLNSFEQLCINYTN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 973 ERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLpDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGS 1049
Cdd:cd14930 382 EKLQQLFNHTMFVLEQEEYQREGIPwtfLDFGL-DLQPCIDLIERPANPP---------------GLLALLDEECWFPKA 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1050 SDSVVLERLCaafEKKGAGTEGSSAlRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKReelrs 1129
Cdd:cd14930 446 TDKSFVEKVA---QEQGGHPKFQRP-RHLRDQADFSVLHYAG--KVDYKANEWLMKNMDPLND-NVAALLHQSTD----- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1130 lfQARAKLPPVCRAVAGLEGTSQQAL-QRSRMVRRTFASSLAAVRRKApcsqiklqMDALTSMIKRSRLHFIHCLVPNPv 1208
Cdd:cd14930 514 --RLTAEIWKDVEGIVGLEQVSSLGDgPPGGRPRRGMFRTVGQLYKES--------LSRLMATLSNTNPSFVRCIVPNH- 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1209 vESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKLMst 1288
Cdd:cd14930 583 -EKRAGKLEP--------------RLVLD------QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-- 639
|
730 740 750
....*....|....*....|....*....|....
gi 970949420 1289 segIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
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 ... |
586-1322 |
9.13e-39 |
|
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: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKwlpvynAEVVAAYRGKK--RSEAPPHIFSISDNAYQYMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSVD--------GRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14917 80 GESGAGKTVNTKRVIQYFAVIAAIGDrskkdqtpGKGTLEdQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFAQLQ 807
Cdd:cd14917 160 LASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASiddAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPS 887
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGN-----------MKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 RWGLEDEETSSGLKMTGVDCVEG-MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14917 305 RVKVGNEYVTKGQNVQQVIYATGaLAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFEQL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEVHV 1046
Cdd:cd14917 379 CINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLQACIDL---IEKPMGIMSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1047 EGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1126
Cdd:cd14917 443 PKATDMTFKAKLFDNHLGKSNNFQKPRNIKG-KPEAHFSLIHYAGT--VDYNIIGWLQKNKDPLNE-TVVGLYQKSSLKL 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1127 LRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMvrrtfaSSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1206
Cdd:cd14917 519 LSNLFANYAG------ADAPIEKGKGKAKKGSSF------QTVSALHRE--------NLNKLMTNLRSTHPHFVRCIIPN 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1207 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1286
Cdd:cd14917 579 ---ETKS-------------------PGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE-- 634
|
730 740 750
....*....|....*....|....*....|....*.
gi 970949420 1287 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14917 635 --GQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
587-1277 |
1.61e-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: 155.45 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 587 VLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAGKVPKGR-----RDGLPAHIGSMAQRAYWALLNQ----RRDQSIV 657
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKY-LHIYEKEVSQKykcekKSSLPPHIFAVADRAYQSMLGRlargPKNQCIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 658 ALGWSGAGKTTCCEQVLEHLVGMAgsvDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQL 736
Cdd:cd14889 82 ISGESGAGKTESTKLLLRQIMELC---RGNSQLEQqILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHVKGAKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 737 QTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKpEDKQKAAAAFAQLQGAMEMLGIS 816
Cdd:cd14889 158 NEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCK-REVQYWKKKYDEVCNAMDMVGFT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 817 ESEQRAVWRVLAAIYHLGA-------AGACKVGRKQfmrFEWANYAAEALGCEYEEL-----NTATF-------KHHLRQ 877
Cdd:cd14889 237 EQEEVDMFTILAGILSLGNitfemddDEALKVENDS---NGWLKAAAGQFGVSEEDLlktltCTVTFtrgeqiqRHHTKQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 878 IIQqmtfgpsrwgledeetssglkmtgvDCVEGMASGLYQELFAAVVSLINRSFS---SHHLSMASIMVVDSPGFQnprH 954
Cdd:cd14889 314 QAE-------------------------DARDSIAKVAYGRVFGWIVSKINQLLApkdDSSVELREIGILDIFGFE---N 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 955 QGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgtTVAVVDQNPSQQVRLpagggaQDAR 1034
Cdd:cd14889 366 FAVNR---FEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWK----------EITYKDNKPILDLFL------NKPI 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1035 GLFWVLDEEVHVEGSSDSVVLERLCAAFekKGAGTEGSSALRTceqPLqCEIFHQLGwdPVRYDLTGWLHRAKPNLSAld 1114
Cdd:cd14889 427 GILSLLDEQSHFPQATDESFVDKLNIHF--KGNSYYGKSRSKS---PK-FTVNHYAG--KVTYNASGFLEKNRDTIPA-- 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1115 apqvlhqSKREE-LRSLFQARAKLPPVCRAVAGLEGTSQQALQRSrmvrrtfASSLAAVRRKAPCSQIKLQMDALTSMIK 1193
Cdd:cd14889 497 -------SIRTLfINSATPLLSVLFTATRSRTGTLMPRAKLPQAG-------SDNFNSTRKQSVGAQFKHSLGVLMEKMF 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1194 RSRLHFIHCLVPNPVvesrsgqespppPQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQ 1273
Cdd:cd14889 563 AASPHFVRCIKPNHV------------KVPGQ----------LDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAER 620
|
....
gi 970949420 1274 FQVL 1277
Cdd:cd14889 621 YKIL 624
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
587-1016 |
2.67e-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: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfkRLPHLYDAHMMEqyKGAPLGeLSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 662 SGAGKTTCCEQVLEHLVGMAG--SVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGraVTEGRSVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGMGVWSKPEDkqkaaaaFAQLQGAMEML 813
Cdd:cd01384 163 LLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 814 GISESEQRAVWRVLAAIYHLG--------AAGACKVGRKQfMRFEWANyAAEALGCEYEELNTATFKhhlRQIIqqmtfg 885
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGniefskgeEDDSSVPKDEK-SEFHLKA-AAELLMCDEKALEDALCK---RVIV------ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 886 psrwgLEDEETSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQnprhQGKDRaaTFE 964
Cdd:cd01384 305 -----TPDGIITKPLDPDAaTLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE----SFKTN--SFE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970949420 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-------DLPDPSPGTTVAVVDQ 1016
Cdd:cd01384 374 QFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDwsyIEFvdnqdvlDLIEKKPGGIIALLDE 435
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
585-1322 |
2.74e-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: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKvpKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVA 658
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYkwlpvyTAPVVAAYK--GKRRSEAPPHIYAIADNAYNDMLRNRENQSMLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 659 LGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFT-------------VLRAFGSVSMAHSRSATRFSMVMSLDF 725
Cdd:cd14927 79 TGESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTggtledqiieanpAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 726 NATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqMADSSSFGMGVWSKPE---DKQKAAAA 802
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDML----LVSMNPYDYHFCSQGVttvDNMDDGEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 803 FAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQfmRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQM 882
Cdd:cd14927 235 LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNM---KFKQKQ--REE----QAEADGTESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 883 TFGPSRWGleDEETSSGLKMTGVD-CVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVyAVGALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEIFEFN------ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-----DLPdpspgttvAVVDQnpsqqvrlpagggAQDARGL 1036
Cdd:cd14927 378 SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFidfglDLQ--------ACIDL-------------IEKPLGI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1037 FWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTCEQPLQCEIFHQLGWDPvrYDLTGWLHRAKPNLSALDAP 1116
Cdd:cd14927 437 LSILEEECMFPKASDASFKAKLYDNHLGKSPNFQKPRPDKKRKYEAHFEVVHYAGVVP--YNIVGWLDKNKDPLNETVVA 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1117 qVLHQSKREELRSLFQARAKLPPVCRAVAGLEGtsqqalqrsrmvRRTFASSLAAVrrkapcSQI-KLQMDALTSMIKRS 1195
Cdd:cd14927 515 -IFQKSQNKLLATLYENYVGSDSTEDPKSGVKE------------KRKKAASFQTV------SQLhKENLNKLMTNLRAT 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1196 RLHFIHCLVPNpvvESRSgqesppppqpgrdkPGAGGPLaLDIPALRVQlagfHILEALRLHRTGYADHMGLTRFRRQFQ 1275
Cdd:cd14927 576 QPHFVRCIIPN---ETKT--------------PGVMDPF-LVLHQLRCN----GVLEGIRICRKGFPNRILYADFKQRYR 633
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 970949420 1276 VLDAPLLKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14927 634 ILNPSAIPD----DKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
586-1322 |
3.11e-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: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVP--KGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyqPIAGLYEPATMEqySRRHLGeLPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEK-------IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITA 733
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSLELSLKEKtscveqaILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 734 AQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL------NLHQMADSssfgmGVWSkpEDKQKAAAAFAQLQ 807
Cdd:cd14873 162 GRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFylstpeNYHYLNQS-----GCVE--DKTISDQESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLG-----AAGACKVGRKQFMrfewaNYAAEALGCEYEELNTAtfkhhlrqIIQQM 882
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGniefiTAGGAQVSFKTAL-----GRSAELLGLDPTQLTDA--------LTQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 883 TFgpsrwgLEDEETSSGLKM-TGVDCVEGMASGLYQELFAAVVSLINRSFSSHHlSMASIMVVDSPGFQNPRHQgkdraa 961
Cdd:cd14873 302 MF------LRGEEILTPLNVqQAVDSRDSLAMALYARCFEWVIKKINSRIKGKE-DFKSIGILDIFGFENFEVN------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 962 TFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPSPGTTVAVVDQNpsqqvrlpagggaqdaRGLFWVLD 1041
Cdd:cd14873 369 HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGL-VWEDIDWIDNGECLDLIEKK----------------LGLLALIN 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1042 EEVHVEGSSDSVVLERLcaafekKGAGTEGSSALRTCEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQ 1121
Cdd:cd14873 432 EESHFPQATDSTLLEKL------HSQHANNHFYVKPRVAVNNFGVKHYAG--EVQYDVRGILEKNRDTFRD-DLLNLLRE 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1122 SKREELRSLFQARAKlppvcravAGLEGTSQQALQRsrmvrrtfasslaavRRKAPCSQIKLQMDALTSMIKRSRLHFIH 1201
Cdd:cd14873 503 SRFDFIYDLFEHVSS--------RNNQDTLKCGSKH---------------RRPTVSSQFKDSLHSLMATLSSSNPFFVR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1202 CLVPNpvVESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYAdhmgltrFRRQFQvldaPL 1281
Cdd:cd14873 560 CIKPN--MQKMPDQFDQ--------------AVVLN------QLRYSGMLETVRIRKAGYA-------VRRPFQ----DF 606
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 970949420 1282 LKKLMSTSEGI----DERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14873 607 YKRYKVLMRNLalpeDVRGKCTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1322 |
3.11e-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: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14915 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeaasGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFA 804
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEitvPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTF 884
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAAYLTSLNSADLLKALCY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 885 gpSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14915 306 --PRVKVGNEYVTKGQTVQQVyNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEE 1043
Cdd:cd14915 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1044 VHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqsk 1123
Cdd:cd14915 442 CMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN------------ 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1124 rEELRSLFQaRAKLPPVCRAVAGLEGTSQQALQRSRMVRRTFAS--SLAAVRRKapcsqiklQMDALTSMIKRSRLHFIH 1201
Cdd:cd14915 507 -ETVVGLYQ-KSGMKTLAFLFSGGQTAEAEGGGGKKGGKKKGSSfqTVSALFRE--------NLNKLMTNLRSTHPHFVR 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1202 CLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPL 1281
Cdd:cd14915 577 CLIPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASA 634
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 970949420 1282 LKKlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14915 635 IPE----GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
586-1322 |
8.20e-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: 8.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG------PSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKwlpvynPEVVTAYRGKK--RQEAPPHIFSISDNAYQFMLTDRENQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMA------------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14912 80 GESGAGKTVNTKRVIQYFATIAvtgekkkeeitsGKMQGTLEDQIISAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPEDKQKA---AAAFA 804
Cdd:cd14912 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYDYPFVSQGEISVASiddQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 805 QLQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEElnTATFKHHLRQIIQQMTF 884
Cdd:cd14912 235 ATDSAIDILGFTNEEKVSIYKLTGAVMHYG-----NLKFKQKQREE----QAEPDGTEVAD--KAAYLQSLNSADLLKAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 885 GPSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTF 963
Cdd:cd14912 304 CYPRVKVGNEYVTKGQTVEQVtNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 964 EELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEE 1043
Cdd:cd14912 378 EQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEK----------------PMGIFSILEEE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1044 VHVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAldapQVLHQSK 1123
Cdd:cd14912 442 CMFPKATDTSFKNKLYEQHLGKSANFQKPKVVKG-KAEAHFSLIHYAG--VVDYNITGWLDKNKDPLNE----TVVGLYQ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1124 REELRSLfqarAKLPPVCRAVAGlEGTSQQALQRSRMVRRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCL 1203
Cdd:cd14912 515 KSAMKTL----AYLFSGAQTAEG-ASAGGGAKKGGKKKGSSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCI 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1204 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1283
Cdd:cd14912 581 IPN---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIP 638
|
730 740 750
....*....|....*....|....*....|....*....
gi 970949420 1284 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
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 ... |
586-1322 |
1.05e-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: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVAAYRgkkRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 662 SGAGKTTCCEQVLEHLVGMAG-----------SVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAigdrskkenpnANKGTLEDQIIQAN-PALEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAG-----LDLDLRTElNLHQMADSSSFGMGVWSKPEDKqkaaaAFAQ 805
Cdd:cd14916 161 LASADIETYLLEKSRVIFQLKAERNYHIFYQILSNkkpelLDMLLVTN-NPYDYAFVSQGEVSVASIDDSE-----ELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFG 885
Cdd:cd14916 235 TDSAFDVLGFTAEEKAGVYKLTGAIMHYGN-----------MKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLC 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 886 PSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14916 304 HPRVKVGNEYVTKGQSVQQVyYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------SFE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdlpdpspgttvavVDQNPSQQVRLPAgggAQDARGLFWVLDEEV 1044
Cdd:cd14916 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLQACIDL---IEKPMGIMSILEEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1045 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1124
Cdd:cd14916 442 MFPKASDMTFKAKLYDNHLGKSNNFQKPRNVKG-KQEAHFSLVHYAG--TVDYNILGWLEKNKDPLNE-TVVGLYQKSSL 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1125 EELRSLFQARAKlppvcrAVAGLEGTSQQALQRSRMVRrtfasSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCLV 1204
Cdd:cd14916 518 KLMATLFSTYAS------ADTGDSGKGKGGKKKGSSFQ-----TVSALHRE--------NLNKLMTNLKTTHPHFVRCII 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1205 PNPvvesrsgqesppppqpgRDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKK 1284
Cdd:cd14916 579 PNE-----------------RKAPG-----VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPE 636
|
730 740 750
....*....|....*....|....*....|....*...
gi 970949420 1285 lmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14916 637 ----GQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
586-994 |
2.69e-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: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRY-KAQLLHTCTGPDLIVLQP------RGPSVPSA--GKvPKGRRDglPaHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd01380 2 AVLHNLKVRFcQRNAIYTYCGIVLVAINPyedlpiYGEDIIQAysGQ-NMGELD--P-HIFAIAEEAYRQMARDEKNQSI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 657 VALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd01380 78 IVSGESGAGKTVSAKYAMRYFATVGGSSSGETQVEeKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqmADSSSF---GMGvwSKPE-DKQKAAAAFAQLQGAME 811
Cdd:cd01380 158 MRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHL---GSAEDFfytNQG--GSPViDGVDDAAEFEETRKALT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 812 MLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQFMRFEWA---NYAAEALGCEYEElntatFKHHL-RQIIQQMTfgps 887
Cdd:cd01380 233 LLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDehlQIACELLGIDESQ-----LAKWLcKRKIVTRS---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 rwgledEETSSGLKMT-GVDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MASIMVVDSPGFQ----Nprhqgkdra 960
Cdd:cd01380 304 ------EVIVKPLTLQqAIVARDALAKHIYAQLFDWIVDRINKALASPVKEkqHSFIGVLDIYGFEtfevN--------- 368
|
410 420 430
....*....|....*....|....*....|....
gi 970949420 961 aTFEELCHNYAHERLQLLFYQRTFvstlQRYQEE 994
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 ... |
586-1322 |
3.35e-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: 3.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR---RDGLPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPyKWLPVYNAEVVTAYRgkkRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 662 SGAGKTTCCEQVLEHLVGMAGSVDGR---VSVEKIRATFT--------VLRAFGSVSMAHSRSATRFSMVMSLDFNATGR 730
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKkeeATSGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSF-GMGVWSKPEdkQKAAAAFAQLQGA 809
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYDYAFvSQGEITVPS--IDDQEELMATDSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 810 MEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRW 889
Cdd:cd14910 240 IEILGFTSDERVSIYKLTGAVMHYGN-----------MKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 890 GLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCH 968
Cdd:cd14910 309 KVGNEYVTKGQTVQQVyNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 969 NYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEVHVEG 1048
Cdd:cd14910 383 NFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEECMFPK 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1049 SSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCE--IFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREE 1126
Cdd:cd14910 447 ATDTSFKNKL---YEQHLGKSNNFQKPKPAKGKVEAHfsLIHYAG--TVDYNIAGWLDKNKDPLNE-TVVGLYQKSSMKT 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1127 LRSLFQARAKLPpvCRAVAGLEGTSQQAlqrsrmvrRTFASSLAAVRRkapcsqiklQMDALTSMIKRSRLHFIHCLVPN 1206
Cdd:cd14910 521 LALLFSGAAAAE--AEEGGGKKGGKKKG--------SSFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCIIPN 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1207 pvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLKKlm 1286
Cdd:cd14910 582 ---ETKT-------------------PGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPE-- 637
|
730 740 750
....*....|....*....|....*....|....*.
gi 970949420 1287 stSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14910 638 --GQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
585-1322 |
5.39e-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: 150.99 E-value: 5.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVP--KGR-RDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPyKNLPIYSEEIVEmyKGKkRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGS------------VDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslalSHGELEKQLLQAN-PILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKqkAAAAFAQLQG 808
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQ--DKDLFTETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 809 AMEMLGISESEQRAVWRVLAAIYHLGAAgACKVGRKQFMRFEWANYAAEALgCEYEELNTATFKhhlRQIIQ-QMTFGps 887
Cdd:cd15896 238 AFRIMGIPEDEQIGMLKVVASVLQLGNM-SFKKERHTDQASMPDNTAAQKV-CHLMGMNVTDFT---RAILSpRIKVG-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 888 RWGLEDEETSSGLKMTgvdcVEGMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQnprhqgKDRAATFEEL 966
Cdd:cd15896 311 RDYVQKAQTQEQAEFA----VEALAKATYERMFRWLVMRINKALDKTKRQGASfIGILDIAGFE------IFELNSFEQL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPdpspgttvavVDQNPS-QQVRLPAgggaqDARGLFWVLDEEV 1044
Cdd:cd15896 381 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFiDFG----------LDLQPCiDLIEKPA-----SPPGILALLDEEC 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1045 HVEGSSDSVVLERLcaaFEKKGAGTEGSSALRTCEQPLQCeIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKR 1124
Cdd:cd15896 446 WFPKATDKSFVEKV---LQEQGTHPKFFKPKKLKDEADFC-IIHYAG--KVDYKADEWLMKNMDPLND-NVATLLNQSTD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1125 EELRSLFQARAKLPPVCRaVAGLEGTSQQALQRSRMVRRTfasslaavrrkapcSQI-KLQMDALTSMIKRSRLHFIHCL 1203
Cdd:cd15896 519 KFVSELWKDVDRIVGLDK-VSGMSEMPGAFKTRKGMFRTV--------------GQLyKEQLSKLMATLRNTNPNFVRCI 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1204 VPNPvvESRSGQESPpppqpgrdkpgaggPLALDipalrvQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1283
Cdd:cd15896 584 IPNH--EKKAGKLDP--------------HLVLD------QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIP 641
|
730 740 750
....*....|....*....|....*....|....*....
gi 970949420 1284 KLMstsegIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd15896 642 KGF-----MDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
586-1322 |
4.24e-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: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPR------GPSVPSAGKVPKgrRDGLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYkwlpvyNPEVVAAYRGKK--RQEAPPHIFSISDNAYQFMLTDRDNQSILIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMA-----------GSVDGRVSVEKIRATfTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT 728
Cdd:cd14923 80 GESGAGKTVNTKRVIQYFATIAvtgdkkkeqqpGKMQGTLEDQIIQAN-PLLEAFGNAKTVRNDNSSRFGKFIRIHFGAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 729 GRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAgldlDLRTELNLHQMADSSSFGMGVWSKPE---DKQKAAAAFAQ 805
Cdd:cd14923 159 GKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEvtvASIDDSEELLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 806 LQGAMEMLGISESEQRAVWRVLAAIYHLGaagacKVGRKQFMRFEwanyAAEALGCEYEELNTATFKHHLRQIIQQMTFg 885
Cdd:cd14923 235 TDNAIDILGFSSEEKVGIYKLTGAVMHYG-----NMKFKQKQREE----QAEPDGTEVADKAGYLMGLNSAEMLKGLCC- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 886 pSRWGLEDEETSSGLKMTGV-DCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFE 964
Cdd:cd14923 305 -PRVKVGNEYVTKGQNVQQVtNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 965 ELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDPSPGTTVAVVDQnpsqqvrlpagggaqdARGLFWVLDEEV 1044
Cdd:cd14923 378 QLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEK----------------PMGIFSILEEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1045 HVEGSSDSVVLERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSalDAPQVLHQSKR 1124
Cdd:cd14923 442 MFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKG-KAEAHFSLVHYAG--TVDYNIAGWLDKNKDPLN--ETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1125 EELRS-LFQARAKlppvcrAVAGLEGTSQQALQRsrmvRRTFASSLAAVRRKapcsqiklQMDALTSMIKRSRLHFIHCL 1203
Cdd:cd14923 517 LKLLSfLFSNYAG------AEAGDSGGSKKGGKK----KGSSFQTVSAVFRE--------NLNKLMTNLRSTHPHFVRCL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1204 VPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLLK 1283
Cdd:cd14923 579 IPN---ETKT-------------------PGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIP 636
|
730 740 750
....*....|....*....|....*....|....*....
gi 970949420 1284 KlmstSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14923 637 E----GQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
551-1359 |
9.95e-36 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 148.64 E-value: 9.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 551 DKTITEVDEEHVHRANPP-ELDQVEDLASLISVNESSVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGR 628
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPfKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 629 R----DGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV-GMAGSVDGRVSvEKIRATFTVLRAF 703
Cdd:PTZ00014 155 DakdsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFAsSKSGNMDLKIQ-NAIMAANPVLEAF 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 704 GSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMA--- 780
Cdd:PTZ00014 234 GNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEeyk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 781 -------------DSSSFGMGVWSkpedkqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLGAA----------- 836
Cdd:PTZ00014 314 yinpkcldvpgidDVKDFEEVMES------------------FDSMGLSESQIEDIFSILSGVLLLGNVeiegkeegglt 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 837 -GACKVGRKQfmrfEWANYAAEALGCEYEELntatfKHHLrqIIQQMTFGP----SRWGLEDEETSsglkmtgvdcVEGM 911
Cdd:PTZ00014 376 dAAAISDESL----EVFNEACELLFLDYESL-----KKEL--TVKVTYAGNqkieGPWSKDESEML----------KDSL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 912 ASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQ----NprhqgkdraaTFEELCHNYAHERLQLLFYQRTFVST 987
Cdd:PTZ00014 435 SKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 988 LQRYQEEGVPvqfdlpdpspgtTVAVVDQNPSQQVRLPAGGGaqdaRGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKga 1067
Cdd:PTZ00014 505 SKLYKDEGIS------------TEELEYTSNESVIDLLCGKG----KSVLSILEDQCLAPGGTD----EKFVSSCNTN-- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1068 gTEGSSALRTCE--QPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFqaraklppvcrava 1145
Cdd:PTZ00014 563 -LKNNPKYKPAKvdSNKNFVIKHTIG--DIQYCASGFLFKNKDVLRP-ELVEVVKASPNPLVRDLF-------------- 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1146 glEGtsqQALQRSRMVRRTFASslaavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNpvvESRSgqesppppqpgr 1225
Cdd:PTZ00014 625 --EG---VEVEKGKLAKGQLIG-----------SQFLNQLDSLMSLINSTEPHFIRCIKPN---ENKK------------ 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1226 dkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVLDAPLlkklmSTSEGIDERKAVEELLETL 1305
Cdd:PTZ00014 674 -------PLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAV-----SNDSSLDPKEKAEKLLERS 741
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1306 DLEKKAVAVGHSQVFLKAGVISRL-EKQREKLVS-QSIV-LFQAACKGFLSRQEFKK 1359
Cdd:PTZ00014 742 GLPKDSYAIGKTMVFLKKDAAKELtQIQREKLAAwEPLVsVLEALILKIKKKRKVRK 798
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
586-1321 |
1.07e-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: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-----------RGPSVPSAGKVPKGRRDgLPAHIGSMAQRAYWALLNQRR-- 652
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPfrrlplyddetKEAYYEHGERRAAGERK-LPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 653 --DQSIVALGWSGAGKTTCCEQVLEHLVGMA------GSVDGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsatthgQNATERENVrDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 724 DFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPEDKQKAAAAF 803
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 804 AQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfMRFEWANYAAEALGCEYEELNTATFKHHL--RQIIQQ 881
Cdd:cd14901 241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEG-GTFSMSSLANVRAACDLLGLDMDVLEKTLctREIRAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 882 MTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRS--FSSHHLSMASIMVVDSPGF----QNprhq 955
Cdd:cd14901 320 GEYITMPLSVEQALLTR----------DVVAKTLYAQLFDWLVDRINESiaYSESTGASRFIGIVDIFGFeifaTN---- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFdLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarG 1035
Cdd:cd14901 386 ------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF-VEYPNNDACVAMFEARPT---------------G 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1036 LFWVLDEEVHVEGSSDsvvlERLCAAFekkgagtegssalrtceqplqceifhqlgwdpvrYDLTGwlhrAKPNLSAlda 1115
Cdd:cd14901 444 LFSLLDEQCLLPRGND----EKLANKY----------------------------------YDLLA----KHASFSV--- 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1116 pqvlhqSKREELRSLFQARAKLPPVCRAVAGL-----EGTSQQALQRSRMVRRTFASSLAAvrrkapcSQIKLQMDALTS 1190
Cdd:cd14901 479 ------SKLQQGKRQFVIHHYAGAVCYATDGFcdknkDHVHSEALALLRTSSNAFLSSTVV-------AKFKVQLSSLLE 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1191 MIKRSRLHFIHCLVPNPVVESRSgqesppppqpgrdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRF 1270
Cdd:cd14901 546 VLNATEPHFIRCIKPNDVLSPSE----------------------FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAF 603
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1271 RRQFQVLDAPLLKKLMSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFL 1321
Cdd:cd14901 604 VHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVFL 654
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
585-1206 |
1.65e-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: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKV-----------PKGRRDGLPAHIGSMAQRAYWALLNQR 651
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPykQIDNLFSEEVMqmykeqiiqngEYFDIKKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 652 RDQSIVALGWSGAGKT---TCC--------------EQVLEHLVGMAGSVDGRVSVE-KIRATFTVLRAFGSVSMAHSRS 713
Cdd:cd14907 81 KKQAIVISGESGAGKTenaKYAmkfltqlsqqeqnsEEVLTLTSSIRATSKSTKSIEqKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 714 ATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhqMADSSSFGMGVWSK 792
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGL--KNQLSGDRYDYLKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 793 PE----DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG----------AAGACKVGRKQFMRfewanYAAEA 858
Cdd:cd14907 239 SNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGnlqfddstldDNSPCCVKNKETLQ-----IIAKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 859 LGCEYEELNTA-TFKhhLRQIIQQMTFGPsrwgledeetssglkMTGVDCV---EGMASGLYQELFAAVVSLINRSFSSH 934
Cdd:cd14907 314 LGIDEEELKEAlTTK--IRKVGNQVITSP---------------LSKKECInnrDSLSKELYDRLFNWLVERLNDTIMPK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 935 HLS--------MASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQFDLP 1003
Cdd:cd14907 377 DEKdqqlfqnkYLSIGLLDIFGFEVFQNNS------FEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylNQLSYT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1004 DPSPgtTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAafekkgagTEGSSALRTCEQPLQ 1083
Cdd:cd14907 451 DNQD--VIDLLDKPPI---------------GIFNLLDDSCKLATGTDEKLLNKIKK--------QHKNNSKLIFPNKIN 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1084 CEIF---HQLGwdPVRYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQAraklppvcravaglEGTSQQALQRSRM 1160
Cdd:cd14907 506 KDTFtirHTAK--EVEYNIEGFREKNKDEIS-QSIINCIQNSKNRIISSIFSG--------------EDGSQQQNQSKQK 568
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 970949420 1161 VRRtfasslaaVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1206
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 ... |
586-1322 |
9.65e-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: 9.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSV-PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALGW 661
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKflPIYnPKYVKMYQNRRLGkLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 662 SGAGKTTCCEQVLEHLVgmAGSVDGRVS-VEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTM 739
Cdd:cd01385 82 SGSGKTESTNFLLHHLT--ALSQKGYGSgVEQtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 740 LLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL------HQMADSSSFGmgvwskpEDKQKAAAAFAQLQGAMEML 813
Cdd:cd01385 160 LLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAMEMV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 814 GISESEQRAVWRVLAAIYHLgaagackvGRKQFMRfeWANYAAEALGCEYEE-LNTATfkhHLRQIIQQMtfgpsrwgLE 892
Cdd:cd01385 233 GFLPETQRQIFSVLSAVLHL--------GNIEYKK--KAYHRDESVTVGNPEvLDIIS---ELLRVKEET--------LL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 893 DEETSSGLKMTGVDCV------------EGMASGLYQELFAAVV-----SLINRSFSSHHlSMASIMVVDSPGFQNPRHQ 955
Cdd:cd01385 292 EALTTKKTVTVGETLIlpyklpeaiatrDAMAKCLYSALFDWIVlrinhALLNKKDLEEA-KGLSIGVLDIFGFEDFGNN 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 956 gkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP-VQFDLPDPSpgTTVAVVDQNPSqqvrlpagggaqdar 1034
Cdd:cd01385 371 ------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGISwHNIEYTDNT--GCLQLISKKPT--------------- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1035 GLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtegssalRTCEQPLQCE----IFHQLGwdPVRYDLTGWLHRAKPNL 1110
Cdd:cd01385 428 GLLCLLDEESNFPGATNQTLLAKFKQQHKDN----------KYYEKPQVMEpafiIAHYAG--KVKYQIKDFREKNLDLM 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1111 SAlDAPQVLHQSK----RE-------------ELRSLFQARAKLPPVCRA----VAGLEGTSQQALQRSRMVRRTfassl 1169
Cdd:cd01385 496 RP-DIVAVLRSSSsafvREligidpvavfrwaVLRAFFRAMAAFREAGRRraqrTAGHSLTLHDRTTKSLLHLHK----- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1170 aavRRKAPCSQIKLQ--MDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAG 1247
Cdd:cd01385 570 ---KKKPPSVSAQFQtsLSKLMETLGQAEPFFIRCIKSN------------------AEK----KPLRFDDELVLRQLRY 624
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970949420 1248 FHILEALRLHRTGYADHMGLTRFRRQFQVLdapLLKKLMSTSEGIderkavEELLETLDLEKKAVAVGHSQVFLK 1322
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, ... |
585-1261 |
5.78e-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: 138.35 E-value: 5.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSV---PSAGKVPKGRRDG-LPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDiygLEQVQQYSGRALGeLPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAtGRITAAQLQTML 740
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLVT-EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL---------HQMADSSSFGMGvwskpedkqkAAAAFAQLQGAME 811
Cdd:cd01387 159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLqeaekyfylNQGGNCEIAGKS----------DADDFRRLLAAMQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 812 MLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMRfewanYAAEALGCEYEELNTA-TFKhhLRQII 879
Cdd:cd01387 229 VLGFSSEEQDSIFRILASVLHLGnvyfhkrqlrhGQEGVSVGSDAEIQ-----WVAHLLQISPEGLQKAlTFK--VTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 880 QQMTFGPsrwgLEDEEtssglkmtGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdr 959
Cdd:cd01387 302 RERIFTP----LTIDQ--------ALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN---- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 960 aaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGTTVAVVDQNPSQQVRlpagggAQDARGLFWV 1039
Cdd:cd01387 366 --SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQI----------DWTEIAFADNQPVINLI------SKKPVGILHI 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1040 LDEEVHVEGSSDSVVLERlCaafEKKGAGTEGSSALRTCEQPLQceIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVL 1119
Cdd:cd01387 428 LDDECNFPQATDHSFLEK-C---HYHHALNELYSKPRMPLPEFT--IKHYAG--QVWYQVHGFLDKNRDQLRQ-DVLELL 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1120 HQSKREELRSLF-----QARAKLPpvcravAGLEGTSQQALQRSRMVRRTFASSLaavrrkapcsqiklqMDALTSMiKR 1194
Cdd:cd01387 499 VSSRTRVVAHLFsshraQTDKAPP------RLGKGRFVTMKPRTPTVAARFQDSL---------------LQLLEKM-ER 556
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1195 SRLHFIHCLVPNpvvesrsgqesppppqpgRDKpgagGPLALDIPALRVQLAGFHILEALRLHRTGY 1261
Cdd:cd01387 557 CNPWFVRCLKPN------------------HKK----EPMLFDMDVVMAQLRYSGMLETIRIRKEGY 601
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
585-1277 |
1.87e-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: 133.37 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP----SVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSlplfSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLVGMAGSVDgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQTML 740
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQT-EDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVGASVSHYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 741 LEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLhQMADSSSF----GMGVWSKPEDKqkaaAAFAQLQGAMEMLGIS 816
Cdd:cd14896 159 LETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSL-QGPETYYYlnqgGACRLQGKEDA----QDFEGLLKALQGLGLC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 817 ESEQRAVWRVLAAIYHLGaaGACkvgrkqFMRFEWANYAAEALGCEYEELNTATFKH----HLRQII-QQMTFGPSRWgl 891
Cdd:cd14896 234 AEELTAIWAVLAAILQLG--NIC------FSSSERESQEVAAVSSWAEIHTAARLLQvppeRLEGAVtHRVTETPYGR-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 892 edeeTSSGLKMTG-VDCVEGMASGLYQELFAAVVSLINRSFS--SHHLSMASIMVVDSPGFQNPRHQGkdraatFEELCH 968
Cdd:cd14896 304 ----VSRPLPVEGaIDARDALAKTLYSRLFTWLLKRINAWLAppGEAESDATIGVVDAYGFEALRVNG------LEQLCI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 969 NYAHERLQLLFYQRTFVSTLQRYQEE---GVPVqfdlPDPSPGTTVAVVDQNPsqqvrlpagggaqdaRGLFWVLDEEVH 1045
Cdd:cd14896 374 NLASERLQLFSSQTLLAQEEEECQREllpWVPI----PQPPRESCLDLLVDQP---------------HSLLSILDDQTW 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1046 VEGSSDSVVLErlcaafekKGAGTEGSSALRTCEQpLQCEIF---HQLGwdPVRYDLTGWLHRakpNLSALDaPQVLH-- 1120
Cdd:cd14896 435 LSQATDHTFLQ--------KCHYHHGDHPSYAKPQ-LPLPVFtvrHYAG--TVTYQVHKFLNR---NRDQLD-PAVVEml 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1121 -QSKREELRSLFQaraklppvcravaglEGTSQQALQRSRmvrrtfaSSLAavrrkapcSQIKLQMDALTSMIKRSRLHF 1199
Cdd:cd14896 500 aQSQLQLVGSLFQ---------------EAEPQYGLGQGK-------PTLA--------SRFQQSLGDLTARLGRSHVYF 549
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 1200 IHCLVPNPVvesrsgqesppppqpgrDKPGaggplALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1277
Cdd:cd14896 550 IHCLNPNPG-----------------KLPG-----LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGAL 605
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
586-1210 |
1.50e-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: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP-RGPSVPSAGKVPKGRRD-----GLPAHIGSMAQRAYWALLNQRRDQSIVAL 659
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDinqnkSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 660 GWSGAGKTTCCEQVLEHLVGMAGSV--------DGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNAT-G 729
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnnNNNNSIEKdILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSdG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 730 RITAAQLQTMLLEKSRVARQPEGES-NFLVFSQMLAGLDLDLRTELNLHQMADS-----------SSF---GMGVWSKPE 794
Cdd:cd14906 162 KIDGASIETYLLEKSRISHRPDNINlSYHIFYYLVYGASKDERSKWGLNNDPSKyryldarddviSSFksqSSNKNSNHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 795 DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEwanyaAEALGCEYEELnTATFKHH 874
Cdd:cd14906 242 NKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGN-----------IEFE-----EDSDFSKYAYQ-KDKVTAS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 875 LRQIIQQMTFGPSRWglEDEETSSGLKMTGVDCV--------------EGMASGLYQELFAAVVSLINRSF----SSHHL 936
Cdd:cd14906 305 LESVSKLLGYIESVF--KQALLNRNLKAGGRGSVycrpmevaqseqtrDALSKSLYVRLFKYIVEKINRKFnqntQSNDL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 937 SMAS-------IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpvqfdlpdpsPGT 1009
Cdd:cd14906 383 AGGSnkknnlfIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGI----------PWS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1010 TVAVVDQNPSQQVRlpagggAQDARGLFWVLDEEVHVEGSSDSVVLERlcaaFEKKGAGTEgSSALRTCEQpLQCEIFHQ 1089
Cdd:cd14906 447 NSNFIDNKECIELI------EKKSDGILSLLDDECIMPKGSEQSLLEK----YNKQYHNTN-QYYQRTLAK-GTLGIKHF 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1090 LGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLFQARAKLPPvcravaglegTSQQalqrsrmvRRTFASSL 1169
Cdd:cd14906 515 AG--DVTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT----------NTTK--------KQTQSNTV 573
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 970949420 1170 AavrrkapcSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVE 1210
Cdd:cd14906 574 S--------GQFLEQLNQLIQTINSTSVHYIRCIKPNQTMD 606
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
633-998 |
2.14e-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: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLV--GMAGSVDGRVSVEKIRATFT------------ 698
Cdd:cd14891 55 PYAIAEMAYQQMCLGSGRMQNQSIVISGESGAGKTETSKIILRFLTtrAVGGKKASGQDIEQSSKKRKlsvtslderlmd 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 699 ---VLRAFGSVSMAHSRSATRFSMVMSLDFNATG-RITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL 774
Cdd:cd14891 135 tnpILESFGNAKTLRNHNSSRFGKFMKLQFTKDKfKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKEL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 775 NLhqmadsssfgmgvwSKPEDKQKAAAAF-------------AQLQGAMEMLGISESEQRAVWRVLAAIYHLG------- 834
Cdd:cd14891 215 LL--------------LSPEDFIYLNQSGcvsddniddaanfDNVVSALDTVGIDEDLQLQIWRILAGLLHLGniefdee 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 835 --AAGACKVGRKQFMrfEWANYAAEALGCEYEELntatfkhhLRQIIQQ--MTFGPSRWGLEDEETSSGLKmtgvdcvEG 910
Cdd:cd14891 281 dtSEGEAEIASESDK--EALATAAELLGVDEEAL--------EKVITQReiVTRGETFTIKRNAREAVYSR-------DA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 911 MASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNprhqgKDRAATFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14891 344 IAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFES-----FETKNDFEQLLINYANEALQATFNQQVFIAEQEL 418
|
....*...
gi 970949420 991 YQEEGVPV 998
Cdd:cd14891 419 YKSEGIDV 426
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
635-1212 |
2.75e-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: 2.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 635 HIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSV---EKIRATFTVLRAFGSVSMAHS 711
Cdd:cd14887 63 HPFGLAEFAYCRLVRDRRSQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQgleARLLQSGPVLEAFGNAHTVLN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 712 RSATRFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLdlrtelnlhqmadSSSFGMGVWS 791
Cdd:cd14887 143 ANSSRFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVA-------------AATQKSSAGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 792 K-PEdkqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGACKVGRKQfmRFEWANYAAEALGC--------- 861
Cdd:cd14887 210 GdPE-----STDLRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPE--TSKKRKLTSVSVGCeetaadrsh 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 862 --EYEELN-----TATFKHHLRQIIQQMTFGPSRWGLED----------EETSSGLKMTGVDCVEGMAS-GLYQELFAAV 923
Cdd:cd14887 283 ssEVKCLSsglkvTEASRKHLKTVARLLGLPPGVEGEEMlrlalvsrsvRETRSFFDLDGAAAARDAACkNLYSRAFDAV 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 924 VSLINRSFSSHHLSMAS--------------IMVVDSPGFQNPRHQGKDRaatFEELCHNYAHERLQLLFYQRTFVSTLQ 989
Cdd:cd14887 363 VARINAGLQRSAKPSESdsdedtpsttgtqtIGILDLFGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHM 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 990 RYQEEGV---------PVQFDLPDPSPGTTVAVVDQNPSQQVRlpAGGGAQDARGLFWVLDEEVHVEGSSDSVVLERLCA 1060
Cdd:cd14887 440 LYTQEGVfqnqdcsafPFSFPLASTLTSSPSSTSPFSPTPSFR--SSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDNS 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1061 --AFEKKGAGTEGSSALRTCEQPLQCE-----IFHQLGwdPVRYDLTGWLHRAKPNLSaldapqvlhqskrEELRSLFQA 1133
Cdd:cd14887 518 dlFYEKLNKNIINSAKYKNITPALSREnleftVSHFAC--DVTYDARDFCRANREATS-------------DELERLFLA 582
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 1134 raklppvCRAVaglegTSQQALQRSRMVRrtfassLAAVRRKAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESR 1212
Cdd:cd14887 583 -------CSTY-----TRLVGSKKNSGVR------AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAG 643
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
585-1290 |
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 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQP------RGPSVPSAGKVPKGRR-DGLPAHIGSMAQRAYWALLNQRRDQSIV 657
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPykelpiYSTMVSQLYLSSSGQLcSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 658 ALGWSGAGKTTCCEQVLEHLVGMAGSvdGRVSVE-KIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDF-NATGRITAAQ 735
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS--SRTTFDsRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVwskPEDKQKAAAAFAQLQ-----GAM 810
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTM---REDVSTAERSLNREKlavlkQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 811 EMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFEWANYAAEALGCEYEELNtatfkhhlrQIIQQMTFGPsrwg 890
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGD-----------IRFTALTEADSAFVSDLQLLE---------QVAGMLQVST---- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 891 ledEETSSGLkMTGVDCVEG------------------MASGLYQELFAAVVSLINRSFSSHH----LSMASIMVVDSPG 948
Cdd:cd14878 292 ---DELASAL-TTDIQYFKGdmiirrhtiqiaefyrdlLAKSLYSRLFSFLVNTVNCCLQSQDeqksMQTLDIGILDIFG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 949 FQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLpdpSPGTTVAVVD---QNPSqqvrlp 1025
Cdd:cd14878 368 FEEFQKN------EFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTMETAY---SPGNQTGVLDfffQKPS------ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1026 agggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGT------EGSSALRTCEQPLQCEIFHQLGwdPVRYDL 1099
Cdd:cd14878 433 ---------GFLSLLDEESQMIWSVEPNLPKKLQSLLESSNTNAvyspmkDGNGNVALKDQGTAFTVMHYAG--RVMYEI 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1100 TGWLHRAKPNLSaldapQVLhqskreelrsLFQARaklppvcravaglegTSQQALqrsrmVRRTFASSLAAVrrkapCS 1179
Cdd:cd14878 502 VGAIEKNKDSLS-----QNL----------LFVMK---------------TSENVV-----INHLFQSKLVTI-----AS 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1180 QIKLQMDALTSMIKRSRLHFIHCLVPNpvvesrsgqesppppqpgrdkpGAGGPLALDIPALRVQLAGFHILEALRLHRT 1259
Cdd:cd14878 542 QLRKSLADIIGKLQKCTPHFIHCIKPN----------------------NSKLPDTFDNFYVSAQLQYIGVLEMVKIFRY 599
|
730 740 750
....*....|....*....|....*....|...
gi 970949420 1260 GYADHMGLTRFRRQFQVLDAPLL--KKLMSTSE 1290
Cdd:cd14878 600 GYPVRLSFSDFLSRYKPLADTLLgeKKKQSAEE 632
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
631-1274 |
3.28e-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: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 631 GLPAHIGSMAQRAYWALLNQ-RRDQSIVALGWSGAGKTTCCEQVLEHLVGMA----GSVDGRVSVEKIRATFT----VLR 701
Cdd:cd14875 53 LLPPHIWQVAHKAFNAIFVQgLGNQSVVISGESGSGKTENAKMLIAYLGQLSymhsSNTSQRSIADKIDENLKwsnpVME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 702 AFGSVSMAHSRSATRFSMVMSLDFN-ATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTEL-NLHQM 779
Cdd:cd14875 133 SFGNARTVRNDNSSRFGKYIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 780 AD------SSSF-GMGVWSKPEDKqkaAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAagackvgrkqfMRFE-- 850
Cdd:cd14875 213 QDykclngGNTFvRRGVDGKTLDD---AHEFQNVRHALSMIGVELETQNSIFRVLASILHLME-----------VEFEsd 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 851 ------WANYAAEALGCEYEELNTATfkhhLRQIIqqmtfgpsrwgLEDEETSSGLKMTGVDCVEGM----ASGLYQELF 920
Cdd:cd14875 279 qndkaqIADETPFLTACRLLQLDPAK----LRECF-----------LVKSKTSLVTILANKTEAEGFrnafCKAIYVGLF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 921 AAVVSLINRSFSSHH--LSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPV 998
Cdd:cd14875 344 DRLVEFVNASITPQGdcSGCKYIGLLDIFGFENFTRNS------FEQLCINYANESLQNHYNKYTFINDEEECRREGIQI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 999 -QFDLPDPSpgTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRT 1077
Cdd:cd14875 418 pKIEFPDNS--ECVNMFDQKRT---------------GIFSMLDEECNFKGGTT----ERFTTNLWDQWANKSPYFVLPK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1078 CEQPLQCEIFHQLGWdpVRYDLTGWLHRakpNLSAL--DAPQVLHQSKREELRSLFQARAKLPpvcravaglegtsqqal 1155
Cdd:cd14875 477 STIPNQFGVNHYAAF--VNYNTDEWLEK---NTDALkeDMYECVSNSTDEFIRTLLSTEKGLA----------------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1156 QRSRMVRRTFASSLAAVRrkapcsqiklqmdaltSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLA 1235
Cdd:cd14875 535 RRKQTVAIRFQRQLTDLR----------------TELESTETQFIRCIKPNMEAS----------------------PSF 576
|
650 660 670
....*....|....*....|....*....|....*....
gi 970949420 1236 LDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQF 1274
Cdd:cd14875 577 LDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYF 615
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
586-996 |
1.09e-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: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGK--VPKGRRDGLPaHIGSMAQRAYWALLNQRrDQSIVALGWSG 663
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYETIYGAGAMkaYLKNYSHVEP-HVYDVAEASVQDLLVHG-NQTIVISGESG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 664 AGKTTCCEQVLEHLV-GMAGSVdgrvSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNatGRITAAQLQTMLL 741
Cdd:cd14898 80 SGKTENAKLVIKYLVeRTASTT----SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETYLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 742 EKSRVARQPEGESNFLVFSQMLAGLDLDLRTELnlhqmADSSSFGmgvwSKPEDKQKAAAAFAQLQGAMEMLGISESeqR 821
Cdd:cd14898 154 EKSRVTHHEKGERNFHIFYQFCASKRLNIKNDF-----IDTSSTA----GNKESIVQLSEKYKMTCSAMKSLGIANF--K 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 822 AVWRVLAAIYHLGAAGACKVGRKQFMRFEWANYAAEALGCEYEELNTATFKhhlrqiiqqmtfGPSRWGLEDEETSSGLK 901
Cdd:cd14898 223 SIEDCLLGILYLGSIQFVNDGILKLQRNESFTEFCKLHNIQEEDFEESLVK------------FSIQVKGETIEVFNTLK 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 902 mTGVDCVEGMASGLYQELFAAVVSLINRSFSSHhlSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQ 981
Cdd:cd14898 291 -QARTIRNSMARLLYSNVFNYITASINNCLEGS--GERSISVLDIFGFEIFESNG------LDQLCINWTNEKIQNDFIK 361
|
410
....*....|....*
gi 970949420 982 RTFVSTLQRYQEEGV 996
Cdd:cd14898 362 KMFRAKQGMYKEEGI 376
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
586-1206 |
1.23e-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: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPK--------------GRRDGLPAHIGSMAQRAYWALLN 649
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfqKLPGLYSSDTMAKyllsfearssstrnKGSDPMPPHIYQVAGEAYKAMML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 650 QRR----DQSIVALGWSGAGKTTCCEQVLEHLvGMAGSVDGRVSV----------EKIRATFTVLRAFGSVSMAHSRSAT 715
Cdd:cd14900 82 GLNgvmsDQSILVSGESGSGKTESTKFLMEYL-AQAGDNNLAASVsmgkstsgiaAKVLQTNILLESFGNARTLRNDNSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 716 RFSMVMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSssfgmgvwskped 795
Cdd:cd14900 161 RFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDMYRRVMDA------------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 796 kqkaaaafaqlqgaMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQFM--RFEWA-NYAAEALGCEYEE 865
Cdd:cd14900 228 --------------MDIIGFTPHERAGIFDLLAALLHIGnltfehdENSDRLGQLKSDLapSSIWSrDAAATLLSVDATK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 866 LNTATfkhHLRQIIQQMTFGPSRWGLEDEETSSglkmtgvdcvEGMASGLYQELFAAVVSLINRSF-----SSHHLSMAS 940
Cdd:cd14900 294 LEKAL---SVRRIRAGTDFVSMKLSAAQANNAR----------DALAKALYGRLFDWLVGKMNAFLkmddsSKSHGGLHF 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 941 IMVVDSPGFQN-PRHqgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP---VQF-DLPDpspgtTVAVVD 1015
Cdd:cd14900 361 IGILDIFGFEVfPKN-------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFcDNQD-----CVNLIS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1016 QNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKgagtEGSSALRTCEQPLQCEIFHQLGwdPV 1095
Cdd:cd14900 429 QRPT---------------GILSLIDEECVMPKGSDTTLASKLYRACGSH----PRFSASRIQRARGLFTIVHYAG--HV 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1096 RYDLTGWLHRAKpnlsaldapQVLHQskreELRSLFQAraklppvcravaglegtsqqalqrsrmvrrtfasslaavrrk 1175
Cdd:cd14900 488 EYSTDGFLEKNK---------DVLHQ----EAVDLFVY------------------------------------------ 512
|
650 660 670
....*....|....*....|....*....|.
gi 970949420 1176 apCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1206
Cdd:cd14900 513 --GLQFKEQLTTLLETLQQTNPHYVRCLKPN 541
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
585-1206 |
2.45e-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: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPsVPSAgKVPKGRRD--------GLPAHIGSMAQRAYWALLNQRR--DQ 654
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKP-VPQL-YSPELMREyhaapqpqKLKPHIFTVGEQTYRNVKSLIEpvNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 655 SIVALGWSGAGKTTCCEQVLEHLVGMAGSV---DGRVSVEKIRATF----TVLRAFGSVSMAHSRSATRFSMVMSLDFNA 727
Cdd:cd14880 79 SIVVSGESGAGKTWTSRCLMKFYAVVAASPtswESHKIAERIEQRIlnsnPVMEAFGNACTLRNNNSSRFGKFIQLQLNR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 728 TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSsfgmgvWSKPEDKQKAAAAFAQLQ 807
Cdd:cd14880 159 AQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFS------WLPNPERNLEEDCFEVTR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLG---------AAGACKV--GRKQFMRFewanyAAEALGCEYEELNTATFKHHLR 876
Cdd:cd14880 233 EAMLHLGIDTPTQNNIFKVLAGLLHLGniqfadsedEAQPCQPmdDTKESVRT-----SALLLKLPEDHLLETLQIRTIR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 877 QIIQQMTF-GPSRWGLEDeetssglkmTGVDCvegMASGLYQELFAAVVSLINRSFSSHHLSMAS-IMVVDSPGFQNPRH 954
Cdd:cd14880 308 AGKQQQVFkKPCSRAECD---------TRRDC---LAKLIYARLFDWLVSVINSSICADTDSWTTfIGLLDVYGFESFPE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 955 QgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDPSpgTTVAVVDQNPSQqvrlpagggaqda 1033
Cdd:cd14880 376 N------SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSFiNYQDNQ--TCLDLIEGSPIS------------- 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1034 rgLFWVLDEEVHVEGSSDSVVLErlcAAFEKKGAGTEGSSALRTCEQPlQCEIFHQLGwdPVRYDLTGWLHRAK----PN 1109
Cdd:cd14880 435 --ICSLINEECRLNRPSSAAQLQ---TRIESALAGNPCLGHNKLSREP-SFIVVHYAG--PVRYHTAGLVEKNKdpvpPE 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1110 LSaldapQVLHQSKREELRSLFQARAKlppvcravaglEGTSQQALQRSRmvrrtfASSLAAVrrkapcSQIKLQMDALT 1189
Cdd:cd14880 507 LT-----RLLQQSQDPLLQKLFPANPE-----------EKTQEEPSGQSR------APVLTVV------SKFKASLEQLL 558
|
650
....*....|....*..
gi 970949420 1190 SMIKRSRLHFIHCLVPN 1206
Cdd:cd14880 559 QVLHSTTPHYIRCIKPN 575
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
587-1322 |
6.84e-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: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP-------------RGPSVPSAGKvpkgrrdgLPAHIGSMAQRAYWALLNQRRD 653
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirKYRDAPDLTK--------LPPHVFYTARRALENLHGVNKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 654 QSIVALGWSGAGKTTCCEQVLEHL-VGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRIT 732
Cdd:cd14876 75 QTIIVSGESGAGKTEATKQIMRYFaSAKSGNMDLRIQ-TAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 733 AAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMAD-----SSSFGMGVWSKPEDkqkaaaaFAQLQ 807
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEykflnPKCLDVPGIDDVAD-------FEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 808 GAMEMLGISESEQRAVWRVLAAIYHLGAAgacKVGRKQFMRFEwanYAAEALGCEYEELNTATFKHHL------RQIIQQ 881
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNV---KITGKTEQGVD---DAAAISNESLEVFKEACSLLFLdpealkRELTVK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 882 MTF-GP----SRWGLEDEETssgLKMTgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQg 956
Cdd:cd14876 301 VTKaGGqeieGRWTKDDAEM---LKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDIFGFEVFKNN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 957 kdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVqfdlPDPSPGTTVAVVDqnpsqqvrLPAGGGaqdaRGL 1036
Cdd:cd14876 370 -----SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIPT----AELEYTSNAEVID--------VLCGKG----KSV 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1037 FWVLDEEVHVEGSSDsvvlERLCAAFEKKGAGTEGSSALRTcEQPLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSAlDAP 1116
Cdd:cd14876 429 LSILEDQCLAPGGSD----EKFVSACVSKLKSNGKFKPAKV-DSNINFIVVHTIG--DIQYNAEGFLFKNKDVLRA-ELV 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1117 QVLHQSKREELRSLFqaraklppvcravaglEGtsqQALQRSRMVRrtfaSSLAAvrrkapcSQIKLQMDALTSMIKRSR 1196
Cdd:cd14876 501 EVVQASTNPVVKALF----------------EG---VVVEKGKIAK----GSLIG-------SQFLKQLESLMGLINSTE 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1197 LHFIHCLVPNpvvESRSgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQV 1276
Cdd:cd14876 551 PHFIRCIKPN---ETKK-------------------PLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKF 608
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 970949420 1277 LDAPLlkklmSTSEGIDERKAVEELLETLDLEKKAVAVGHSQVFLK 1322
Cdd:cd14876 609 LDLGI-----ANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVFLK 649
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
586-1284 |
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 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPSAGK--VPKGRRDG------------LPAHIGSMAQRAYWALLN-Q 650
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPF-QRLPLYGKeiLESYRQEGllrsqgiespqaLGPHVFAIADRSYRQMMSeI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 651 RRDQSIVALGWSGAGKTTCCEQVLEHL--VGMAGSV-------DGRVSV-EKIRATFTVLRAFGSVSMAHSRSATRFSMV 720
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLttLGNGEEGapnegeeLGKLSImDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 721 MSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFG------MGVWSKPE 794
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQLpnefhyTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 795 -DKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-----------AAGACKVGRKQFMrfewaNYAAEALGCE 862
Cdd:cd14908 241 lREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGqlefeskeedgAAEIAEEGNEKCL-----ARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 863 YEELNTAtfkhhLRQIIQQMTFGPSRWGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINRSFSSHHLS--MAS 940
Cdd:cd14908 316 VDKLLRA-----LTSKIIVVRGKEITTKLTPHKAY--------DARDALAKTIYGALFLWVVATVNSSINWENDKdiRSS 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 941 IMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQF-DLPDpspgttvavvDQNPS 1019
Cdd:cd14908 383 VGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFiEFPD----------NQDCL 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1020 QQVRLPagggaqdARGLFWVLDEEvhvegssdsvvlerlCAAFEKkgaGTEGSSALRTCEQPLQceifhqlgwdpvrydl 1099
Cdd:cd14908 447 DTIQAK-------KKGILTMLDDE---------------CRLGIR---GSDANYASRLYETYLP---------------- 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1100 tgwlhrakpnlsalDAPQVLHQSKREELRSLfqARAKLppvCRAVAGLEGTSQQALQRSRMVRRTFASSLAAVRRKAPCS 1179
Cdd:cd14908 486 --------------EKNQTHSENTRFEATSI--QKTKL---IFAVRHFAGQVQYTVETTFCEKNKDEIPLTADSLFESGQ 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1180 QIKLQMDALTSMIKRSRLHFIHCLVPNPVVEsrsgqesppppqpgrdkpgaggPLALDIPALRVQLAGFHILEALRLHRT 1259
Cdd:cd14908 547 QFKAQLHSLIEMIEDTDPHYIRCIKPNDAAK----------------------PDLVTRKRVTEQLRYGGVLEAVRVARS 604
|
730 740
....*....|....*....|....*
gi 970949420 1260 GYADHMGLTRFRRQFQVLdAPLLKK 1284
Cdd:cd14908 605 GYPVRLPHKDFFKRYRML-LPLIPE 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
585-1275 |
1.77e-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: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP---SVPSAGKVPKGRRDGL-----------PAHIGSMAQRAYWALLNQ 650
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPlpiYTPDHMQAYNKSREQTplyekdtvndaPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 651 RRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVE-----------KIRATFTVLRAFGSVSMAHSRSATRFSM 719
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEgasgvlhpigqQILHAFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 720 VMSLDFNATGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLD--LRTELNLHQMADssSFGMGVWSKPE--D 795
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVN--EFVMLKQADPLatN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 796 KQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLG-------AAGACKVGRKQfmrfewANYAAEALGCEYEELNT 868
Cdd:cd14893 239 FALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGnvdfvpdPEGGKSVGGAN------STTVSDAQSCALKDPAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 869 ATFKHHLRQ---IIQQMTFGPSRWGLED-EETSSGLKMTGV----DCVEGMASGLYQELFAAVVSLIN-------RSFSS 933
Cdd:cd14893 313 ILLAAKLLEvepVVLDNYFRTRQFFSKDgNKTVSSLKVVTVhqarKARDTFVRSLYESLFNFLVETLNgilggifDRYEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 934 HHLSMAS--IMVVDSPGFQN--PRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQFDLPDpspGT 1009
Cdd:cd14893 393 SNIVINSqgVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDESQQVENRLTV---NS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1010 TVAVV-DQNPSQQVRlpagggAQDARGLFWVLDEEVHVEGSSDSVVLERLCAAFEK--------KGAGTEGSSALRTCEQ 1080
Cdd:cd14893 464 NVDITsEQEKCLQLF------EDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnMGADTTNEYLAPSKDW 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1081 PLQCEIFHQLGwdPVRYDLTGWLHRAKPNLSALDApQVLHQSKREELRSLFQARAklppvcrAVAGLEGTSQQALQRSRm 1160
Cdd:cd14893 538 RLLFIVQHHCG--KVTYNGKGLSSKNMLSISSTCA-AIMQSSKNAVLHAVGAAQM-------AAASSEKAAKQTEERGS- 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1161 VRRTFASSLAAVRR-----KAPCSQIKLQMDALTSMIKRSRLHFIHCLVPNPVVESRsgqesppppqpgrdkpgaggplA 1235
Cdd:cd14893 607 TSSKFRKSASSAREsknitDSAATDVYNQADALLHALNHTGKNFLVCIKPNETLEEG----------------------V 664
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 970949420 1236 LDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQ 1275
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 ... |
587-996 |
3.97e-23 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 107.28 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 587 VLNTLLQRYKAQLLHTCTGPDLIVLQP--RGPSVPSAGKVPKGRR--------DGLPAHIGSMAQRAYWALLNQRRDQSI 656
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfkQIRNLYGTEVIGRYRQadtsrgfpSDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 657 VALGWSGAGKTTCCEQVLEHLVgmAGSVDGRVSVEK-IRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQ 735
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFA--YGHSTSSTDVQSlILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 736 LQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMaDSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLgI 815
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSL-ESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-F 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 816 SESEQRAVWRVLAAIYHLGAAGACKVGRkqfMRFEwaNYAAEALGCEYEEL------NTATFKHHLRQ---IIQQMTFgp 886
Cdd:cd14886 239 SKNEIDSFYKCISGILLAGNIEFSEEGD---MGVI--NAAKISNDEDFGKMcellgiESSKAAQAIITkvvVINNETI-- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 887 srwgledeeTSSGLKMTGVDCVEGMASGLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEEL 966
Cdd:cd14886 312 ---------ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------TYEQL 376
|
410 420 430
....*....|....*....|....*....|
gi 970949420 967 CHNYAHERLQLLFYQRTFVSTLQRYQEEGV 996
Cdd:cd14886 377 LINYANERLQQYFINQVFKSEIQEYEIEGI 406
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1402-2087 |
5.71e-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: 107.83 E-value: 5.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1402 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1481
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HEQVQKKLGDVNKQLEEAQQKIqlndlernptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1561
Cdd:TIGR02168 332 LDELAEELAELEEKLEELKEEL-------------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1562 QSAYDGAKKMAHQLKRKchhltcdledtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVfEKGLREKVTQENT----- 1636
Cdd:TIGR02168 399 NNEIERLEARLERLEDR--------------RERLQQEIEELLKKLEEAELKELQAELEEL-EEELEELQEELERleeal 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1637 -SVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGspsLGENCVAGLKERLWKlessaleqqkiqSQQENTIKQL 1715
Cdd:TIGR02168 464 eELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG---FSEGVKALLKNQSGL------------SGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1716 EQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDqi 1790
Cdd:TIGR02168 529 ISVDEGYEAAIEaalggRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKD-- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1791 gHRDFDVEKRL------------------RRDLRRTHALLSDVQL---LLG-----TMEDGKTSVS----KEELEKVHSQ 1840
Cdd:TIGR02168 607 -LVKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIVTLdgdLVRpggviTGGSAKTNSSilerRREIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1841 LEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1920
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1921 DIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRD 1999
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2000 SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA 2079
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
....*...
gi 970949420 2080 DLQAALEE 2087
Cdd:TIGR02168 926 QLELRLEG 933
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
585-1277 |
1.66e-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: 101.87 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKgrrdglPAHIGSMAQRAYWALL-NQRRDQSIVALGWSG 663
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIK------KCHISGVAENALDRIKsMSSNAESIVFGGESG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 664 AGKTTCCEQVLEHLVGMAGSvdgRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNaTGRITAAQLQ-TMLLE 742
Cdd:cd14874 75 SGKSYNAFQVFKYLTSQPKS---KVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLTGLNLKyTVPLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 743 KSRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMadSSSFGMGVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRA 822
Cdd:cd14874 151 VPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDDHCIS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 823 VWRVLAAIYHLGaagackvgrKQFMRFEWANYAAEALGcEYEELNTATFKHHLRQI-IQQMtfgpSRWGLEDEETSSGLK 901
Cdd:cd14874 229 IYKIISTILHIG---------NIYFRTKRNPNVEQDVV-EIGNMSEVKWVAFLLEVdFDQL----VNFLLPKSEDGTTID 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 902 M-TGVDCVEGMASGLYQELFAAVVSLINRSFSShHLSMASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFY 980
Cdd:cd14874 295 LnAALDNRDSFAMLIYEELFKWVLNRIGLHLKC-PLHTGVISILDHYGFEKYNNNG------VEEFLINSVNERIENLFV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 981 QRTFVSTLQRYQEEGVPVQFDLPDP-SPGTTVAVVDQNPsqqvrlpagggaqdaRGLFWVLDEEVHVEGSSDSVVLERLC 1059
Cdd:cd14874 368 KHSFHDQLVDYAKDGISVDYKVPNSiENGKTVELLFKKP---------------YGLLPLLTDECKFPKGSHESYLEHCN 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1060 AAFEKKGAGTEGSSALRtceqpLQCEIFHQLG--WdpvrYDLTGWLHRAKPNLSaLDAPQVLHQSKREELRSLFQARAKl 1137
Cdd:cd14874 433 LNHTDRSSYGKARNKER-----LEFGVRHCIGttW----YNVTDFFSRNKRIIS-LSAVQLLRSSKNPIIGLLFESYSS- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1138 ppvcravagleGTSQQALQRSRMVRRTfASSLAavrrkapcsqiklqmdaltSMIKRSRLHFIHCLvpnpvvesRSGQES 1217
Cdd:cd14874 502 -----------NTSDMIVSQAQFILRG-AQEIA-------------------DKINGSHAHFVRCI--------KSNNER 542
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1218 ppppQPGRdkpgaggplaLDIPALRVQLAGFHILEALRLHRTGYADHMGLTRFRRQFQVL 1277
Cdd:cd14874 543 ----QPKK----------FDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCL 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1327-2096 |
1.95e-20 |
|
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: 99.76 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1327 SRLEKQREKL--VSQSIVLFQAACKgfLSRQEFKKLKIRRLAAQCIQknvAVFLAVKDWPWWQLLGSLQPLLsatigtEQ 1404
Cdd:TIGR02169 170 RKKEKALEELeeVEENIERLDLIID--EKRQQLERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALE------RQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1405 LRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADerfkgdvacqvLESERAERLQafREVQELKSKHEQ 1484
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD-----------LGEEEQLRVK--EKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1485 VQKKLGDVNKQLEEAQQKIQLNDLERnptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSA 1564
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEI------DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1565 YDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALgesvfeKGLREKVTQ---ENTSVRWE 1641
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELADLNAAI------AGIEAKINEleeEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1642 LgqlqqqlKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLES--SALEQQKIQSQQE---------- 1709
Cdd:TIGR02169 450 I-------KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQRelAEAEAQARASEERvrggraveev 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1710 ---------NTIKQLEQLRQRFELEIE-----RMKQMHQKDREDQEEELEDVRQSCQKRLHQL---EMQLEQEYEEkqmV 1772
Cdd:TIGR02169 516 lkasiqgvhGTVAQLGSVGERYATAIEvaagnRLNNVVVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLS---I 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 LHEkqdlEGLIGTLCDQIghrDFDVEKR-----------LRRDLRRTHALLSDVQLLL---------GTM------EDGK 1826
Cdd:TIGR02169 593 LSE----DGVIGFAVDLV---EFDPKYEpafkyvfgdtlVVEDIEAARRLMGKYRMVTlegelfeksGAMtggsraPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1827 TSVSKEELEKVHS------QLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLvdeQLYRLQFEKADLLKRIDED 1900
Cdd:TIGR02169 666 ILFSRSEPAELQRlrerleGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK---EIEQLEQEEEKLKERLEEL 742
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1901 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLqvAQMRIEYLEQSTVD-RAIVSRQEAVICDLENK 1979
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKlEEEVSRIEARLREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1980 tefqkvqIKRFEVLVIRLRDsliKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEE 2059
Cdd:TIGR02169 821 -------LNRLTLEKEYLEK---EIQELQEQRIDLKEQIKS----IEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
810 820 830
....*....|....*....|....*....|....*..
gi 970949420 2060 LAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTE 2096
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELK 923
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
586-1054 |
2.55e-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: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRgpsvpsagkvpkgRRDGLPAHIGSMAQRA-YWALLN-------QRRD---- 653
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY-------------RDVGNPLTLTSTRSSPlAPQLLKvvqeavrQQSEtgyp 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 654 QSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATR---FSMVMSLDfnatGR 730
Cdd:cd14881 69 QAIILSGTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRighFIEVQVTD----GA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 731 ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELNL--HQMADSS--SFGMGVWSKPEDKqkaaAAFAQL 806
Cdd:cd14881 145 LYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLdgYSPANLRylSHGDTRQNEAEDA----ARFQAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 807 QGAMEMLGISESEqraVWRVLAAIYHLG--------AAGACKVGRKQFmrfewaNYAAEALGCE----YEELNTATfkHH 874
Cdd:cd14881 221 KACLGILGIPFLD---VVRVLAAVLLLGnvqfidggGLEVDVKGETEL------KSVAALLGVSgaalFRGLTTRT--HN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 875 LR-QIIQQmtfgpsrwgLEDEETSSGLKmtgvDCvegMASGLYQELFAAVVSLINR-----SFSSHHLSMASIMVVDSPG 948
Cdd:cd14881 290 ARgQLVKS---------VCDANMSNMTR----DA---LAKALYCRTVATIVRRANSlkrlgSTLGTHATDGFIGILDMFG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 949 FQNPrhqgkdRAATFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVP--VQFDLPDPSPgttvaVVDQNPSQQVrlpa 1026
Cdd:cd14881 354 FEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQceVEVDYVDNVP-----CIDLISSLRT---- 418
|
490 500
....*....|....*....|....*...
gi 970949420 1027 gggaqdarGLFWVLDEEVHVEGSSDSVV 1054
Cdd:cd14881 419 --------GLLSMLDVECSPRGTAESYV 438
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
585-1206 |
5.46e-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: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRgPSVPS--AGKVPKG--------------RRDGLPAHIGSMAQRAYWALL 648
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPF-QDLPQlyGDEILRGyaydhnsqfgdrvtSTDPREPHLFAVARAAYIDIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 649 NQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGS---------------VDGRVSVE-KIRATFTVLRAFGSVSMAHSR 712
Cdd:cd14899 80 QNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnltnsesisppaSPSRTTIEeQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 713 SATRFSMVMSLDFNATGR-ITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGLDLDLRTELN--LHQMADSSSFGM-- 787
Cdd:cd14899 160 NSSRFGKFIELRFRDERRrLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSADNNCVSKEQKqvLALSGGPQSFRLln 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 788 -GVWSKPEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGA---------------AGACKVGRKQFMRFEW 851
Cdd:cd14899 240 qSLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNvdfeqiphkgddtvfADEARVMSSTTGAFDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 852 ANYAAEALGCEYEELNTATFKhhlrqiiqqmtfgpsRWGLEDEETSsglkMTGVDCVEG------MASGLYQELFAAVVS 925
Cdd:cd14899 320 FTKAAELLGVSTEALDHALTK---------------RWLHASNETL----VVGVDVAHArntrnaLTMECYRLLFEWLVA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 926 LINRSFSSH---------------HLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHERLQLLFYQRTFVSTLQR 990
Cdd:cd14899 381 RVNNKLQRQasapwgadesdvddeEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 991 YQEEGVPVQFdLPDPSPGTTVAVVDQNPSqqvrlpagggaqdarGLFWVLDEEVHVEGSSDSVVLERLCAAFEKKGAGTE 1070
Cdd:cd14899 455 YRDEGIRWSF-VDFPNNRACLELFEHRPI---------------GIFSLTDQECVFPQGTDRALVAKYYLEFEKKNSHPH 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1071 GSSAlRTCEQPLQCEIFHQLGWdpVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSLfqARAKLPPVCRAVAGLEGT 1150
Cdd:cd14899 519 FRSA-PLIQRTTQFVVAHYAGC--VTYTIDGFLAKNKDSFCE-SAAQLLAGSSNPLIQAL--AAGSNDEDANGDSELDGF 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 970949420 1151 SQQALQRSRmvrrtfaSSLAAVrrkAPCSQIKLQMDALTSMIKRSRLHFIHCLVPN 1206
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 ... |
1387-2072 |
1.81e-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: 96.40 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1387 QLLGSLQPLLSATIGTEQLRAK-EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvaCQVLESER 1465
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK----NIKLSKDV 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1466 AERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENefLRKRLQQCEERLD 1545
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD--MKKKLEEDAGTLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1546 SELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfEK 1625
Cdd:pfam01576 542 ALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE-------EK 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1626 GLREKVTQENTSVRWElgqlqqqLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESS-------- 1697
Cdd:pfam01576 615 AISARYAEERDRAEAE-------AREKETRALSLARALEEALEAKEEL-------ERTNKQLRAEMEDLVSSkddvgknv 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1698 --------ALEQQ----KIQSQQ-ENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ 1764
Cdd:pfam01576 681 helerskrALEQQveemKTQLEElEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELED 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1765 EYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRdLRRTHALLSDVQlllgtmedgktsvskEELEKVHSQLEQS 1844
Cdd:pfam01576 761 ERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ-LKKLQAQMKDLQ---------------RELEEARASRDEI 824
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1845 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMqkhkdliaqsaadiGQ 1924
Cdd:pfam01576 825 LAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLE--------------AR 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1925 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL------EQSTVDRAIVSRQEAVICDLENKTEFQKV--QIK-RFEVLVI 1995
Cdd:pfam01576 891 IAQLEEELEEEQSNTELLNDRLRKSTLQVEQLttelaaERSTSQKSESARQQLERQNKELKAKLQEMegTVKsKFKSSIA 970
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1996 RLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL--------------KADMEELVQREAEASRRCMELEKYVEELA 2061
Cdd:pfam01576 971 ALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVllqvederrhadqyKDQAEKGNSRMKQLKRQLEEAEEEASRAN 1050
|
730
....*....|.
gi 970949420 2062 AVRQTLQTDLE 2072
Cdd:pfam01576 1051 AARRKLQRELD 1061
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1404-2091 |
3.17e-18 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 92.16 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1404 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVA----------CQVLESERAERLQAFR 1473
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAekqrrdlgeeLEALKTELEDTLDTTA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1474 EVQELKSKHEQvqkKLGDVNKQLEEAQQ--KIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE--------- 1542
Cdd:pfam01576 317 AQQELRSKREQ---EVTELKKALEEETRshEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaelqael 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1543 ------RLDSElTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQL-- 1614
Cdd:pfam01576 394 rtlqqaKQDSE-HKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLqd 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1615 AQALG--ESVFEKGLREKVTQ---ENTSVRWELGQLQQQLKQKEQEASQLKQQvemLQDHKREllgspslgencvagLKE 1689
Cdd:pfam01576 473 TQELLqeETRQKLNLSTRLRQledERNSLQEQLEEEEEAKRNVERQLSTLQAQ---LSDMKKK--------------LEE 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1690 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSC------QKRLHQL---EM 1760
Cdd:pfam01576 536 DAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD-KLEKTKNRLQQELDDLLVDLDHQRQLVsnlekkQKKFDQMlaeEK 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1761 QLEQEY-EEKQMVLHEKQDLEGLIGTLCdqighRDFDVEKRLRRDLRRTHALL-SDVQLLLGTMEDGKTSVskEELEKVH 1838
Cdd:pfam01576 615 AISARYaEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTNKQLrAEMEDLVSSKDDVGKNV--HELERSK 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1839 SQLEQSeakcEEALKTQkvltadLESMHSELEnMTRNKSL---VDEQLYRLQFE-------------KADLLKRIDEDQD 1902
Cdd:pfam01576 688 RALEQQ----VEEMKTQ------LEELEDELQ-ATEDAKLrleVNMQALKAQFErdlqardeqgeekRRQLVKQVRELEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1903 DLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLeQSTVDRAIVSRQEAVICDLENKTef 1982
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESEK-- 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1983 qkvQIKRFEVLVIRLRDSLI--------------KMGEELSQAATSESQQRESsqyyQRRLEELKADMEELVQREAEAS- 2047
Cdd:pfam01576 834 ---KLKNLEAELLQLQEDLAaserarrqaqqerdELADEIASGASGKSALQDE----KRRLEARIAQLEEELEEEQSNTe 906
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 970949420 2048 -------RRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASS 2091
Cdd:pfam01576 907 llndrlrKSTLQVEQLTTELAAERSTSQKSesaRQQLERQNKELKAKLQEMEGT 960
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
586-1206 |
1.60e-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: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGP-------------------SVPSAGKVPkgrrdglPAHIGSMAQRAYWA 646
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPYKPlkelydqdvmnvylhkksnSAASAAPFP-------KAHIYDIANMAYKN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 647 LLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFN 726
Cdd:cd14884 75 MRGKLKRQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 727 A---------TGRITAAQLQTMLLEKSRVARQPEGESNFLVFSQMLAGL-DLDL---RTELNLH----------QMADSS 783
Cdd:cd14884 155 EventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLsDEDLarrNLVRNCGvygllnpdesHQKRSV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 784 SFGMGVWSK-----PEDKQKAAAAFAQLQGAMEMLGISESEQRAVWRVLAAIYHLGAAGackvgrkqfmrfewANYAAEA 858
Cdd:cd14884 235 KGTLRLGSDsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRA--------------YKAAAEC 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 859 LGCEYEELNTaTFKHHLRQIIQQMTFGPSRwglEDEETSSglkmtgvdcVEGMASGLYQELFAAVVSLINR--------- 929
Cdd:cd14884 301 LQIEEEDLEN-VIKYKNIRVSHEVIRTERR---KENATST---------RDTLIKFIYKKLFNKIIEDINRnvlkckekd 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 930 SFSSHHLSM---ASIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVpVQFDLPDPS 1006
Cdd:cd14884 368 ESDNEDIYSineAIISILDIYGFEELSGND------FDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDVAPS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1007 PGTTVAVVDQ---NPSQQVRLPAgGGAQDARGLFW---------VLDEEVHVEGSsdsvVLERLCAAFEKKGAGTEGSSA 1074
Cdd:cd14884 441 YSDTLIFIAKifrRLDDITKLKN-QGQKKTDDHFFryllnnerqQQLEGKVSYGF----VLNHDADGTAKKQNIKKNIFF 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1075 LRtceqplqceifHQLGwdPVRYDLTGWLHRAKPNLSAlDAPQVLHQSKREELRSlfqaraklppvcravAGLEGTSQQA 1154
Cdd:cd14884 516 IR-----------HYAG--LVTYRINNWIDKNSDKIET-SIETLISCSSNRFLRE---------------ANNGGNKGNF 566
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 970949420 1155 LQRSRMVrrtfasslaavrrkapcsqIKlQMDALTSMIKRSRLHFIHCLVPN 1206
Cdd:cd14884 567 LSVSKKY-------------------IK-ELDNLFTQLQSTDMYYIRCFLPN 598
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
586-999 |
2.17e-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: 89.03 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVP-----SAGKVPKGRRDGLPaHIGSMAQRAYWALLNQRRDQSIVALG 660
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEypqefHAKYRCKSRSDNAP-HIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 661 WSGAGKTTCCEQVLEHLvGMAGSVDGRVSvEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTML 740
Cdd:cd14882 81 ESYSGKTTNARLLIKHL-CYLGDGNRGAT-GRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 741 LEKSRVARQPEGESNFLVFSQMLAGL-------DLDLRTELNLHQM----ADSSSFGMGVWSKPEDKQKAAAAFAQLQGA 809
Cdd:cd14882 159 LEKLRVSTTDGNQSNFHIFYYFYDFIeaqnrlkEYNLKAGRNYRYLrippEVPPSKLKYRRDDPEGNVERYKEFEEILKD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 810 MEMlgiSESEQRAVWRVLAAIYHLGAAGACKV-GRKQFMRFEWANYAAEALGceyeeLNTATFKHHLRQIIQQMTFGPSR 888
Cdd:cd14882 239 LDF---NEEQLETVRKVLAAILNLGEIRFRQNgGYAELENTEIASRVAELLR-----LDEKKFMWALTNYCLIKGGSAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 889 WGLEDEETSsglkmtgvDCVEGMASGLYQELFAAVVSLINrsfssHHLSMA--------SIMVVDSPGFQNPRHQGkdra 960
Cdd:cd14882 311 RKHTTEEAR--------DARDVLASTLYSRLVDWIINRIN-----MKMSFPravfgdkySISIHDMFGFECFHRNR---- 373
|
410 420 430
....*....|....*....|....*....|....*....
gi 970949420 961 atFEELCHNYAHERLQLLFYQRTFVSTLQRYQEEGVPVQ 999
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 ... |
585-999 |
2.34e-17 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 88.92 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 585 SSVLNTLLQRYKAQLLHTCTGPDLIVLQPRGPSVPSAGKVPKGRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWSGA 664
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISGESGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 665 GKTTCCEQVLE-HLVGMagSVDGRVSVEKIRATFtVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLEK 743
Cdd:cd14937 81 GKTEASKLVIKyYLSGV--KEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIFLLEN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 744 SRVARQPEGESNFLVFSQMLAGLDLDLRTELNLHQMADSSSFGMGVWSKPE-DKQKAAAAFAQLQGAMEMLGISESeqra 822
Cdd:cd14937 158 IRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLMISFDKMNMHDMKDD---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 823 VWRVLAAIYHLG--------AAGACKVGRKQFMRFEWANYAAEALGCEYEEL-NTATFKHhlRQIIQQMTFGPsrwgLED 893
Cdd:cd14937 234 LFLTLSGLLLLGnveyqeieKGGKTNCSELDKNNLELVNEISNLLGINYENLkDCLVFTE--KTIANQKIEIP----LSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 894 EETSSGLKMTGVDcvegmasgLYQELFAAVVSLINRSFSSHHLSMASIMVVDSPGFQNPRHQgkdraaTFEELCHNYAHE 973
Cdd:cd14937 308 EESVSICKSISKD--------LYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN------SLEQLLINIANE 373
|
410 420
....*....|....*....|....*.
gi 970949420 974 RLQLLFYQRTFVSTLQRYQEEGVPVQ 999
Cdd:cd14937 374 EIHSIYLYIVYEKETELYKAEDILIE 399
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1403-1958 |
9.52e-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: 87.00 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLAD---ERFKGDVACQVLES--ERAERLQAfrEVQE 1477
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKkiQKNKSLES--QISE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1478 LKSKH-------EQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLdSELT 1549
Cdd:TIGR04523 223 LKKQNnqlkdniEKKQQEINEKTTEISNTQTQLnQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEI-SDLN 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1550 ARKE-------------LEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQ-QSRNHELEKKQKKfdLQLA 1615
Cdd:TIGR04523 302 NQKEqdwnkelkselknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN----SESEnSEKQRELEEKQNE--IEKL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1616 QALGESVFEKglREKVTQENTSVRWELgqlqqqlKQKEQEASQLKQQVEMLQDHKRELLGspslgencvaglkerlwkle 1695
Cdd:TIGR04523 376 KKENQSYKQE--IKNLESQINDLESKI-------QNQEKLNQQKDEQIKKLQQEKELLEK-------------------- 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1696 ssalEQQKIQSQ---QENTIKQLEQLRQRFELEIERMKQMhqkdREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQ-- 1770
Cdd:TIGR04523 427 ----EIERLKETiikNNSEIKDLTNQDSVKELIIKNLDNT----RESLETQLKVLSRSINKIKQNLE-QKQKELKSKEke 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1771 --MVLHEKQDLEGLIGTLCDQIghrdfdvekrlrrdlrrthallsdvqlllgtmedgktSVSKEELEKVHSQLEQSEAKC 1848
Cdd:TIGR04523 498 lkKLNEEKKELEEKVKDLTKKI-------------------------------------SSLKEKIEKLESEKKEKESKI 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1849 EEalktqkvLTADLESMHSEL--ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQ 1926
Cdd:TIGR04523 541 SD-------LEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS 613
|
570 580 590
....*....|....*....|....*....|..
gi 970949420 1927 ELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1958
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ 645
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1409-2087 |
1.42e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 EEELTTLRRKLEKSEKLRnELRQntDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1488
Cdd:TIGR02168 199 ERQLKSLERQAEKAERYK-ELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1489 LGDVNKQLEEAQQK-----IQLNDLERNptggADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQS 1563
Cdd:TIGR02168 276 VSELEEEIEELQKElyalaNEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1564 AYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQalgesvfekgLREKVTQentsvrwelg 1643
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------LEARLER---------- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1644 qlqqqlkqkeqeasqLKQQVEMLQDHKRELLGSPSLGEncvagLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFE 1723
Cdd:TIGR02168 412 ---------------LEDRRERLQQEIEELLKKLEEAE-----LKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1724 LEIERMKQmhqkdREDQEEELedvrQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfDVEKRLRR 1803
Cdd:TIGR02168 472 EAEQALDA-----AERELAQL----QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELI-----SVDEGYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1804 DLRRthALLSDVQLLLgtMEDgktsvsKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLV 1879
Cdd:TIGR02168 538 AIEA--ALGGRLQAVV--VEN------LNAAKKAIAFLKQNELGrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1880 DEqlYRLQFEKA--DLLKR--IDEDQDDLNELMQKHK----------DLIA-------QSAADIGQIQELQLQLEEAKKE 1938
Cdd:TIGR02168 608 VK--FDPKLRKAlsYLLGGvlVVDDLDNALELAKKLRpgyrivtldgDLVRpggvitgGSAKTNSSILERRREIEELEEK 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1939 KHKLQEQLQVAQMRIEYLEQSTVDraivsrqeavicdLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQ 2018
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEE-------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2019 ressqyyQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:TIGR02168 753 -------SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
586-1058 |
2.25e-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: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 586 SVLNTLLQRYKAQLLHTCTGPDLIVLQPRG--PSVPSAGKVPK-GRRDGLPAHIGSMAQRAYWALLNQRRDQSIVALGWS 662
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRylPFLHSQELVRNyNQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 663 GAGKTTCCEQVLEHLVGMAGSvDGRVSVEKIRATFTVLRAFGSVSMAHSRSATRFSMVMSLDFNATGRITAAQLQTMLLE 742
Cdd:cd14905 82 GSGKSENTKIIIQYLLTTDLS-RSKYLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYFLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 743 KSRVARQPEGESNFLVFSQMLAGLDLDlrtELNLHQMADSSSF-------GMGVWSKPEDKqkaaaAFAQLQGAMEMLGI 815
Cdd:cd14905 161 ENRVTYQNKGERNFHIFYQFLKGITDE---EKAAYQLGDINSYhylnqggSISVESIDDNR-----VFDRLKMSFVFFDF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 816 SESEQRAVWRVLAAIYHLGAAgackvgrkQFMRFEWANYAAEALGCEYEELNTATFKHHLRQIIQQMTFGPSRWGLEDEE 895
Cdd:cd14905 233 PSEKIDLIFKTLSFIIILGNV--------TFFQKNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENRD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 896 TssglkmtgvdcvegMASGLYQELFAAVVSLINRSFSSHHLSMaSIMVVDSPGFQNPRHQGkdraatFEELCHNYAHERL 975
Cdd:cd14905 305 S--------------LARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------YEQFSINFLEERL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 976 QLLFYQRTFVSTLQRYQEEGVPVQfdlpdpspgTTVAVVDQNPSQQVrlpagggaqdARGLFWVLDEEVHVEGSSDSVVL 1055
Cdd:cd14905 364 QQIYLQTVLKQEQREYQTERIPWM---------TPISFKDNEESVEM----------MEKIINLLDQESKNINSSDQIFL 424
|
...
gi 970949420 1056 ERL 1058
Cdd:cd14905 425 EKL 427
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1385-2023 |
5.60e-16 |
|
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: 85.02 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1385 WW--QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdllESKIADLTSDLADERFKGDVACQVLE 1462
Cdd:TIGR00618 243 AYltQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARK-----AAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1463 SERAERLQAFrevqelkSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE 1542
Cdd:TIGR00618 318 SKMRSRAKLL-------MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1543 RLDSELTARKELEQKLGEL-QSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGE 1620
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQaTIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQeSAQSLKE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1621 SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQE--ASQLKQQVEMLQDHKRELLGSPSL-GENCVAGLKERLWKLE-- 1695
Cdd:TIGR00618 471 REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYhq 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1696 -SSALEQQKIQSQQENTIKQ----LEQLRQRFELEIERMKQMHQKDREDQEEELEDvRQSCQKRLHQLEMQLEQEYEEKQ 1770
Cdd:TIGR00618 551 lTSERKQRASLKEQMQEIQQsfsiLTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA-EDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1771 MVLHEKQ----------DLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVS--KEELEKVH 1838
Cdd:TIGR00618 630 VRLHLQQcsqelalkltALHALQLTLTQE------RVREHALSIRVLPKELLASRQLALQKMQSEKEQLTywKEMLAQCQ 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1839 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1918
Cdd:TIGR00618 704 TLLRELETHIEEYDREFNEIENASSSLGSDLA---AREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAEL 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1919 AADIGQIQELQLQLEEAKKEKHKLQEQLQvaQMRIEYLEQSTV-DRAIVSRQEAVICDLENKTEfqkvqikrfevLVIRL 1997
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLLKTLEAEIG--QEIPSDEDILNLqCETLVQEEEQFLSRLEEKSA-----------TLGEI 847
|
650 660
....*....|....*....|....*.
gi 970949420 1998 RDSLIKMGEELSQAATSESQQRESSQ 2023
Cdd:TIGR00618 848 THQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1473-2103 |
2.02e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1473 REVQELKSKHEQVQKKLGDVNKQLEEAQQKI-QLNDLERNPTGGADEWQMRFDcaqmENEFLRKRLQQCEERLDSELTAR 1551
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREInEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1552 KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdledtcvllenqqsrnhELEKKQKKFdlqlaQALGEsvfekgLREKV 1631
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELK------------------ELKEKAEEY-----IKLSE------FYEEY 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1632 TQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvAGLKERLWKLESSALEQQKIQSQQENt 1711
Cdd:PRK03918 306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-----------KELEKRLEELEERHELYEEAKAKKEE- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1712 ikqLEQLRQRFE-LEIERMKQMHQKDREDQEEELEDVRQSCQKRlhqleMQLEQEYEEKQMVLHEkqdLEGLIGTlCDQI 1790
Cdd:PRK03918 374 ---LERLKKRLTgLTPEKLEKELEELEKAKEEIEEEISKITARI-----GELKKEIKELKKAIEE---LKKAKGK-CPVC 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1791 GhRDFDVEKRLRRdLRRTHALLSDVqlllgtmedgktSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTAdLESMHSELE 1870
Cdd:PRK03918 442 G-RELTEEHRKEL-LEEYTAELKRI------------EKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1871 NmtrnkslVDEQLYRLQFEKadlLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQ 1950
Cdd:PRK03918 507 E-------LEEKLKKYNLEE---LEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1951 MRIEYLEQSTVDraivsrqeavicDLENKTEFQKVQIKRFevlvIRLRDSLIKMGEELSQAATSESQQRESSQYYQR--- 2027
Cdd:PRK03918 577 KELEELGFESVE------------ELEERLKELEPFYNEY----LELKDAEKELEREEKELKKLEEELDKAFEELAEtek 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2028 RLEELKADMEEL-----VQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAV 2102
Cdd:PRK03918 641 RLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKAL 720
|
.
gi 970949420 2103 D 2103
Cdd:PRK03918 721 E 721
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1403-2072 |
3.22e-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: 82.53 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNEL-RQNTDLLESKIA---------DLTSDLADERFKGDVACQVLES---ERAERL 1469
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELeKKHQQLCEEKNAlqeqlqaetELCAEAEEMRARLAARKQELEEilhELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1470 QAFRE-VQELKSKHEQVQKKLGDVNKQLEE---AQQKIQLNDLernpTGGADEWQMRFDCAQME--NEFLRKRLQQCEER 1543
Cdd:pfam01576 85 EEEEErSQQLQNEKKKMQQHIQDLEEQLDEeeaARQKLQLEKV----TTEAKIKKLEEDILLLEdqNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1544 LDSELTARKELEQKLgelqsaydgakKMAHQLKRKCHHLTCDLEDTcvlLENQQSRNHELEKKQKKFDLQLAQALGESVF 1623
Cdd:pfam01576 161 ISEFTSNLAEEEEKA-----------KSLSKLKNKHEAMISDLEER---LKKEEKGRQELEKAKRKLEGESTDLQEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1624 EKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL---------------GSPSLGENCVAgLK 1688
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQedleseraarnkaekQRRDLGEELEA-LK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1689 ERLWKLESSALEQQKIQSQQENTI----KQLEQLRQRFELEIERMKQMHQKDREDQEEELED---VRQSCQKRLHQLEMQ 1761
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVtelkKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQakrNKANLEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1762 LEQEYEEKQMVLHEKQDLEgligtlcdqigHRdfdvEKRLRRDLRRTHALLSDVQLLLGTMEDgKTSVSKEELEKVHSQL 1841
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSE-----------HK----RKKLEGQLQELQARLSESERQRAELAE-KLSKLQSELESVSSLL 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1842 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAAD 1921
Cdd:pfam01576 450 NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDM 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1922 IGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY------------------LEQSTVDraiVSRQEAVICDLENKTefq 1983
Cdd:pfam01576 530 KKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEkaaaydklektknrlqqeLDDLLVD---LDHQRQLVSNLEKKQ--- 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1984 kvqiKRFEVLVIRLRDSLIKMGEELSQA----------ATSESQQRESSQYYQRRLEE----LKADMEELVQREAEASRR 2049
Cdd:pfam01576 604 ----KKFDQMLAEEKAISARYAEERDRAeaeareketrALSLARALEEALEAKEELERtnkqLRAEMEDLVSSKDDVGKN 679
|
730 740
....*....|....*....|...
gi 970949420 2050 CMELEKYVEELAAVRQTLQTDLE 2072
Cdd:pfam01576 680 VHELERSKRALEQQVEEMKTQLE 702
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1395-2088 |
9.72e-15 |
|
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: 80.88 E-value: 9.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1395 LLSATIGTEQLRAKEEELttlRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFRE 1474
Cdd:TIGR02169 296 IGELEAEIASLERSIAEK---ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1475 VQELKSKHEQVQKKLGDVNKQLEEAQQKIqlNDLERNPTGGADEWQ-MRFDCAQMENEFLRKRLQQCEerLDSEL-TARK 1552
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI--NELKRELDRLQEELQrLSEELADLNAAIAGIEAKINE--LEEEKeDKAL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1553 ELEQKLGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ--ALGESVFEKGLREK 1630
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQELYD--------------LKEEYDRVEKELSKLQRELAEAEAQarASEERVRGGRAVEE 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1631 VTQENT-----SVRwELGQLQQQLKQKEQEASQLKQQVEMLQDHkrellgspSLGENCVAGLKER---------LWKLES 1696
Cdd:TIGR02169 515 VLKASIqgvhgTVA-QLGSVGERYATAIEVAAGNRLNNVVVEDD--------AVAKEAIELLKRRkagratflpLNKMRD 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1697 SALEQQKI---------------QSQQENTIKQLEQ---LRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQL 1758
Cdd:TIGR02169 586 ERRDLSILsedgvigfavdlvefDPKYEPAFKYVFGdtlVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGG 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1759 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRD---FDVEKRLRRDLRRTHALLSDVQLLlgtmeDGKTSVSKEELE 1835
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEnrlDELSQELSDASRKIGEIEKEIEQL-----EQEEEKLKERLE 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1836 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENmtrnkslVDEQLYRLqfEKADLLKRIDEDQDDLNELMQKHKDLI 1915
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK-------LEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1916 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsRQEAVICDLENKTEfqkvQIKRFEVLVI 1995
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK---------EIENLNGKKEELEE----ELEELEAALR 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1996 RLRDSLI-------KMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRqtlq 2068
Cdd:TIGR02169 879 DLESRLGdlkkerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE---- 954
|
730 740
....*....|....*....|
gi 970949420 2069 tDLETSIRRIADLQAALEEV 2088
Cdd:TIGR02169 955 -DVQAELQRVEEEIRALEPV 973
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1403-1944 |
1.71e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 79.72 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLR---NELRQNTDLLESKIADLTSDLaderfkgdvacqvleSERAERLqafrevQELK 1479
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKeeiEELEKELESLEGSKRKLEEKI---------------RELEERI------EELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1480 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE---RLDSELTARKELEQ 1556
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1557 KLGELQS---AYDGAKKMAHQLKRKCHHLTC-DLEDTCVLLENQQSRNHELEKKQKKfdlqLAQALGESVFEKGLREKVT 1632
Cdd:PRK03918 353 RLEELEErheLYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISK----ITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1633 QENTSVRWELGQLQQqlkqkeqeasqlkqqvEMLQDHKRELLGSPSLG----ENCVAGLKERLWKLESSALEQQKIQSQQ 1708
Cdd:PRK03918 429 EELKKAKGKCPVCGR----------------ELTEEHRKELLEEYTAElkriEKELKEIEEKERKLRKELRELEKVLKKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1709 ENTIKQLEQLRQRFELEiERMKQMHQKDREDQEEELEDVRQ---SCQKRLHQLEMQLEQEYE---EKQMVLHEKQDLEGL 1782
Cdd:PRK03918 493 SELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEYEKLKEkliKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEE 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1783 IGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGtmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADL 1862
Cdd:PRK03918 572 LAELLKELEELGFESVEELEERLKELEPFYNEYLELKD---------AEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1863 ESMHSELENMTRNKSLVD-EQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHK 1941
Cdd:PRK03918 643 EELRKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALER 722
|
...
gi 970949420 1942 LQE 1944
Cdd:PRK03918 723 VEE 725
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1831-2099 |
2.30e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.60 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1910
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1911 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENKTEFQKVQIKRF 1990
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA------LLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1991 EVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2070
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
250 260
....*....|....*....|....*....
gi 970949420 2071 LETSIRRIADLQAALEEVASSDSDTESVQ 2099
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 ... |
1688-2124 |
2.53e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 79.45 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1688 KERLWKLESSALEQQKIQSQ--QENTIKQlEQLRQRFEL--EIERMKQMhqkdREDQEEELEDVrqscqkrLHQLEMQLE 1763
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQlcEEKNALQ-EQLQAETELcaEAEEMRAR----LAARKQELEEI-------LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1764 QEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEE--LEKVHSQL 1841
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQDLEEQLDEEE-AARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERklLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1842 EQSEAKCEEALKTQKVLTADLESMHSELENMTRNkslvdEQLYRLQFEKADllKRIDEDQDDLNElmqkhkdliaqsaad 1921
Cdd:pfam01576 165 TSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKK-----EEKGRQELEKAK--RKLEGESTDLQE--------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1922 igQIQELQLQLEEAKKEKHKLQEQLQVAQMRieyLEQSTVDRAIVSRQ----EAVICDLE----------NKTEFQKVQI 1987
Cdd:pfam01576 223 --QIAELQAQIAELRAQLAKKEEELQAALAR---LEEETAQKNNALKKirelEAQISELQedleseraarNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1988 -KRFEVLVIRLRDSL----------IKMGEELSQ--------AATSESQQRESSQYYQRRLEELKADMEELVQREAEASR 2048
Cdd:pfam01576 298 gEELEALKTELEDTLdttaaqqelrSKREQEVTElkkaleeeTRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 2049 RCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQT-AVDCGSSGRKEMDNVSILSSQPEG 2124
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAeLAEKLSKLQSELESVSSLLNEAEG 454
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1409-2090 |
1.89e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 76.51 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 EEELTTLRRKLEKSEKLRNELRQNTDLLE--SKIA----DLTSDLadERFKGDVACQVLESERAERLQAFREVQELKSKH 1482
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQLEPLErqAEKAeryrELKEEL--KELEAELLLLKLRELEAELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1483 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGAdewqmrfdcaqmENEfLRKRLQQCEERLDSELTARKELEQKLGELQ 1562
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAE------------EYE-LLAELARLEQDIARLEERRRELEERLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1563 SAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWEL 1642
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1643 GQLQQQLKQKEQEASQLKQQVEMLQDHKRELLgspslgencvAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRF 1722
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELE----------EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1723 ELEiermkqmhQKDREDQEEELEDVRQscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEK--- 1799
Cdd:COG1196 473 ALL--------EAALAELLEELAEAAA---RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAale 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1800 -----RLRRDLRRTHALLSDVQLLLGTMEDGKtsVSKEELEKVHsQLEQSEAKCEEALKTQKVLTADLESMHSELENMTR 1874
Cdd:COG1196 542 aalaaALQNIVVEDDEVAAAAIEYLKAAKAGR--ATFLPLDKIR-ARAALAAALARGAIGAAVDLVASDLREADARYYVL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1875 NKSLVDEQLYRLQFEKAD-LLKRIDEDQDDLNELMqkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1953
Cdd:COG1196 619 GDTLLGRTLVAARLEAALrRAVTLAGRLREVTLEG----EGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1954 EYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDsLIKMGEELSQAATSESQQRESSQYYQRRLEELK 2033
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 2034 ADMEEL------VQREAEasrrcmELEKYVEELAAVRQTLQ---TDLETSIRRI-----ADLQAALEEVAS 2090
Cdd:COG1196 774 REIEALgpvnllAIEEYE------ELEERYDFLSEQREDLEearETLEEAIEEIdretrERFLETFDAVNE 838
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1434-2099 |
2.44e-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: 76.16 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1434 DLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREvQELKSKHEQVQKkLGDVNKQLEEAQQKIQLndlernpt 1513
Cdd:TIGR00618 171 NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP-CMPDTYHERKQV-LEKELKHLREALQQTQQ-------- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1514 ggADEWQMRFDCAQMENEFLRKRLQQCEERLDsELTArkeLEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLL 1593
Cdd:TIGR00618 241 --SHAYLTQKREAQEEQLKKQQLLKQLRARIE-ELRA---QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1594 EnQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEA-----SQLKQQVEMLQD 1668
Cdd:TIGR00618 315 E-LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqhiHTLQQQKTTLTQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1669 HKRELLGSPSLGENCVAGLKERLwkLESSALEQQKI--QSQQENTIKQLEQLRQRFE--LEIERMKQMHQKDREDQEEEL 1744
Cdd:TIGR00618 394 KLQSLCKELDILQREQATIDTRT--SAFRDLQGQLAhaKKQQELQQRYAELCAAAITctAQCEKLEKIHLQESAQSLKER 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1745 EdvrqscqKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDfdvekrlrrdlrrTHALLSDvqlllgtmED 1824
Cdd:TIGR00618 472 E-------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPN-------------PARQDID--------NP 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1825 GKTSVSKEELEKVHSQLEQSEAK----CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID-- 1898
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSEEDvyhqLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEkl 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1899 -EDQDDLNELMQKHKDLIAQSAADIGQIQEL-QLQLEEAKKEKHKLQEQLQVAQMRI-EYLEQSTVDRA-IVSRQEAVIC 1974
Cdd:TIGR00618 604 sEAEDMLACEQHALLRKLQPEQDLQDVRLHLqQCSQELALKLTALHALQLTLTQERVrEHALSIRVLPKeLLASRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1975 DLENKTEF---------QKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESS------QYYQRRLEELKADMEEL 2039
Cdd:TIGR00618 684 KMQSEKEQltywkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAlnqslkELMHQARTVLKARTEAH 763
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2040 VQREAEASRRCMELEKYvEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQ 2099
Cdd:TIGR00618 764 FNNNEEVTAALQTGAEL-SHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQ 822
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1403-2087 |
3.40e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.87 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRnELRQNTDLLESKIADLTSDL--ADERFKGDVACQVLESERAERLQAFREVQ--EL 1478
Cdd:PTZ00121 1144 EARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVrkAEELRKAEDARKAEAARKAEEERKAEEARkaED 1222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1479 KSKHEQVqKKLGDVNKQLEEAQQKiqlnDLERNptggaDEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKL 1558
Cdd:PTZ00121 1223 AKKAEAV-KKAEEAKKDAEEAKKA----EEERN-----NEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKA 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1559 GELQSAYDgaKKMAHQLKRKChhltcdledtcvllenQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQ-ENTS 1637
Cdd:PTZ00121 1293 DEAKKAEE--KKKADEAKKKA----------------EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaEAEA 1354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1638 VRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK--ERLWKLESSALEQQKIQSQQENtIKQL 1715
Cdd:PTZ00121 1355 AADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkaDELKKAAAAKKKADEAKKKAEE-KKKA 1433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1716 EQLRQRFEleiERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEmqLEQEYEEKQMVLHEKQDLEgligtlcdqighrdf 1795
Cdd:PTZ00121 1434 DEAKKKAE---EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAE--------------- 1493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1796 dvEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSvskEELEKVHSQLEQSEA-KCEEALKTQKVLTADLESMHSELENMTR 1874
Cdd:PTZ00121 1494 --EAKKKADEAKKAAEAKKKADEAKKAEEAKKA---DEAKKAEEAKKADEAkKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1875 NKSlvDEQLYRLQFEKADLLKRIDEDQddLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKhklQEQLQVAQMRIE 1954
Cdd:PTZ00121 1569 AKK--AEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE---EEKKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1955 YLEQstVDRAIVSRQEavicdlENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAatsESQQRESSQYYQRRLEElKA 2034
Cdd:PTZ00121 1642 EAEE--KKKAEELKKA------EEENKIKAAEEAKKA-------EEDKKKAEEAKKA---EEDEKKAAEALKKEAEE-AK 1702
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 970949420 2035 DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1402-1947 |
3.82e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1402 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQAFREVQELKSK 1481
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewqmrfDCAQMENEFLRKRLQQcEERLDSELTARKELEQKLGEL 1561
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELA------------EAEEALLEAEAELAEA-EEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1562 QSAYDGAKKMAHQLKRKCHHLTCDLEDtcvLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWE 1641
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEE---LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1642 LGQLQQQLKQKEQEASQLKQQVEMLQDH------KRELLGSPSLGENCVAGLKERLWKLESSALEQqkiqsqqentikql 1715
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYegflegVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-------------- 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1716 eqlrqrfELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDF 1795
Cdd:COG1196 542 -------AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1796 ------------DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE 1863
Cdd:COG1196 615 yyvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELE 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1864 SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELqLQLEEAKKEKHKLQ 1943
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
....
gi 970949420 1944 EQLQ 1947
Cdd:COG1196 774 REIE 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1824-2089 |
1.92e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.10 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1824 DGKTSVSKEELEKVHSQLEQSEAKCEE-------------------ALKTQK------VLTADLESMHSELENMTRNKSL 1878
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEkrqqlerlrrerekaeryqALLKEKreyegyELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1879 VDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI--------GQIQELQLQLEEAKKEKHKLQEQLQVAQ 1950
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1951 MRIEyleqstvdraivsRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLE 2030
Cdd:TIGR02169 329 AEID-------------KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2031 ELKADMEELvqrEAEASRRCMELEKYVEELAAVRQtlqtDLETSIRRIADLQAALEEVA 2089
Cdd:TIGR02169 396 KLKREINEL---KRELDRLQEELQRLSEELADLNA----AIAGIEAKINELEEEKEDKA 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1403-2070 |
3.63e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELttlrrklEKSEKLRN--ELRQNTDLLESKIADLTSDL-ADERFKGD---VACQVLESERAERLQAFREVQ 1476
Cdd:PTZ00121 1233 EEAKKDAEEA-------KKAEEERNneEIRKFEEARMAHFARRQAAIkAEEARKADelkKAEEKKKADEAKKAEEKKKAD 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1477 ELKSKHEQvQKKLGDVNKQLEEAQQKiqlndlernptggADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ 1556
Cdd:PTZ00121 1306 EAKKKAEE-AKKADEAKKKAEEAKKK-------------ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1557 KLGELQSAYDGAKKMAHQlKRKCHHLTCDLEDTCVLLENQQSRNHELEK----KQKKFDLQLAQALGESVFEKGLREKVT 1632
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEE-KKKADEAKKKAEEDKKKADELKKAAAAKKKadeaKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1633 QENTSVRweLGQLQQQLKQKEQEASQLKQQVEmlqdHKRELLGSPSLGENCvaglKERLWKLESSALEQQKI-QSQQENT 1711
Cdd:PTZ00121 1451 KKAEEAK--KAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEA----KKKADEAKKAAEAKKKAdEAKKAEE 1520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1712 IKQLEQLRQRFEL-EIERMKQMHQKDREDQEEELEDVRQSCQKRLHQlemQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI 1790
Cdd:PTZ00121 1521 AKKADEAKKAEEAkKADEAKKAEEKKKADELKKAEELKKAEEKKKAE---EAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1791 GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMH---- 1866
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDkkka 1677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1867 SELENMTRNKSLVDEQLYRLQFEKadllKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQ--- 1943
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEA----KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKkde 1753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1944 -EQLQVAQMRIEYLEQSTVDRaivSRQEAVICD-LENKTEFQKVQIKR--------FEVLV-------IRLRDSLIKMGE 2006
Cdd:PTZ00121 1754 eEKKKIAHLKKEEEKKAEEIR---KEKEAVIEEeLDEEDEKRRMEVDKkikdifdnFANIIeggkegnLVINDSKEMEDS 1830
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 2007 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTD 2070
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1404-2059 |
4.89e-11 |
|
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: 68.59 E-value: 4.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1404 QLRAKEEELTTLRRKLEK---------------SEKLRNELRQNTDLLESKIAD--LTSDLADERFKGDVACQVLESERA 1466
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAqrkaiqelqfenekvSLKLEEEIQENKDLIKENNATrhLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1467 ERLQAFREV-----------QELKSKHEQVQKKLgdvNKQLEEAQQKIQlnDLErnptggaDEWQMRFDCAQMENEFLRK 1535
Cdd:pfam05483 180 ETRQVYMDLnnniekmilafEELRVQAENARLEM---HFKLKEDHEKIQ--HLE-------EEYKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1536 RLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKkqkkfDLQLA 1615
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEE-----DLQIA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1616 QalgESVFEkglrekVTQENTSVRWELGqlqQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLE 1695
Cdd:pfam05483 323 T---KTICQ------LTEEKEAQMEELN---KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1696 SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVL 1773
Cdd:pfam05483 391 SELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgkEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1774 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALL---SDVQLLLGTMEDGKTSVSKEElEKVHSQLEQSEakcee 1850
Cdd:pfam05483 471 KEVEDLK----TELEKEKLKNIELTAHCDKLLLENKELTqeaSDMTLELKKHQEDIINCKKQE-ERMLKQIENLE----- 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1851 alKTQKVLTADLESMHSEL---------------ENMTRNKSLV---DEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK 1912
Cdd:pfam05483 541 --EKEMNLRDELESVREEFiqkgdevkckldkseENARSIEYEVlkkEKQMKILENKCNNLKKQIENKNKNIEELHQENK 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1913 DLIAQSAADIGQ-------IQELQLQLEEAKKekhKLQEQLQVAQMRIEYLEQS------TVDRAIVSRQEAVICDLENK 1979
Cdd:pfam05483 619 ALKKKGSAENKQlnayeikVNKLELELASAKQ---KFEEIIDNYQKEIEDKKISeeklleEVEKAKAIADEAVKLQKEID 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1980 TEFQKvQIKRFEVLVIRLRDSLIKMGEEL-SQAATSESQQRESSQyyqrrleeLKADME-ELVQREAE--ASRRCMELEK 2055
Cdd:pfam05483 696 KRCQH-KIAEMVALMEKHKHQYDKIIEERdSELGLYKNKEQEQSS--------AKAALEiELSNIKAEllSLKKQLEIEK 766
|
....
gi 970949420 2056 YVEE 2059
Cdd:pfam05483 767 EEKE 770
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1403-1892 |
1.48e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.47 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTT---LRRKLEKSEKLRNELRQNTDllESKIADLTSDLADERFKGDVACQVLESER-AERL----QAFRE 1474
Cdd:PTZ00121 1381 DAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAA--AKKKADEAKKKAEEKKKADEAKKKAEEAKkADEAkkkaEEAKK 1458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1475 VQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDcAQMENEFLRK--------RLQQCEERLDS 1546
Cdd:PTZ00121 1459 AEEAKKKAEE-AKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE-AKKKADEAKKaeeakkadEAKKAEEAKKA 1536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1547 ELTARKELEQKLGELQSAYDGAK----KMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESV 1622
Cdd:PTZ00121 1537 DEAKKAEEKKKADELKKAEELKKaeekKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1623 FEKGLREKVTQENtSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK----------ERLW 1692
Cdd:PTZ00121 1617 EAKIKAEELKKAE-EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeedekkaaEALK 1695
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1693 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQE--EEL---EDVRQSCQKRLHQLEMQLEQEYE 1767
Cdd:PTZ00121 1696 KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKkaEEAkkdEEEKKKIAHLKKEEEKKAEEIRK 1775
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1768 EKQMVLHEKQDLE-------------------------GLIGTLCDQIGHRDFDVEKR---LRRDLRRTHALLSDVQLLL 1819
Cdd:PTZ00121 1776 EKEAVIEEELDEEdekrrmevdkkikdifdnfaniiegGKEGNLVINDSKEMEDSAIKevaDSKNMQLEEADAFEKHKFN 1855
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970949420 1820 GTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKAD 1892
Cdd:PTZ00121 1856 KNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRD 1928
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1403-2087 |
2.52e-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: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTS-DLADERFKGDVACQVLE-----SERAERLQAF--RE 1474
Cdd:TIGR00606 238 EIVKSYENELDPLKNRLKEIEHNLSKIMK----LDNEIKALKSrKKQMEKDNSELELKMEKvfqgtDEQLNDLYHNhqRT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1475 VQELKSKHEQVQKKLGDVNKQLEE-AQQKIQLNDLERNPTGGADEWQ---MRFDCAQMENEfLRKRLQQCEERLDSELTA 1550
Cdd:TIGR00606 314 VREKERELVDCQRELEKLNKERRLlNQEKTELLVEQGRLQLQADRHQehiRARDSLIQSLA-TRLELDGFERGPFSERQI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1551 R--------------KELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSrnhelEKKQKKFDLQLAQ 1616
Cdd:TIGR00606 393 KnfhtlvierqedeaKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQE-----ELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1617 ALGESVFEKglrekvTQENTSVRWELgqlqqQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGL---KERLWK 1693
Cdd:TIGR00606 468 GSSDRILEL------DQELRKAEREL-----SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhhTTTRTQ 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1694 LESSALEQ----QKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQ--EEELEDVRQSCQKrLHQLEMQLEQEYE 1767
Cdd:TIGR00606 537 MEMLTKDKmdkdEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINqtRDRLAKLNKELAS-LEQNKNHINNELE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1768 EKQMVLHEKQDlegligTLCDQIGHRDFDVE-KRLRRDLRRTHALLSdvqlllgtMEDGKTSVSKEELEKVHSQLEQSEA 1846
Cdd:TIGR00606 616 SKEEQLSSYED------KLFDVCGSQDEESDlERLKEEIEKSSKQRA--------MLAGATAVYSQFITQLTDENQSCCP 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1847 KCEEALKTQKVL---TADLESM-------HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIA 1916
Cdd:TIGR00606 682 VCQRVFQTEAELqefISDLQSKlrlapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1917 QSAADIGQiQELQLQLEEAKKEKHKLQeQLQVAQMRIEYLEQSTVDRAI---VSRQEAVICDLENKTEFQKVQIKRFEVl 1993
Cdd:TIGR00606 762 RLKNDIEE-QETLLGTIMPEEESAKVC-LTDVTIMERFQMELKDVERKIaqqAAKLQGSDLDRTVQQVNQEKQEKQHEL- 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1994 virlrDSLIKMGEELSQAAtseSQQRESSQYYQRRLEELKADMEELvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2073
Cdd:TIGR00606 839 -----DTVVSKIELNRKLI---QDQQEQIQHLKSKTNELKSEKLQI----GTNLQRRQQFEEQLVELSTEVQSLIREIKD 906
|
730
....*....|....
gi 970949420 2074 SIRRIADLQAALEE 2087
Cdd:TIGR00606 907 AKEQDSPLETFLEK 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1409-1786 |
3.30e-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: 65.85 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKK 1488
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1489 LGDVNKQLEEAQQKIQlndlernptggADEWQMRFDCAQMENefLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGA 1568
Cdd:TIGR02168 763 IEELEERLEEAEEELA-----------EAEAEIEELEAQIEQ--LKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1569 KKMAHQLKRkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVfekgLREKVTQENTSVRWELGQLQQQ 1648
Cdd:TIGR02168 830 ERRIAATER---RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN----ERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1649 LKQKEQEASQLKQQVEMLQDHkrellgspslgencvaglkerlwkLESSALEQQKIQSQQENtikQLEQLRQRFELEIER 1728
Cdd:TIGR02168 903 LRELESKRSELRRELEELREK------------------------LAQLELRLEGLEVRIDN---LQERLSEEYSLTLEE 955
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 970949420 1729 MKQMHQKDREDQEEeledvrqsCQKRLHQLEMQLE----------QEYEE----KQMVLHEKQDLEGLIGTL 1786
Cdd:TIGR02168 956 AEALENKIEDDEEE--------ARRRLKRLENKIKelgpvnlaaiEEYEElkerYDFLTAQKEDLTEAKETL 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1698-2094 |
3.80e-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: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1698 ALEQQKIQSQQENTIKQLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQ----KRLHQLEMQLEQEYEEKQMVL 1773
Cdd:COG4913 283 LWFAQRRLELLEAELEELRAELARLEAELER----LEARLDALREELDELEAQIRgnggDRLEQLEREIERLERELEERE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1774 HEKQDLEgligTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVqlllgtmedgktsvsKEELEKVHSQLEQSEAKceealk 1853
Cdd:COG4913 359 RRRARLE----ALLAALGLPLPASAEEFAALRAEAAALLEAL---------------EEELEALEEALAEAEAA------ 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1854 tQKVLTADLESMHSELENMTRNKSLVDEQLYRLqfeKADLLKRIDEDQDDLN---ELMQ-KHKDLIAQSAAdigqiqELQ 1929
Cdd:COG4913 414 -LRDLRRELRELEAEIASLERRKSNIPARLLAL---RDALAEALGLDEAELPfvgELIEvRPEEERWRGAI------ERV 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1930 L------------QLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD---------------------RAIVSRQEAVIC 1974
Cdd:COG4913 484 LggfaltllvppeHYAAALRwvNRLHLRGRLVYERVRTGLPDPERPRldpdslagkldfkphpfrawlEAELGRRFDYVC 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1975 dLENKTEFQKVqikRFEVlvirLRDSLIKMGEELSQAATsesQQRESSQYY-----QRRLEELKADMEELVQREAEASRR 2049
Cdd:COG4913 564 -VDSPEELRRH---PRAI----TRAGQVKGNGTRHEKDD---RRRIRSRYVlgfdnRAKLAALEAELAELEEELAEAEER 632
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 970949420 2050 CMELEKYVEELAAVRQTLQT---------DLETSIRRIADLQAALEEVASSDSD 2094
Cdd:COG4913 633 LEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDASSDD 686
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1684-2104 |
4.75e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1684 VAGLKERlwKLESsaleQQKIQSQQENtIKQLEQLRqrFELE-----IERMKQMHQKDRE--DQEEELEdvRQSCQKRLH 1756
Cdd:TIGR02168 167 ISKYKER--RKET----ERKLERTREN-LDRLEDIL--NELErqlksLERQAEKAERYKElkAELRELE--LALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1757 QLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQI-GHRDFDVEkrLRRDLRRTHALLSDVQLLLGTMEdGKTSVSKEELE 1835
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLeELRLEVSE--LEEEIEELQKELYALANEISRLE-QQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1836 KVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1915
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1916 AQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAvicdLENKTEfqkvqikRFEVLVI 1995
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE----LEELQE-------ELERLEE 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1996 RLrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSi 2075
Cdd:TIGR02168 462 AL--------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD- 532
|
410 420 430
....*....|....*....|....*....|..
gi 970949420 2076 rriADLQAALEEVASSDSD---TESVQTAVDC 2104
Cdd:TIGR02168 533 ---EGYEAAIEAALGGRLQavvVENLNAAKKA 561
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1480-2087 |
5.00e-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: 65.04 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1480 SKHEQVQKKLGDVNKQLEEAQQKIQlnDLERNPTGGADEWQmrfdcaQMENEFlrKRLQQCEERLDSELTARKeleQKLG 1559
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELK--NLDKNLNKDEEKIN------NSNNKI--KILEQQIKDLNDKLKKNK---DKIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1560 ELQSaydGAKKMAHQLKRKchhltcdlEDTCVLLENQQSRnheLEKKQKKFDLQLAQALGESVFEKGLREKVTQENtsvr 1639
Cdd:TIGR04523 100 KLNS---DLSKINSEIKND--------KEQKNKLEVELNK---LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKY---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1640 welgqlqqqlkqkeqeaSQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLR 1719
Cdd:TIGR04523 162 -----------------NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1720 QRFElEIERMKQMHQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMVLHEKQ-DLE---GLIGTLCDQIghrdf 1795
Cdd:TIGR04523 225 KQNN-QLKDNIEKKQQEINEKTTEISNTQT-------QLN-QLKDEQNKIKKQLSEKQkELEqnnKKIKELEKQL----- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1796 dvekrlrrdlrrtHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRN 1875
Cdd:TIGR04523 291 -------------NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1876 KSLVDEQLYrlqfEKADLLKRIDEDQDDLNELMQKHKDliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEY 1955
Cdd:TIGR04523 358 NSEKQRELE----EKQNEIEKLKKENQSYKQEIKNLES----------QINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1956 LEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSqyyQRRLEELKA 2034
Cdd:TIGR04523 424 LEKEIERlKETIIKNNSEIKDLTNQDSVKELIIKNLD----NTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEK 496
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 970949420 2035 DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNK 549
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1403-2288 |
1.51e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKS-EKLRNELRQNTDLLESKIADLTSDLAderfkgdVACQVLESERAERLQAFREVQELKsk 1481
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTvSQLRSELREAKRMYEDKIEELEKQLV-------LANSELTEARTERDQFSQESGNLD-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 hEQVQKKLGDVNKQ-----LEEAQQKiQLNDLERNPTGGADEWQMRFDCAQMENEflrkRLQQCEERLDSEltARKELEQ 1556
Cdd:pfam15921 377 -DQLQKLLADLHKRekelsLEKEQNK-RLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE--CQGQMER 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1557 KLGELQSAYDGAKKMAhqlkrkchHLTCDLEDTCVLL----ENQQSRNHELEKKQKKFDlQLAQALGESvfEKGLrEKVT 1632
Cdd:pfam15921 449 QMAAIQGKNESLEKVS--------SLTAQLESTKEMLrkvvEELTAKKMTLESSERTVS-DLTASLQEK--ERAI-EATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1633 QENTSVRwelgqlqqqlkqkeqeaSQLKQQVEMLQDHKREllgspslGENcvaglkerlwkLESSALEQQKIQSQQENTI 1712
Cdd:pfam15921 517 AEITKLR-----------------SRVDLKLQELQHLKNE-------GDH-----------LRNVQTECEALKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1713 KQLEQLRQrfelEIERMKQM-HQKDREDQEEELEdvrqscqkrlhqlEMQLEQEYEEKQMVLHEKQDLEgligtlcdqig 1791
Cdd:pfam15921 562 KVIEILRQ----QIENMTQLvGQHGRTAGAMQVE-------------KAQLEKEINDRRLELQEFKILK----------- 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1792 hrdfdvEKRLRRdLRRTHALLSDVQL----LLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1865
Cdd:pfam15921 614 ------DKKDAK-IRELEARVSDLELekvkLVNAGSERLRAVKdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNK 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1866 HSELEnMTRNKslvdeqlYRLQFEKADllkridedqddlNELMQKHKDLIAQSAADiGQIQELQLQLEEAKKEKhklQEQ 1945
Cdd:pfam15921 687 SEEME-TTTNK-------LKMQLKSAQ------------SELEQTRNTLKSMEGSD-GHAMKVAMGMQKQITAK---RGQ 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1946 LQVAQMRIEYLEQSTVDraivsrqeavicdlENKTefqkvqiKRFevlvirLRDSLIKMGEELSQAATSESQ---QRESS 2022
Cdd:pfam15921 743 IDALQSKIQFLEEAMTN--------------ANKE-------KHF------LKEEKNKLSQELSTVATEKNKmagELEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2023 QYYQRRLEELKADMEELVQREAEASRRCMELEKYvEELAAVRQTLQTDLETS------IRRIADLQAALEEVASSDSDTE 2096
Cdd:pfam15921 796 RSQERRLKEKVANMEVALDKASLQFAECQDIIQR-QEQESVRLKLQHTLDVKelqgpgYTSNSSMKPRLLQPASFTRTHS 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2097 SVQTAVDCGSSGRKEMDNVSILSSQPEGSLQSWLSCTLSL-----ATDTMRTPSRQSATSSRILSPRINEEAgdterTQS 2171
Cdd:pfam15921 875 NVPSSQSTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVineepTVQLSKAEDKGRAPSLGALDDRVRDCI-----IES 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2172 ALALSRARSTNVHSKTSGDKpVSPHFVRRQKYCHFGDGEVLAVQRKSTERLEPASSPLASRSTNTSPlsrEKLPSPSaAL 2251
Cdd:pfam15921 950 SLRSDICHSSSNSLQTEGSK-SSETCSREPVLLHAGELEDPSSCFTFPSTASPSVKNSASRSFHSSP---KKSPVHS-LL 1024
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 970949420 2252 SEFVEGLRRKRAQRGQGSTL----GLEDWPTLPIyQTTGAS 2288
Cdd:pfam15921 1025 TSSAEGSIGSSSQYRSAKTIhspdSVKDSQSLPI-ETTGKT 1064
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1656-2098 |
1.52e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.52 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1656 ASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES------SALEQQKIQSQQENtiKQLEQLRQRFELEIERM 1729
Cdd:PRK02224 281 VRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDrdeelrDRLEECRVAAQAHN--EEAESLREDADDLEERA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1730 KQMHQK----------------DREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghr 1793
Cdd:PRK02224 359 EELREEaaeleseleeareaveDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL--- 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1794 dfdveKRLRRDLRRTHALLsdvqlllgtmEDGKTSVSKEELEKvhSQLEQSEAKCEEALKTQKVLTADLESMHSELEN-M 1872
Cdd:PRK02224 436 -----RTARERVEEAEALL----------EAGKCPECGQPVEG--SPHVETIEEDRERVEELEAELEDLEEEVEEVEErL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1873 TRNKSLV--DEQLYRLQfEKADLLK--------RIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKL 1942
Cdd:PRK02224 499 ERAEDLVeaEDRIERLE-ERREDLEeliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAEL 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1943 QEQLQVAQMRIEYLEqstvdraivsRQEAVICDLENktefqkvqikrfevlvirLRDSLIKMGEELSQAATSESQQRESS 2022
Cdd:PRK02224 578 NSKLAELKERIESLE----------RIRTLLAAIAD------------------AEDEIERLREKREALAELNDERRERL 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2023 QYYQRRLEELKAD-----MEELVQREAEASRRCMELEKYVEELAAVRQTLQTD---LETSIRRIADLQAALEEVASSDSD 2094
Cdd:PRK02224 630 AEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVEA 709
|
....
gi 970949420 2095 TESV 2098
Cdd:PRK02224 710 LEAL 713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1591-2086 |
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 970949420 1591 VLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1670
Cdd:COG4717 46 MLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1671 R--ELLGSPSLGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR 1748
Cdd:COG4717 126 QllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1749 QSCQkrlhqlemQLEQEYEEKQMVLHE-KQDLEGLigtlcdQIGHRDFDVEKRLRRdLRRTHALLSDVQLLLGTMEDGKT 1827
Cdd:COG4717 206 QRLA--------ELEEELEEAQEELEElEEELEQL------ENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1828 SVskeelekvhsqleqseakceeaLKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQfekaDLLKRIDEDQDDLNEL 1907
Cdd:COG4717 271 LI----------------------LTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ----ALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1908 MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEylEQSTVDRAIVSRQEAVICDLENKTEFQKVQi 1987
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAGVEDEEELRAALEQAEEYQELK- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1988 KRFEVLVIRLRDSLIKMGEELsqAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEK--YVEELAAVRQ 2065
Cdd:COG4717 402 EELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQELE 479
|
490 500
....*....|....*....|.
gi 970949420 2066 TLQTDLETSIRRIADLQAALE 2086
Cdd:COG4717 480 ELKAELRELAEEWAALKLALE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1399-1860 |
2.03e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1399 TIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvacqvlesERAERLQAFREVQEL 1478
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELR------------EELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1479 KSKHEQVQKKLGDVNKQLEEAQQKIQ-LNDLERnptggadewqmrfDCAQMENEFLRKRLQQCEERLDSELTARKELEQ- 1556
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEeLRELEE-------------ELEELEAELAELQEELEELLEQLSLATEEELQDl 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1557 --KLGELQSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQE 1634
Cdd:COG4717 198 aeELEELQQRLAELEEELEEAQEELEELEEELEQ----LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1635 N-----------TSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK-RELLGSPSLGENcvaGLKERLWKLESSALEQQ 1702
Cdd:COG4717 274 TiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEElEELLAALGLPPD---LSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1703 KIQSQQENTIKQLEQlrQRFELEIER-MKQMHQKDREDQEEELEDVRQSCQ--KRLHQLEMQLEQEYEEKQMVL--HEKQ 1777
Cdd:COG4717 351 ELLREAEELEEELQL--EELEQEIAAlLAEAGVEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLeaLDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1778 DLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGktsvskEELEKVHSQLEQSEAKCEEALKTQKV 1857
Cdd:COG4717 429 ELEEELEELEEEL--------EELEEELEELREELAELEAELEQLEED------GELAELLQELEELKAELRELAEEWAA 494
|
...
gi 970949420 1858 LTA 1860
Cdd:COG4717 495 LKL 497
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1541-2087 |
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 970949420 1541 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTcdLEDTCVLLENQ--QSRNHELEKKQKKFDLQLAQAL 1618
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELE--EEYLLYLDYLKlnEERIDLLQELLRDEQEEIESSK 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1619 GESVFEKglrEKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspSLGENCVAGLKERLWKLESSA 1698
Cdd:pfam02463 258 QEIEKEE---EKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK----VDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1699 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEE---ELEDVRQSCQKRLHQLEMQLEQEYEEKQMV--L 1773
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEEllaKKKLESERLSSAAKLKEEELELKSEEEKEAqlL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1774 HEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKT-SVSKEELEKVHSQLEQSEAKCEEAL 1852
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDElELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1853 KTQKVLTAD-LESMHSELENMtrNKSLVDEQLYRLQFEKADLLKRIDE-DQDDLNELMQKHKDLIAQSAADIGQIQELQL 1930
Cdd:pfam02463 491 SRQKLEERSqKESKARSGLKV--LLALIKDGVGGRIISAHGRLGDLGVaVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1931 QLEEAKKEKHKLQEQLQVAQMRIeyleqstVDRAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ 2010
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPL-------KSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESA 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 2011 AATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:pfam02463 642 KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLE 718
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1411-2098 |
2.74e-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: 62.93 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1411 ELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDL--ADERFKGDVA-CQVLESER--------------AERLQAFR 1473
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaADAAVAKDRSeLEALEDQHgafldadietaaadQEQLPSWQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1474 -EVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLnDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLdseltaRK 1552
Cdd:pfam12128 354 sELENLEERLKALTGKHQDVTAKYNRRRSKIKE-QNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL------RE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1553 ELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDlEDTCVLLENQQSRNHELEKKQKK-----FDLQLAQALGESVFEKGL 1627
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT-PELLLQLENFDERIERAREEQEAanaevERLQSELRQARKRRDQAS 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1628 rEKVTQENTSVRWELGQLQQQLKQKEQEASQL----KQQVEMLQDH-----KRELLG----SPSLGENCVAG-------- 1686
Cdd:pfam12128 506 -EALRQASRRLEERQSALDELELQLFPQAGTLlhflRKEAPDWEQSigkviSPELLHrtdlDPEVWDGSVGGelnlygvk 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1687 -----------------LKERLWKLESSALEQQKIQSQQEntiKQLEQLRQRFE---LEIERMKQMHQKDREDQeEELED 1746
Cdd:pfam12128 585 ldlkridvpewaaseeeLRERLDKAEEALQSAREKQAAAE---EQLVQANGELEkasREETFARTALKNARLDL-RRLFD 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1747 VRQSCQKRLHQlemqleQEYEEKQMVLHEKQDLEGLIGTLcdQIGHRDFDVEKRlRRDLRRTHALLSDVQLLLGTMEDGK 1826
Cdd:pfam12128 661 EKQSEKDKKNK------ALAERKDSANERLNSLEAQLKQL--DKKHQAWLEEQK-EQKREARTEKQAYWQVVEGALDAQL 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1827 TSVsKEELEKVHSQLEQSEAKCEEALKT---------QKV--LTADLESMHSELENMTRNKSLVDE--QLYRLQF--EKA 1891
Cdd:pfam12128 732 ALL-KAAIAARRSGAKAELKALETWYKRdlaslgvdpDVIakLKREIRTLERKIERIAVRRQEVLRyfDWYQETWlqRRP 810
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1892 DLLKRIDEDQDDLNELMQkhkDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYL----EQSTVDRAIVS 1967
Cdd:pfam12128 811 RLATQLSNIERAISELQQ---QLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkEDANSEQAQGS 887
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1968 RQEAVIC--DLENKTEFQKVQIKRFevlvIRLRDSLI--KMGEELsqAATSESqQRESSQYYQRRLEELKADMEELVQRE 2043
Cdd:pfam12128 888 IGERLAQleDLKLKRDYLSESVKKY----VEHFKNVIadHSGSGL--AETWES-LREEDHYQNDKGIRLLDYRKLVPYLE 960
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2044 AEASRRCMELEKYVEELAAVRQTLQTD----LETSIRRIADLQAALEEVASSDSDTESV 2098
Cdd:pfam12128 961 QWFDVRVPQSIMVLREQVSILGVDLTEfydvLADFDRRIASFSRELQREVGEEAFFEGV 1019
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1406-1873 |
5.92e-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: 61.73 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1406 RAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDladerfKGDVACQVLESERAERLqAFREVQELKSKHEQV 1485
Cdd:pfam01576 632 REKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSS------KDDVGKNVHELERSKRA-LEQQVEEMKTQLEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1486 QKKLG---------DVNKQLEEAQqkiqlndLERnptggadEWQMRFDCAQMENEFLRKRLQQCEERLDSE-------LT 1549
Cdd:pfam01576 705 EDELQatedaklrlEVNMQALKAQ-------FER-------DLQARDEQGEEKRRQLVKQVRELEAELEDErkqraqaVA 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1550 ARKELEQKLGELQSAYDGA-----------KKMAHQLKrkchHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQAL 1618
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAAnkgreeavkqlKKLQAQMK----DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQ 846
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1619 GESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgencvagLKERLWKLESSA 1698
Cdd:pfam01576 847 EDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTEL-------LNDRLRKSTLQV 919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1699 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQkdredqeeELEDVRQSCQK--------RLHQLEMQLEQEYEEKQ 1770
Cdd:pfam01576 920 EQLTTELAAERSTSQKSESARQQLERQNKELKAKLQ--------EMEGTVKSKFKssiaaleaKIAQLEEQLEQESRERQ 991
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1771 MVlhekqdlegligtlcdqighrdfdvekrlRRDLRRTHALLSDVqLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEE 1850
Cdd:pfam01576 992 AA-----------------------------NKLVRRTEKKLKEV-LLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEE 1041
|
490 500
....*....|....*....|...
gi 970949420 1851 ALKTQKVLTADLESMHSELENMT 1873
Cdd:pfam01576 1042 AEEEASRANAARRKLQRELDDAT 1064
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1885-2087 |
6.34e-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: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1885 RLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdra 1964
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1965 ivsrqeavicDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREA 2044
Cdd:COG4942 98 ----------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 970949420 2045 EASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAE 210
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1403-2081 |
6.80e-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: 61.62 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1482
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1483 EQVQKKLGDVNKQLEEAQQKiqLNDLERnptggadewqmRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQ------ 1556
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEE--YDRVEK-----------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAsiqgvh 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1557 ----KLGELQSAYDGAKKMAhqLKRKCHHLTCDLEDTCV-----LLENQQSRNHEL---EKKQKKFDLQLAQALGESVFE 1624
Cdd:TIGR02169 525 gtvaQLGSVGERYATAIEVA--AGNRLNNVVVEDDAVAKeaielLKRRKAGRATFLplnKMRDERRDLSILSEDGVIGFA 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1625 KGLREKVTQENTSVRWELGQLQQqlkqkeqeasqlkqqVEMLqDHKRELLGspslgencvaglKERLWKLESSALEQQKI 1704
Cdd:TIGR02169 603 VDLVEFDPKYEPAFKYVFGDTLV---------------VEDI-EAARRLMG------------KYRMVTLEGELFEKSGA 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1705 QSQQENTIKQLEQLRQRFELEIERMKqmhqkdreDQEEELEDVRQSCQKRLHQLEMQLEQeyeekqmVLHEKQDLEGLIG 1784
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLR--------ERLEGLKRELSSLQSELRRIENRLDE-------LSQELSDASRKIG 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1785 TLCDQIghrdfdveKRLRRDLRRTHALLSDVQLLLGTMEDGKTSV--SKEELEKVHSQLEQSEAKCEEALktqkvltADL 1862
Cdd:TIGR02169 720 EIEKEI--------EQLEQEEEKLKERLEELEEDLSSLEQEIENVksELKELEARIEELEEDLHKLEEAL-------NDL 784
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1863 ESM--HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKH 1940
Cdd:TIGR02169 785 EARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1941 KLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTEFQKVQIKRFEVLVIRLRDSLIKMGEELSQ------AAT 2013
Cdd:TIGR02169 865 ELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedpkgEDE 944
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 2014 SESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADL 2081
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1684-2190 |
1.56e-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: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1684 VAGLKERLwkLESSAL-EQQKIQSQQenTIKQLEQLRQRFELEIERMKQMHQKDREDQEeeleDVRQSCQKRLHQLEmql 1762
Cdd:pfam15921 87 VKDLQRRL--NESNELhEKQKFYLRQ--SVIDLQTKLQEMQMERDAMADIRRRESQSQE----DLRNQLQNTVHELE--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1763 eqeyEEKQMvlheKQDLEGLIGTLCDQighrdfdvekrLRRDLRRTHALLSDVQLLLGTMEDGKTsvskeelEKVHSQLE 1842
Cdd:pfam15921 156 ----AAKCL----KEDMLEDSNTQIEQ-----------LRKMMLSHEGVLQEIRSILVDFEEASG-------KKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1843 QSeakceealktqkvlTADLESMHSELENMTRNkslVDEQLYRLQ---FEKADLLKRI-DEDQDDLNELMQKHKDLIAQ- 1917
Cdd:pfam15921 210 MS--------------TMHFRSLGSAISKILRE---LDTEISYLKgriFPVEDQLEALkSESQNKIELLLQQHQDRIEQl 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1918 -SAADIgQIQELQLQLEEAKKEKHKLQEQLQVAQmrieylEQSTVDRAIVSRQeavICDLEN-----KTEFQKVQiKRFE 1991
Cdd:pfam15921 273 iSEHEV-EITGLTEKASSARSQANSIQSQLEIIQ------EQARNQNSMYMRQ---LSDLEStvsqlRSELREAK-RMYE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1992 VLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEelvQREAEASrrcmeLEKYVEELAAVRQT----- 2066
Cdd:pfam15921 342 DKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH---KREKELS-----LEKEQNKRLWDRDTgnsit 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2067 ---LQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSgrKEMDNVSILSSQPEGSLQSWLSCTLSLATDTMRT 2143
Cdd:pfam15921 414 idhLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKN--ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTL 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 970949420 2144 PSRQSATSSriLSPRINEEAGDTERTQSALALSRAR-----STNVHSKTSGD 2190
Cdd:pfam15921 492 ESSERTVSD--LTASLQEKERAIEATNAEITKLRSRvdlklQELQHLKNEGD 541
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1831-2087 |
1.99e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1910
Cdd:COG4372 51 REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1911 HKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKTEFQKVQIKR- 1989
Cdd:COG4372 131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIe 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1990 FEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQT 2069
Cdd:COG4372 211 SLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
250
....*....|....*...
gi 970949420 2070 DLETSIRRIADLQAALEE 2087
Cdd:COG4372 291 AALELKLLALLLNLAALS 308
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1404-1952 |
7.19e-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: 58.19 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1404 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------LESKIADLTSDLADERfkgdVACQvleseraerlqafREVQ 1476
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLqdenlkeLIEKKDHLTKELEDIK----MSLQ-------------RSMS 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1477 ELKSKHEQVQKKLGDVNKQLEEAQQKIQlndlERNPTGGADEW---QMRFDCAQMEnEFLRKRLQQCEERLDSELTARKE 1553
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEEKEAQME----ELNKAKAAHSFvvtEFEATTCSLE-ELLRTEQQRLEKNEDQLKIITME 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1554 LEQKLGELQSAydgaKKMAHQLKRKCHHLTCDL-EDTCVLLENQQSRNHELEKKQKKFDLQ-LAQALGESVFEkgLREKV 1631
Cdd:pfam05483 386 LQKKSSELEEM----TKFKNNKEVELEELKKILaEDEKLLDEKKQFEKIAEELKGKEQELIfLLQAREKEIHD--LEIQL 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1632 TQENTSVRWelgqlqqqlkqkeqeasQLKQQVEMLQDHKRELLGSPSLGENCvaglkeRLWKLESSALEQQ------KIQ 1705
Cdd:pfam05483 460 TAIKTSEEH-----------------YLKEVEDLKTELEKEKLKNIELTAHC------DKLLLENKELTQEasdmtlELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1706 SQQENTIKQLEQlRQRFELEIERMKQMHQKDREdqeeELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGT 1785
Cdd:pfam05483 517 KHQEDIINCKKQ-EERMLKQIENLEEKEMNLRD----ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKI 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1786 LCDQIGHRDFDVEKRLR--RDLRRTHALLSDVqlllGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTADL 1862
Cdd:pfam05483 592 LENKCNNLKKQIENKNKniEELHQENKALKKK----GSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1863 ESMHSELENMTRNKSLVDEQLyRLQFEkadLLKRIDEDQDDLNELMQKHK---DLIA----------------QSAADIG 1923
Cdd:pfam05483 668 ISEEKLLEEVEKAKAIADEAV-KLQKE---IDKRCQHKIAEMVALMEKHKhqyDKIIeerdselglyknkeqeQSSAKAA 743
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 970949420 1924 QIQEL------------QLQLEEAKKEKHKLQEQLQVAQMR 1952
Cdd:pfam05483 744 LEIELsnikaellslkkQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1425-2011 |
9.02e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 9.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1425 LRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQ 1504
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1505 LNDLERnptggadewqmrfdcaqmENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTC 1584
Cdd:COG4717 127 LLPLYQ------------------ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1585 ----DLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGE--SVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASq 1658
Cdd:COG4717 189 ateeELQDLAEELEELQQRLAELEEELEEAQEELEELEEEleQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1659 lkqqvemLQDHKRELLGSPSLgencVAGLkerLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE 1738
Cdd:COG4717 268 -------LLSLILTIAGVLFL----VLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1739 DQEEELEDVRQSCQKrLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGhrdfDVEKRLRRDLRRthallsdVQLl 1818
Cdd:COG4717 334 LSPEELLELLDRIEE-LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE----ELRAALEQAEEY-------QEL- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1819 lgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKtqkvlTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRID 1898
Cdd:COG4717 401 ------------KEELEELEEQLEELLGELEELLE-----ALDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1899 --EDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLE--EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavic 1974
Cdd:COG4717 464 qlEEDGELAELLQELEELKAELRELAEEWAALKLALEllEEAREEYREERLPPVLERASEYFSRLTDGR----------- 532
|
570 580 590
....*....|....*....|....*....|....*..
gi 970949420 1975 dlenkteFQKVQIKRFEVLVIRLRDSLIKMGEELSQA 2011
Cdd:COG4717 533 -------YRLIRIDEDLSLKVDTEDGRTRPVEELSRG 562
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1798-2088 |
1.23e-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: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1798 EKRLRRDLRRTHALlsdvqlllgtmedGKTSVSK-EELEKVHSQLEQSEAKCEEALKTQKVLTADLE---SMHSELENMT 1873
Cdd:COG4913 591 EKDDRRRIRSRYVL-------------GFDNRAKlAALEAELAELEEELAEAEERLEALEAELDALQerrEALQRLAEYS 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1874 RNKSLVDEQLYRLQfEKADLLKRIDEDQDDLNELMQKHKDLIAQsaadigqIQELQLQLEEAKKEKHKLQEQLQVAQMRI 1953
Cdd:COG4913 658 WDEIDVASAEREIA-ELEAELERLDASSDDLAALEEQLEELEAE-------LEELEEELDELKGEIGRLEKELEQAEEEL 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1954 EYLeQSTVDRAIVSRQEAVICDLENKteFQKVQI-KRFEVLVIRLRDSLIKMGEELSQAATS-ESQQR------------ 2019
Cdd:COG4913 730 DEL-QDRLEAAEDLARLELRALLEER--FAAALGdAVERELRENLEERIDALRARLNRAEEElERAMRafnrewpaetad 806
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 2020 -----ESSQYYQRRLEELKADmeELVQREAEASRRCMELEKyvEELAAVRQTLQTDLETSIRRIADLQAALEEV 2088
Cdd:COG4913 807 ldadlESLPEYLALLDRLEED--GLPEYEERFKELLNENSI--EFVADLLSKLRRAIREIKERIDPLNDSLKRI 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1405-1914 |
1.24e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1405 LRAKEEELTTLRRKLEksEKLRNELRQNTDLLESKIADLTSDLadERFkgdvacqvlESERAERLQAFREVQELKSKHEQ 1484
Cdd:PRK02224 182 LSDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEI--ERY---------EEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1485 VQKKLGDVNKQLEEAQQKI-------------------QLNDLERNPTGGADEwqMRFDCAQMEN-----EFLRKRLQQC 1540
Cdd:PRK02224 249 RREELETLEAEIEDLRETIaeterereelaeevrdlreRLEELEEERDDLLAE--AGLDDADAEAvearrEELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1541 EERLDselTARKELEQKLGELQSAYDGAKKM---AHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKK----QKKF--- 1610
Cdd:PRK02224 327 RDRLE---ECRVAAQAHNEEAESLREDADDLeerAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRERFgda 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1611 --DLQLAQALGESVFEKglREKVTQENTSVRWELgqlqqqlkqkEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLK 1688
Cdd:PRK02224 404 pvDLGNAEDFLEELREE--RDELREREAELEATL----------RTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1689 ERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELE--IERMKQMHQ---KDREDQEEELEDVRQSCQ---KRLHQLEM 1760
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEdrIERLEERREdleELIAERRETIEEKRERAEelrERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1761 QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEK--RLRRDLRRTHALLSDVQLL------LGTMEDGKTSVSKE 1832
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLrekreaLAELNDERRERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1833 ELEKvHSQLEQS--EAKCEEAlktqkvlTADLESMHSELENmtrnkslVDEQLYRLQFEKADLLKRI---DEDQDDLNEL 1907
Cdd:PRK02224 632 KRER-KRELEAEfdEARIEEA-------REDKERAEEYLEQ-------VEEKLDELREERDDLQAEIgavENELEELEEL 696
|
....*..
gi 970949420 1908 MQKHKDL 1914
Cdd:PRK02224 697 RERREAL 703
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1713-2092 |
1.62e-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: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1713 KQLEQLRqRFELEIE-RMKQMHQKDREDQE--EELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEK---QDLEGLIGTL 1786
Cdd:pfam05483 85 KEAEKIK-KWKVSIEaELKQKENKLQENRKiiEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnatRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1787 CDQIGHRDFDVEKRlRRDLRRTHA-LLSDVQLLLGTMEDGKTSVSKEELEkVHSQLEQSEAKCEEALktqkvltadlESM 1865
Cdd:pfam05483 164 CARSAEKTKKYEYE-REETRQVYMdLNNNIEKMILAFEELRVQAENARLE-MHFKLKEDHEKIQHLE----------EEY 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1866 HSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK-------DLIAQSAADIGQIQELQLQLEEAKKE 1938
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKlqdenlkELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1939 KHKLQEQLQVAQMRIEYL--------EQSTVDRA----IVSRQEAVICDLEnktEFQKVQIKRFEvlviRLRDSLIKMGE 2006
Cdd:pfam05483 312 QKALEEDLQIATKTICQLteekeaqmEELNKAKAahsfVVTEFEATTCSLE---ELLRTEQQRLE----KNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2007 ELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALE 2086
Cdd:pfam05483 385 ELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK----QFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
....*.
gi 970949420 2087 EVASSD 2092
Cdd:pfam05483 461 AIKTSE 466
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1403-1565 |
1.70e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQ----------------NTDLLESKIADLTSDLADERfKGDVACQVLEsERA 1466
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEREIAELEAELERLD-ASSDDLAALE-EQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1467 ERLQAfrEVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQM-ENEFLRKRLQQCEERLD 1545
Cdd:COG4913 695 EELEA--ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfAAALGDAVERELRENLE 772
|
170 180
....*....|....*....|....
gi 970949420 1546 SEL----TARKELEQKLGELQSAY 1565
Cdd:COG4913 773 ERIdalrARLNRAEEELERAMRAF 796
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1403-1910 |
1.73e-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: 56.95 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSD---LADERFKGDVACQVLESERAERLQafrEVQELK 1479
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEnseKQRELEEKQNEIEKLKKENQSYKQ---EIKNLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1480 SKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewqmrfdcaQMENEFlrKRLQQCEERLDSELtarKELEQKLG 1559
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---------------LLEKEI--ERLKETIIKNNSEI---KDLTNQDS 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1560 ELQSAYDGAKKMAHQLKRKchhltcdLEDtcvlLENQ-QSRNHELEKKQKKFDLQlaqalgesvfekglrekvtqentsv 1638
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQ-------LKV----LSRSiNKIKQNLEQKQKELKSK------------------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1639 rwelgqlqqqlkqkeqeasqlKQQVEMLQDHKRELlgspslgENCVAGLKErlwKLESSALEQQKIqsqqENTIKQLEQL 1718
Cdd:TIGR04523 495 ---------------------EKELKKLNEEKKEL-------EEKVKDLTK---KISSLKEKIEKL----ESEKKEKESK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1719 RQRFELEIERMKQMHQKdredqeEELEDVRQSCQKRLHQLEMQ---LEQEYEEKQMVLHEKQDlegLIGTLCDQIGHRDF 1795
Cdd:TIGR04523 540 ISDLEDELNKDDFELKK------ENLEKEIDEKNKEIEELKQTqksLKKKQEEKQELIDQKEK---EKKDLIKEIEEKEK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1796 DVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLE------------ 1863
Cdd:TIGR04523 611 KISS-LEKELEKAKKENEKLSSIIKNIKSKKNKL-KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiielmkdwlke 688
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 970949420 1864 -SMHSE--LENMTRNKSLvdEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1910
Cdd:TIGR04523 689 lSLHYKkyITRMIRIKDL--PKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1387-2061 |
2.13e-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: 56.98 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1387 QLLGSLQPLLSATIGTEQLRAKEEELTTLRRKLEKSEKlrnelRQNTDLLESKIADLTSDLADerfkgdvacqVLESERA 1466
Cdd:TIGR00606 455 ELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEK-----NSLTETLKKEVKSLQNEKAD----------LDRKLRK 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1467 ErlqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNdlernptggadEWQMRFDCAQMENEFLRKRlqQCEERLDS 1546
Cdd:TIGR00606 520 L-----DQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI-----------KSRHSDELTSLLGYFPNKK--QLEDWLHS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1547 ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLE-------DTCVlLENQQSRNHELEKKQKKFDLQLAQALG 1619
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSsyedklfDVCG-SQDEESDLERLKEEIEKSSKQRAMLAG 660
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1620 ESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgENCVAGLKERLWKLESSAL 1699
Cdd:TIGR00606 661 ATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKST-------ESELKKKEKRRDEMLGLAP 733
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1700 EQQKIQSQQENTIKQLEQLRQRFELEIERMKQmhqkDREDQEEELEDVR------QSCQKRLHQLEMQLEQEYEEKQMVL 1773
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN----DIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIA 809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1774 HEKQDLEGLIGTLCDQighrdfDVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVskEELEKVHSQLEQSEAKCEEALK 1853
Cdd:TIGR00606 810 QQAAKLQGSDLDRTVQ------QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI--QHLKSKTNELKSEKLQIGTNLQ 881
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1854 TQKVLTADLESMHSELENM------TRNKSLVDEQ-LYRLQFEKADLLKRIDED----QDDLNELMQKHKDLIAQSAADI 1922
Cdd:TIGR00606 882 RRQQFEEQLVELSTEVQSLireikdAKEQDSPLETfLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGYMKDIE 961
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1923 GQIQE---------------LQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTV---DRAIVSRQEAVICDLENKTEFQK 1984
Cdd:TIGR00606 962 NKIQDgkddylkqketelntVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERwlqDNLTLRKRENELKEVEEELKQHL 1041
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1985 VQIKRFEVLviRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELA 2061
Cdd:TIGR00606 1042 KEMGQMQVL--QMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREMMIVMRTTELV 1116
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1829-2088 |
2.59e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1829 VSKEELEKVHSQLEQSEaKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL- 1907
Cdd:PRK03918 142 ESDESREKVVRQILGLD-DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1908 --MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraivsrqeavICDLENKTEFQKv 1985
Cdd:PRK03918 221 eeLEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKE-------------IEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1986 QIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEEL---KADMEELVQREAEASRRCMELEKYVEELAA 2062
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELeekEERLEELKKKLKELEKRLEELEERHELYEE 366
|
250 260 270
....*....|....*....|....*....|.
gi 970949420 2063 VRQtLQTDLET-----SIRRIADLQAALEEV 2088
Cdd:PRK03918 367 AKA-KKEELERlkkrlTGLTPEKLEKELEEL 396
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1704-2085 |
2.98e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 55.67 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1704 IQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQEEELEDVRQSCQkRLHQLEMQLEQEYEEKQMVLHEKQDLE 1780
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAanrQREKEKERYKRDREQWERQRRELESRVA-ELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1781 GLIGTLCDQIGHRDFDVEKRLRRdlrrthaLLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEAKCEEALKTQKVL 1858
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRE-------LEEDIKTLTQRVLERETELErmKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1859 TADLESMHSELENMTRNKSLVDEQLYRLQfekadllkridedqDDLNELMQKhkdliaqsaadIGQIQELQLQLEEAKKE 1938
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQ--------------DTITTLTQK-----------LTTAHRKEAENEALLEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1939 KHKLQEQLQVAQMRIEYLEQSTvdRAIVSRQEAVICDLeNKTEFQKVQikrfevLVIRLRDSLIKMGEELSQAATSESQQ 2018
Cdd:pfam07888 239 LRSLQERLNASERKVEGLGEEL--SSMAAQRDRTQAEL-HQARLQAAQ------LTLQLADASLALREGRARWAQERETL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2019 RESSQYYQRRLEELKAD---MEELVQREAeasrrcMELEKYVEELAAVRQTLQTDLETSIRRIADLQAAL 2085
Cdd:pfam07888 310 QQSAEADKDRIEKLSAElqrLEERLQEER------MEREKLEVELGREKDCNRVQLSESRRELQELKASL 373
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1925-2179 |
3.79e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 55.42 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1925 IQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIV----------SRQEAVICDLEN-KTEFQKVQiKRFEVL 1993
Cdd:pfam05701 79 IEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVaakaqlevakARHAAAVAELKSvKEELESLR-KEYASL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1994 VIRlRDSLIKMGEElsqaATSESQQREssqyyqRRLEELKAD----MEEL-----VQREAEASRRC-------------- 2050
Cdd:pfam05701 158 VSE-RDIAIKRAEE----AVSASKEIE------KTVEELTIEliatKESLesahaAHLEAEEHRIGaalareqdklnwek 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2051 ------MELEKYVEELAAVRQtLQTDLETSIRRIADLQA--------ALEEVASSDSDTE----SVQTAVDcgsSGRKEM 2112
Cdd:pfam05701 227 elkqaeEELQRLNQQLLSAKD-LKSKLETASALLLDLKAelaaymesKLKEEADGEGNEKktstSIQAALA---SAKKEL 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 2113 DNV--SILSSQPE--------GSLQSWLSCTLS-LATdtmrtpSRQSATSSRILSPRINEEagdTERTQSALALSRAR 2179
Cdd:pfam05701 303 EEVkaNIEKAKDEvnclrvaaASLRSELEKEKAeLAS------LRQREGMASIAVSSLEAE---LNRTKSEIALVQAK 371
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1832-2101 |
3.94e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1832 EELEKvhsQLEQSEAKCEEALKTQKvLTADLEsmhselenmtrnksLVDEQLYRLQFEKADllKRIDEDQDDLNELMQKH 1911
Cdd:COG1196 196 GELER---QLEPLERQAEKAERYRE-LKEELK--------------ELEAELLLLKLRELE--AELEELEAELEELEAEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1912 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlenktefqkvQIKRFE 1991
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------------------------DIARLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1992 VLVIRLRDSLIKMGEELSQAATSESQQREssqyyqrRLEELKADMEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDL 2071
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEA---EEELEEAEAELAEAEEALLEAEAELAEAE 378
|
250 260 270
....*....|....*....|....*....|
gi 970949420 2072 ETSIRRIADLQAALEEVASSDSDTESVQTA 2101
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1684-2173 |
4.20e-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: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1684 VAGLKERLWKLESSaLEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLE 1763
Cdd:pfam15921 233 ISYLKGRIFPVEDQ-LEALKSESQN-----KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1764 QEYEEKQMVLHEKQDLEGLIgtlcdqighrdfdveKRLRRDLRRTHALLSDvqlllgtmedgktsvSKEELEK--VHSQL 1841
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTV---------------SQLRSELREAKRMYED---------------KIEELEKqlVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1842 EQSEAKCEEALKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQFEKA------DLLKRideDQDDLNELMQKHKD 1913
Cdd:pfam15921 357 ELTEARTERDQFSQESgnLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTgnsitiDHLRR---ELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1914 LIA------------QSAADIG------QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAvicd 1975
Cdd:pfam15921 434 LLKamksecqgqmerQMAAIQGknesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER-TVSDLTASLQEK---- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1976 lENKTEFQKVQIKRFEVLV-IRLRD--SLIKMGEELSQAATSESQQRESSQYYQRRLEELKADME--------------- 2037
Cdd:pfam15921 509 -ERAIEATNAEITKLRSRVdLKLQElqHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnmtqlvgqhgrtaga 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2038 ---ELVQREAEASRRCMELEKYveelaavrQTLQTDLETSIR----RIADLQaaLEEVASSDSDTESVQTAVDCgssgRK 2110
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEF--------KILKDKKDAKIReleaRVSDLE--LEKVKLVNAGSERLRAVKDI----KQ 653
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 970949420 2111 EMDNVSILSSQPEGSLQSwLSCTLSLATDTMRTPSRQSATSSRILSPRINEEAGDTERTQSAL 2173
Cdd:pfam15921 654 ERDQLLNEVKTSRNELNS-LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1513-1899 |
4.25e-07 |
|
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: 55.83 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1513 TGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEdtcvl 1592
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA----- 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1593 lenqqsrnhELEKKQKKFDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHkre 1672
Cdd:TIGR02168 737 ---------RLEAEVEQLEERIAQLSKE-------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE--- 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1673 llgspslgencVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHqKDREDQEEELEDVRQSCQ 1752
Cdd:TIGR02168 798 -----------LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI-EELSEDIESLAAEIEELE 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1753 KRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIgHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME--------- 1823
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEEL-RELESKRSELRRELEELREKLAQLELRLEGLEvridnlqer 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1824 -DGKTSVSKEELEKVHSQLEQSEAKCEEALKT-QKVLTA----DLESMhSELENMTRNKSLVDEQLYRLQFEKADLLKRI 1897
Cdd:TIGR02168 945 lSEEYSLTLEEAEALENKIEDDEEEARRRLKRlENKIKElgpvNLAAI-EEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
..
gi 970949420 1898 DE 1899
Cdd:TIGR02168 1024 EE 1025
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1901-2089 |
4.92e-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: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1901 QDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAIVSRQEAvicdLEN 1978
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiAEAEAEIEERREE----LGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1979 KTEFQKVQIKRFEVLvirlrdSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVE 2058
Cdd:COG3883 91 RARALYRSGGSVSYL------DVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190
....*....|....*....|....*....|.
gi 970949420 2059 ELAAVRQTLQTDLETSIRRIADLQAALEEVA 2089
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAE 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1849-2084 |
7.81e-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: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1849 EEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAqsaadigQIQEL 1928
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1929 QLQLEEAKKEkhkLQEQLQVAQM--RIEYLE----QSTVDRAIVSRQ--EAVICDLENKTEFQKVQIKRfevlVIRLRDS 2000
Cdd:COG4942 96 RAELEAQKEE---LAELLRALYRlgRQPPLAlllsPEDFLDAVRRLQylKYLAPARREQAEELRADLAE----LAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2001 LIKMGEELSQAATSESQQRessqyyqRRLEELKADMEELVqreAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD 2080
Cdd:COG4942 169 LEAERAELEALLAELEEER-------AALEALKAERQKLL---ARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
....
gi 970949420 2081 LQAA 2084
Cdd:COG4942 239 AAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1813-2087 |
9.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.66 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1813 SDVQLLLGTMEDGKtsvsKEELEKVHSQLEQSEAKceEALKTQKVLTADLESMHSELENMTRNKSLVDEQLyrlqfEKAD 1892
Cdd:PRK02224 172 SDARLGVERVLSDQ----RGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-----DEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1893 L-LKRIDEDQDDLNELMQkhkdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLE--------QSTVDR 1963
Cdd:PRK02224 241 EvLEEHEERREELETLEA--------------EIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1964 AIVSRQEAVICDLENKTEF-------QKVQIKRFEVLVIRLRDSLIKMGEEL----SQAATSESQ---QRESSQYYQRRL 2029
Cdd:PRK02224 307 ADAEAVEARREELEDRDEElrdrleeCRVAAQAHNEEAESLREDADDLEERAeelrEEAAELESEleeAREAVEDRREEI 386
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970949420 2030 EELKADMEELVQREAEASRRCMELEKYVEELAAVRQ-------TLQTDLETSIRRIADLQAALEE 2087
Cdd:PRK02224 387 EELEEEIEELRERFGDAPVDLGNAEDFLEELREERDelrereaELEATLRTARERVEEAEALLEA 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1465-2116 |
9.28e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 9.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1465 RAERLQAfrEVQELKSKHEQVQK-KLGDVNKQLEEA-QQKIQ---LNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQ 1539
Cdd:pfam12128 242 EFTKLQQ--EFNTLESAELRLSHlHFGYKSDETLIAsRQEERqetSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1540 CEERLDSeLTARKELEQKLGELQSAYDgaKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKFDLQLAQALg 1619
Cdd:pfam12128 320 DRSELEA-LEDQHGAFLDADIETAAAD--QEQLPSWQSELENLEERLK---ALTGKHQDVTAKYNRRRSKIKEQNNRDI- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1620 eSVFEKGLREkvtQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLES 1696
Cdd:pfam12128 393 -AGIKDKLAK---IREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLksrLGELKLRLNQATATPELLLQLEN 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1697 SALEQQKIQSQQENTIKQLE-------QLRQRFELEIERMKQMHQKdredqeeeLEDVRQSCQKRLHQLEMQleqeyeeK 1769
Cdd:pfam12128 469 FDERIERAREEQEAANAEVErlqselrQARKRRDQASEALRQASRR--------LEERQSALDELELQLFPQ-------A 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1770 QMVLH----EKQDLEGLIGTLCD--QIGHRDFDVEKrlrrdlrrTHALLSDVQLLLGTMEDGKtSVSKEELEKVHSQLEQ 1843
Cdd:pfam12128 534 GTLLHflrkEAPDWEQSIGKVISpeLLHRTDLDPEV--------WDGSVGGELNLYGVKLDLK-RIDVPEWAASEEELRE 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1844 SEAKCEEALKTQKVLTADLESMHSELenmtrNKSLvDEQLYRLQFEKADlLKRIDEDQDDLNELMQKHKDLIAQSAADIG 1923
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQA-----NGEL-EKASREETFARTA-LKNARLDLRRLFDEKQSEKDKKNKALAERK 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1924 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQST-------------------VDRAIVSRQEAV-----ICDLENK 1979
Cdd:pfam12128 678 DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTekqaywqvvegaldaqlalLKAAIAARRSGAkaelkALETWYK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1980 TEFQKVQIKrfEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQR-----------RLEELKADMEEL------VQR 2042
Cdd:pfam12128 758 RDLASLGVD--PDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQEtwlqrrprlatQLSNIERAISELqqqlarLIA 835
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 970949420 2043 EAEASRRCMELEKYVEELAAVRQT-LQTDLETSIRRIADLQaaleEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2116
Cdd:pfam12128 836 DTKLRRAKLEMERKASEKQQVRLSeNLRGLRCEMSKLATLK----EDANSEQAQGSIGERLAQLEDLKLKRDYLS 906
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1870-2099 |
1.05e-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: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1870 ENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHK--DLIAQSAADIGQIQELQLQLEEAkkekhklQEQLQ 1947
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEA-------RAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1948 VAQMRIEYLEQ---STVDRAIVSRQEAVICDLenKTEFQKVQIKRFEvLVIRLRDSLIKMGEELSQAATSESQQRESSqy 2024
Cdd:COG3206 237 EAEARLAALRAqlgSGPDALPELLQSPVIQQL--RAQLAELEAELAE-LSARYTPNHPDVIALRAQIAALRAQLQQEA-- 311
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2025 yQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQT---LQTDLETSIRRIADLQAALEEV-ASSDSDTESVQ 2099
Cdd:COG3206 312 -QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARELYESLLQRLEEArLAEALTVGNVR 389
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1598-1879 |
2.06e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.20 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1598 SRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQ--DHKRELlg 1675
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqeERKREL-- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1676 sPSLGENCVAGLKERLWKLESSALEQQ----KIQSQQENTIKQ--LEQLRQR------FELEIERMKQMHQKDR------ 1737
Cdd:pfam17380 363 -ERIRQEEIAMEISRMRELERLQMERQqkneRVRQELEAARKVkiLEEERQRkiqqqkVEMEQIRAEQEEARQRevrrle 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1738 EDQEEELEDVRQSCQKRLHQLEM--QLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDv 1815
Cdd:pfam17380 442 EERAREMERVRLEEQERQQQVERlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEK- 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 1816 qlllgTMEDGKTSVSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRNKSLV 1879
Cdd:pfam17380 521 -----EMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEE-RSRLEAMEREREMM 578
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1403-1837 |
2.33e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTS----------------DLADERFKGDVACQVLESERA 1466
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsefyeEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1467 ERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMEN-----EFLRKRLQQCE 1541
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKlekelEELEKAKEEIE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1542 ERLdSELTARK-ELEQKLGELQSAYDGAKKMahqlKRKC---------HH-------LTCDLED---------------- 1588
Cdd:PRK03918 405 EEI-SKITARIgELKKEIKELKKAIEELKKA----KGKCpvcgrelteEHrkelleeYTAELKRiekelkeieekerklr 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1589 -------TCVLLENQQSRNH-------ELEKKQKKFDLQLAQALGESvFEKGLRE--KVTQENTSVRWELGQLQQQLKQK 1652
Cdd:PRK03918 480 kelreleKVLKKESELIKLKelaeqlkELEEKLKKYNLEELEKKAEE-YEKLKEKliKLKGEIKSLKKELEKLEELKKKL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1653 EQEASQLKQQVEMLQDHKRELLgspSLGENCVAGLKERLWKLES------------SALE-----QQKIQSQQENTIKQL 1715
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPfyneylelkdaeKELEreekeLKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1716 EQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVlheKQDLEGLigtlcdqigHRDF 1795
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKL---------KEEL 703
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 970949420 1796 DVEKRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKV 1837
Cdd:PRK03918 704 EEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKV 745
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1693-1958 |
2.64e-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: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1693 KLESSALEQQKIQSQQENTIKQLEQLRQR----------FELEIERMKQM--HQKDREDQEE--ELEDVRQSCQKRLHQL 1758
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARieeleedlhkLEEALNDLEARlsHSRIPEIQAElsKLEEEVSRIEARLREI 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1759 EMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKE------ 1832
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKErdelea 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1833 ELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkSLVDEQLYRLQFEKADLLKrIDEDQDDLNELMQKHK 1912
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-------SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIR 968
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 970949420 1913 DLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ 1958
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1409-2018 |
2.66e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 EEELTTLRRKLEKSEKLRNELRQNTDLLES---KIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQV 1485
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1486 QKklgdVNKQLEEAQQKIQLNDLERNPTGGADEWQMRF--DCAQMENEFLRK---------RLQQCEERLDSELTARKEL 1554
Cdd:PRK01156 252 NR----YESEIKTAESDLSMELEKNNYYKELEERHMKIinDPVYKNRNYINDyfkykndieNKKQILSNIDAEINKYHAI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1555 EQKLGELQSAYDGAKKMAHQ---LKRKCHHLTCDLEDTCVLLENQQSRN---HELEKKQKKFDLQLAQALGESVFE---- 1624
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKSRyddLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMSAFISEILKIQEIDpdai 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1625 KGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGE----NCVAGLKERLWKLESSALE 1700
Cdd:PRK01156 408 KKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEeksnHIINHYNEKKSRLEEKIRE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1701 QQKIQSQQENTIKQLEQLRQRFEL-EIERMKQMHQKdREDQEEELEDVRQScQKRLHQLEMQLEQEYEE-KQMVLhekQD 1778
Cdd:PRK01156 488 IEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNK-IESARADLEDIKIK-INELKDKHDKYEEIKNRyKSLKL---ED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1779 LEGLIGTLCDQIGHRD-FDVEK-RLRRDlrrthallsDVQLLLGTMEDGKTSVsKEELEKVHSQLEQSEAKCEEALKTqk 1856
Cdd:PRK01156 563 LDSKRTSWLNALAVISlIDIETnRSRSN---------EIKKQLNDLESRLQEI-EIGFPDDKSYIDKSIREIENEANN-- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1857 vltadLESMHSELENmtrNKSLVDEqlyrLQFEKADLLKRI---DEDQDDLNELMQKhkdlIAQSAADIGQIQElqlQLE 1933
Cdd:PRK01156 631 -----LNNKYNEIQE---NKILIEK----LRGKIDNYKKQIaeiDSIIPDLKEITSR----INDIEDNLKKSRK---ALD 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1934 EAKKEKHKLQEQLQVAQMRIEYLEQSTVDRaivsrqeavicdleNKTEFQKVQIKRFEVLVIRLRDSLIKMG------EE 2007
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDI--------------NETLESMKKIKKAIGDLKRLREAFDKSGvpamirKS 757
|
650
....*....|.
gi 970949420 2008 LSQAATSESQQ 2018
Cdd:PRK01156 758 ASQAMTSLTRK 768
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1389-1761 |
3.18e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.81 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1389 LGSLQPLLSATigTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAER 1468
Cdd:pfam15921 463 VSSLTAQLEST--KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1469 lqafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERL--DS 1546
Cdd:pfam15921 541 ----DHLRNVQTECEALKLQMAEKDKVIEILRQQIE-NMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDK 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1547 ELTARKELEQKLGELQ--------------SAYDGAKKMAHQLKRKCHHLTCDL----EDTCVLLENQQSRNHELEKKQK 1608
Cdd:pfam15921 616 KDAKIRELEARVSDLElekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELnslsEDYEVLKRNFRNKSEEMETTTN 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1609 KFDLQLAQALGEsvfekglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDhKRELLGSPSLGENcvaglK 1688
Cdd:pfam15921 696 KLKMQLKSAQSE-------LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQS-KIQFLEEAMTNAN-----K 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1689 ER-LWKLESSALEQQ--KIQSQQENTIKQLEQLR---QRFELEIERMK--------QMHQKDREDQEEELEDVRQSCQKR 1754
Cdd:pfam15921 763 EKhFLKEEKNKLSQElsTVATEKNKMAGELEVLRsqeRRLKEKVANMEvaldkaslQFAECQDIIQRQEQESVRLKLQHT 842
|
....*..
gi 970949420 1755 LHQLEMQ 1761
Cdd:pfam15921 843 LDVKELQ 849
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1687-2093 |
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 970949420 1687 LKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFEL---EIERMKQMHQKDREDQE-EELEDVRQSCQKRLHQLEMQL 1762
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreELEKLEKLLQLLPLYQElEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1763 eQEYEEKQmvlHEKQDLEGLIGTLCDQI----GHRDFDVEKRLRRDLRRTHALLSDVQLLLGTMEDgktsvSKEELEKVH 1838
Cdd:COG4717 156 -EELRELE---EELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEE-----AQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1839 SQLEQSEAKCEEALKTQK---------------------------------VLTADLESMHSELENMTRNKSLVDEQLYR 1885
Cdd:COG4717 227 EELEQLENELEAAALEERlkearlllliaaallallglggsllsliltiagVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1886 LQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmrIEYLEQstvdrai 1965
Cdd:COG4717 307 LQ----ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-----LEELEQ------- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1966 vsrqeavicdlENKTEFQKVQIKrfevlvirLRDSLIKMGEELSQAAtsesQQRESSQYYQRRLEELKADMEELVQREAE 2045
Cdd:COG4717 371 -----------EIAALLAEAGVE--------DEEELRAALEQAEEYQ----ELKEELEELEEQLEELLGELEELLEALDE 427
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 970949420 2046 AsrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2093
Cdd:COG4717 428 E-----ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1419-2088 |
6.50e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.14 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1419 LEKSEKLRNELRQNTDLLESKIADL---TSDLADERFKGDVacQVLESERAERLQ----------AFREVQELKSKHEQV 1485
Cdd:PTZ00440 597 IQQIEELINEALFNKEKFINEKNDLqekVKYILNKFYKGDL--QELLDELSHFLDdhkylyheakSKEDLQTLLNTSKNE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1486 QKKLGDVN------------------KQLEEAQQKIQLNDLERNPTGGAD-------EWQMRFDCAQMENEFLRKRLQQC 1540
Cdd:PTZ00440 675 YEKLEFMKsdnidniiknlkkelqnlLSLKENIIKKQLNNIEQDISNSLNqytikynDLKSSIEEYKEEEEKLEVYKHQI 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1541 EERLDSELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLTCDLEdtcVLLENQQSRNHELEKKQKKfDLQLAQALGE 1620
Cdd:PTZ00440 755 INRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDIN---ILKENKKNNQDLLNSYNIL-IQKLEAHTEK 830
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1621 SVFE-KGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEmLQDHKRELLGSPSLGENcvaglkerlwkleSSAL 1699
Cdd:PTZ00440 831 NDEElKQLLQKFPTEDENLN--LKELEKEFNENNQIVDNIIKDIE-NMNKNINIIKTLNIAIN-------------RSNS 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1700 EQQKIQSQQENTIKQLEQLRQRFElEIERMKQMHQKDREDQEEELEDVRQSCQKRL-----HQLEMQLEQ--EYEEKQmv 1772
Cdd:PTZ00440 895 NKQLVEHLLNNKIDLKNKLEQHMK-IINTDNIIQKNEKLNLLNNLNKEKEKIEKQLsdtkiNNLKMQIEKtlEYYDKS-- 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 lheKQDLEGLIGTLCDQighrdFDVEKRLRRDLRRT-HALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEa 1851
Cdd:PTZ00440 972 ---KENINGNDGTHLEK-----LDKEKDEWEHFKSEiDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKEKGKEIEE- 1042
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1852 lKTQKVLTAdLESMHSELENMTRNK-------SLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS------ 1918
Cdd:PTZ00440 1043 -KVDQYISL-LEKMKTKLSSFHFNIdikkyknPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNAdkeknk 1120
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1919 --------AADIG----QIQELQLQLEEAKKEKHKLQEqlqVAQMRIEYleqstvDRAIVSRQEAVICDLENKTEFQKVQ 1986
Cdd:PTZ00440 1121 qtehynkkKKSLEkiykQMEKTLKELENMNLEDITLNE---VNEIEIEY------ERILIDHIVEQINNEAKKSKTIMEE 1191
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1987 IKRFEVLVIRLRDSLIKmgEELSQAATSESQQressqyYQRRLEELKADMEELVQrEAEASRRCMELEKYVEELAAVRQT 2066
Cdd:PTZ00440 1192 IESYKKDIDQVKKNMSK--ERNDHLTTFEYNA------YYDKATASYENIEELTT-EAKGLKGEANRSTNVDELKEIKLQ 1262
|
730 740
....*....|....*....|..
gi 970949420 2067 LQTDLETSIRRIADLQAALEEV 2088
Cdd:PTZ00440 1263 VFSYLQQVIKENNKMENALHEI 1284
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1412-1949 |
8.32e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1412 LTTLRRKLEKSEKlrnELRQNTDLLESKIADLTSDLADERFKG---DVACQVLESERAERLQAFREVQELkskHEQVQKK 1488
Cdd:pfam05557 11 LSQLQNEKKQMEL---EHKRARIELEKKASALKRQLDRESDRNqelQKRIRLLEKREAEAEEALREQAEL---NRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1489 LGDVNKQLEE-AQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDG 1567
Cdd:pfam05557 85 LEALNKKLNEkESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1568 AKKMAHQLKRKCHHLtCDLEDTCVLLENQQS---RNHELEKKQKKFDLQLAQaLGESVFEKG-LREKVTQENTSVRWELG 1643
Cdd:pfam05557 165 LAEAEQRIKELEFEI-QSQEQDSEIVKNSKSelaRIPELEKELERLREHNKH-LNENIENKLlLKEEVEDLKRKLEREEK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1644 QLQQQLK---QKEQEASQLKQQVEMLQDHKRELLGSPSLGENCV------AGLKERLWKLESSALEQQKIQSQQENTIKQ 1714
Cdd:pfam05557 243 YREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEqlqqreIVLKEENSSLTSSARQLEKARRELEQELAQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1715 LeqLRQRFELEIERMKQMHQKDR---------------------EDQE--------------EELEDVRQSCQKRLHQLE 1759
Cdd:pfam05557 323 Y--LKKIEDLNKKLKRHKALVRRlqrrvllltkerdgyrailesYDKEltmsnyspqlleriEEAEDMTQKMQAHNEEME 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1760 MQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRthallsDVQLLLgtMEDGKTSVSKEELEkvhS 1839
Cdd:pfam05557 401 AQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRR------KLETLE--LERQRLREQKNELE---M 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1840 QLEQSEAKCEEALKTQKVLtadlesmHSELENMTRNKSLVDEQLYRLQFEKA---DLLKRIDEDQDDLNELMQKHKDLIA 1916
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVL-------HLSMNPAAEAYQQRKNQLEKLQAEIErlkRLLKKLEDDLEQVLRLPETTSTMNF 542
|
570 580 590
....*....|....*....|....*....|...
gi 970949420 1917 QSAADigqiqeLQLQLEEAKKEKHKLQEQLQVA 1949
Cdd:pfam05557 543 KEVLD------LRKELESAELKNQRLKEVFQAK 569
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1474-1963 |
9.14e-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: 51.01 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1474 EVQELKSK-HEQVQKKLGDVNKQLEEAQQkiqLNDlernptggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARK 1552
Cdd:pfam06160 46 KFEEWRKKwDDIVTKSLPDIEELLFEAEE---LND------------KYRFKKAKKALDEIEELLDDIEEDIKQILEELD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1553 ELEQKLGELQSAYDGAKKMAHQLKRKchhltcdledtcvLLENqqsrNHELEKKQKKFDLQLAQAlgESVFEKglrekVT 1632
Cdd:pfam06160 111 ELLESEEKNREEVEELKDKYRELRKT-------------LLAN----RFSYGPAIDELEKQLAEI--EEEFSQ-----FE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1633 QENTSvrwelgqlqqqlkQKEQEASQLKQQVEMLQDHKRELLGS-PSLGENCVAGLKERLWKLES--SALEQQKIQSQQE 1709
Cdd:pfam06160 167 ELTES-------------GDYLEAREVLEKLEEETDALEELMEDiPPLYEELKTELPDQLEELKEgyREMEEEGYALEHL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1710 NTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDvrqscqkRLHQLEMQLEQEYEEKQMVLHEKQDLEgligtlcDQ 1789
Cdd:pfam06160 234 NVDKEIQQLEEQLEENLALLENLELDEAEEALEEIEE-------RIDQLYDLLEKEVDAKKYVEKNLPEIE-------DY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1790 IGHRDfDVEKRLRRDLRRT---------------------HALLSDVQLLLGTMEDGKTSVS--KEELEKVHSQLEQSEA 1846
Cdd:pfam06160 300 LEHAE-EQNKELKEELERVqqsytlnenelervrglekqlEELEKRYDEIVERLEEKEVAYSelQEELEEILEQLEEIEE 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1847 KCEEALKTQKVLTAD-------LESMHSELENM-----TRNKSLVDEQlYRLQFEKA-DLLKRIDED------------- 1900
Cdd:pfam06160 379 EQEEFKESLQSLRKDelearekLDEFKLELREIkrlveKSNLPGLPES-YLDYFFDVsDEIEDLADElnevplnmdevnr 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1901 -----QDDLNELMQKHKDLIaQSAADIGQ-IQ----------ELQLQLEEAKK--EKHKLQEQLQVAQMRIEYLEQSTVD 1962
Cdd:pfam06160 458 lldeaQDDVDTLYEKTEELI-DNATLAEQlIQyanryrssnpEVAEALTEAELlfRNYDYEKALEIAATALEKVEPGAYE 536
|
.
gi 970949420 1963 R 1963
Cdd:pfam06160 537 R 537
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1704-2029 |
1.31e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 50.67 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1704 IQSQQENTIKQLEQLrqrfeleiERMKQMHQKDrEDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLI 1783
Cdd:PLN02939 102 MQRDEAIAAIDNEQQ--------TNSKDGEQLS-DFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1784 GTLcdqighrdfdvEKRLRRdlrrthallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---SEAKCEEA-------LK 1853
Cdd:PLN02939 173 NIL-----------EMRLSE---------TDARIKLAAQEKIHVEILEEQLEKLRNELLIrgaTEGLCVHSlskeldvLK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1854 TQKV-LTADLESMHSELENMT----------RNKSLVDEQLYRLQFE----KADLLK----RID---EDQDDLNELMQKH 1911
Cdd:PLN02939 233 EENMlLKDDIQFLKAELIEVAeteervfkleKERSLLDASLRELESKfivaQEDVSKlsplQYDcwwEKVENLQDLLDRA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1912 KDLIAQSAADIGQ-------IQELQLQLEEAKKEKHKLqEQLQVAQMRIEYLEqstvdraivSRQEAviCDLENKTefqk 1984
Cdd:PLN02939 313 TNQVEKAALVLDQnqdlrdkVDKLEASLKEANVSKFSS-YKVELLQQKLKLLE---------ERLQA--SDHEIHS---- 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 970949420 1985 vQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRL 2029
Cdd:PLN02939 377 -YIQLYQESIKEFQDTLSKLKEESKKRSLEHPADDMPSEFWSRIL 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1699-2103 |
1.59e-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: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1699 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDRE-DQEEELEDVRQSCQKRLH--------QLEM--------- 1760
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAeaeealreQAELnrlkkkyle 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1761 ---QLEQEYEEKQMVLHEKQD-LEGLIGTLCDQIGHRDFDVE------KRLRRDLRRTHALLSDVQLLLGTMEdGKTSVS 1830
Cdd:pfam05557 87 alnKKLNEKESQLADAREVIScLKNELSELRRQIQRAELELQstnselEELQERLDLLKAKASEAEQLRQNLE-KQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVhSQLE---QSEAKCEEALKTQKVLTADLESMHSELE----------NMTRNKSLVDEQLYRLQFEkadlLKRI 1897
Cdd:pfam05557 166 AEAEQRI-KELEfeiQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRK----LERE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1898 DEDQDDLNELMQKHKDLIA--QSAADIGQIQEL-------------QLQLEEA--KKEKHKLQEQLQVAQMRIEYLEQSt 1960
Cdd:pfam05557 241 EKYREEAATLELEKEKLEQelQSWVKLAQDTGLnlrspedlsrrieQLQQREIvlKEENSSLTSSARQLEKARRELEQE- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1961 vdraiVSRQEAVICDLENKTEFQKVQIKRFE---VLVIRLRDSLIKMGEELSqaatSESQQRESSQYYQRRLEELkADME 2037
Cdd:pfam05557 320 -----LAQYLKKIEDLNKKLKRHKALVRRLQrrvLLLTKERDGYRAILESYD----KELTMSNYSPQLLERIEEA-EDMT 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 2038 ELVQREAEASRrcMELEKYVEELAAVRQTLQTD-LETSIRRiadLQAALEEVASSDSDTESVQTAVD 2103
Cdd:pfam05557 390 QKMQAHNEEME--AQLSVAEEELGGYKQQAQTLeRELQALR---QQESLADPSYSKEEVDSLRRKLE 451
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1403-1764 |
2.18e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.83 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKL-EKSEKLRNELRQNT-------DLLESKIADLTSDLadERFkgdvacqVLESERAERLQAFRE 1474
Cdd:PRK04778 129 QELLESEEKNREEVEQLkDLYRELRKSLLANRfsfgpalDELEKQLENLEEEF--SQF-------VELTESGDYVEAREI 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1475 VQELKSKHEQVQKKLGDVNKQLEEAQQKI--QLNDLERnptgGADEWQM---RFDCAQMENEF--LRKRLQQC------- 1540
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELpdQLQELKA----GYRELVEegyHLDHLDIEKEIqdLKEQIDENlalleel 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1541 ------------EERLDS-------ELTARKELEQKLGELQSAYDGAKKMAHQLKRKCHHLtcdledtcvllenQQSR-- 1599
Cdd:PRK04778 276 dldeaeekneeiQERIDQlydilerEVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRV-------------KQSYtl 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1600 NHELEKKQKKFDLQLAQAlgESVFEKgLREKVTQENTSvrwelgqlqqqlkqkeqeASQLKQQVEMLQDHkrellgspsl 1679
Cdd:PRK04778 343 NESELESVRQLEKQLESL--EKQYDE-ITERIAEQEIA------------------YSELQEELEEILKQ---------- 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1680 gencvaglkerlwklessaLEQqkIQSQQENTIKQLEQLR----------QRFELEIERMKQMHQKDR-----EDQEEEL 1744
Cdd:PRK04778 392 -------------------LEE--IEKEQEKLSEMLQGLRkdeleareklERYRNKLHEIKRYLEKSNlpglpEDYLEMF 450
|
410 420
....*....|....*....|
gi 970949420 1745 EDVrqscQKRLHQLEMQLEQ 1764
Cdd:PRK04778 451 FEV----SDEIEALAEELEE 466
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1831-2047 |
2.70e-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: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESmHSELENMTRnkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQK 1910
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNGLVDLSEEA-KLLLQQLSE----LESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1911 HKDLIAQSAAD--IGQIQELQLQLEEAKK---EKH----KLQEQLQVAQmrieyleqstvdRAIVSRQEAVICDLENKTE 1981
Cdd:COG3206 256 LPELLQSPVIQqlRAQLAELEAELAELSArytPNHpdviALRAQIAALR------------AQLQQEAQRILASLEAELE 323
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 970949420 1982 FQKVQIKrfevlviRLRDSLIKMGEELSQAATSESQQREssqyYQRRLEELKADMEELVQREAEAS 2047
Cdd:COG3206 324 ALQAREA-------SLQAQLAQLEARLAELPELEAELRR----LEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1402-1563 |
3.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1402 TEQLRAKEEELTTLR-----RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacQVLESERAERLQA-FREV 1475
Cdd:COG4913 268 RERLAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALR-------EELDELEAQIRGNgGDRL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1476 QELKSKHEQVQKKLGDVNKQLEEAQQkiQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELE 1555
Cdd:COG4913 341 EQLEREIERLERELEERERRRARLEA--LLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
....*...
gi 970949420 1556 QKLGELQS 1563
Cdd:COG4913 419 RELRELEA 426
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1832-2060 |
3.34e-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: 3.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1832 EELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKH 1911
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1912 KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAI--VSRQEAVICDLENKTEFQKVQIKR 1989
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGD-LERAEerAELAESKIVELEEELKVVGNNLKS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1990 FEVlvirlrdslikmgeelsqaATSESQQRESSqyYQRRLEELKADMEELVQREAEASRRCMELEKYVEEL 2060
Cdd:pfam00261 160 LEA-------------------SEEKASEREDK--YEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1860-2093 |
6.13e-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: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1860 ADLESMHSELENMTRnkslvdeqlyrlqfeKADLLKRIDEDQDDLNELMQKHKDLiaQSAADIGQIQELQLQLEEAKKEK 1939
Cdd:COG4913 235 DDLERAHEALEDARE---------------QIELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1940 HKLQEQLQVAQMRIEYLEQsTVDRAIVSRQEAVICDLENKTEfqkvQIKRFEvlvirlrdslikmgEELSQAATSESQQR 2019
Cdd:COG4913 298 EELRAELARLEAELERLEA-RLDALREELDELEAQIRGNGGD----RLEQLE--------------REIERLERELEERE 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 2020 ESSQYYQRRLEELK----ADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDS 2093
Cdd:COG4913 359 RRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1748-2087 |
6.34e-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: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1748 RQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKRLRRDLRRTHALLSDVQlllGTMEDGKT 1827
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALR---EQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1828 SvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELENMtrnkslvDEQLYRLQFEKADLLKRIDEDQDDLNEL 1907
Cdd:pfam05557 81 K--KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRA-------ELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1908 MQKHKDLIAQ---SAADIGQIQEL--QLQLEEAKKE--KHKLQEQLQVAQMRIEyLEQSTVDRAIVSRQEAVICDLENKT 1980
Cdd:pfam05557 152 EQLRQNLEKQqssLAEAEQRIKELefEIQSQEQDSEivKNSKSELARIPELEKE-LERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1981 EFQKVQIKRFEvlviRLRDSLIKMGEELSQAATSESQQRESSQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYV 2057
Cdd:pfam05557 231 EDLKRKLEREE----KYREEAATLELEKEKLEQELQSWVKLAQDTGlnlRSPEDLSRRIEQLQQREIVLKEENSSLTSSA 306
|
330 340 350
....*....|....*....|....*....|
gi 970949420 2058 EELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:pfam05557 307 RQLEKARRELEQELAQYLKKIEDLNKKLKR 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1624-2116 |
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 970949420 1624 EKGLREKVTQENTSvRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLESSALEQQK 1703
Cdd:TIGR00618 228 LKHLREALQQTQQS-HAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1704 IQSQQENTIKQleqlRQRFELEIERMK-QMHQKDREDQEE----------ELEDVRQSCQKRLHQLEmQLEQEYEEKQMV 1772
Cdd:TIGR00618 307 QQAQRIHTELQ----SKMRSRAKLLMKrAAHVKQQSSIEEqrrllqtlhsQEIHIRDAHEVATSIRE-ISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 LHEKQDLEGLIGTLcdQIGHRDFDVEKRLRRDLRRTHALLSDVQLLLGTME-DGKTSVSKEELEKVHSQLEQSEAKCEE- 1850
Cdd:TIGR00618 382 HTLQQQKTTLTQKL--QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKi 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1851 -------ALKTQKVLTADLESMHselENMTRNKSLVDEQLYRLQFEKADLLKRIDEdqddLNELMQKHKDLIAQSAADIG 1923
Cdd:TIGR00618 460 hlqesaqSLKEREQQLQTKEQIH---LQETRKKAVVLARLLELQEEPCPLCGSCIH----PNPARQDIDNPGPLTRRMQR 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1924 QIQELQLQLEEAKKEKHKLQEQLQVAQmriEYLEQSTvdRAIVSRQEAVICDLENKTEFQKVQIKRFEVL-VIRLRDSLI 2002
Cdd:TIGR00618 533 GEQTYAQLETSEEDVYHQLTSERKQRA---SLKEQMQ--EIQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2003 KMGEELSQAATSESQ-----------QRESSQYYQRRLEELKADMEELVQ-REAEASRRCMELEkyvEELAAVRQTLQTD 2070
Cdd:TIGR00618 608 DMLACEQHALLRKLQpeqdlqdvrlhLQQCSQELALKLTALHALQLTLTQeRVREHALSIRVLP---KELLASRQLALQK 684
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 970949420 2071 LETSIRRIADLqaaLEEVASSDSDTESVQTAVDCGSSGRKEMDNVS 2116
Cdd:TIGR00618 685 MQSEKEQLTYW---KEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1658-2088 |
1.12e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1658 QLKQQVEMLQDHKREllgspslGENCVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIE-RMKQMHQKD 1736
Cdd:TIGR04523 51 NKEKELKNLDKNLNK-------DEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKnDKEQKNKLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1737 RE--DQEEELEDVRQSCQK---RLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIGHRDFDVEKrLRRDLRRTHAL 1811
Cdd:TIGR04523 124 VElnKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDK-IKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1812 LSDVQLLlgtMEDGKTSVSK-EELEKVHSQLEQSEAKceealKTQKV--LTADLESMHSELENMTRNKSLVDEQLYRLQF 1888
Cdd:TIGR04523 203 LSNLKKK---IQKNKSLESQiSELKKQNNQLKDNIEK-----KQQEIneKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1889 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ---------- 1958
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEqisqlkkelt 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1959 ------STVDRAIVSRQEAVIcDLENKTEFQKVQIKRFEVLVIRLRdSLIKMGEELSQAATSESQQRESS-QYYQRRLEE 2031
Cdd:TIGR04523 353 nsesenSEKQRELEEKQNEIE-KLKKENQSYKQEIKNLESQINDLE-SKIQNQEKLNQQKDEQIKKLQQEkELLEKEIER 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 2032 LKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2088
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1416-1889 |
1.21e-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: 47.54 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1416 RRKLEKSEKLRNELRQNTDLLESKIADLTSDLAderfkgdvacQVLESERAERLqafrEVQELKSKHEQVQKKLGDVNKQ 1495
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELD----------ELLESEEKNRE----EVEELKDKYRELRKTLLANRFS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1496 LEEAQQKI--QLNDLE--------RNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDselTARKELEQKLGELQSAY 1565
Cdd:pfam06160 144 YGPAIDELekQLAEIEeefsqfeeLTESGDYLEAREVLEKLEEETDALEELMEDIPPLYE---ELKTELPDQLEELKEGY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1566 DgakkmahQLKRKCHHLT-CDLEDTCVLLENQQSRNHELEKKqkkfdLQLAQAlgesvfEKGLREkvtqentsvrwelgq 1644
Cdd:pfam06160 221 R-------EMEEEGYALEhLNVDKEIQQLEEQLEENLALLEN-----LELDEA------EEALEE--------------- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1645 lqqqlkqkeqEASQLKQQVEMLQdhkRELLGSPSLGENcVAGLKERLwklessaleqQKIQSQQENTIKQLEQLRQRFEL 1724
Cdd:pfam06160 268 ----------IEERIDQLYDLLE---KEVDAKKYVEKN-LPEIEDYL----------EHAEEQNKELKEELERVQQSYTL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1725 eiermkqmhqkdredQEEELEDVRQScQKRLHQLE---MQLEQEYEEKQMVLHEKQD-LEGLIGTLcDQI--GHRDFDVE 1798
Cdd:pfam06160 324 ---------------NENELERVRGL-EKQLEELEkryDEIVERLEEKEVAYSELQEeLEEILEQL-EEIeeEQEEFKES 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1799 -KRLRRDLRRTHALLSDVQLLLGTMedgKTSVSK------------------EELEKVHSQLEQS-------EAKCEEAl 1852
Cdd:pfam06160 387 lQSLRKDELEAREKLDEFKLELREI---KRLVEKsnlpglpesyldyffdvsDEIEDLADELNEVplnmdevNRLLDEA- 462
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 970949420 1853 ktqkvlTADLESMHSELENMTRNKSLVdEQL------YRLQFE 1889
Cdd:pfam06160 463 ------QDDVDTLYEKTEELIDNATLA-EQLiqyanrYRSSNP 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1881-2072 |
1.47e-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: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1881 EQLYRLQfekaDLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQst 1960
Cdd:COG1579 7 RALLDLQ----ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1961 vdraivsRQEAV-----ICDLENKTEFQKVQIKRFEvlvirlrDSLIKMGEELSQAATSESQQREssqyyqrRLEELKAD 2035
Cdd:COG1579 81 -------QLGNVrnnkeYEALQKEIESLKRRISDLE-------DEILELMERIEELEEELAELEA-------ELAELEAE 139
|
170 180 190
....*....|....*....|....*....|....*..
gi 970949420 2036 MEELvqrEAEASRRCMELEKYVEELAAVRQTLQTDLE 2072
Cdd:COG1579 140 LEEK---KAELDEELAELEAELEELEAEREELAAKIP 173
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1330-1763 |
1.52e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1330 EKQREKLVSQSIVLFQAACKGFLSRQEFKKLKIRRLAAQCIQKNV-AVFLAVKDWPWWQLLGSLQPLLSATIGTEQLRAK 1408
Cdd:TIGR00618 415 RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 -EEELTTLRRKLEKSEKLRNELRQNTDL----------LESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQE 1477
Cdd:TIGR00618 495 rLLELQEEPCPLCGSCIHPNPARQDIDNpgpltrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1478 LKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1557
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1558 LG------------ELQSAYDGAKKMAHQ-LKRKCHHLTCDLEDtcvlLENQQSRNHELEKKQKKFDL---QLAQALGES 1621
Cdd:TIGR00618 655 LTqervrehalsirVLPKELLASRQLALQkMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDRefnEIENASSSL 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1622 VFEKGLREKVTQENTS-----VRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLGENCVAGLKERLWKLES 1696
Cdd:TIGR00618 731 GSDLAAREDALNQSLKelmhqARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQ 810
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 1697 SALEQQKIQS-QQENTIKQLEQLRQRFEleiERMKQMHQKDRedQEEELEDVRQ------SCQKRLHQLEMQLE 1763
Cdd:TIGR00618 811 EIPSDEDILNlQCETLVQEEEQFLSRLE---EKSATLGEITH--QLLKYEECSKqlaqltQEQAKIIQLSDKLN 879
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
1693-1943 |
1.82e-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: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1693 KLESSALEQQKiqsqQENTIKqlEQLRQRFELEIERMKQMHQKDredqeeeledvrqscQKRLHQLEMQLEQEYEEKQMV 1772
Cdd:pfam09728 71 KLEKLCRELQK----QNKKLK--EESKKLAKEEEEKRKELSEKF---------------QSTLKDIQDKMEEKSEKNNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 LHEKQDLEGLIGTLCDQIGHRDFDVEKRLR-RDLrrthallsDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEAKCEEA 1851
Cdd:pfam09728 130 REENEELREKLKSLIEQYELRELHFEKLLKtKEL--------EVQLAEAKLQQATEEEEKKAQEKEVAKARELKAQVQTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1852 LKTQKVLTADLeSMHS----ELENmTRNKSLVDEQLYRLQFEK-ADLLKRIDEDqddlNELMQKHKDLIAQSAADIGQ-I 1925
Cdd:pfam09728 202 SETEKELREQL-NLYVekfeEFQD-TLNKSNEVFTTFKKEMEKmSKKIKKLEKE----NLTWKRKWEKSNKALLEMAEeR 275
|
250
....*....|....*...
gi 970949420 1926 QELQLQLEEAKKEKHKLQ 1943
Cdd:pfam09728 276 QKLKEELEKLQKKLEKLE 293
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1709-2046 |
1.91e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1709 ENTIKQLEQLRQRFELEIERMKQMHQKDREdQEEELEDVRQSCQKRL----HQ-------LEMQLEQ------------- 1764
Cdd:PRK04778 111 ESLLDLIEEDIEQILEELQELLESEEKNRE-EVEQLKDLYRELRKSLlanrFSfgpaldeLEKQLENleeefsqfvelte 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1765 --EYEEKQMVLHEKQDLEGLIGTLCDQI--------------------GHRD----------FDVEKRLRR---DLRRTH 1809
Cdd:PRK04778 190 sgDYVEAREILDQLEEELAALEQIMEEIpellkelqtelpdqlqelkaGYRElveegyhldhLDIEKEIQDlkeQIDENL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1810 ALLSdvQLLLGTMEDGKTSVSkEELEKVHSQLEQS-EAKcEEALKTQKVLTADLEsmHSElenmTRNKSLVDE-----QL 1883
Cdd:PRK04778 270 ALLE--ELDLDEAEEKNEEIQ-ERIDQLYDILEREvKAR-KYVEKNSDTLPDFLE--HAK----EQNKELKEEidrvkQS 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1884 YRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQ--VAQMRIEylEQSTV 1961
Cdd:PRK04778 340 YTLNESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSemLQGLRKD--ELEAR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1962 DRAIVSRQEavicdLENktefqkvqIKRfevLVIRLR---------DSLIKMGEELSQAATSESQQRESSQYYQRRLEEL 2032
Cdd:PRK04778 418 EKLERYRNK-----LHE--------IKR---YLEKSNlpglpedylEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEA 481
|
410
....*....|....
gi 970949420 2033 KADMEELvQREAEA 2046
Cdd:PRK04778 482 TEDVETL-EEETEE 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1604-1976 |
2.05e-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: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1604 EKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLgENC 1683
Cdd:COG5185 232 EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDI-KKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1684 VAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMhqKDREDQEEELEDVRQScQKRLHQLEMQLE 1763
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAI--KEEIENIVGEVELSKS-SEELDSFKDTIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1764 ---QEYEEKQMVLhEKQDLEGLIgTLCDQIGHRDFDVEkRLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQ 1840
Cdd:COG5185 388 stkESLDEIPQNQ-RGYAQEILA-TLEDTLKAADRQIE-ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1841 LEQSEAKCEEALKTQK-VLTADLESMHSELENMTRNkslVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1919
Cdd:COG5185 465 LEEAYDEINRSVRSKKeDLNEELTQIESRVSTLKAT---LEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1920 ADIGQIQELQLQLEEakkekHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDL 1976
Cdd:COG5185 542 ENLIPASELIQASNA-----KTDGQAANLRTAVIDELTQYLSTIESQQAREDPIPDQ 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1802-2102 |
2.15e-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: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1802 RRDLRRTHALLSDVQLLLGTME----------DGKTSVSKEELEKVHSQLEQSEAKCEealKTQKVLTADLESMHSELEn 1871
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMElehkrarielEKKASALKRQLDRESDRNQELQKRIR---LLEKREAEAEEALREQAE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1872 MTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDL-NELMQKHKdliaqsaadigQIQELQLQLEEAKKEKHKLQEQLQVAQ 1950
Cdd:pfam05557 77 LNRLKKKYLEALNKKLNEKESQLADAREVISCLkNELSELRR-----------QIQRAELELQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1951 MRIEYLEQstvdraivsrqeaVICDLENKTEFQKVQIKRFEVLVIRLR----DSLI--KMGEELSQAATSESQQR----- 2019
Cdd:pfam05557 146 AKASEAEQ-------------LRQNLEKQQSSLAEAEQRIKELEFEIQsqeqDSEIvkNSKSELARIPELEKELErlreh 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2020 ---------------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSiRRIADLQ-- 2082
Cdd:pfam05557 213 nkhlnenienklllkEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLS-RRIEQLQqr 291
|
330 340
....*....|....*....|..
gi 970949420 2083 --AALEEVASSDSDTESVQTAV 2102
Cdd:pfam05557 292 eiVLKEENSSLTSSARQLEKAR 313
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1658-2067 |
2.96e-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: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1658 QLKQQVEMLQDHKRELLGspslgENcvAGLKERLWKLES------------SALEQQKIQSQQENTikQLEQLRQRFELE 1725
Cdd:pfam05622 18 ELDQQVSLLQEEKNSLQQ-----EN--KKLQERLDQLESgddsgtpggkkyLLLQKQLEQLQEENF--RLETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1726 IERMK------QMHQKDREDQEEELE------DVRQSCQKRLHQLEMQLE------QEYEE--KQMVLHEKQDLEGLIGT 1785
Cdd:pfam05622 89 CEELEkevlelQHRNEELTSLAEEAQalkdemDILRESSDKVKKLEATVEtykkklEDLGDlrRQVKLLEERNAEYMQRT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1786 LcdqighrdfdvekRLRRDLRRTHALLSDVQLLlgtmedgktsvsKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESM 1865
Cdd:pfam05622 169 L-------------QLEEELKKANALRGQLETY------------KRQVQELHGKLSEESKKADKLEFEYKKLEEKLEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1866 HSELENMTRN----KSLVDE----QLYRLQFEKAD-LLKRIDEDQDDLN-ELM------------QKHKDL-IAQSAADI 1922
Cdd:pfam05622 224 QKEKERLIIErdtlRETNEElrcaQLQQAELSQADaLLSPSSDPGDNLAaEIMpaeireklirlqHENKMLrLGQEGSYR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1923 GQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQStVDRAIVSRQEAvicdlENKTEFQKVQIKRFEVLVIRLRdsli 2002
Cdd:pfam05622 304 ERLTELQQLLEDANRRKNELETQNRLANQRILELQQQ-VEELQKALQEQ-----GSKAEDSSLLKQKLEEHLEKLH---- 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2003 KMGEELS--QAATSESQQRESSQyYQRRLEELkadMEELVQREAEAsrRCME--LEKYVEELAAVRQTL 2067
Cdd:pfam05622 374 EAQSELQkkKEQIEELEPKQDSN-LAQKIDEL---QEALRKKDEDM--KAMEerYKKYVEKAKSVIKTL 436
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1409-1796 |
3.50e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1409 EEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleseraERLQAFREVQELKSKHEQVQKK 1488
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS---------------DHLNLVQTALRQQEKIERYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1489 LGDVNKQLEEAQQKIQLndlernptggADEWQMRfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGELQSAYDGA 1568
Cdd:PRK04863 357 LEELEERLEEQNEVVEE----------ADEQQEE----------NEARAEAAEEEVD-------ELKSQLADYQQALDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1569 KKMAHQ------LKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVTQENTSVR 1639
Cdd:PRK04863 410 QTRAIQyqqavqALERAKQL-CGLPD--LTADNAEDWLEEFQAKEQEATeelLSLEQKLSVAQAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1640 WELgqlqqqlkqkeqEASQLKQQ-VEMLQDHKRELLGSPSLGencvaGLKERLWKLESSALEQQkiqsQQENTIKQLEQl 1718
Cdd:PRK04863 487 GEV------------SRSEAWDVaRELLRRLREQRHLAEQLQ-----QLRMRLSELEQRLRQQQ----RAERLLAEFCK- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1719 RQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1791
Cdd:PRK04863 545 RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQlqariqRLAARAPAWLAAQDaLA----RLREQSG 620
|
....*
gi 970949420 1792 HRDFD 1796
Cdd:PRK04863 621 EEFED 625
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
221-513 |
4.37e-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: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 221 LGDPGQGTVAlkkgeEGQSivgKGLGTPKTTEL-KEAEPQGKDRQGTrpQAQGPGEGVRPGKAEKEGAEPTNtvEKGNVS 299
Cdd:TIGR00927 627 LGDLSKGDVA-----EAEH---TGERTGEEGERpTEAEGENGEESGG--EAEQEGETETKGENESEGEIPAE--RKGEQE 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 300 KDVGSEGKhvRPQIPGRKWGGFLGRRSKWDGPQNKKDKEGVLLSKAEKTG-EPQTQMEKTSQVQGElGDDLRMGEKAGEL 378
Cdd:TIGR00927 695 GEGEIEAK--EADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEdEGEGEAEGKHEVETE-GDRKETEHEGETE 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 379 RSTTGKAGESWDKKEKMGQPQGKSG--NAGEARSQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGA 456
Cdd:TIGR00927 772 AEGKEDEDEGEIQAGEDGEMKGDEGaeGKVEHEGETEAGEKDEHEGQSETQADDTEVKDE-TGEQELNAENQGEAKQDEK 850
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 457 GAlETELEGPSQPALEKDAERPRIRKENQDGPAPQEEGKGGQSRDSDQAPEDRWYEA 513
Cdd:TIGR00927 851 GV-DGGGGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSLEWPETRQKQA 906
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1462-1780 |
5.23e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1462 ESERAERLQAFREVQELKSKHEQvQKKLGDVNKQLEEAQQKIQLNDLERNPTG--GADEWQMRFDCAQMENEFLRKRLQQ 1539
Cdd:pfam02029 3 DEEEAARERRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSELKPSGqgGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1540 CEER---LDSELTARKE---LEQKLGELQSAYDGAKkmahQLKRKCHHLTCDLEDTcvllenqqsrnHELEKKQKKFDLQ 1613
Cdd:pfam02029 82 ALERqkeFDPTIADEKEsvaERKENNEEEENSSWEK----EEKRDSRLGRYKEEET-----------EIREKEYQENKWS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1614 LAQALGESVFEKglREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELL-GSPSLGENCVAGLK---E 1689
Cdd:pfam02029 147 TEVRQAEEEGEE--EEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPeVKSQNGEEEVTKLKvttK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1690 RLWKLESSALEQQKIQSQQENTIKQLEQLRQRF-ELEIERMKQMHQKDRE-DQE-EELEDVRQSCQKRLHQLEMQLEQEY 1766
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRqEKESEEFEKLRQKQQEaELElEELKKKREERRKLLEEEEQRRKQEE 304
|
330
....*....|....*....
gi 970949420 1767 EEKQMVLHE-----KQDLE 1780
Cdd:pfam02029 305 AERKLREEEekrrmKEEIE 323
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1681-2090 |
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 970949420 1681 ENCVAGLKERLWKLE---SSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKRLHQ 1757
Cdd:TIGR00606 244 ENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1758 LEMQLEQEYEEKQMVLHEKQDLEGLIGTLC-------DQIGHRDFD-----------------------------VEKRL 1801
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQlqadrhqEHIRARDSLiqslatrleldgfergpfserqiknfhtlVIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1802 RRDLRRTHALLSDVQ------------------LLLGTMEDGKTSVSKE--ELEKVHSQLEQSEAKCEEALKTQKVLTAD 1861
Cdd:TIGR00606 404 EDEAKTAAQLCADLQskerlkqeqadeirdekkGLGRTIELKKEILEKKqeELKFVIKELQQLEGSSDRILELDQELRKA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1862 LESMhSELENMTRNKSLVDEQLYrLQFEKADLLK---RIDEDQDDLN------------------------ELMQKHKDL 1914
Cdd:TIGR00606 484 EREL-SKAEKNSLTETLKKEVKS-LQNEKADLDRklrKLDQEMEQLNhhtttrtqmemltkdkmdkdeqirKIKSRHSDE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1915 IAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVD-RAIVSRQEAVICDLENKTeFQKVQIKRFEVL 1993
Cdd:TIGR00606 562 LTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHiNNELESKEEQLSSYEDKL-FDVCGSQDEESD 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1994 VIRLRDSLIKMGEELSQAATsesqqreSSQYYQRRLEELkadmeelvqreAEASRRCMELEKYVEELAAVRQTLQTDLET 2073
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAG-------ATAVYSQFITQL-----------TDENQSCCPVCQRVFQTEAELQEFISDLQS 702
|
490
....*....|....*..
gi 970949420 2074 SIRRIADLQAALEEVAS 2090
Cdd:TIGR00606 703 KLRLAPDKLKSTESELK 719
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1402-1570 |
6.40e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1402 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAERLQAFREVQELKSK 1481
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREE-------AQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGgadewQMRFDCAQMENEFLRKRLQQCEERldsELTAR-KELEQKLGE 1560
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSID-----KLRKEIERLEWRQQTEVLSPEEEK---ELVEKiKELEKELEK 151
|
170
....*....|
gi 970949420 1561 LQSAYDGAKK 1570
Cdd:COG1340 152 AKKALEKNEK 161
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1875-2097 |
6.41e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 6.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1875 NKSLVDEQlyrlqfekADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQ-IQELQLQLEEAKKEKHKLQEQLQVAQMRI 1953
Cdd:PHA02562 172 NKDKIREL--------NQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1954 EYLEQSTVDRAivsrqeAVICDLENKTEFQKVQIKRFevlvirlrDSLIKMGEE----------LSQAATSESQQRESSQ 2023
Cdd:PHA02562 244 LNLVMDIEDPS------AALNKLNTAAAKIKSKIEQF--------QKVIKMYEKggvcptctqqISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 970949420 2024 YYQRRLEELKADMEELVQREAEASrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTES 2097
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFN----EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1693-1947 |
6.92e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.14 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1693 KLESSALEQQKIQSQQENTIKQLEQLRQRFELEIermkqmhqKDREDQEEELEDVRQSCQK----RLhQLEMQLE--QEY 1766
Cdd:pfam00038 62 QLDTLTVERARLQLELDNLRLAAEDFRQKYEDEL--------NLRTSAENDLVGLRKDLDEatlaRV-DLEAKIEslKEE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1767 EEKQMVLHEKQdleglIGTLCDQIGHRDFDVEKRLRRDLRRTHALlSDVQlllgTMEDGKTSVSKEELEkvhsqlEQSEA 1846
Cdd:pfam00038 133 LAFLKKNHEEE-----VRELQAQVSDTQVNVEMDAARKLDLTSAL-AEIR----AQYEEIAAKNREEAE------EWYQS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1847 KCEEALKTQKVLTADLESMHSELENMTRnkslvdeQLYRLQFEKADLLKRIDEDQDDLNELMQKHkdliaqsAADIGQIQ 1926
Cdd:pfam00038 197 KLEELQQAAARNGDALRSAKEEITELRR-------TIQSLEIELQSLKKQKASLERQLAETEERY-------ELQLADYQ 262
|
250 260
....*....|....*....|..
gi 970949420 1927 ELQLQLEEAKKE-KHKLQEQLQ 1947
Cdd:pfam00038 263 ELISELEAELQEtRQEMARQLR 284
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1881-2087 |
7.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1881 EQLYRL---QFEKA-DLLKRIdedQ-----DDLNELMQKH-------KDLIAQSAADIGQIQELQLQLEEAKKEKHKLQE 1944
Cdd:COG4913 180 ARLRRRlgiGSEKAlRLLHKT---QsfkpiGDLDDFVREYmleepdtFEAADALVEHFDDLERAHEALEDAREQIELLEP 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1945 QLQVAQMRIEYLEQSTVDRAIVSRQEAvicdlenktEFQKVQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRES--- 2021
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRL---------WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREElde 327
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 2022 --SQYYQ---RRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:COG4913 328 leAQIRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1403-1783 |
7.86e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQntdlleskiadltsdladerfkgdvacqvlESERA-ERLQAFREVQELKSK 1481
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQ------------------------------DYQAAsDHLNLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HEQVQKKLGDVNKQLEEAQQKIQLNDlernptGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1561
Cdd:PRK04863 350 IERYQADLEELEERLEEQNEVVEEAD------EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1562 QSA----------YDGAKKMAHQLKRKCHHLTCDLEDtcvlLEnQQSRNHELEKKQKKFDLQLAQALGESV--------F 1623
Cdd:PRK04863 424 ERAkqlcglpdltADNAEDWLEEFQAKEQEATEELLS----LE-QKLSVAQAAHSQFEQAYQLVRKIAGEVsrseawdvA 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1624 EKGLREKVTQENTSVRweLGQLQQQLKQKEQEASQLKQQVEMLQDHKREL---LGSPSLGENCVAGLKERLWKLESSALE 1700
Cdd:PRK04863 499 RELLRRLREQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1701 QQKIQSQQENTIKQLEQLRQRFEleiERMKQMHQKD------REDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQmVLH 1774
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLA---ARAPAWLAAQdalarlREQSGEEFEDSQDVTEYMQQLLERERELTVERDE-LAA 652
|
....*....
gi 970949420 1775 EKQDLEGLI 1783
Cdd:PRK04863 653 RKQALDEEI 661
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1830-1939 |
8.65e-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: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1830 SKEELEKVHSQ---LEQSEAKCEEALKTQKVLTADLE----SMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQD 1902
Cdd:pfam05911 686 LKEEFEQLKSEkenLEVELASCTENLESTKSQLQESEqliaELRSELASLKESNSLAETQLKCMAESYEDLETRLTELEA 765
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1903 DLNELMQK--------------HKDLIAQSaadigqiQELQLQLEEAKKEK 1939
Cdd:pfam05911 766 ELNELRQKfealeveleeekncHEELEAKC-------LELQEQLERNEKKE 809
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1705-1920 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1705 QSQQENTIKQLEQLRQRFELEIERMKQMhQKDREDQEEELEDVRQSCQKRLHQLEmQLEQEYEEKQMVLhekQDLEGLIG 1784
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIR-ALEQELAALEAEL---AELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1785 TLCDQIGHRDFDVEKRLRRDLRrtHALLSDVQLLLGTmEDGKTSVSK---------------EELEKVHSQLEQSEAKCE 1849
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYR--LGRQPPLALLLSP-EDFLDAVRRlqylkylaparreqaEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1850 EALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSAA 1920
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1702-2099 |
1.23e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1702 QKIQSQQENTIKQlEQLRQRFELEIERmKQMHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEG 1781
Cdd:PTZ00440 546 KYYLQSIETLIKD-EKLKRSMKNDIKN-KIKYIEENVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQE 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1782 LIGTLCDQIGHRDFDvekrlrrdlrrthALLSDvqlLLGTMEDGKTSV----SKEELEKVHSQLEQSEAKCEEalKTQKV 1857
Cdd:PTZ00440 624 KVKYILNKFYKGDLQ-------------ELLDE---LSHFLDDHKYLYheakSKEDLQTLLNTSKNEYEKLEF--MKSDN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1858 LTADLESMHSELENM-TRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKdliaqsaADIGQIQELQLQLEEAK 1936
Cdd:PTZ00440 686 IDNIIKNLKKELQNLlSLKENIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYK-------EEEEKLEVYKHQIINRK 758
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1937 KE--------KHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQeAVICDlENKTEFQKvQIKRFEVLVIRLRDSLIKMGEEL 2008
Cdd:PTZ00440 759 NEfilhlyenDKDLPDGKNTYEEFLQYKDTILNKENKISND-INILK-ENKKNNQD-LLNSYNILIQKLEAHTEKNDEEL 835
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2009 SQaatsesqqreSSQYYQRRLEELKADmeelvqreaeasrrcmELEKYVEELAAVRQTLQTDLETSIRRIADLQAALEEV 2088
Cdd:PTZ00440 836 KQ----------LLQKFPTEDENLNLK----------------ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAI 889
|
410
....*....|.
gi 970949420 2089 ASSDSDTESVQ 2099
Cdd:PTZ00440 890 NRSNSNKQLVE 900
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1839-2109 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1839 SQLEQSEAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1918
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1919 AADIGQIQELQLQLEeakkekhklQEQLQVAQMRIEYLEQ-STVDRAIVSRQEAVICDLENKTEFQKVQIKrfevlviRL 1997
Cdd:COG3883 96 YRSGGSVSYLDVLLG---------SESFSDFLDRLSALSKiADADADLLEELKADKAELEAKKAELEAKLA-------EL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1998 RDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR 2077
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
250 260 270
....*....|....*....|....*....|..
gi 970949420 2078 IADLQAALEEVASSDSDTESVQTAVDCGSSGR 2109
Cdd:COG3883 240 AAAAASAAGAGAAGAAGAAAGSAGAAGAAAGA 271
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1708-2087 |
1.45e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1708 QENTIKQLEQLRQRFElEIERMkqmhqkdreDQEEELEDVRQscqkrLHqLEMQLEQEYEEKqmvlheKQDLEGLIGTLC 1787
Cdd:PRK04778 24 RKRNYKRIDELEERKQ-ELENL---------PVNDELEKVKK-----LN-LTGQSEEKFEEW------RQKWDEIVTNSL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1788 DQIGHRDFDVEKRLRR-DLRRTHALLSDVQLLLGTMEDGKTSVSKE-----ELEKVHSQL-EQSEAKCEEALKT------ 1854
Cdd:PRK04778 82 PDIEEQLFEAEELNDKfRFRKAKHEINEIESLLDLIEEDIEQILEElqellESEEKNREEvEQLKDLYRELRKSllanrf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1855 -----QKVLTADLESMHSELENMTRNKSLVDEQlyrlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSAADI-GQIQEL 1928
Cdd:PRK04778 162 sfgpaLDELEKQLENLEEEFSQFVELTESGDYV------EAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1929 QL---QLEEAK---------KEKHKLQEQLQVAQMRIEYLEqstVDRAivsrqEAVICDLENKTE-----FQK-VQIKRF 1990
Cdd:PRK04778 236 KAgyrELVEEGyhldhldieKEIQDLKEQIDENLALLEELD---LDEA-----EEKNEEIQERIDqlydiLEReVKARKY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1991 -EVLVIRLRDSLIKMGEELSQ--AATSESQQR--------ESSQYYQRRLEELKADMEELVQREAEASRRCMELEkyvEE 2059
Cdd:PRK04778 308 vEKNSDTLPDFLEHAKEQNKElkEEIDRVKQSytlneselESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ---EE 384
|
410 420
....*....|....*....|....*...
gi 970949420 2060 LAAVRQTLqTDLETSIRRIADLQAALEE 2087
Cdd:PRK04778 385 LEEILKQL-EEIEKEQEKLSEMLQGLRK 411
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1886-2103 |
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 970949420 1886 LQFEKADLLKRIDEDQDDLnelmqkHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQvaqmRIEYLEQStvdrai 1965
Cdd:COG4717 40 LAFIRAMLLERLEKEADEL------FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEE------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1966 VSRQEAVICDLENKTEFQKVQIKRFEVLvirlrdslikmgEELSQAatsesqqRESSQYYQRRLEELKADMEELVQREAE 2045
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLY------------QELEAL-------EAELAELPERLEELEERLEELRELEEE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 2046 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRIA-DLQAALEEVASSDSDTESVQTAVD 2103
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEELQDLAeELEELQQRLAELEEELEEAQEELE 223
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
324-506 |
1.55e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 43.42 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 324 RRSKWDGPQNKKDKEGVLLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEKAGElrsttGKAGESWDKKEKMGQPQGKSG 403
Cdd:PHA03169 34 GRRRGTAARAAKPAPPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEER-----GQGGPSGSGSESVGSPTPSPS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 404 NAGEAR----SQTEKGCEAPKEVSTMVESPAAPGKGGwPGSRGQEAEEPCSRAGDGAGALETELEGPSQPALEKDAERPR 479
Cdd:PHA03169 109 GSAEELasglSPENTSGSSPESPASHSPPPSPPSHPG-PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEP 187
|
170 180
....*....|....*....|....*..
gi 970949420 480 IRKENQDGPAPQEEGKGGQSRDSDQAP 506
Cdd:PHA03169 188 DSPGPPQSETPTSSPPPQSPPDEPGEP 214
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1604-1954 |
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 970949420 1604 EKKQKKFDLQLAQALGESVfEKGLR---EKVT----------QENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHK 1670
Cdd:pfam15742 14 EVQQLRQNLQRLQILCTSA-EKELRyerGKNLdlkqhnsllqEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1671 REllgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQS 1750
Cdd:pfam15742 93 RE---------------------LELEVLKQAQSIKSQNSLQEKLAQEKSRVADAEEKILELQQKLEHAHKVCLTDTCIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1751 CQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIghrdfdveKRLRRDLRRTHALLsdvqlllgTMEDGKTSVS 1830
Cdd:pfam15742 152 EKKQLEERIKEASENEAKLKQQYQEEQQKRKLLDQNVNEL--------QQQVRSLQDKEAQL--------EMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtrnkslvdeqlyRLQFEKADLLKRIDEDQDDLNELMQK 1910
Cdd:pfam15742 216 IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKE--------------ALQEELQQVLKQLDVHVRKYNEKHHH 281
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 970949420 1911 HKdliaqsaADIGQIQELQLQLEEAKKEKHK-LQEQLQVAQMRIE 1954
Cdd:pfam15742 282 HK-------AKLRRAKDRLVHEVEQRDERIKqLENEIGILQQQSE 319
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1832-2083 |
1.61e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1832 EELEKVHSQLEQSEAKCEEAlktqkvltadlesmHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQ---------- 1901
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEA--------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQtraiqyqqav 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1902 ---DDLNELMQKhKDLIAQSAADIgqIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQ--STVDRAI--VSRQEA--V 1972
Cdd:PRK04863 421 qalERAKQLCGL-PDLTADNAEDW--LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAgeVSRSEAwdV 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1973 ICDLENKTEFQKVQIKRFEVLVIRLRDslikMGEELSQAATSESQQRESSQYYQRRLEElkADMEELVQREAEASRRcmE 2052
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSE----LEQRLRQQQRAERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE--S 569
|
250 260 270
....*....|....*....|....*....|.
gi 970949420 2053 LEKYVEELAAVRQTLQTDLETSIRRIADLQA 2083
Cdd:PRK04863 570 LSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1403-1577 |
1.69e-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: 43.21 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkGDVACQVLESERAER-------------L 1469
Cdd:COG4942 55 KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK--EELAELLRALYRLGRqpplalllspedfL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1470 QAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewqmrfdcaqmENEFLRKRLQQCEERLDSELT 1549
Cdd:COG4942 133 DAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-----------------ELEALLAELEEERAALEALKA 195
|
170 180 190
....*....|....*....|....*....|..
gi 970949420 1550 ARK----ELEQKLGELQSAYDGAKKMAHQLKR 1577
Cdd:COG4942 196 ERQkllaRLEKELAELAAELAELQQEAEELEA 227
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1889-2081 |
1.76e-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: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1889 EKADLLKRIDEDQDDLNELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQlqvaqmrieyleqstvdRAIVSR 1968
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSLKNL-----------------KARLKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1969 QEAVICDLEnktEFQKVQIKRFEVLViRLRDSLIKMGEElsqaATSESQQRES--SQYYQRRLEELKADMEelvQREAea 2046
Cdd:pfam13851 97 LEKELKDLK---WEHEVLEQRFEKVE-RERDELYDKFEA----AIQDVQQKTGlkNLLLEKKLQALGETLE---KKEA-- 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 970949420 2047 srrcmELEKYV-------EELAAVRQTLQTDLETSIRRIADL 2081
Cdd:pfam13851 164 -----QLNEVLaaanldpDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1379-1582 |
1.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1379 AVKDWPWWQLLGSLQplLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNtDLLESKIADLTSDLADErfkgdvac 1458
Cdd:COG4717 315 ELEEEELEELLAALG--LPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1459 qvlESERAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLErnptggadewqmrfdcAQMENefLRKRLQ 1538
Cdd:COG4717 384 ---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELE----------------EELEE--LEEELE 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 970949420 1539 QCEERLDSELTARKELEQKLGELQS--AYDGAKKMAHQLKRKCHHL 1582
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEdgELAELLQELEELKAELREL 488
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1403-1666 |
2.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKH 1482
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1483 EQVQKKLGDVNKQLEEAQQKI-----QLNDLERNPTggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1557
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIaereeELKELEEQLE------SLQEELAALEQELQALSEAEAEQALDELLKEANRNAEK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1558 LGELQSAYDGAKKMAHQLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTS 1637
Cdd:COG4372 199 EEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEEL 278
|
250 260
....*....|....*....|....*....
gi 970949420 1638 VRWELGQLQQQLKQKEQEASQLKQQVEML 1666
Cdd:COG4372 279 EIAALELEALEEAALELKLLALLLNLAAL 307
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1658-2103 |
2.00e-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: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1658 QLKQQVEMLQDHKR-----------ELLGSPSLGENCVaglkerlWKLESSALEQQKIQSQQENTIKQLEQLR---QRFE 1723
Cdd:pfam10174 71 HLQLTIQALQDELRaqrdlnqllqqDFTTSPVDGEDKF-------STPELTEENFRRLQSEHERQAKELFLLRktlEEME 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1724 LEIERMKQ--------------MHQKD---REDQEEELEDVRQ--SCQKRLHQLEMQLEQEYEEKQMV---LHEK---QD 1778
Cdd:pfam10174 144 LRIETQKQtlgardesikklleMLQSKglpKKSGEEDWERTRRiaEAEMQLGHLEVLLDQKEKENIHLreeLHRRnqlQP 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1779 LEGLIGTLCDQIGHRDFDVEKrLRRDLRRthaLLSDVQLL----LGTMEDGKTSVSKEELEKVHS--------QLEQSEA 1846
Cdd:pfam10174 224 DPAKTKALQTVIEMKDTKISS-LERNIRD---LEDEVQMLktngLLHTEDREEEIKQMEVYKSHSkfmknkidQLKQELS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1847 KCEEALKTqkvLTADLESMHSELENMTRNKSLVDEQLYR-------LQFEKADLLKRIDEDQDDLNELMQKHKDLIAQSA 1919
Cdd:pfam10174 300 KKESELLA---LQTKLETLTNQNSDCKQHIEVLKESLTAkeqraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1920 ADIGQIQELQ--LQLEEAK-----KEKHKLQEQL-----QVAQM--RIEYLEQ--STVDRAIVSRQEAvICDLENKTEFQ 1983
Cdd:pfam10174 377 TLAGEIRDLKdmLDVKERKinvlqKKIENLQEQLrdkdkQLAGLkeRVKSLQTdsSNTDTALTTLEEA-LSEKERIIERL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1984 KVQIKRFEVLVIRLRDSLIKMGEELSQAATS---ESQQRESSqyyqrrLEELKADMEELVQREAEASRRC----MELEKY 2056
Cdd:pfam10174 456 KEQREREDRERLEELESLKKENKDLKEKVSAlqpELTEKESS------LIDLKEHASSLASSGLKKDSKLksleIAVEQK 529
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 970949420 2057 VEELAAVRQTLQT-----DLETSIRRIADLQAALE-EVASSDSDTESVQTAVD 2103
Cdd:pfam10174 530 KEECSKLENQLKKahnaeEAVRTNPEINDRIRLLEqEVARYKEESGKAQAEVE 582
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1845-2102 |
2.04e-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: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1845 EAKCEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRlqfEKADLLKRIDEDQDDLNELMQKHKDLIAQSaadigq 1924
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEEKY------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1925 iQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdraivsrqeavicdlENKTEFQKVQIKrfEVLVIRLRDSLIKM 2004
Cdd:pfam07888 104 -KELSASSEELSEEKDALLAQRAAHEARIRELEE------------------DIKTLTQRVLER--ETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2005 GEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMELEKYVeelaavrQTLQTDLETSIRRIADLQAA 2084
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTI-------TTLTQKLTTAHRKEAENEAL 235
|
250
....*....|....*...
gi 970949420 2085 LEEVASSDSDTESVQTAV 2102
Cdd:pfam07888 236 LEELRSLQERLNASERKV 253
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1404-1544 |
2.05e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1404 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDL--------LESKIADLTSDLADerfkgdvacqvLESERAERLQAFREV 1475
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEasferlaeLRDELAELEEELEA-----------LKARWEAEKELIEEI 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1476 QELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDLERNPTGGADE-------W------QMrfdcaqMENEflRKRLQQCEE 1542
Cdd:COG0542 474 QELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDiaevvsrWtgipvgKL------LEGE--REKLLNLEE 545
|
..
gi 970949420 1543 RL 1544
Cdd:COG0542 546 EL 547
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1551-2127 |
2.08e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1551 RKELEQKLGELQSAYDGAKKmahqLKRKCHHLTCDLEDTCVLLENQQSRNHELEKKQKkfdlQLAQAlgESVFEKGLREK 1630
Cdd:PRK01156 151 RKKILDEILEINSLERNYDK----LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKK----QIADD--EKSHSITLKEI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1631 vtqENTSVrwELGQLQQQLKQKEQEASQLKQQVEMLQDHKREL------LGSPSLGENCVAGLKERLWKLESSALeqqki 1704
Cdd:PRK01156 221 ---ERLSI--EYNNAMDDYNNLKSALNELSSLEDMKNRYESEIktaesdLSMELEKNNYYKELEERHMKIINDPV----- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1705 qsqqentIKQLEQLRQRFELeiermkqmhQKDREDQEEELEDVRQSCQK--RLHQLEMQLEQEYEEKQMVLHEKQDLegl 1782
Cdd:PRK01156 291 -------YKNRNYINDYFKY---------KNDIENKKQILSNIDAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDL--- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1783 igtlcdqighrdfdveKRLRRDLRRTHallSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQSEakceealkTQKVLTADL 1862
Cdd:PRK01156 352 ----------------NNQILELEGYE---MDYNSYLKSIESLKKKIEEYSKNIERMSAFISE--------ILKIQEIDP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1863 ESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNEL--------------MQKHKDLIAQSAADIGQIQEl 1928
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEE- 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1929 qlQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSrqeavicdlENKTEFQKVQIKRFEVLVIRLRDSLIKmgeel 2008
Cdd:PRK01156 484 --KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINE---------YNKIESARADLEDIKIKINELKDKHDK----- 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2009 SQAATSESQQRESSQYYQRRLEELKA-------DMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRRIAD- 2080
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRTSWLNAlavisliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENe 627
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 970949420 2081 ---LQAALEEVASSDSDTESVQTAVDCGSSGRKEMDnvSILSSQPEGSLQ 2127
Cdd:PRK01156 628 annLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID--SIIPDLKEITSR 675
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1379-1837 |
2.14e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1379 AVKDWPWWQLLGSLQpllsatigtEQLRAKEEELTTLRRKLEKSEKLRNELRQntdlLESKIADLTSDLADERfkgdvac 1458
Cdd:COG4717 124 LLQLLPLYQELEALE---------AELAELPERLEELEERLEELRELEEELEE----LEAELAELQEELEELL------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1459 qvleseRAERLQAFREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQlnDLERnptggadewqmrfDCAQMENEFLRKRLQ 1538
Cdd:COG4717 184 ------EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEE-------------ELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1539 QCEERLDSELTARKELEQKLGELQSAYDGAKKMAhqlkrkchhltcdlEDTCVLLENQQSRNHELEKKQKKFDLQLAQAL 1618
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTIA--------------GVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1619 GESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSpSLGENCVAGLKERLWKLESSA 1698
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1699 LEQQKIQSQQENTIKQLEQLRQRFELEIERMKQ-MHQKDREDQEEELEDVRQscqkRLHQLEMQLEQEYEEKQMVLHEKQ 1777
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELLGELEElLEALDEEELEEELEELEE----ELEELEEELEELREELAELEAELE 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1778 DLEGliGTLCDQIGHRDFDVEKRLRRDLRRTHALlsdvQLLLGTMEDGKTSVSKEELEKV 1837
Cdd:COG4717 464 QLEE--DGELAELLQELEELKAELRELAEEWAAL----KLALELLEEAREEYREERLPPV 517
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1924-2088 |
2.15e-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: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1924 QIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQstvdrAIVSRQEAVicdlenktEFQKVQIKRFEVLVIRLRDSLIK 2003
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEA-----RLEAAKTEL--------EDLEKEIKRLELEIEEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 2004 MGEELSQAATsesqQRESsQYYQRRLEELKADMEELVQREAEASRRCMELEKYVEELAAVRQTLQTDLETSIRR----IA 2079
Cdd:COG1579 78 YEEQLGNVRN----NKEY-EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEldeeLA 152
|
....*....
gi 970949420 2080 DLQAALEEV 2088
Cdd:COG1579 153 ELEAELEEL 161
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1403-2055 |
2.17e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.59 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRrKLEKSEKLRNElRQNTDLLESKIADLTSDLADERFKGDVA-CQVLESERAERLQafREVQELKSK 1481
Cdd:pfam07111 73 QELRRLEEEVRLLR-ETSLQQKMRLE-AQAMELDALAVAEKAGQAEAEGLRAALAgAEMVRKNLEEGSQ--RELEEIQRL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HeqvQKKLGDVNKQLEEAQQKI---------QLNDLERNPTGGADEWQMrfdcAQMENEFLRKRLQQCEERLDSELTARK 1552
Cdd:pfam07111 149 H---QEQLSSLTQAHEEALSSLtskaeglekSLNSLETKRAGEAKQLAE----AQKEAELLRKQLSKTQEELEAQVTLVE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1553 ELEQKLGElqSAYDGAKKMAHQLKRK-----CHHLT---CDLEDTCVLLENQ-QSRNHELEKKQKKF--DLQLAQALgES 1621
Cdd:pfam07111 222 SLRKYVGE--QVPPEVHSQTWELERQelldtMQHLQedrADLQATVELLQVRvQSLTHMLALQEEELtrKIQPSDSL-EP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1622 VFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQdhkrellgspslgencvaglkerlwklessalEQ 1701
Cdd:pfam07111 299 EFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQ--------------------------------EQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1702 QKIQSQQENTIKQLEQLRQRfELEIERMKQMHQKDREDQEEEledVRQSCQKRLHQLEMQLeqeyeeKQMVLHEKQDLEG 1781
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAA-EVEVERMSAKGLQMELSRAQE---ARRRQQQQTASAEEQL------KFVVNAMSSTQIW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1782 LIGTLC--DQIGHRDFDVEKRLRRDLRRTHALLsdvqlllGTMEDgKTSVSKEELEkvhsqleqSEAKCEEALKTQKVLT 1859
Cdd:pfam07111 417 LETTMTrvEQAVARIPSLSNRLSYAVRKVHTIK-------GLMAR-KVALAQLRQE--------SCPPPPPAPPVDADLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1860 ADLESMHSElenmtRNKSLVDEQL--YRLQFEKADLLKRIDEDQDDLNELMQkhkdliaqsaadigqiqELQLQLEEAKK 1937
Cdd:pfam07111 481 LELEQLREE-----RNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVAQ-----------------QLEQELQRAQE 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1938 EKHKLQEQLQVAQMRieylEQSTVDRAIVSRQEavicdLENKTEF--QKVQIKRFEVLViRLRDSLIKMGEELSQAATSE 2015
Cdd:pfam07111 539 SLASVGQQLEVARQG----QQESTEEAASLRQE-----LTQQQEIygQALQEKVAEVET-RLREQLSDTKRRLNEARREQ 608
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 970949420 2016 SQQRESSQYYQRRLEELKADMEELVQREAEA--------SRRCMELEK 2055
Cdd:pfam07111 609 AKAVVSLRQIQHRATQEKERNQELRRLQDEArkeegqrlARRVQELER 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1402-1731 |
2.40e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1402 TEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLEskiadltsdladerfkgdvacqvlesERAERLQAFREVQELKSK 1481
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQ--------------------------ERREALQRLAEYSWDEID 662
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1482 HEQVQKKLGDVNKQLEEAQQkiqlndlernptgGADEWQMrfdcaqmenefLRKRLQQCEERLDseltarkELEQKLGEL 1561
Cdd:COG4913 663 VASAEREIAELEAELERLDA-------------SSDDLAA-----------LEEQLEELEAELE-------ELEEELDEL 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1562 QSAYDGAKKMAHQLKRKCHHLTCDLEDtcvlLENQQSRNHELEkkqkkFDLQLAQALGESVfEKGLREKVTQENTSVRwe 1641
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEA----AEDLARLELRAL-----LEERFAAALGDAV-ERELRENLEERIDALR-- 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1642 lgqlqqqlkqkeQEASQLKQQVE-MLQDHKRE-----LLGSPSLGENcvAGLKERLWKLESSAL---EQQKIQSQQENTI 1712
Cdd:COG4913 780 ------------ARLNRAEEELErAMRAFNREwpaetADLDADLESL--PEYLALLDRLEEDGLpeyEERFKELLNENSI 845
|
330
....*....|....*....
gi 970949420 1713 KQLEQLRQRFELEIERMKQ 1731
Cdd:COG4913 846 EFVADLLSKLRRAIREIKE 864
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1416-1791 |
2.45e-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: 43.40 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1416 RRKLEKSEKLRNELRQNTDLLESKIADLTsDLADERFKGDVACQVLESE---RAERLQAFREVQELKSKHEQVQKKLGDV 1492
Cdd:COG3096 281 RELSERALELRRELFGARRQLAEEQYRLV-EMARELEELSARESDLEQDyqaASDHLNLVQTALRQQEKIERYQEDLEEL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1493 NKQLEEAQQKIQlndlernptgGADEWQMRfdcaqmenefLRKRLQQCEERLDSELTARKELEQKLGELQSAyDGAKKMA 1572
Cdd:COG3096 360 TERLEEQEEVVE----------EAAEQLAE----------AEARLEAAEEEVDSLKSQLADYQQALDVQQTR-AIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1573 HQLKRKCHHLtCDLEDtcVLLENQQSRNHELEKKQKKFD---LQLAQALGESVFEKGLREKVtqentsvrWELGQLQQQL 1649
Cdd:COG3096 419 VQALEKARAL-CGLPD--LTPENAEDYLAAFRAKEQQATeevLELEQKLSVADAARRQFEKA--------YELVCKIAGE 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1650 KQKEQEASQLKQQVEMLQDHKrellgspSLGENcVAGLKERLWKLESSALEQQKIQSQQENTIKQLEQLRQRFElEIERM 1729
Cdd:COG3096 488 VERSQAWQTARELLRRYRSQQ-------ALAQR-LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE-ELEEL 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 1730 KQMHQKDREDQEEELEDvrqsCQKRLHQLEMQLEQ------EYEEKQMVLHEKQD-LEgligTLCDQIG 1791
Cdd:COG3096 559 LAELEAQLEELEEQAAE----AVEQRSELRQQLEQlrarikELAARAPAWLAAQDaLE----RLREQSG 619
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1681-1776 |
2.67e-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: 42.18 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1681 ENCVAGLKERLWKLESSALEQQKIQSQQentikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVRQSCQKrlhQLEM 1760
Cdd:cd16269 199 EIEAERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALESKLK---EQEA 270
|
90
....*....|....*.
gi 970949420 1761 QLEQEYEEKQMVLHEK 1776
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1831-1973 |
2.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVDEQLYRLQFEKADLLKR----IDEDQDDLN 1905
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEeKKEKLQEEEDKLLEEAEKEAQQAIKEakkeADEIIKELR 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1906 ELMQ-KHKDLIAQSAADI-GQIQELQLQLEEAKKEKHKLQEQLQVAQ-MRIEYLEQSTVDRAIVSRQEAVI 1973
Cdd:PRK00409 595 QLQKgGYASVKAHELIEArKRLNKANEKKEKKKKKQKEKQEELKVGDeVKYLSLGQKGEVLSIPDDKEAIV 665
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1693-1935 |
3.41e-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: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1693 KLESSALEQQKIQSQQENTIKQLEQLRQrfelEIERMkqmhQKDREDQEEELEDVRQscqkrlhQLEmQLEQEYEEKQMV 1772
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQA----ELEEL----NEEYNELQAELEALQA-------EID-KLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 LHEKQDlegligtlcdqighrdfDVEKRLRrDLRRTHALLSDVQLLLG-----TMEDGKTSVSK---------EELEKVH 1838
Cdd:COG3883 81 IEERRE-----------------ELGERAR-ALYRSGGSVSYLDVLLGsesfsDFLDRLSALSKiadadadllEELKADK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1839 SQLEQSEAKCEEALKTQKVLTADLESMHSELEnmtRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLIAQS 1918
Cdd:COG3883 143 AELEAKKAELEAKLAELEALKAELEAAKAELE---AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
250
....*....|....*..
gi 970949420 1919 AADIGQIQELQLQLEEA 1935
Cdd:COG3883 220 AAAAAAAAAAAAAAAAA 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1684-2087 |
3.70e-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: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1684 VAGLKERLWKLESsALEQQKIQSQQENTikQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QS 1750
Cdd:COG3096 838 LAALRQRRSELER-ELAQHRAQEQQLRQ--QLDQLKEQLQLLNKLLPQANLLADETLADRLEELReeldaaqeaqafiQQ 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1751 CQKRLHQLEM-------------QLEQEYEEKQmvlHEKQDLEGLIGTLCDQIGhrdfdvekrlrrdlRRTHALLSDVQL 1817
Cdd:COG3096 915 HGKALAQLEPlvavlqsdpeqfeQLQADYLQAK---EQQRRLKQQIFALSEVVQ--------------RRPHFSYEDAVG 977
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1818 LLGTmedgktsvSKEELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELenmtrnkslvdeqlyrlqfekADLLKRI 1897
Cdd:COG3096 978 LLGE--------NSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVL---------------------ASLKSSR 1028
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1898 DEDQDDLNELMQKHKDLIAQSAADIgqiqelqlqLEEAKKEKHKLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLE 1977
Cdd:COG3096 1029 DAKQQTLQELEQELEELGVQADAEA---------EERARIRRDELHEELSQNRSRRSQLEKQ------LTRCEAEMDSLQ 1093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1978 N---KTEfQKVQIKRFEV--------LVIRL-RDSLIKMG---EELsqAATSESQQRESSQYYQRRLEELKADMEEL--V 2040
Cdd:COG3096 1094 KrlrKAE-RDYKQEREQVvqakagwcAVLRLaRDNDVERRlhrREL--AYLSADELRSMSDKALGALRLAVADNEHLrdA 1170
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 970949420 2041 QREAEASRRCmelEKYVEELAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:COG3096 1171 LRLSEDPRRP---ERKVQFYIAVYQHLRERIRQDIIRTDDPVEAIEQ 1214
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1807-1915 |
3.91e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 40.29 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1807 RTHALLSDVQLLLGTMEDGKTsvskeELEKVHSQLEQSEAKCEEALKTQKVLTADLESMHSELEnmTRNKSLVDEQLYRL 1886
Cdd:pfam09744 44 RNQEHNVELEELREDNEQLET-----QYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLE--EENRRLEADHVSRL 116
|
90 100
....*....|....*....|....*....
gi 970949420 1887 QFEKADLLKRIDEDQDDLNELMQKHKDLI 1915
Cdd:pfam09744 117 EEKEAELKKEYSKLHERETEVLRKLKEVV 145
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1601-2110 |
4.00e-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: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1601 HELEKKQKKFDLQLAQALGESVFEKGLREKVTQENTSVRWELGQLQQQLKQKEQEASQLKQQVEMLQDHKRELLGSPSLG 1680
Cdd:pfam12128 241 PEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1681 ENCVAGLKERLWKLESSALEQQKIQSQQENTIK-QLEQLRQRFELEIERmkqmHQKDREDQEEELEDVRQSCQKRLHQLE 1759
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGK----HQDVTAKYNRRRSKIKEQNNRDIAGIK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1760 MQLEQEYEEKQMVLH-EKQDLEGLIGTLCDQI--GHRDF-DVEKRLRRDLRRTHALLSDVQlllgtmedgktsVSKEELE 1835
Cdd:pfam12128 397 DKLAKIREARDRQLAvAEDDLQALESELREQLeaGKLEFnEEEYRLKSRLGELKLRLNQAT------------ATPELLL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1836 kvhsQLEQSEAKCEEALKTQKVLTADLESMHSELenmTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQKHKDLI 1915
Cdd:pfam12128 465 ----QLENFDERIERAREEQEAANAEVERLQSEL---RQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1916 A---QSAAD----IGQI----QELQLQLEEAKKEKHKLQEQ----LQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 1980
Cdd:pfam12128 538 HflrKEAPDweqsIGKVispeLLHRTDLDPEVWDGSVGGELnlygVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAR 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1981 EfqkvQIKRFEVLVIRLRDSLIKMGEELSQAATSESQQRESSQYYQRRLEELKADMEELV---QREAEASRRCMELEKYV 2057
Cdd:pfam12128 618 E----KQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALaerKDSANERLNSLEAQLKQ 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 970949420 2058 EELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTAVDCGSSGRK 2110
Cdd:pfam12128 694 LDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAK 746
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
1831-1964 |
4.01e-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: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1831 KEELEKvhSQLEQSEAK-CEEALKTQKVLTADLESMHSELENMTRNKSLVDEQLYRLQFEKADLLKRIDEDQDDLNELMQ 1909
Cdd:pfam06785 62 KEKFEK--SFLEEKEAKlTELDAEGFKILEETLEELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRL 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 970949420 1910 KHKDLIAQSAAdigQIQELQLQLEEAKKEKHKLQEQlqvaqmrIEYLEQSTVDRA 1964
Cdd:pfam06785 140 ESEEQLAEKQL---LINEYQQTIEEQRSVLEKRQDQ-------IENLESKVRDLN 184
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1417-1629 |
4.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1417 RKLEKSEKLRNELRQNTDLLeskIADLTSDLADERFKGDVACQVLESERAERLQAFREVQELKSKHEQVQKKLGDVNKQL 1496
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGIL---IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1497 EEAQQKIQLNDLERNPTggadewQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYDGAKKMAHQLK 1576
Cdd:COG4372 83 EELNEQLQAAQAELAQA------QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 970949420 1577 RKCHHLTCDLEDTcvlleNQQSRNHELEKKQKKFDLQLAQALGESVFEKGLRE 1629
Cdd:COG4372 157 EQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
633-723 |
4.10e-03 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 40.41 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 633 PAHIGSMAQRAYWALLNQRRDQSIVALGWSGAGKTTCCEQVLEHLVGMAGSVDGR--------------VSVEKIRATFT 698
Cdd:cd01363 32 QPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgetegwvylteitvTLEDQILQANP 111
|
90 100
....*....|....*....|....*
gi 970949420 699 VLRAFGSVSMAHSRSATRFSMVMSL 723
Cdd:cd01363 112 ILEAFGNAKTTRNENSSRFGKFIEI 136
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1403-1616 |
4.65e-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: 42.06 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLaderfkgdvacQVLESERAErlqAFREVQELKSKH 1482
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----------RALEQELAA---LEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1483 EQVQKKLGDVNKQLEEAQQKIQLNDLERNPT-----GGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQK 1557
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 1558 LGELQSAYDGAKKMAHQLKRkchhltcdledtcvLLENQQSRNHELEKKQKKFDLQLAQ 1616
Cdd:COG4942 173 RAELEALLAELEEERAALEA--------------LKAERQKLLARLEKELAELAAELAE 217
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1894-2101 |
4.67e-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: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1894 LKRIDEDQDDLNELmqkhKDLIAQSAAdigQIQELQLQLEEAKKeKHKLQEQLQVAQMRIEYLEqstvDRAIVSRQEAvi 1973
Cdd:COG1196 178 ERKLEATEENLERL----EDILGELER---QLEPLERQAEKAER-YRELKEELKELEAELLLLK----LRELEAELEE-- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1974 cdLENKTEFQKVQIKRFEvlvirlrdslikmgEELSQAATSESQQRESSQYYQRRLEELKADMEELVQREAEASRRCMEL 2053
Cdd:COG1196 244 --LEAELEELEAELEELE--------------AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 970949420 2054 EKYVEELAAVRQTLQTDLETSIRRIADLQAALEEVASSDSDTESVQTA 2101
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1417-1779 |
4.93e-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: 42.20 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1417 RKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgDVACQVLESERAERLQAF----REVQELKSKHEQVQKKLGDV 1492
Cdd:pfam15964 353 KALIQCEQLKSELERQKERLEKELASQQEKRAQEK---EALRKEMKKEREELGATMlalsQNVAQLEAQVEKVTREKNSL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1493 NKQLEEAQQKIQLNDLERNPTGGadewQMRF--DCAQMENEFLRKRLQQCEERLDSELTARkelEQKLGELQSAYDGAKK 1570
Cdd:pfam15964 430 VSQLEEAQKQLASQEMDVTKVCG----EMRYqlNQTKMKKDEAEKEHREYRTKTGRQLEIK---DQEIEKLGLELSESKQ 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1571 MAHQLKRKCHHLTCDLEDTCVLLENQQSRNH----ELEKKQKKFDLQL-AQALGESVFEKGLREKVTQENTSVRWELGQL 1645
Cdd:pfam15964 503 RLEQAQQDAARAREECLKLTELLGESEHQLHltrlEKESIQQSFSNEAkAQALQAQQREQELTQKMQQMEAQHDKTVNEQ 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1646 QQQLKQKEQEASQLKQQVEMLQDHKRELlgspslgencvaglkerlwkLESSALEQQKIQSQQENTIKQLEQLRQRFElE 1725
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEECCTLAKKLEEI--------------------TQKSRSEVEQLSQEKEYLQDRLEKLQKRNE-E 641
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 970949420 1726 IERMKQMHQKDREDQEEELEDVRQSCQ---KRLHQLEMQLEQEYEEKQMVLHEKQDL 1779
Cdd:pfam15964 642 LEEQCVQHGRMHERMKQRLRQLDKHCQataQQLVQLLSKQNQLFKERQNLTEEVQSL 698
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1403-1608 |
4.93e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.42 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELT---TLRRKLEKSEKLRNEL--RQNTDLLESKIADLTSDLADERFKGDVACQVLESERAERL----QAFR 1473
Cdd:pfam17380 299 ERLRQEKEEKArevERRRKLEEAEKARQAEmdRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIameiSRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1474 EVQEL----KSKHEQVQKKLGDVNKQL---EEAQQKIQLNDLE----RNPTGGADEWQMRFDCAQMENEFLRKRLQQCEE 1542
Cdd:pfam17380 379 ELERLqmerQQKNERVRQELEAARKVKileEERQRKIQQQKVEmeqiRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 970949420 1543 RLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKChhLTCDLEDT-CVLLENQQSRN---HELEKKQK 1608
Cdd:pfam17380 459 QQQVERLRQQEEERKRKKLELEKEKrDRKRAEEQRRKI--LEKELEERkQAMIEEERKRKlleKEMEERQK 527
|
|
| PHA03169 |
PHA03169 |
hypothetical protein; Provisional |
261-514 |
6.20e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 223003 [Multi-domain] Cd Length: 413 Bit Score: 41.49 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 261 KDRQGTRPQAQGPGEGVRPGKAEKeGAEPTNTVEKGNVSKDVGSEGKHVRPQIPGRKWGGFLGRRSKwDGPQNKKDKEGV 340
Cdd:PHA03169 24 KRHGGTREQAGRRRGTAARAAKPA-PPAPTTSGPQVRAVAEQGHRQTESDTETAEESRHGEKEERGQ-GGPSGSGSESVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 341 LLSKAEKTGEPQTQMEKTSQVQGELGDDLRMGEkaGELRSTTGKAGESWDKKEKMGQPQGKSGNAGEARSQTEKGCEAPK 420
Cdd:PHA03169 102 SPTPSPSGSAEELASGLSPENTSGSSPESPASH--SPPPSPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 421 EVSTMVESPAA-------PGKGGWPGSRGQEAEEPCSRAGDGA--------GALETELEGPSQPALEKDAERPRIRKENQ 485
Cdd:PHA03169 180 PPTSEPEPDSPgppqsetPTSSPPPQSPPDEPGEPQSPTPQQApspntqqaVEHEDEPTEPEREGPPFPGHRSHSYTVVG 259
|
250 260 270
....*....|....*....|....*....|....*.
gi 970949420 486 DGPAPQEEG-------KGGQSRDSDQAPEDRWYEAE 514
Cdd:PHA03169 260 WKPSTRPGGvpklclrCTSHPSHRSRLPEGQQSEDK 295
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1393-1765 |
6.72e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1393 QPLLSATIGTEQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADL-----TSDLADERFKgdVACQVLESERae 1467
Cdd:PRK10929 48 EALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVppnmsTDALEQEILQ--VSSQLLEKSR-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1468 rlqafrEVQELKSKHEQVQKKLGDVNKQLEEAQQkiQLNDLERN----PTGGADEWQMRFDCAQMENEFLRKRLQQCEEr 1543
Cdd:PRK10929 124 ------QAQQEQDRAREISDSLSQLPQQQTEARR--QLNEIERRlqtlGTPNTPLAQAQLTALQAESAALKALVDELEL- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1544 ldSELTA--RKELEQKLGELqsaydgakkmahqLKRKCHHLTCDLEDTCVLLENQQSRNHE--LEK-------------- 1605
Cdd:PRK10929 195 --AQLSAnnRQELARLRSEL-------------AKKRSQQLDAYLQALRNQLNSQRQREAEraLEStellaeqsgdlpks 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1606 --KQKKFDLQLAQALGESVFEKGL----REKVTQENTSVRWELgqlqqqlkqkeqeaSQLKQQVEMLQDhkrellgSPSL 1679
Cdd:PRK10929 260 ivAQFKINRELSQALNQQAQRMDLiasqQRQAASQTLQVRQAL--------------NTLREQSQWLGV-------SNAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1680 GEncvaGLKERLWKLEssalEQQKIQsQQENTIKQLEQLRQRFELEIERMKQMHQKdREDQEEELEdvrqSCQKRLHQLE 1759
Cdd:PRK10929 319 GE----ALRAQVARLP----EMPKPQ-QLDTEMAQLRVQRLRYEDLLNKQPQLRQI-RQADGQPLT----AEQNRILDAQ 384
|
....*.
gi 970949420 1760 MQLEQE 1765
Cdd:PRK10929 385 LRTQRE 390
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1656-1960 |
6.91e-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: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1656 ASQLKQQV-EMLQDHKRELLGSPSLGEncvaglkERLWKLESSALEQQKIQsQQENTIKQLEQLRQRFELEIERMKQ--- 1731
Cdd:pfam07888 89 LRQSREKHeELEEKYKELSASSEELSE-------EKDALLAQRAAHEARIR-ELEEDIKTLTQRVLERETELERMKErak 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1732 ---MHQKDREDQEEELEDVRQSCQKRLHQLEMQLEQEYEEKQMVLHEKQDLEGLIGTLCDQIG--HRDFDVEKRLRRDLR 1806
Cdd:pfam07888 161 kagAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTtaHRKEAENEALLEELR 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1807 RTHALLSdvqlllgtMEDGKTSVSKEELEKV-----HSQLEQSEAKCEEALKTQKVLTADLE------SMHSELENMTRN 1875
Cdd:pfam07888 241 SLQERLN--------ASERKVEGLGEELSSMaaqrdRTQAELHQARLQAAQLTLQLADASLAlregraRWAQERETLQQS 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1876 KSLVDEQLYRLQFEKADLLKRIDEDQDDLN----ELMQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQM 1951
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEERMEREklevELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
....*....
gi 970949420 1952 RIEYLEQST 1960
Cdd:pfam07888 393 YIRQLEQRL 401
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1404-1570 |
7.02e-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: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1404 QLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvLESERAErlqafREVQELKSKHE 1483
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE---------KEIKRLE-----LEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1484 QVQKKLGDV--NKQLEEAQQKIQLndlernptggadewqmrfdcAQMENEFLRKRLQQCEERLDSELTARKELEQKLGEL 1561
Cdd:COG1579 77 KYEEQLGNVrnNKEYEALQKEIES--------------------LKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
....*....
gi 970949420 1562 QSAYDGAKK 1570
Cdd:COG1579 137 EAELEEKKA 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1698-2087 |
7.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1698 ALEQQKIQSQQENtiKQLEQLRQRFELEIERMKQMHQKDREDQEEELEDVR-------------QSCQKRLHQLEMQL-- 1762
Cdd:PRK04863 852 ALADHESQEQQQR--SQLEQAKEGLSALNRLLPRLNLLADETLADRVEEIReqldeaeeakrfvQQHGNALAQLEPIVsv 929
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1763 ----EQEYEE-KQMVLHEKQDLegligtlcdqighRDFDVEKRLRRDL--RRTHALLSDVQLLLGtmedgKTSVSKEELE 1835
Cdd:PRK04863 930 lqsdPEQFEQlKQDYQQAQQTQ-------------RDAKQQAFALTEVvqRRAHFSYEDAAEMLA-----KNSDLNEKLR 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1836 KVHSQLEQSEAKCEEALKTQKvltadlesmhselENMTRNKslvdeQLYrlqfekADLLKRIDEDQDDLNELMQKHKDLI 1915
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ-------------AQLAQYN-----QVL------ASLKSSYDAKRQMLQELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1916 AQsaADIGQIQELQLQLEEakkekhkLQEQLQVAQMRIEYLEQStvdraiVSRQEAVICDLENK-TEFQK--VQIKRFEV 1992
Cdd:PRK04863 1048 VP--ADSGAEERARARRDE-------LHARLSANRSRRNQLEKQ------LTFCEAEMDNLTKKlRKLERdyHEMREQVV 1112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1993 -------LVIRL-RDSLIK---MGEELsqAATSESQQRESSQYYQRRLEELKADMEEL--VQREAEASRRcmeLEKYVEE 2059
Cdd:PRK04863 1113 nakagwcAVLRLvKDNGVErrlHRREL--AYLSADELRSMSDKALGALRLAVADNEHLrdVLRLSEDPKR---PERKVQF 1187
|
410 420
....*....|....*....|....*...
gi 970949420 2060 LAAVRQTLQTDLETSIRRIADLQAALEE 2087
Cdd:PRK04863 1188 YIAVYQHLRERIRQDIIRTDDPVEAIEQ 1215
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1403-2078 |
8.03e-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: 41.86 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDL-------------LESKIADLTSDLADERFKGDVACQVLE------S 1463
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAasdhlnlvqtalrQQEKIERYQEDLEELTERLEEQEEVVEeaaeqlA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1464 ERAERLQAFR-EVQELKSKHEQVQKKLgDVN-----------KQLEEAQQKIQLNDLERNptgGADEWQMRFDcAQmENE 1531
Cdd:COG3096 379 EAEARLEAAEeEVDSLKSQLADYQQAL-DVQqtraiqyqqavQALEKARALCGLPDLTPE---NAEDYLAAFR-AK-EQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1532 FLRKRLQQcEERLDSELTARKELEQKLGELQSAYDG-AKKMAHQLKRKchhLTCDLEDTCVLLENQQS---RNHELEKK- 1606
Cdd:COG3096 453 ATEEVLEL-EQKLSVADAARRQFEKAYELVCKIAGEvERSQAWQTARE---LLRRYRSQQALAQRLQQlraQLAELEQRl 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1607 ---QKKFDL--QLAQALGESVFEKGLREKVTQENTSVRWELgqlQQQLKQKEQEASQLKQQVEMLQDHKRELlgspslge 1681
Cdd:COG3096 529 rqqQNAERLleEFCQRIGQQLDAAEELEELLAELEAQLEEL---EEQAAEAVEQRSELRQQLEQLRARIKEL-------- 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1682 ncvaGLKERLWKLESSALEQ------------QKIQSQQENTIK----------QLEQLRQRFELEIERmkqMHQKD-RE 1738
Cdd:COG3096 598 ----AARAPAWLAAQDALERlreqsgealadsQEVTAAMQQLLErereatverdELAARKQALESQIER---LSQPGgAE 670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1739 DQE--------------EELEDV---------------RQ--------SCQKRLHQLEMQLE---------QEYEEKqmv 1772
Cdd:COG3096 671 DPRllalaerlggvllsEIYDDVtledapyfsalygpaRHaivvpdlsAVKEQLAGLEDCPEdlyliegdpDSFDDS--- 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1773 LHEKQDLEgliGTLCDQIGHRDFDVEK-----RLRRDLRRTHALLSDVQLLLGTMEDGKTSVSKEELEKVHSQLEQ---- 1843
Cdd:COG3096 748 VFDAEELE---DAVVVKLSDRQWRYSRfpevpLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgg 824
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1844 -----SEAKCEEALKTQKVLTADLESMHSELE-NMTRNKSLVD------EQLYRLQ-----FEKADLLKRIDEDQDDLNE 1906
Cdd:COG3096 825 hlavaFAPDPEAELAALRQRRSELERELAQHRaQEQQLRQQLDqlkeqlQLLNKLLpqanlLADETLADRLEELREELDA 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1907 L------MQKHKDLIAQSAADIGQIQELQLQLEEAKKEKHKLQEQLQVAQMRIEYLEQSTVDRAIVSRQEAVICDLENKT 1980
Cdd:COG3096 905 AqeaqafIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLLGENSD 984
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1981 efqkvqikrfevLVIRLRDSLIKMGEELSQAATS-ESQQRESSQYYQRR-------------LEELKADMEEL-VQREAE 2045
Cdd:COG3096 985 ------------LNEKLRARLEQAEEARREAREQlRQAQAQYSQYNQVLaslkssrdakqqtLQELEQELEELgVQADAE 1052
|
810 820 830
....*....|....*....|....*....|...
gi 970949420 2046 ASRRCMELEKYVEELAAVRQTLQTDLETSIRRI 2078
Cdd:COG3096 1053 AEERARIRRDELHEELSQNRSRRSQLEKQLTRC 1085
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1403-1504 |
8.35e-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: 8.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERfkgdvacqvleSERAERLQAFREVQELKSKH 1482
Cdd:COG2433 406 RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDREI 474
|
90 100
....*....|....*....|..
gi 970949420 1483 EQVQKKLGDVNKQLEEAQQKIQ 1504
Cdd:COG2433 475 ERLERELEEERERIEELKRKLE 496
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1372-1508 |
8.54e-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: 8.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1372 KNVAVFLAVKDW-PW-WQLLGSLQPLLSATIGT-----EQLRAKEEELTTLRRKLEKS-----EKLRNELRQNTDLLESK 1439
Cdd:smart00787 123 KTFARLEAKKMWyEWrMKLLEGLKEGLDENLEGlkedyKLLMKELELLNSIKPKLRDRkdaleEELRQLKQLEDELEDCD 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 970949420 1440 IADLtsDLADERFKGDVACQVLESERAERLQafREVQELKSKHEQVQKKLGDVNKQLEEAQQKIQLNDL 1508
Cdd:smart00787 203 PTEL--DRAKEKLKKLLQEIMIKVKKLEELE--EELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRG 267
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
1511-1633 |
9.49e-03 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 40.46 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1511 NPTGGADEWQMRFDCAQMENEFLRKRLQQCEERLDSELTARKELEQKLGELQSAYdGAKKMAHQ-------LKRKCHHLT 1583
Cdd:pfam15294 123 NEGGGSALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQ-GAKKDVKSnlkeisdLEEKMAALK 201
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 970949420 1584 CDLEDTCVLLENQQ--------SRNHELEKKQKkfdlQLAQAlgesvfEKGLREKVTQ 1633
Cdd:pfam15294 202 SDLEKTLNASTALQksleedlaSTKHELLKVQE----QLEMA------EKELEKKFQQ 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1403-1570 |
9.79e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1403 EQLRAKEEELTTLRRKLEKSEKLRNELRQNTDLLESKIADLTSDLADERFKgdvacqvLESERAER-LQAF-REVQELKS 1480
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-------LGNVRNNKeYEALqKEIESLKR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970949420 1481 KHEQVQKKLGDVNKQLEEAQQKIQLNDLERNptggadewQMRFDCAQMENEfLRKRLQQCEERLDSELTARKELEQKLGE 1560
Cdd:COG1579 104 RISDLEDEILELMERIEELEEELAELEAELA--------ELEAELEEKKAE-LDEELAELEAELEELEAEREELAAKIPP 174
|
170
....*....|.
gi 970949420 1561 -LQSAYDGAKK 1570
Cdd:COG1579 175 eLLALYERIRK 185
|
|
| |
