|
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 ... |
120-877 |
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: 1128.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGtKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 279
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG-GVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 359
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 360 QKTCWLILASIYHLGAAGATKEPleeqdeaaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQ 439
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAA--------SAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 440 GPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHN 519
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 520 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASH--LVRSLAHADEARGLLWLLEEEALVPGAT 597
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqaLVRSDLRDEDRRGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 598 EDALLDRLFSYYGPQEGDkKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKiisnl 677
Cdd:cd01386 472 DDTFLERLFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE----- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 678 flgragsatvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEG 757
Cdd:cd01386 546 ---------------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNA 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 758 WPGEPRsassrrvsssseldlppGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 837
Cdd:cd01386 587 GKDERS-----------------TSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLT 649
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907082239 838 KKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd01386 650 KKLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
121-877 |
3.27e-143 |
|
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: 460.90 E-value: 3.27e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS-----VEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 274
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 275 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEN---NVFGIVPLSKPEEKQKAAQQFSKLQAAMK 351
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 352 VLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTl 431
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVAD------DESLKAAAKLLGVDAEDLEEALTTRTIKVGG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 432 qrstsfrqgpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSS--QHSLCSMMIVDTPGFQNPEWggsar 509
Cdd:cd00124 315 -----------ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 510 gASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVAD------DSV-AAVDQASHLvrslahade 579
Cdd:cd00124 379 -NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSfidFPDNQDCLDliegkpLGIlSLLDEECLF--------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 580 argllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFllGHSHGTNWVEYNVAGWLNYTKQNpat 659
Cdd:cd00124 449 --------------PKGTDATFLEKLYSAHGSHPRFFSK-----KRKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 660 qnaprllqdsqkkiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDT 739
Cdd:cd00124 505 ----------------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDT 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 740 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 819
Cdd:cd00124 530 LNSTQPHFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVR 580
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 820 MVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd00124 581 LPFDEFLKRYRILAPGATEKA-----SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
101-889 |
4.10e-112 |
|
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: 373.42 E-value: 4.10e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 101 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 180
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 181 TAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFS 258
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 259 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFgivpLSKPEEKQK 338
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 339 A----AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSL 414
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGN-------IEFEEGRNDNAASTVKDKEELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 415 EELSSAIfkhqlkggtLQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIV 494
Cdd:smart00242 307 EELEKAL---------TKRKIKTGGEVITKPL---NVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 495 DTPGFQ----NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqa 567
Cdd:smart00242 375 DIYGFEifevN----------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDwtfIDFFDNQDCID--------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 568 shLVRS-----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGT 639
Cdd:smart00242 436 --LIEKkppgiLSLLDEE----------CRFPKGTDQTFLEKLNQHH--------KKHPHFSKPKKKgrtEFIIKHYAGD 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 640 nwVEYNVAGWLnytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGM 717
Cdd:smart00242 496 --VTYDVTGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 718 aavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLR 797
Cdd:smart00242 550 ----------QFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPG-----------------------------DFDSSLVL 590
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 798 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:smart00242 591 HQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLR 665
|
810
....*....|..
gi 1907082239 878 AGTLARLEEQRD 889
Cdd:smart00242 666 PGQLAELEELRE 677
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
109-877 |
1.94e-107 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 359.67 E-value: 1.94e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 109 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 188
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 189 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGT-SGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDF 265
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 266 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---------NHLAENNVFGIvplskpeek 336
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 337 qKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEaaeagrkqFARHEWAQKAAYLLGCSLEE 416
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV--------PDDTENLQKAASLLGIDSTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 417 LSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVD 495
Cdd:pfam00063 303 LEKALCKRRIKTGRETVSKPQ------------NVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 496 TPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVR 572
Cdd:pfam00063 371 IYGFEIFEKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID-----------LIE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 573 S-----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEY 644
Cdd:pfam00063 434 KkplgiLSLLDEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEY 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 645 NVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkks 724
Cdd:pfam00063 494 NVEGFLEKNK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS------- 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 725 lciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSR 804
Cdd:pfam00063 559 ---QFKESLGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNG 606
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 805 LLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:pfam00063 607 VLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-1603 |
2.27e-107 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 378.65 E-value: 2.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 82 KLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMH 161
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 162 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--L 239
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 240 LEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL--- 316
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 317 ---NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAgatkEPLEEQDEAAeag 393
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGNI----EFKEDRNGAA--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 394 rkQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGG--TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFT 471
Cdd:COG5022 347 --IFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ--------------ALAIRDSLAKALYSNLFD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 472 LLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---L 548
Cdd:COG5022 411 WIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 549 AFDDLEPVADDSvaavdQASHLVRSLAHADEArgllwlleeeALVPGATEDALLDRLFSYYgPQEGDKKGQSPLLRSSKp 628
Cdd:COG5022 485 DYFDNQPCIDLI-----EKKNPLGILSLLDEE----------CVMPHATDESFTSKLAQRL-NKNSNPKFKKSRFRDNK- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 629 rhFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLALRRATS 708
Cdd:COG5022 548 --FVVKHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGRFPTLGS 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 709 MrktfttgmaavkkkslciqIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagl 788
Cdd:COG5022 610 R-------------------FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW---------------------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 789 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDEKRAVEELLESLDLEKSSCC 868
Cdd:COG5022 643 -TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEELVIDSSKYQ 720
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 869 LGLSRVFFRAGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWPWWKLFTTV 947
Cdd:COG5022 721 IGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYELKWRLFIKL 799
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 948 RPLIQVQLSEEQIRNKDEEIQQLRSKLEKV----EKERNELRLSSDRLETRISEltSELTDERNTGESASQLLDAETAER 1023
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETIYLQSAQRV 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1024 LRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKKRLQQELED 1099
Cdd:COG5022 878 ELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIEYVKLPELN 957
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1100 KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEETQ 1179
Cdd:COG5022 958 KLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EVAELQSASK 1033
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1180 REKLQREKLQREKDMLLAEAFSLKQQME-EKDLdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAK---V 1255
Cdd:COG5022 1034 IISSESTELSILKPLQKLKGLLLLENNQlQARY-------KALKLRRENSLL---DDKQLYQLESTENLLKTINVKdleV 1103
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1256 KDQEEELDEQAGSIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEvqlEEEYEDKQKALREK 1333
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLE---ALPSPPPFAALSEK 1180
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1334 RELESKL----STLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLknqleESEFTCAAA 1406
Cdd:COG5022 1181 RLYQSALydekSKLSSSEVNdlkNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNL-----NKKFDTPAS 1255
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1407 VKarkameveMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLeeDQEDMNEL-MKKHKAAVAQASRDmaqmnDLQA 1485
Cdd:COG5022 1256 MS--------NEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALrTKASSLRWKSATEV-----NYNS 1320
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1486 QIEESNKEKQELQEklqaLQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKT-QVKRLENlasrlketmeklteeRD 1564
Cdd:COG5022 1321 EELDDWCREFEISD----VDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKS---------------RY 1381
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|
gi 1907082239 1565 QRAAAENR-EKEQNKRLQRQLRDTKEEMSELARKEAEASR 1603
Cdd:COG5022 1382 DPADKENNlPKEILKKIEALLIKQELQLSLEGKDETEVHL 1421
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
121-877 |
1.02e-99 |
|
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: 337.13 E-value: 1.02e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 272
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 273 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFgIVPLSKPEEKQKAAQQFSKLQAAMKV 352
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 353 LAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT-- 430
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDG--------TEEADKAAHLLGVNSSDLLKALLKPRIKVGRew 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 431 LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----Npewgg 506
Cdd:cd01377 312 VTKGQNKEQ--------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 507 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----DDLEPVADdsvaavdqashLVRS-----LAHA 577
Cdd:cd01377 373 -----SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-----------LIEKpnmgiLSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 578 DEargllwlleeEALVPGATEDALLDRLFSYygpQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLnyTK-QN 656
Cdd:cd01377 437 DE----------ECVFPKATDKTFVEKLYSN---HLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWL--EKnKD 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 657 PATQNAPRLLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDAL 736
Cdd:cd01377 500 PLNENVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NKL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 737 IDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGY 816
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKGF 606
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 817 PDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd01377 607 PNRIIFAEFKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
120-877 |
8.28e-90 |
|
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: 308.48 E-value: 8.28e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 272
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 273 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF--GIVPLSkpeeKQKAAQQFSKLQAAM 350
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 351 KVLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT 430
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKE--RNTDQAS------MPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 431 --LQRSTsfrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgs 507
Cdd:cd14920 308 dyVQKAQ--------------TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 508 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaAVDQASHLVRSLAHADEargl 583
Cdd:cd14920 372 ----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGVLALLDE---- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 584 lwlleeEALVPGATEDALLDRLfsyygpqEGDKKGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQ 660
Cdd:cd14920 440 ------ECWFPKATDKTFVEKL-------VQEQGSHSKFQKPRQLKdkaDFCIIHYAGK--VDYKADEWL-MKNMDPLND 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 661 NAPRLLQDSQKKIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTI 740
Cdd:cd14920 504 NVATLLHQSSDRFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATL 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 741 KRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 820
Cdd:cd14920 571 RNTNPNFVRCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 821 VFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14920 622 VFQEFRQRYEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
120-877 |
1.52e-83 |
|
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: 289.99 E-value: 1.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIA----GTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 273
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 274 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNV--FGIVPLSkpeeKQKAAQQFSKLQAAMK 351
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 352 VLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtl 431
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKE--RNTDQAS------MPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 432 qrsTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsarg 510
Cdd:cd14921 307 ---RDVVQKAQ-------TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 511 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeE 590
Cdd:cd14921 372 -SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDE----------E 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 591 ALVPGATEDALLDRLFSyygPQEGDKKGQSPLLRSSKPRHFLLghsHGTNWVEYNVAGWLNyTKQNPATQNAPRLLQDSQ 670
Cdd:cd14921 441 CWFPKATDKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 671 KKIISNLFLGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKRSKMHFVHC 750
Cdd:cd14921 514 DKFVADLWKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 751 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 830
Cdd:cd14921 581 IIPNHEKRSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082239 831 VLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14921 632 ILAANAIPKG-----FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
120-877 |
3.88e-83 |
|
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: 288.80 E-value: 3.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSV-------EKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLD 264
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 265 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVF---GIVPLSKPEEkqkaAQ 341
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 342 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAI 421
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE--RNNDQAT------LPDNTVAQKIAHLLGLSVTDMTRAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 422 FKHQLKGGtlqrstsfRQGPEESGLGEGTKLSalecLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQ 500
Cdd:cd14911 308 LTPRIKVG--------RDFVTKAQTKEQVEFA----VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 501 NPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaavdqashLVrslah 576
Cdd:cd14911 376 IFELN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-----------LI----- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 577 aDEARGLLWLLEEEALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYT 653
Cdd:cd14911 434 -DKPGGIMALLDEECWFPKATDKTFVDKLVSAH--------SMHPKFMKTDFRgvaDFAIVHYAGR--VDYSAAKWL-MK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 654 KQNPATQNAPRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQV 733
Cdd:cd14911 502 NMDPLNENIVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 734 DALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYR 813
Cdd:cd14911 565 AKLMDTLRNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICR 615
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 814 QGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14911 616 QGFPNRIPFQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
120-877 |
4.09e-81 |
|
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: 283.07 E-value: 4.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTK------VFS---VEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQA 268
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKkdqssiALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 269 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQA 348
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQ----DEAAeagrkqfarhewAQKAAYLLGCSLEELSSAIFKH 424
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQasmpDDTA------------AQKVCHLLGMNVTDFTRAILSP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 425 QLKGGtlqrsTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPE 503
Cdd:cd14932 306 RIKVG-----RDYVQKAQ-------TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 504 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargl 583
Cdd:cd14932 374 LN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDE---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 584 lwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPlLRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAP 663
Cdd:cd14932 444 ------ECWFPKATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 664 RLLQDSQKKIISNLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKRS 743
Cdd:cd14932 511 TLLNQSTDKFVSELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNT 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 744 KMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 823
Cdd:cd14932 577 NPNFVRCIIPNHEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 824 EFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14932 628 EFRQRYEILTPNAIPKG-----FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
120-877 |
7.10e-81 |
|
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: 281.86 E-value: 7.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKvfsvEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 272
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALedqimqaNPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 273 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDATLRTELHLN------HLAENNVFGIvplskpeEKQKAAQQFSKL 346
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 347 QAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQL 426
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGT--------ENADKAAFLMGINSSELVKGLIHPRI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 427 KGGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEW 504
Cdd:cd14929 301 KVGNeyVTRSQNIEQVTYAVG--------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 505 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaddsvAAVDQASHLVRSLAHADEARGLL 584
Cdd:cd14929 367 N------SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDW-------------VSIDFGLDLQACIDLIEKPMGIF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 585 WLLEEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKPR------HFLLGHSHGTnwVEYNVAGWLNYTKqNPA 658
Cdd:cd14929 428 SILEEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKNK-DLL 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 659 TQNAPRLLQDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqiklqvDALID 738
Cdd:cd14929 498 NETVVAVFQKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL--------NKLMT 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 739 TIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPD 818
Cdd:cd14929 557 NLKSTAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICREGFPN 607
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 819 HMVFSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14929 608 RLLYADFKQRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
120-877 |
3.37e-79 |
|
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: 277.36 E-value: 3.37e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 276
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 277 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAAMKVLAIS 356
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 357 PEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTS 436
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKE--RNTDQAS------MPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG-----RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 437 FRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 515
Cdd:cd14919 306 YVQKAQ-------TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 516 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 595
Cdd:cd14919 373 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDE----------ECWFPK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 596 ATEDALLDRLFSYYGPQegdKKGQSPLLRSSKPrHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIIS 675
Cdd:cd14919 443 ATDKSFVEKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 676 NLFlgRAGSATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLPVA 755
Cdd:cd14919 516 ELW--KDVDRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNH 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 756 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 835
Cdd:cd14919 583 EKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 633
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082239 836 LTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14919 634 SIPKG-----FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
120-877 |
1.47e-75 |
|
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: 266.55 E-value: 1.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAA 349
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGG 429
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPD--------NTAAQKVCHLMGMNVTDFTRAILSPRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 430 T--LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGg 506
Cdd:cd15896 311 RdyVQKAQTQEQ--------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 507 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwl 586
Cdd:cd15896 376 -----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDE------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 leeEALVPGATEDALLDRLFSYYGPQEGDKKGQspllRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLL 666
Cdd:cd15896 444 ---ECWFPKATDKSFVEKVLQEQGTHPKFFKPK----KLKDEADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLL 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 667 QDSQKKIISNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKM 745
Cdd:cd15896 514 NQSTDKFVSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRNTNP 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd15896 578 NFVRCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 826 RRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd15896 629 RQRYEILTPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
120-877 |
7.64e-74 |
|
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: 261.81 E-value: 7.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQ 267
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 268 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN------HLAENNVFGIVPLSKPEEkqkaaq 341
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 342 qFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAI 421
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 422 FKHQLKGGtlQRSTSFRQGPEESGLGEGtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQN 501
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVYAVG----------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 502 PEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDqashLVrslahaDEAR 581
Cdd:cd14927 374 FEFN------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDF---GLDLQACID----LI------EKPL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 582 GLLWLLEEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTK 654
Cdd:cd14927 435 GILSILEEECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPdkkrkyeAHFEVVHYAGV--VPYNIVGWLDKNK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 655 qNPATQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvD 734
Cdd:cd14927 506 -DPLNETVVAIFQKSQNKLLATLYENYVGSD-----STEDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------N 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 735 ALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQ 814
Cdd:cd14927 567 KLMTNLRATQPHFVRCIIPNETKTPG-----------------------------VMDPFLVLHQLRCNGVLEGIRICRK 617
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 815 GYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14927 618 GFPNRILYADFKQRYRILNPSAIPDDK----FVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
120-877 |
1.40e-71 |
|
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: 254.76 E-value: 1.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 273
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 274 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaeNNVFGIVPLSKPE---EKQKAAQQFSKLQAAM 350
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 351 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGT 430
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGE--------EEGGRVSKLFGCDTAELYKNLLKPRIKVGN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 431 lQRSTSFRQgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGsarg 510
Cdd:cd14909 309 -EFVTQGRN-----------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 511 asFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwlleeE 590
Cdd:cd14909 373 --FEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDF---GMDLLACIDLIEKPMGILSILEE----------E 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 591 ALVPGATEDALLDRLFSyygpqegDKKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAP 663
Cdd:cd14909 438 SMFPKATDQTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTVV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 664 RLLQDSQKKIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIKRS 743
Cdd:cd14909 508 DQFKKSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRST 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 744 KMHFVHCFLPvaegwpgeprsassrrvsssSELDLPpgdpceaGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 823
Cdd:cd14909 568 QPHFVRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYP 618
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 824 EFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14909 619 DFKMRYKILNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
121-877 |
3.31e-71 |
|
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: 253.82 E-value: 3.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAGT------SGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 272
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakkKDSKMKGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 273 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---A 349
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGG 429
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKTAYLMGLNSSDLLKALCFPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 430 TlqrstsfrqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsar 509
Cdd:cd14913 310 N-----------EYVTKGQ-TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 510 gaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEE 589
Cdd:cd14913 374 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 590 EALVPGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQD 668
Cdd:cd14913 439 ECMFPKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQK 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 669 SQKKIISNLFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHF 747
Cdd:cd14913 514 SSNRLLAHLYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 748 VHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 827
Cdd:cd14913 572 VRCIIPNETKTPGA-----------------------------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 828 RFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14913 623 RYRVLNASAIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
120-877 |
3.12e-70 |
|
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: 250.78 E-value: 3.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGT-SGTKVFSV-----EKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 273
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 274 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQkaaQQFSKLQAAMKVL 353
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 354 AISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqr 433
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPD--------NTAAQKLCRLLGLGVTDFSRALLTPRIKVG---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 434 sTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaS 512
Cdd:cd14930 306 -RDYVQKAQ-------TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 513 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEAL 592
Cdd:cd14930 372 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDE----------ECW 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 593 VPGATEDALLDRLfsyygpqeGDKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLL 666
Cdd:cd14930 442 FPKATDKSFVEKV--------AQEQGGHP--KFQRPRHlrdqadFSVLHYAGK--VDYKANEWL-MKNMDPLNDNVAALL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 667 QDSQKKIISNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIKRSK 744
Cdd:cd14930 509 HQSTDRLTAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTN 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 745 MHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 824
Cdd:cd14930 572 PSFVRCIVPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 825 FRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14930 623 FRQRYEILTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
121-834 |
6.60e-68 |
|
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: 243.38 E-value: 6.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAMKV 352
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGVDD-------AKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 353 LAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQ 432
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVAD--------EAVSTAASLLGCNANDLMLALSTRKIQAGGDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 433 RSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQH-SLCSMMIVDTPGFQnpewggSARGA 511
Cdd:cd01383 300 IVKKL------------TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE------SFQKN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 512 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEpvadDSVAAVDqashLVRS-----LAHADEargllwl 586
Cdd:cd01383 362 SFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLD----LIEKkplglISLLDE------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 leeEALVPGATEDALLDRLFSYYGPQEGDKKGQSpllrsskpRHFLLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLL 666
Cdd:cd01383 427 ---ESNFPKATDLTFANKLKQHLKSNSCFKGERG--------GAFTIRHYAGE--VTYDTSGFLE--------KNRDLLH 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 667 QDsqkkiISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMH 746
Cdd:cd01383 486 SD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLENTTPH 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 747 FVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 826
Cdd:cd01383 552 FIRCIKPNNKQLPGV-----------------------------FDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFA 602
|
....*...
gi 1907082239 827 RRFDVLAP 834
Cdd:cd01383 603 RRYGFLLP 610
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
120-877 |
1.99e-67 |
|
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: 242.24 E-value: 1.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 274
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 275 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEKQKAaqqfsklQA 348
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQIT-------DV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 428
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTT--------EVADKVAHLMGLNSGELQKGITRPRVKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 506
Cdd:cd14934 305 GNefVQKGQNMEQCNNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 507 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQashlvrslahADEARGLLWL 586
Cdd:cd14934 370 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDF---GLDLQACIDL----------LEKPMGIFSI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 LEEEALVPGATE--------DALLDRLFSYYGPQEGDKKGQSPllrsskprHFLLGHSHGTnwVEYNVAGWLNYTKqNPA 658
Cdd:cd14934 432 LEEQCVFPKATDatfkaalyDNHLGKSSNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK-DPL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 659 TQNAPRLLQDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQIKLQVDALID 738
Cdd:cd14934 501 NETVVGLFQKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNKLMT 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 739 TIKRSKMHFVHCFLpvaegwpgeprsassrrvsssseldlpPGDPCEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPD 818
Cdd:cd14934 555 TLHSTAPHFVRCIV---------------------------PNEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKGFPN 605
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 819 HMVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14934 606 RLQYPEFKQRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
121-877 |
2.94e-67 |
|
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: 241.93 E-value: 2.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAG---------TSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 271
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 272 ASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 348
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML----LITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAagaTKEPLEEQDEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 428
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGN---MKFKQKQREEQAEPDGT-----EEADKSAYLMGLNSADLLKGLCHPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 506
Cdd:cd14917 309 GNeyVTKGQNVQQVIYATG--------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 507 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWL 586
Cdd:cd14917 374 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---GMDLQACIDLI----------EKPMGIMSI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 LEEEALVPGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 665
Cdd:cd14917 436 LEEECMFPKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 666 LQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKM 745
Cdd:cd14917 511 YQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd14917 570 HFVRCIIPNETKSPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 826 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14917 621 RQRYRILNPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
120-877 |
1.32e-65 |
|
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: 236.84 E-value: 1.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 191
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTG-SILV-------AVnpykelpiYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 192 DQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTkvFSVEKwQAL--STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd14883 73 NQSVIISGESGAGKTETTKLILQYLC--AVTNNH--SWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACG--DATLRTELHL---NHLAENNVFGIVPLSKPEEKQKaaqqFS 344
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 345 KLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSA-IFK 423
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGN-------LTFEDIDGETGALTVEDKEILKIVAKLLGVDPDKLKKAlTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 424 HQLKGGTLqrsTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPE 503
Cdd:cd14883 297 QINVRGNV---TEIPLKVQE----------ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 504 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVADdsvaAVDQASHLVRSLAhADEA 580
Cdd:cd14883 364 VN------SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDNQECLD----LIEKPPLGILKLL-DEEC 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 581 RgllwlleeealVPGATEDALLDRLFSYYGPQEGDKKgqsPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNytkQNPATQ 660
Cdd:cd14883 433 R-----------FPKGTDLTYLEKLHAAHEKHPYYEK---PDRRRWKTE-FGVKHYAGE--VTYTVQGFLD---KNKDTQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 661 --NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALI 737
Cdd:cd14883 493 qdDLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLV 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 738 DTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYP 817
Cdd:cd14883 556 DVLSATQPWYVRCIKPNSLKEPN-----------------------------VFDDELVLAQLRYAGMLEIIRIRKEGFP 606
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 818 DHMVFSEFRRRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14883 607 IHLTFKEFVDRYLCLDPRARSADHK-----ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
121-877 |
7.78e-65 |
|
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: 234.96 E-value: 7.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAgTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 270
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTLedqiiqanplLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 271 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 348
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELssaifkhqLK 427
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAGYLMGLNSAEM--------LK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 428 GGTLQRstsFRQGPEESGLGEGTKlSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgs 507
Cdd:cd14923 301 GLCCPR---VKVGNEYVTKGQNVQ-QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 508 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLL 587
Cdd:cd14923 375 ----SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 588 EEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQ 667
Cdd:cd14923 438 EEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 668 DSQKKIISNLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHF 747
Cdd:cd14923 514 KSSLKLLSFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 748 VHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 827
Cdd:cd14923 575 VRCLIPNETKTPG-----------------------------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 828 RFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14923 626 RYRILNASAIPEGQ----FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
121-877 |
1.71e-64 |
|
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: 233.85 E-value: 1.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 270
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 271 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 348
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLK 427
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 428 GGT--LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 505
Cdd:cd14910 310 VGNeyVTKGQTVQQ--------------VYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 506 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLW 585
Cdd:cd14910 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 586 LLEEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 665
Cdd:cd14910 437 ILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 666 LQDSQKKIISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 745
Cdd:cd14910 513 YQKSSMKTLALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd14910 573 HFVRCIIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 826 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14910 624 KQRYKVLNASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
122-839 |
2.08e-64 |
|
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: 232.95 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 122 VLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIaVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKV 352
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 353 LAISPEEQKTCWLILASIYHLG----AAGATKEPLEEQDEAAEagrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQlkg 428
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniefSKGEEDDSSVPKDEKSE---------FHLKAAAELLMCDEKALEDALCKRV--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 gtlqrstsfRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSA 508
Cdd:cd01384 303 ---------IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 509 RGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----------DDLEPVADDSVAAVDQASHLVRSlahad 578
Cdd:cd01384 368 KTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYiefvdnqdvlDLIEKKPGGIIALLDEACMFPRS----- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 579 eargllwlleeealvpgaTEDALLDRLFSYYgpqeGDKKgqspllRSSKPR----HFLLGHSHGTnwVEYNVAGWLNYTK 654
Cdd:cd01384 443 ------------------THETFAQKLYQTL----KDHK------RFSKPKlsrtDFTIDHYAGD--VTYQTDLFLDKNK 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 655 QN--PATQNaprLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQ 732
Cdd:cd01384 493 DYvvAEHQA---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQ 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 733 VDALIDTIKRSKMHFVHCFLPVAEgwpgeprsassrrvsssseldLPPGDPCEAGLLQldvsllraQLRGSRLLDAMRMY 812
Cdd:cd01384 540 LQELMETLNTTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRIS 590
|
730 740
....*....|....*....|....*..
gi 1907082239 813 RQGYPDHMVFSEFRRRFDVLAPHLTKK 839
Cdd:cd01384 591 CAGYPTRKPFEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
121-877 |
7.63e-64 |
|
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: 231.93 E-value: 7.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIA---------GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLED-QIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA- 348
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 --AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQL 426
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 427 KGGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEW 504
Cdd:cd14915 309 KVGNeyVTKGQTVQQVYNSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 505 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLL 584
Cdd:cd14915 375 N------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIF 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 585 WLLEEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPR 664
Cdd:cd14915 436 SILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVG 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 665 LLQDSQKKIISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSK 744
Cdd:cd14915 512 LYQKSGMKTLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTH 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 745 MHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 824
Cdd:cd14915 572 PHFVRCLIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 825 FRRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14915 623 FKQRYKVLNASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
122-877 |
1.07e-63 |
|
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: 231.55 E-value: 1.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 122 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSS 201
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 202 GSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQ--------ALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 273
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 274 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---AM 350
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 351 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGT 430
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKALCYPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 431 lqrstsfrqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 510
Cdd:cd14918 311 -----------EYVTKGQ-TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN----- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 511 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEE 590
Cdd:cd14918 374 -SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPLGIFSILEEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 591 ALVPGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQ 670
Cdd:cd14918 440 CMFPKATDTSFKNKLYDQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 671 KKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqiklQVDALIDTIKRSKMHFVHC 750
Cdd:cd14918 516 MKTLASLFSTYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 751 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 830
Cdd:cd14918 575 IIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 625
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082239 831 VLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14918 626 VLNASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
121-877 |
9.35e-63 |
|
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: 228.85 E-value: 9.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 270
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 271 VASASIQTMLLEKLRVARRPASEATFNVFYYLlacgDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 348
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLK 427
Cdd:cd14912 238 sAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 428 GGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 505
Cdd:cd14912 310 VGNeyVTKGQTVEQVTNAVG--------------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 506 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLW 585
Cdd:cd14912 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 586 LLEEEALVPGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 665
Cdd:cd14912 437 ILEEECMFPKATDTSFKNKLYEQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 666 LQDSQKKIISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 745
Cdd:cd14912 513 YQKSAMKTLAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd14912 575 HFVRCIIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 826 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14912 626 KQRYKVLNASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
121-834 |
4.01e-62 |
|
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: 226.86 E-value: 4.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 271
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAaiGDRSKKENPNANKGTLedqiiqaNPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 272 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 348
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 428
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT--------EDADKSAYLMGLNSADLLKGLCHPRVKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GT--LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 506
Cdd:cd14916 310 GNeyVTKGQSVQQ--------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 507 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWL 586
Cdd:cd14916 375 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---GMDLQACIDLI----------EKPMGIMSI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 LEEEALVPGATEDALLDRLF-SYYGPQEGDKKGQSplLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 665
Cdd:cd14916 437 LEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 666 LQDSQKKIISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 745
Cdd:cd14916 512 YQKSSLKLMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHP 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd14916 572 HFVRCIIPNERKAPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
....*....
gi 1907082239 826 RRRFDVLAP 834
Cdd:cd14916 623 RQRYRILNP 631
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
120-834 |
2.25e-61 |
|
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: 224.27 E-value: 2.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 194
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 195 IVLLGSSGSGKTTSFQHLVQYLATIagTSGTKVFSVEKWQALST------------------LLEAFGNSPTIMNGSATR 256
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 257 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlaENNVFGIVPLSK--PE 334
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 335 EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAG--ATKEPLEEQDEAAeagrkqfarHEWAQKAAYLLGC 412
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDfeSENDTTVLEDATT---------LQSLKLAAELLGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 413 SLEELSSAIFKHQL--KGGTLQRstsfrqgPEESGLGEgTKLSALeclegmASGLYSELFTLLISLVNRALKSSQHSLCS 490
Cdd:cd14890 306 NEDALEKALLTRQLfvGGKTIVQ-------PQNVEQAR-DKRDAL------AKALYSSLFLWLVSELNRTISSPDDKWGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 491 MMIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADDSVAAVDQA 567
Cdd:cd14890 372 IGVLDIYGFEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLELIEGKVNGK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 568 SHLVRSLahaDEARGLLWLLEEEALVpgatedALLDRLF--SYYGPQEGDKKGQSPLLRSSK---PRHFLLGHSHGTnwV 642
Cdd:cd14890 446 PGIFITL---DDCWRFKGEEANKKFV------SQLHASFgrKSGSGGTRRGSSQHPHFVHPKfdaDKQFGIKHYAGD--V 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 643 EYNVAGwlnYTKQNPATqnaprlLQDSQKKIIsnlflgragsatvlsgsiagleggsqlalrrATSMRktfttgmaAVKK 722
Cdd:cd14890 515 IYDASG---FNEKNNET------LNAEMKELI-------------------------------KQSRR--------SIRE 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 723 KSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagLLQLDVSLlraQLRG 802
Cdd:cd14890 547 VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGK--------------------------FDGLDCLR---QLKY 597
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082239 803 SRLLDAMRMYRQGYP---DHMVFseFrRRFDVLAP 834
Cdd:cd14890 598 SGMMEAIQIRQQGFAlreEHDSF--F-YDFQVLLP 629
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
120-834 |
3.45e-61 |
|
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: 223.50 E-value: 3.45e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 198
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAennVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 358
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 359 EQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFR 438
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGD------QGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 439 qgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCH 518
Cdd:cd14903 310 ------------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 519 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDS-VAAVDQASHLVRSLAHADEARgllwlleeealvPGAT 597
Cdd:cd14903 372 NYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF---ADNQdVLAVIEDRLGIISLLNDEVMR------------PKGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 598 EDALLDRLFSYYgpqeGDKKGQSPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNYTKQNpatqnaprLLQD-------SQ 670
Cdd:cd14903 437 EESFVSKLSSIH----KDEQDVIEFPRTSRTQ-FTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 671 KKIISNLFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHC 750
Cdd:cd14903 502 KPFLRMLFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRC 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 751 FLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 830
Cdd:cd14903 566 IKPNSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
....
gi 1907082239 831 VLAP 834
Cdd:cd14903 617 LFLP 620
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
120-753 |
5.69e-60 |
|
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: 219.72 E-value: 5.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPslLVLST---RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 196
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGH--VLISVnpfKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 197 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVeKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 274
Cdd:cd01378 78 ISGESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 275 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQA 348
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFDVDGIDD-------AADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAGATKeplEEQDEAAEAGRKQfarhewAQKAAYLLGCSLEELSSAIFKHQLKG 428
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSV------LDFVAYLLGVDPDQLEKALTHRTIET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GTLQRSTSfrqgpeESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGF----QNpe 503
Cdd:cd01378 301 GGGGRSVY------EVPL---NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 504 wggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDlEPVADdsvaavdqashLVRS-----L 574
Cdd:cd01378 370 --------SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNN-KIICD-----------LIEEkppgiF 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 575 AHADEArgllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPllRSSKPRHFLLGHSHGTnwVEYNVAGwlnYTK 654
Cdd:cd01378 430 AILDDA---------CLTAGDATDQTFLQKLNQLFSNHPHFECPSGH--FELRRGEFRIKHYAGD--VTYNVEG---FLD 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 655 QNPAT--QNAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkkslciQIKLQ 732
Cdd:cd01378 494 KNKDLlfKDLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT----------KFKNS 541
|
650 660
....*....|....*....|.
gi 1907082239 733 VDALIDTIKRSKMHFVHCFLP 753
Cdd:cd01378 542 ANALVETLMKKQPSYIRCIKP 562
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
120-834 |
5.40e-58 |
|
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: 214.04 E-value: 5.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 191
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTG-SILV-------AVnpyqilpiYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 192 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGtsgtKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd01381 73 DQCVVISGESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIvplskpeEKQKAAQQF 343
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 344 SKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGaTKEPLEEQDEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFK 423
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIK-FEATVVDNLDASE-----VRDPPNLERAAKLLEVPKQDLVDALTT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 424 HQL--KGGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLCSMMIVDTPG 498
Cdd:cd01381 295 RTIftRGETVVSPLSAEQ--------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 499 FQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsVAAVDQAShlvrSLA 575
Cdd:cd01381 361 FENFEVN------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMN----IMS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 576 HADEargllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLlghshGTnwVEYNVAGWLNytKQ 655
Cdd:cd01381 429 LIDE----------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KN 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 656 NPA-TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVD 734
Cdd:cd01381 490 RDTfSADLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLD 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 735 ALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQ 814
Cdd:cd01381 540 QLMKTLSACQPFFVRCIKPNEYKKPML-----------------------------FDRELCVRQLRYSGMMETIRIRKA 590
|
730 740
....*....|....*....|
gi 1907082239 815 GYPDHMVFSEFRRRFDVLAP 834
Cdd:cd01381 591 GYPIRHTFEEFVERYRVLVP 610
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
121-679 |
5.13e-57 |
|
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: 210.70 E-value: 5.13e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTkvFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 279
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH----------LAENNVFGIVplskpEEKQKAAQQFSKLQAA 349
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchrilrddNRNRPVFNDS-----EELEYYRQMFHDLTNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISPEEQKTCWLILASIYHLgaAGATKEPLEEQDEAaeagrkQFARHEWAQKAAYLLGCSLEELSSAIF--KHQLK 427
Cdd:cd14897 235 MKLIGFSEEDISVIFTILAAILHL--TNIVFIPDEDTDGV------TVADEYPLHAVAKLLGIDEVELTEALIsnVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 428 GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-----HSLCSMMIVDTPGFQNp 502
Cdd:cd14897 307 GERIQSWKSLRQ--------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFEN- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 503 ewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAfdDLEPVADDSV------------AAVDQASHL 570
Cdd:cd14897 372 -----FKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVlelffkkplgilPLLDEESTF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 571 vrslahadeargllwlleeealvPGATEDALLDRLFSYYGPqegdkkgqSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWL 650
Cdd:cd14897 445 -----------------------PQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFL 493
|
570 580
....*....|....*....|....*....
gi 1907082239 651 NYTKQNpATQNAPRLLQDSQKKIISNLFL 679
Cdd:cd14897 494 EKNRDN-LSSDIVGCLLNSNNEFISDLFT 521
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
121-552 |
8.33e-57 |
|
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: 210.09 E-value: 8.33e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYG-ASLLHTYAGpslLVLStrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 191
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCG---IVLV-----AInpyedlpiYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 192 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd01380 74 NQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAA 349
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISPEEQKTCWLILASIYHLG-----AAGATKEPLEEQDEAaeagrkqfarhewAQKAAYLLGCSLEELSSAIFKH 424
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGnveikATRNDSASISPDDEH-------------LQIACELLGIDESQLAKWLCKR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 425 QLK--GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-HSLCSMM-IVDTPGFQ 500
Cdd:cd01380 298 KIVtrSEVIVKPLTLQQ--------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFE 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 501 NPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDD 552
Cdd:cd01380 364 TFEVN------SFEQFCINYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
121-837 |
3.71e-56 |
|
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: 208.50 E-value: 3.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGpSLL--VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 198
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIG-SILasVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 272
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 273 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhLAEN----NVFGIVPLSKPEEKqkaaQQFSKLQA 348
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAgatkepleeqdEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkg 428
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNI-----------EFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 gtLQRSTSFRqGPEESglgegTKLS---ALECLEGMASGLYSELFTLLISLVNRALKSSQHsLCSMMIVDTPGFQNPEWG 505
Cdd:cd14873 298 --TQRSMFLR-GEEIL-----TPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 506 gsargaSFEELCHNYAQDRLQRLFHERTF-LQELERYKEDnieLAFDDLEPVadDSVAAVDQASHLVRSLAHADEargll 584
Cdd:cd14873 369 ------HFEQFNINYANEKLQEYFNKHIFsLEQLEYSREG---LVWEDIDWI--DNGECLDLIEKKLGLLALINE----- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 585 wlleeEALVPGATEDALLDRLFSyygpqeGDKKGQSPLlrssKPR--HFLLGHSHGTNWVEYNVAGWLnytKQNPAT--Q 660
Cdd:cd14873 433 -----ESHFPQATDSTLLEKLHS------QHANNHFYV----KPRvaVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrD 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 661 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDT 739
Cdd:cd14873 495 DLLNLLRESRFDFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMAT 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 740 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 819
Cdd:cd14873 550 LSSSNPFFVRCIKPNMQKMPD-----------------------------QFDQAVVLNQLRYSGMLETVRIRKAGYAVR 600
|
730
....*....|....*...
gi 1907082239 820 MVFSEFRRRFDVLAPHLT 837
Cdd:cd14873 601 RPFQDFYKRYKVLMRNLA 618
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
120-877 |
5.35e-56 |
|
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: 208.07 E-value: 5.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQTM 279
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTE---------LHLNHLAENNVFGivplskpeekQKAAQQFSKLQAAM 350
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 351 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKqfARHEWaqkAAYLLGCSLEELSSAIfkhqlkggt 430
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSD--AEIQW---VAHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 431 LQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 510
Cdd:cd01387 294 TFKVTETRRERIFTPL---TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 511 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVAddsvaavdqasHLVrslahADEARGLLWLL 587
Cdd:cd01387 366 -SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQPVI-----------NLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 588 EEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllRSSKPR----HFLLGHSHGTNWveYNVAGWLNYTKqNPATQNAP 663
Cdd:cd01387 429 DDECNFPQATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQLRQDVL 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 664 RLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTIK 741
Cdd:cd01387 496 ELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKME 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 742 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMV 821
Cdd:cd01387 556 RCNPWFVRC---------------------------LKPNHKKEPMLFDMDVVM--AQLRYSGMLETIRIRKEGYPVRLP 606
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 822 FSEFRRRFDvlapHLTKKHGRNYIVVDEKRAVeELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd01387 607 FQVFIDRYR----CLVALKLPRPAPGDMCVSL-LSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
121-558 |
6.75e-56 |
|
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: 207.13 E-value: 6.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLaTIAGTSGTKVFSvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTML 280
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 281 LEKLRVARRPASEATFNVFYYLLA-------CGDATLRTELHLNHLAEnnvFGIVPLSKpEEKQKAAQQFSKLQAAMKVL 353
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQN---DGLTVQDI-VNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 354 AISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--KGGTL 431
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDK----SSRISNPEALNNVAKLLGIEADELQEALTSHSVvtRGETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 432 QRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNpewggsA 508
Cdd:cd01379 312 IRNNTVEE--------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFEN------F 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 509 RGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL---AFDDLEPVAD 558
Cdd:cd01379 372 QKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
117-556 |
5.23e-54 |
|
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: 202.01 E-value: 5.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 117 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSTRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 188
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 189 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTS--GTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFD 266
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 267 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF---GIVPL-SKPEEKQkaAQQ 342
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 343 FSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAeagrkqfARHEWA--------QKAAYLLGCSL 414
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHLGN-------LEFTYDHE-------GGEESAvvkntdvlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 415 EELSSAI-FKHQLKGGtlQRSTSFrqgpeesgLG-EGTKLSALEclegMASGLYSELFTLLISLVNRALKSSQHSLCSMM 492
Cdd:cd14879 303 EDLETSLtYKTKLVRK--ELCTVF--------LDpEGAAAQRDE----LARTLYSLLFAWVVETINQKLCAPEDDFATFI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 493 -IVDTPGFQNPewgGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDLEPV 556
Cdd:cd14879 369 sLLDFPGFQNR---SSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFDNSDCV 434
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
120-833 |
5.82e-54 |
|
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: 201.93 E-value: 5.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIagtsGTKVFSVEKWQALSTL--LEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 277
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 278 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAEN----NVFGIVPLSKPEEkqkaAQQFSKLQAAMKVL 353
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 354 AISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWA--QKAAYLLGCSLEELSSAIFKHQLKGGTL 431
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVS--------SWAeiHTAARLLQVPPERLEGAVTHRVTETPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 432 QRSTSFrqgPEEsglgegtklSALECLEGMASGLYSELFTLLISLVNRAL--KSSQHSLCSMMIVDTPGFQnpewggSAR 509
Cdd:cd14896 303 RVSRPL---PVE---------GAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 510 GASFEELCHNYAQDRLQRLFHERTFLQELERYKEDniELAFDDLEPVADDSVA--AVDQASHLVRSLahadeargllwll 587
Cdd:cd14896 365 VNGLEQLCINLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLdlLVDQPHSLLSIL------------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 588 EEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlrsskPRhFLLGHSHGTnwVEYNVAGWLNYTKQ--NPATQNaprL 665
Cdd:cd14896 430 DDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----PV-FTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---M 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 666 LQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKM 745
Cdd:cd14896 499 LAQSQLQLVGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSHV 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 746 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 825
Cdd:cd14896 548 YFIHCLNPNPGKLPG-----------------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
....*...
gi 1907082239 826 RRRFDVLA 833
Cdd:cd14896 599 LARFGALG 606
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
122-832 |
8.22e-53 |
|
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: 198.59 E-value: 8.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 122 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIVL 197
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 198 LGSSGSGKTTSFQHLVQYLATIAgtSGTKVFSVEKWQaLSTLLEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 277
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 278 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL----NHLAENNVFGivplsKPEEKQKAAQQFSKLQAAMKVL 353
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgKYRYLNNGAG-----CKREVQYWKKKYDEVCNAMDMV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 354 AISPEEQKTCWLILASIYHLGAAgatkePLEEQDEaaEAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqlkgGTLQR 433
Cdd:cd14889 234 GFTEQEEVDMFTILAGILSLGNI-----TFEMDDD--EALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 434 STSFRQGpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNPEWGgsarg 510
Cdd:cd14889 297 TVTFTRG--EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 511 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVADDSVAA-------VDQASHLvrslahadea 580
Cdd:cd14889 370 -RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLNKpigilslLDEQSHF---------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 581 rgllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGQspllrsSKPRHFLLGHSHGTnwVEYNVAGWLNYTKQN-PAT 659
Cdd:cd14889 439 -------------PQATDESFVDKLNIHFKGNSYYGKSR------SKSPKFTVNHYAGK--VTYNASGFLEKNRDTiPAS 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 660 QNAprLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDALIDT 739
Cdd:cd14889 498 IRT--LFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEK 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 740 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 819
Cdd:cd14889 561 MFAASPHFVRCIKPNHVKVPG-----------------------------QLDSKYIQDQLRYNGLLETIRIRREGFSWR 611
|
730
....*....|...
gi 1907082239 820 MVFSEFRRRFDVL 832
Cdd:cd14889 612 PSFAEFAERYKIL 624
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
121-834 |
1.97e-52 |
|
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: 197.98 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 200
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLaTIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd01385 82 SGSGKTESTNFLLHHL-TALSQKGYGS-GVEQ-TILGAgpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 358
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 359 EQKTCWLILASIYHLGAAgATKEPLEEQDEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIF--KHQLKGGTLQRSTS 436
Cdd:cd01385 238 TQRQIFSVLSAVLHLGNI-EYKKKAYHRDESVTVGNP-----EVLDIISELLRVKEETLLEALTtkKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 437 FrqgPEesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLC-SMMIVDTPGFQNPEwggsarGAS 512
Cdd:cd01385 312 L---PE-----------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDFG------NNS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 513 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVadDSVAAVdqasHLVRSLAHadearGLLWLLEEEAL 592
Cdd:cd01385 372 FEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGIS--WHNIEYT--DNTGCL----QLISKKPT-----GLLCLLDEESN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 593 VPGATEDALLDRLFS-------YYGPQEgdkkgqspllrssKPRHFLLGHSHGTnwVEYNVAGW----LNYTKQNPATqn 661
Cdd:cd01385 439 FPGATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQIKDFreknLDLMRPDIVA-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 662 aprLLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRRATSMRktfttGMAAVKKKS 724
Cdd:cd01385 502 ---VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSL-----LHLHKKKKP 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 725 LCIQIKLQV--DALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRG 802
Cdd:cd01385 574 PSVSAQFQTslSKLMETLGQAEPFFIRCIKSNAEKKP-----------------------------LRFDDELVLRQLRY 624
|
730 740 750
....*....|....*....|....*....|..
gi 1907082239 803 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 834
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
121-834 |
4.40e-52 |
|
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: 196.45 E-value: 4.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIVL 197
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIaVNPFKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 198 LGSSGSGKTTSFQHLVQYLATiAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQ-------- 267
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 268 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIV--PLSKPEEKQKAAQQFS 344
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 345 KLQ--------------------AAMKVLAISPEEQKTCWLILASIYHLGAAgatkepLEEQDEAAEAGRKQFA-RHEWA 403
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNI------LFENNEACSEGAVVSAsCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 404 QKAAYLLGCSLEELSSAifkhqLKGGTLQRSTSFRQGPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNRAL-K 482
Cdd:cd14888 312 EKVASLLGVDAEDLLNA-----LCYRTIKTAHEFYTKPLRVDEAEDVR-------DALARALYSCLFDKVVERTNESIgY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 483 SSQHSLCSMMIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLE-PVADDSV 561
Cdd:cd14888 380 SKDNSLLFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDNQDCV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 562 AAVDQASHLVrsLAHADEargllwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllrSSKPRHFLLGHSHGTnw 641
Cdd:cd14888 452 DLLQEKPLGI--FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP-- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 642 VEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVK 721
Cdd:cd14888 512 VKYCSDGFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKK 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 722 KKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssSELDlppgdpceagllQLDVSllrAQLR 801
Cdd:cd14888 564 FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFD------------RISVN---EQLK 614
|
730 740 750
....*....|....*....|....*....|...
gi 1907082239 802 GSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 834
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
121-834 |
8.96e-52 |
|
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: 195.55 E-value: 8.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 279
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 359
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 360 QKTCWLILASIYHLGAAgatkePLEEQDEAAEAgrkqFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRQ 439
Cdd:cd14904 240 QRTLFKILSGVLHLGEV-----MFDKSDENGSR----ISNGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 440 gpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALkSSQHSLCSMMI--VDTPGFQNPEWGGsargasFEELC 517
Cdd:cd14904 302 ---ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 518 HNYAQDRLQRLFHERTFLQELERYKEDNieLAFDDLEPVADDSVAAVDQASHLVRSLAHaDEARGllwlleeealvPGAT 597
Cdd:cd14904 372 INYANEKLQQKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEVIDGKMGIIALMN-DHLRQ-----------PRGT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 598 EDALLDRLFSYYGPQEGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVAGWLNytKQNPATQN-APRLLQDSQKKIISN 676
Cdd:cd14904 438 EEALVNKIRTNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 677 LFlgraGSATVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAE 756
Cdd:cd14904 511 LF----GSSEAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNAN 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 757 GWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 834
Cdd:cd14904 568 KSPTE-----------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
121-839 |
9.71e-52 |
|
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: 196.65 E-value: 9.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 190
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 191 QDQSIVLLGSSGSGKTTSFQHLVQYLATI-----AGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSL 263
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 264 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE---NNVFGIVPLSKPEEKQKAA 340
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 341 QQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEA-AEAGRKQFArhewaqKAAYLLGCSLEELSS 419
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvTAASRFHLA------KCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 420 AIFKHQLKGGtlQRSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN---------RALKSSQHSLCS 490
Cdd:cd14902 316 LLSSREIKAG--VEVMVLKLTPEQ----------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELAT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 491 MMIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVaddsVAAVDqa 567
Cdd:cd14902 384 IGILDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC----LALFD-- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 568 shlvrslahaDEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllrsskprHFLLGHSHGTnwVEYNVA 647
Cdd:cd14902 452 ----------DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 648 GWLNyTKQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLC 726
Cdd:cd14902 504 QFVE-KNTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 727 IQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLL 806
Cdd:cd14902 563 AQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPG-----------------------------IFDRERMVEQMRSVGVL 613
|
730 740 750
....*....|....*....|....*....|...
gi 1907082239 807 DAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 839
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
123-833 |
2.38e-51 |
|
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: 194.21 E-value: 2.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 123 LHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 193
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 194 SIVLLGSSGSGKTTSFQHLVQYLATI----AGTSGTKVF-----SVEKWQALS-TLLEAFGNSPTIMNGSATRFSQILSL 263
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAanaheSIEECVLLSnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 264 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEnnvFGIVPLSKPEEKQKA--AQ 341
Cdd:cd14892 162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 342 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagATKEPLEEQDEAAeagrKQFARHEWAQKAAYLLGCSLEELSSAI 421
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVF----AQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 422 FKHQLKGGtlqRSTSFRQ--GPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRAlkSSQHSLCSMMIVDTP-- 497
Cdd:cd14892 313 VTQTTSTA---RGSVLEIklTARE----------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtf 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 498 ----------GFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaaV 564
Cdd:cd14892 378 spfigildifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----L 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 565 DQASHLvrslahadeargllwlleeeALVPGATEDALLDR-------LFSYYgpQEGDKKGQSpllrSSKPR----HFLL 633
Cdd:cd14892 447 IQKKPL--------------------GLLPLLEEQMLLKRkttdkqlLTIYH--QTHLDKHPH----YAKPRfecdEFVL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 634 GHSHGTnwVEYNVAGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktF 713
Cdd:cd14892 501 RHYAGD--VTYDVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------F 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 714 TTgmaavkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPPGDPCEagllqldv 793
Cdd:cd14892 537 RT----------------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE-------- 572
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907082239 794 sLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 833
Cdd:cd14892 573 -LVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
121-877 |
5.03e-51 |
|
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: 193.07 E-value: 5.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIVLL 198
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 276
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQ-RVLLAnpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 277 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaenNVFGIVPLSKPEEKQKA--AQQFSKLQAAMKVLA 354
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 355 ISPEEQKTCWLILASIYHLGAAGatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGgtlQ 432
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIE-----FASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRlmEIKG---C 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 433 RSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSL-CSMMIVDTPGFQNPEWGgsarga 511
Cdd:cd14872 302 DPTRIPLTPAQ----------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 512 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVrslahadEAR--GLLWL 586
Cdd:cd14872 366 SFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-----------LI-------EKKqpGLMLA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 587 LEEEALVPGATEDALLDRLfsyyGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 666
Cdd:cd14872 428 LDDQVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 667 QDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMH 746
Cdd:cd14872 501 SSSKNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPH 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 747 FVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 826
Cdd:cd14872 548 YIRC---------------------------VKPNQEKRARLFDGFMSL--EQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 827 RRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 877
Cdd:cd14872 599 KRYRFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
121-875 |
8.00e-49 |
|
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: 186.53 E-value: 8.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 190
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 191 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLD 264
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 265 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFS 344
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 345 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKepleeqdEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH 424
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-------KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 425 QLKGGTLQRSTSFRqgPEESGLGEgtklsaleclEGMASGLYSELFTLLISLVNRALK--SSQHSLCSMMIVDTPGF--- 499
Cdd:cd14901 315 EIRAGGEYITMPLS--VEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFeif 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 500 -QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLePVADDSVAAVDQASHLVRSLahAD 578
Cdd:cd14901 383 aTN----------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-PNNDACVAMFEARPTGLFSL--LD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 579 EargllwlleeEALVPGATEDALLDrlfSYYgpqegDKKGQSPLLRSSK----PRHFLLGHSHGTnwVEYNVAGWLNYTK 654
Cdd:cd14901 450 E----------QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKlqqgKRQFVIHHYAGA--VCYATDGFCDKNK 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 655 QNPATqNAPRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQVD 734
Cdd:cd14901 510 DHVHS-EALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLS 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 735 ALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDpcEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQ 814
Cdd:cd14901 542 SLLEVLNATEPHFIRC---------------------------IKPND--VLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 815 GYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVF 875
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
120-832 |
1.96e-47 |
|
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: 182.54 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 190
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 191 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAG----------------TSGTKVFSVEKwQALST--LLEAFGNSPTIMNG 252
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQ-KILSCnpILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 253 SATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-NHLAENNVFgivPL 330
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD---YL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 331 SKPE----EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEqDEAAEAGRKQFarhewAQKA 406
Cdd:cd14907 237 KKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDD-NSPCCVKNKET-----LQII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 407 AYLLGCSLEELSSAIFKHQLKGGTlQRSTSfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRAL-- 481
Cdd:cd14907 311 AKLLGIDEEELKEALTTKIRKVGN-QVITS--------------PLSKKECinnRDSLSKELYDRLFNWLVERLNDTImp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 482 ------KSSQHSLCSMMIVDTPGFQNPEwggsarGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-----LAF 550
Cdd:cd14907 376 kdekdqQLFQNKYLSIGLLDIFGFEVFQ------NNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylnqLSY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 551 DDLEPVADdsvaAVDQashlvrslahadEARGLLWLLEEEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllRSSKPRH 630
Cdd:cd14907 450 TDNQDVID----LLDK------------PPIGIFNLLDDSCKLATGTDEKLLNKIKKQHK---NNSKLIFP--NKINKDT 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 631 FLLGHSHGTnwVEYNVAGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrrats 708
Cdd:cd14907 509 FTIRHTAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK-------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 709 mrktfttgmAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdpcEAGL 788
Cdd:cd14907 570 ---------SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KADL 613
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082239 789 LQLDVSLLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 832
Cdd:cd14907 614 FIQGYVLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
121-833 |
1.77e-45 |
|
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: 177.45 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 188
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 189 --SRQDQSIVLLGSSGSGKTTSFQHLVQYLA-----TIAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQ 259
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 260 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvFGIVPLSKPE 334
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 335 EKQKAAQ---QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAA--GATKEPLEEQDEAAEAGRKQFARHEWAQKAAY- 408
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEDNGAASAPCRLASASPSSLTVQq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 409 -------LLGCSLEELSSAIFKHQLKGGtlqrstsfrqgpEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRAL 481
Cdd:cd14895 314 hldivskLFAVDQDELVSALTTRKISVG------------GETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 482 KSSQHSLCS-----------MMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 550
Cdd:cd14895 382 PQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 551 DDLEpvaDDSVA--AVDQASHLVRSLAhaDEargllwlleeEALVPGATEDALLDRLFSYYGpqegDKKGQSPLLRSSKP 628
Cdd:cd14895 456 VDYE---DNSVCleMLEQRPSGIFSLL--DE----------ECVVPKGSDAGFARKLYQRLQ----EHSNFSASRTDQAD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 629 RHFLLGHSHGTnwVEYNVAGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQLALRRATS 708
Cdd:cd14895 517 VAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLRRRSS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 709 MRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGl 788
Cdd:cd14895 587 VLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRC---------------------------IKPNDESASD- 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082239 789 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 833
Cdd:cd14895 629 -QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
121-542 |
3.71e-44 |
|
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: 172.43 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS--VEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 277
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 278 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENnvfgivplskpeekqkaAQQFSKLQAAMKVLAISP 357
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 358 EEQKTCWLILASIYHLGAAgatkePLEEQDEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAI---FKHQLKGGTlqR 433
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNI-----EFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLttrVMQTTRGGA--K 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 434 STSFRQG--PEESGlgegtklSALECLegmASGLYSELFTLLISLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npewg 505
Cdd:cd01382 294 GTVIKVPlkVEEAN-------NARDAL---AKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN---- 356
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907082239 506 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYK 542
Cdd:cd01382 357 ------SFEQFCINYCNEKLQQFFNERILKEEQELYE 387
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
160-547 |
4.55e-44 |
|
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: 172.15 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 160 MHMFKGCRREDMAPHIYAVAQTAYRAMLMSR---QDQSIVLLGSSGSGKTTSFQHLVQYLAT-----IAGTSGTKVFSVE 231
Cdd:cd14891 40 KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 232 KWQALST-----------LLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVF 299
Cdd:cd14891 120 KRKLSVTslderlmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 300 YYLLACGDATLRTELHlnhlaennvfgivpLSKPEEKQKAAQ-------------QFSKLQAAMKVLAISPEEQKTCWLI 366
Cdd:cd14891 200 YQLLAGASAELLKELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 367 LASIYHLGAAGATKEPLEEQD--EAAEAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRqgpees 444
Cdd:cd14891 266 LAGLLHLGNIEFDEEDTSEGEaeIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 445 GLGEGTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEwggsaRGASFEELCHNYA 521
Cdd:cd14891 325 GETFTIKRNAREAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYA 399
|
410 420
....*....|....*....|....*.
gi 1907082239 522 QDRLQRLFHERTFLQELERYKEDNIE 547
Cdd:cd14891 400 NEALQATFNQQVFIAEQELYKSEGID 425
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
121-841 |
3.96e-43 |
|
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: 168.95 E-value: 3.96e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 186
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 187 LMSR----QDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGS 253
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQT-NILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 254 ATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDAtlrtelhlnhlaennvfgivplskp 333
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-GAS------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 334 eEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---AGATKEPLEEQDEAAEAGRKQFARhewaQKAAYLL 410
Cdd:cd14900 213 -EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNltfEHDENSDRLGQLKSDLAPSSIWSR----DAAATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 411 GCSLEELSSAIFKHQLKGGTLQRSTsfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALK----- 482
Cdd:cd14900 288 SVDATKLEKALSVRRIRAGTDFVSM---------------KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddss 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 483 SSQHSLCSMMIVDTPGF----QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEp 555
Cdd:cd14900 353 KSHGGLHFIGILDIFGFevfpKN----------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQ- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 556 vadDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSyygpqegdKKGQSPLLRSSKPRH----F 631
Cdd:cd14900 422 ---DCVNLISQRPTGILSL--IDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglF 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 632 LLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrk 711
Cdd:cd14900 479 TIVHYAGH--VEYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 712 tfttgmaavkkkslCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQL 791
Cdd:cd14900 513 --------------GLQFKEQLTTLLETLQQTNPHYVRC---------------------------LKPNDLCKAGIYER 551
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 792 DVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHG 841
Cdd:cd14900 552 ERVL--NQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLarakNRLLAKKQG 603
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
928-1622 |
2.71e-41 |
|
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: 167.27 E-value: 2.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 928 NIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDE-EIQQLRSKLEKVEKERNELrlssdrlETRISELTSELtder 1006
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1007 ntgESASQLLDAETAERLRTEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1083
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1084 REVDF----TKKRLQQELEdKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1159
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1160 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSqeSKDEA 1239
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1240 --SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1317
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1318 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREIAQL 1392
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1393 KN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1466
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1467 KAAVAQ---------ASRDMAQMND-LQAQIEESNKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1536
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1537 FEKTQ----VKRLENLASRLKETMEKLTEER---DQRAAAENREKEQNKRLQRQLRDTKEEMSelarkEAEASRKKheLE 1609
Cdd:pfam01576 985 QESRErqaaNKLVRRTEKKLKEVLLQVEDERrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS-----RANAARRK--LQ 1057
|
730
....*....|...
gi 1907082239 1610 MDLESLEAANQSL 1622
Cdd:pfam01576 1058 RELDDATESNESM 1070
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
121-845 |
4.37e-41 |
|
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: 164.00 E-value: 4.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 198
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATiagTSGTKVF----------SVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQ 267
Cdd:cd14906 82 GESGSGKTEASKTILQYLIN---TSSSNQQqnnnnnnnnnSIEKDILTSNpILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 268 A-GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDATLRTELHLNH--------LAENNVFGIV------PLS 331
Cdd:cd14906 159 SdGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 332 KPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagaTKEPLEEQDEAAEAGRKQFARHEWAQkAAYLLG 411
Cdd:cd14906 239 NHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLG----NIEFEEDSDFSKYAYQKDKVTASLES-VSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 412 CSLEELSSAIFKHQLKGGTlqRSTSFRQgPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNR-----------A 480
Cdd:cd14906 314 YIESVFKQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRkfnqntqsndlA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 481 LKSSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDlepvA 557
Cdd:cd14906 384 GGSNKKNNLFIGVLDIFGFEN------LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----N 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 558 DDSVAAVDQASHLVRSLAHaDEArgllwlleeeaLVPGATEDALLDRLFSYYgpqegdKKGQSPLLRSSKPRHFLLGHSH 637
Cdd:cd14906 454 KECIELIEKKSDGILSLLD-DEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 638 GTnwVEYNVAGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGM 717
Cdd:cd14906 516 GD--VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTV 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 718 AAvkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDpceagllqLDVSLLR 797
Cdd:cd14906 574 SG--------QFLEQLNQLIQTINSTSVHYIRCIKP---------------------NQTMDCNN--------FNNVHVL 616
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1907082239 798 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 845
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
120-833 |
1.59e-38 |
|
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: 155.36 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 196
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 197 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSveKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASAS 275
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 276 IQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgiVPLSKPEEKQKAA-----QQFSKLQAAM 350
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 351 KVLAISPEEQKTCWLILASIYHLGAAGATKepLEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFK--HQLKG 428
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTA--LTEADSAF------VSDLQLLEQVAGMLQVSTDELASALTTdiQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GTLQRSTSFRQGPEESGLgegtklsaleclegMASGLYSELFTLLISLVNRALKsSQHSLCSMM-----IVDTPGFQNpe 503
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDL--------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEE-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 504 wggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-------------LAFDDLEPVADDSVaaVDQASHL 570
Cdd:cd14878 371 ----FQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTmetayspgnqtgvLDFFFQKPSGFLSL--LDEESQM 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 571 VRSLAHADEARgllwlleeealVPGATEDALLDRLFSYYGPQEGD--KKGQSPLlrsskprhFLLGHSHGTnwVEYNVAG 648
Cdd:cd14878 445 IWSVEPNLPKK-----------LQSLLESSNTNAVYSPMKDGNGNvaLKDQGTA--------FTVMHYAGR--VMYEIVG 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 649 WLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsATVlsgsiaglegGSQLalrratsmrktfttgmaavkKKSLC-I 727
Cdd:cd14878 504 AIEKNK-DSLSQNLLFVMKTSENVVINHLFQSKL--VTI----------ASQL--------------------RKSLAdI 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 728 QIKLQvdalidtikRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLD 807
Cdd:cd14878 551 IGKLQ---------KCTPHFIHCIKPNNSKLPD-----------------------------TFDNFYVSAQLQYIGVLE 592
|
730 740
....*....|....*....|....*.
gi 1907082239 808 AMRMYRQGYPDHMVFSEFRRRFDVLA 833
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLA 618
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
123-877 |
4.03e-38 |
|
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: 154.81 E-value: 4.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 123 LHTLRQRYGA--------SLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 194
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 195 IVLLGSSGSGKTTSFQHLVQYLATI------AGTSGTKvfsvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQA 268
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 269 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDATLRTELHlnhlaennvfgivplSKPEEKQKAAQQFSKLQA 348
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQK---------------SSAGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKQFARHEWAQKAAYLLgcSLEELSSAIFKHQLKG 428
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 429 GTLQRSTSFRQGPEESGLGEGTKLS-----------------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM 491
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsffdldgAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 492 MIVDTP--------------GFQNPEWGGSARgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL-----AFDD 552
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQnqdcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 553 LEPVADDSVAAVDQASHLvrSLAHADEARGLLWLLEEEALVPGATEDALLdrlfsyygpqegdkkgQSPLLRSSKPRHFL 632
Cdd:cd14887 458 SFPLASTLTSSPSSTSPF--SPTPSFRSSSAFATSPSLPSSLSSLSSSLS----------------SSPPVWEGRDNSDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 633 LGHShgtnwVEYNVAGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLAL 703
Cdd:cd14887 520 FYEK-----LNKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 704 RRATSMRKTFTTGMAAvKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdp 783
Cdd:cd14887 588 RLVGSKKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ-------------------------- 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 784 cEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLE 863
Cdd:cd14887 641 -EAGI--FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEIN 711
|
810
....*....|....
gi 1907082239 864 KSSCCLGLSRVFFR 877
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
120-550 |
2.67e-37 |
|
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: 151.54 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 195
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 196 VLLGSSGSGKTTSFQHLVQYLATIAG--TSGTKVFSVEKWQAL----STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAspTSWESHKIAERIEQRilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 270 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnHLAENNVFGIVPLSkpeEKQKAAQQFSKLQAA 349
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQW---HLPEGAAFSWLPNP---ERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKQFARhewaqKAAYLLGCSLEELSSAIFKHQLKGG 429
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVR-----TSALLLKLPEDHLLETLQIRTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 430 TLQRstSFRQgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQN-PEw 504
Cdd:cd14880 310 KQQQ--VFKK-----------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPE- 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082239 505 ggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 550
Cdd:cd14880 376 ------NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
121-550 |
4.60e-37 |
|
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: 151.21 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 190
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 191 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL---------LEAFGNSPTIMNGSATRFSQIL 261
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMdrvlqsnpiLEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 262 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGivplskPEEKQKAAQ 341
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 342 -------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagATKEPLEEqDEAAEAGrkQFARHEWAQKAAY 408
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQ--LEFESKEE-DGAAEIA--EEGNEKCLARVAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 409 LLGCSLEELSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALK--SSQH 486
Cdd:cd14908 311 LLGVDVDKLLRALTSKIIVVRGKEITTKL------------TPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKD 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 487 SLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 550
Cdd:cd14908 379 IRSSVGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
120-829 |
5.60e-37 |
|
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: 151.40 E-value: 5.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 188
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 189 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-------------QALST--LLEAFGNSPTIMNGS 253
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 254 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDATLRTELHLNHLAEN-NVFGI 327
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 328 VPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEA----AEAGRKQFARHEWA 403
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVfadeARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 404 QKAAYLLGCSLEELSSAIFKHQLKGGtlqrSTSFRQGPEESGLGEGTKLSALEClegmasglYSELFTLLISLVNRALK- 482
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHAS----NETLVVGVDVAHARNTRNALTMEC--------YRLLFEWLVARVNNKLQr 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 483 --------------SSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL 548
Cdd:cd14899 389 qasapwgadesdvdDEEDATDFIGLLDIFGFED------MAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 549 AFDDLEpvadDSVAAVDQASHlvrslahadEARGLLWLLEEEALVPGATEDALLDRlfsYYgpQEGDKKGQSPLLRSS-- 626
Cdd:cd14899 463 SFVDFP----NNRACLELFEH---------RPIGIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFRSApl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 627 --KPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQLALR 704
Cdd:cd14899 525 iqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGGRTRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 705 RATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPC 784
Cdd:cd14899 599 RAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRC---------------------------IKPNDSH 641
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082239 785 EAGLLQldVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 829
Cdd:cd14899 642 VGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
86-933 |
5.29e-36 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 149.02 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 86 DGAILDVDEDDIEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK 164
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 165 GCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEK--WQAlSTLLE 241
Cdd:PTZ00014 155 DAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLKIQNaiMAA-NPVLE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 242 AFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE 321
Cdd:PTZ00014 232 AFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 322 NNVfgIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKQFarhE 401
Cdd:PTZ00014 312 YKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGGLTDAAAISDESL---E 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 402 WAQKAAYLLGCSLEELS-SAIFKHQLKGGTLQRStsfRQGPEESglgEGTKLSaleclegMASGLYSELFTLLISLVNRA 480
Cdd:PTZ00014 387 VFNEACELLFLDYESLKkELTVKVTYAGNQKIEG---PWSKDES---EMLKDS-------LSKAVYEKLFLWIIRNLNAT 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 481 LKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDL 553
Cdd:PTZ00014 454 IEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGIsteELEYTSN 523
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 554 EPVAD------DSVAAV--DQashlvrSLAhadeargllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRS 625
Cdd:PTZ00014 524 ESVIDllcgkgKSVLSIleDQ------CLA------------------PGGTDEKFVSSCNTNLKNNPKYKPA-----KV 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 626 SKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIAgleggsqlalrr 705
Cdd:PTZ00014 575 DSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDLFEG----VEVEKGKLA------------ 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 706 atsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDPCE 785
Cdd:PTZ00014 636 ---------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP---------------------NENKKPLDWNS 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 786 AGLLqldvsllrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyivVDEKRAVEELLESLDLEKS 865
Cdd:PTZ00014 680 SKVL--------IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSS-----LDPKEKAEKLLERSGLPKD 746
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 866 SCCLGLSRVFFR---AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHFKKRkIQDLAIrcVQKNIKKNK 933
Cdd:PTZ00014 747 SYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVRKN-IKSLVR--IQAHLRRHL 814
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
121-836 |
1.88e-35 |
|
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: 144.66 E-value: 1.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGpsLLVLSTRGAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIVLLGS 200
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSG--LVFLALNPYETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 201 SGSGKTTSFQHLVQYLatIAGTSGTKvfSVEK-WQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDqaGQVASASIQTM 279
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSkpeekqkaaQQFSKLQAAMKVLAI-SPE 358
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLS---------EKYKMTCSAMKSLGIaNFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 359 EQKTCwliLASIYHLGAAGATKEpleeqdeaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGGTLQRSTS 436
Cdd:cd14898 223 SIEDC---LLGILYLGSIQFVND-----------GILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 437 FRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALK-SSQHSLCsmmIVDTPGFQNPEWGGsargasFEE 515
Cdd:cd14898 289 LKQ--------------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 516 LCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVADDSVaavdqashlvrsLAHADEARGLLWLLEEEALVPG 595
Cdd:cd14898 346 LCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC------------IRDFEKPCGLMDLISEESFNAW 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 596 ATEDALLDRLFSYYGPQEGDKKGQSPLLrsskprhfllghSHGTNWVEYNVAGWLNYTKQNpatqnaprllqdSQKKIIS 675
Cdd:cd14898 412 GNVKNLLVKIKKYLNGFINTKARDKIKV------------SHYAGDVEYDLRDFLDKNREK------------GQLLIFK 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 676 NLFLGRAGSatvlsgsiagleggsqlalrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVA 755
Cdd:cd14898 468 NLLINDEGS-------------------------------------KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNE 510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 756 EGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 835
Cdd:cd14898 511 ECRP-----------------------------WCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
.
gi 1907082239 836 L 836
Cdd:cd14898 562 L 562
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
120-835 |
1.58e-32 |
|
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: 137.41 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 189
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 190 RQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALS----------TLLEAFGNSPTIMNGSATRFSQ 259
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigqqilhafTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 260 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDATLRTELHLNHLAENnvFGIVPLSKPEEKQ 337
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 338 KA--AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPleEQDEAAEAGRKQFARHEWA----QKAAYLLG 411
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDP--EGGKSVGGANSTTVSDAQScalkDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 412 CSLEELSSAIFKHQLKggtLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVN--------RALKS 483
Cdd:cd14893 317 AKLLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNgilggifdRYEKS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 484 -----SQhslcSMMIVDTPGFQNPEwggsARGASFEELCHNYAQDRLQRLFHERTfLQELERYKEDNIELAFDDLepvAD 558
Cdd:cd14893 394 nivinSQ----GVHVLDMVGFENLT----PSQNSFDQLCFNYWSEKVHHFYVQNT-LAINFSFLEDESQQVENRL---TV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 559 DSVAAVDQASHLVRSLAHaDEARGLLWLLEEEALVPGATEDALLDRLFS-------YYGPQEGDKKGQSPLLRSSKPR-H 630
Cdd:cd14893 462 NSNVDITSEQEKCLQLFE-DKPFGIFDLLTENCKVRLPNDEDFVNKLFSgneavggLSRPNMGADTTNEYLAPSKDWRlL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 631 FLLGHSHGTnwVEYNVAGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLSGSIAglEGGSQLALRRATS 708
Cdd:cd14893 541 FIVQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAAASSE--KAAKQTEERGSTS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 709 --MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCE 785
Cdd:cd14893 609 skFRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVC---------------------------IKPNETLE 661
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 786 AGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 835
Cdd:cd14893 662 EGV--FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
121-566 |
9.51e-31 |
|
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: 131.02 E-value: 9.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLATIA-GTSGTkvfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGdGNRGA----TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRteLHLNHLAENNVFGIVPLSKPEEKQKA----------AQQFSKLQA 348
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 349 AMKVLAISPEEQKTCWLILASIYHLGAAgatkePLEEQDEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQL-K 427
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEI-----RFRQNGGYAE-----LENTEIASRVAELLRLDEKKFMWALTNYCLiK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 428 GGTLQRStsfRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN------RALKSSQHSLcsmMIVDTPGFQN 501
Cdd:cd14882 305 GGSAERR---KHTTEE----------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFEC 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 502 PEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIelafddlePVAD----DSVAAVDQ 566
Cdd:cd14882 369 FHRNR------LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDI--------PTINlrfyDNKTAVDQ 423
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
967-1685 |
1.24e-30 |
|
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: 132.50 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 967 IQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLL----DAETAERLR----TEKEMKELQT 1035
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1036 QYDALKKQMEVMEMEVME------ARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQELEDKMEVEQQSR 1108
Cdd:TIGR02169 245 QLASLEEELEKLTEEISElekrleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1109 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1188
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1189 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1261
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1262 LDEQAGSIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1308
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1309 QKKLKQME----------------------------------VQLEEEYEDKQK----------ALREKREL--ESKLST 1342
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAARRLmgKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1343 L-------------------SDQVNQR-DFESEKRLRKDLKRTKALLADAQIMLDHLKNNA--------PSKREIAQLKN 1394
Cdd:TIGR02169 644 LegelfeksgamtggsraprGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1395 QLEESEFTcAAAVKAR--------KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1461
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1462 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1537
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1538 EKTQVKRLENLAS---RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHElEMDLES 1614
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLED 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1615 LEAANQSLQADLklafKRIGDLQAAIEDEMEsdENEDLINSLQDmvtkyqkKKNKLEGDSDvdsELEDRVD 1685
Cdd:TIGR02169 956 VQAELQRVEEEI----RALEPVNMLAIQEYE--EVLKRLDELKE-------KRAKLEEERK---AILERIE 1010
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1091-1671 |
7.42e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 7.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1091 KRLQQELED-KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1169
Cdd:COG1196 216 RELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1249
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1250 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKA 1329
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1330 LREKRELESKLSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcAAAVKA 1409
Cdd:COG1196 448 AEEEAELEEEEEALLELL--------AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG----VKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1410 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQReknEIQNRLEEDQEDMNELMKKHKAAVA-------QASRDMAQMND 1482
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ---NIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1483 LQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE 1562
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1563 RDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1642
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
570 580 590
....*....|....*....|....*....|
gi 1907082239 1643 EMESDENEDL-INSLQDMVTKYQKKKNKLE 1671
Cdd:COG1196 751 EALEELPEPPdLEELERELERLEREIEALG 780
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
951-1673 |
1.76e-29 |
|
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: 129.02 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEKEM 1030
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYDALKkqmevmemevmearliraAEINgevddddaggewrlkyeRAVREVDFTKKRLQQeLEDKMEVEQQSRRQ 1110
Cdd:TIGR02168 284 EELQKELYALA------------------NEIS-----------------RLEQQKQILRERLAN-LERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1111 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1190
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1191 EKDMLLAEAFSLKQQMEEKDLDIAgftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1270
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLE---------EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALD 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1271 M----LEQAKLRLEMeMERMRQTHSKEMESRDEEVEEARQ------------SCQKKLKQ-MEVQL-----------EEE 1322
Cdd:TIGR02168 479 AaereLAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAaIEAALggrlqavvvenLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1323 YEDKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTKALLAD--------AQIMLDHLKNN---APSKREIAQ 1391
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPL-DSIKGTEIQGNDREILKNIEGFLGVAKdlvkfdpkLRKALSYLLGGvlvVDDLDNALE 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1392 LKNQLEESE----------FTCAAAVKARK-------AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE 1454
Cdd:TIGR02168 637 LAKKLRPGYrivtldgdlvRPGGVITGGSAktnssilERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1455 DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKIRELET 1533
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1534 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLE 1613
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1614 SLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDMVTKYQKKKNKLEGD 1673
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
122-547 |
2.36e-29 |
|
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: 126.54 E-value: 2.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 122 VLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 195
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 196 VLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVekwqALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 273
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL----ILGSnpLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 274 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF-GIVPLSKPE-EKQKaaqQFSKLQAAMK 351
Cdd:cd14886 159 GKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnASKCYDAPGiDDQK---EFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 352 VLaISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAeagrkQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtL 431
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAA-----KISNDEDFGKMCELLGIESSKAAQAI---------I 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 432 QRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarga 511
Cdd:cd14886 301 TKVVVINNETIISPV---TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------ 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907082239 512 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE 547
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
173-839 |
3.79e-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: 126.08 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 173 PHIYAVAQTAYRAMLM-SRQDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQalSTLLEA 242
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGqlsymhssnTSQRSIADKIDENLKWS--NPVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 243 FGNSPTIMNGSATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDAT-------LRTEL 314
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkelggLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 315 HLNHLAENNVF---GI--VPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLgaagatkepLEEQDEA 389
Cdd:cd14875 214 DYKCLNGGNTFvrrGVdgKTLDDAHE-------FQNVRHALSMIGVELETQNSIFRVLASILHL---------MEVEFES 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 390 AEAGRKQFARHEwaqkaAYLLGCSLEELSSAifkhQLKGGTLQRS-----TSFRQGPEESGLgegtklsalecLEGMASG 464
Cdd:cd14875 278 DQNDKAQIADET-----PFLTACRLLQLDPA----KLRECFLVKSktslvTILANKTEAEGF-----------RNAFCKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 465 LYSELFTLLISLVNRALKSSQH-SLCSMM-IVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYK 542
Cdd:cd14875 338 IYVGLFDRLVEFVNASITPQGDcSGCKYIgLLDIFGFEN------FTRNSFEQLCINYANESLQNHYNKYTFINDEEECR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 543 EDNIE---LAFDDlepvADDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSYYGpqegdkkGQ 619
Cdd:cd14875 412 REGIQipkIEFPD----NSECVNMFDQKRTGIFSM--LDE----------ECNFKGGTTERFTTNLWDQWA-------NK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 620 SPLL---RSSKPRHFllGHSHGTNWVEYNVAGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagl 695
Cdd:cd14875 469 SPYFvlpKSTIPNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA---------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 696 eggsqlalRRatsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssse 775
Cdd:cd14875 535 --------RR----------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPS--------------- 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 776 ldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 839
Cdd:cd14875 576 --------------FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
965-1672 |
5.58e-29 |
|
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: 127.21 E-value: 5.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 965 EEI-QQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDErntgESASQLLDAEtaeRLRTEKEMKELQTQYDALKKQ 1043
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1044 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQELEDKMEVEQqSRRQLERRLGDLQ 1119
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1120 ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEA 1199
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1200 FSLKQQMEEkdldiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQags 1268
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1269 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS- 1344
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1345 --DQVNQRDFESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1389
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1390 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1453
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1454 EDQEDMNELMKKHKAAVAQAS--RDMAQMN---------DLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1520
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1521 VSRQEAKiRELETRLEFEKTQVKRL-------ENLASRLKETME--KLTEERDQRAAAENREkEQNKRLQRQLRDTKEEM 1591
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELedelqatEDAKLRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1592 SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMEsdENEDLINSLQDMVTKYQKKKNKLE 1671
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQR--ELEEARASRDEILAQSKESEKKLK 836
|
.
gi 1907082239 1672 G 1672
Cdd:pfam01576 837 N 837
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
976-1619 |
6.75e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.59 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 976 KVEKERNELRLSS--DRLEtRISELTSELtdERNTGESASQlldAETAERLRtekemkELQTQYDALKKQMEVMEMEVME 1053
Cdd:COG1196 171 KERKEEAERKLEAteENLE-RLEDILGEL--ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1054 ARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQL 1132
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1133 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD 1212
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1213 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK 1292
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1293 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrkdlkrtkALLADA 1372
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1373 QIMLDHLKNNAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR 1451
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1452 LEEDQEDM-NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRE 1530
Cdd:COG1196 627 LVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA------------ERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1531 LETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEM 1610
Cdd:COG1196 695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
....*....
gi 1907082239 1611 DLESLEAAN 1619
Cdd:COG1196 775 EIEALGPVN 783
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
120-834 |
4.16e-28 |
|
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: 122.67 E-value: 4.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIVLL 198
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSvekwQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 278
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHS----SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 279 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLaeNNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 358
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 359 EQKTCWLILASIYHLGAA--GATKEPLEEQDeAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRSts 436
Cdd:cd14874 225 HCISIYKIISTILHIGNIyfRTKRNPNVEQD-VVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 437 frqgpeesglgegtklSALECLEGMASGLYSELFTLLISLVNRALKSSQHSlCSMMIVDTPGFQNPEWGGsargasFEEL 516
Cdd:cd14874 297 ----------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 517 CHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaDDSVAAVDQASHLVRSLAHADEarGLLWLLEEEALVPGA 596
Cdd:cd14874 354 LINSVNERIENLFVKHSFHDQLVDYAKDGISV---------DYKVPNSIENGKTVELLFKKPY--GLLPLLTDECKFPKG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 597 TEDALLDRL------FSYYGPQegdkkgqspllRSSKPRHFLLGHSHGTNWveYNVAGWLNYTKQNpATQNAPRLLQDSQ 670
Cdd:cd14874 423 SHESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLRSSK 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 671 KKIISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKRSKMHFVHC 750
Cdd:cd14874 489 NPIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHFVRC 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 751 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 830
Cdd:cd14874 536 IKSNNERQPK-----------------------------KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
....
gi 1907082239 831 VLAP 834
Cdd:cd14874 587 CLLP 590
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
122-753 |
4.23e-28 |
|
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: 122.79 E-value: 4.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 122 VLHTLRQRYGASLLHTYAGPSLLVLST---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 186
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 187 LMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEKW-QALSTLLEAFGNSPTIMNGSATRFSQILSLDF 265
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 266 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENN--------VFGIVPLskpeekq 337
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDV------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 338 kaaQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRkqfARHEWAQKAAYLLGCSLEEL 417
Cdd:cd14876 220 ---ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISN---ESLEVFKEACSLLFLDPEAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 418 SSAIF-KHQLKGGtlQRSTSFRQGPEesglGEGTKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDT 496
Cdd:cd14876 294 KRELTvKVTKAGG--QEIEGRWTKDD----AEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 497 PGF---QNpewggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV 564
Cdd:cd14876 361 FGFevfKN---------NSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 565 --DQAshlvrsLAhadeargllwlleeealvPGATEDALLDRLFSyygpQEGDKKGQSPLLRSSKpRHFLLGHSHGTnwV 642
Cdd:cd14876 432 leDQC------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIGD--I 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 643 EYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavk 721
Cdd:cd14876 481 QYNAEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK----------- 537
|
650 660 670
....*....|....*....|....*....|..
gi 1907082239 722 kkslciqiklQVDALIDTIKRSKMHFVHCFLP 753
Cdd:cd14876 538 ----------QLESLMGLINSTEPHFIRCIKP 559
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
951-1682 |
2.19e-27 |
|
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: 121.82 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSE--EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEK 1028
Cdd:pfam01576 227 LQAQIAElrAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESER--------------AARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1029 EMKELQTQYDALKkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVdftKKRLQQELEDKMEVEQQSR 1108
Cdd:pfam01576 293 QRRDLGEELEALK------------------TELEDTLDTTAAQQELRSKREQEVTEL---KKALEEETRSHEAQLQEMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1109 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1188
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1189 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGS 1268
Cdd:pfam01576 432 AEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1269 IQMLEQAKLRLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS-DQV 1347
Cdd:pfam01576 512 KRNVERQLSTLQAQLSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvDLD 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1348 NQRDFES--EKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEESEFTCAAAVKARKAMEVEMEDLH 1421
Cdd:pfam01576 591 HQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1422 LQIDDIAK-------AKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDmaqmndLQAQIEESnkek 1494
Cdd:pfam01576 671 SSKDDVGKnvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERD------LQARDEQG---- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1495 qelQEKLQALQSQVefleqsmvdkslvsrqeakiRELETRLEFEKTQvkRLENLASRLKETMEKLTEERDQRAAAENREK 1574
Cdd:pfam01576 741 ---EEKRRQLVKQV--------------------RELEAELEDERKQ--RAQAVAAKKKLELDLKELEAQIDAANKGREE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1575 --EQNKRLQRQLRDTKEEMSE--LARKEAEASRKkhELEMDLESLEAANQSLQADLKLAFKrigdlqAAIEDEMESDENE 1650
Cdd:pfam01576 796 avKQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQEDLAASER------ARRQAQQERDELA 867
|
730 740 750
....*....|....*....|....*....|...
gi 1907082239 1651 DLINSLQDMVTKYQKKKNKLEGD-SDVDSELED 1682
Cdd:pfam01576 868 DEIASGASGKSALQDEKRRLEARiAQLEEELEE 900
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
121-566 |
1.15e-26 |
|
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: 118.47 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 192
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 193 QSIVLLGSSGSGKTTSFQHLVQYLATIAGTSgTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQ----- 267
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 268 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDATLRT-----ELHLNHLAENNVFGIVPLSK----- 332
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSDEDLARrnlvrNCGVYGLLNPDESHQKRSVKgtlrl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 333 --------PEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagatkepleeqdeaaeagrkqfarhEWAQ 404
Cdd:cd14884 241 gsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG--------------------------NRAY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 405 KAAyllgCSLEELSSAIFKHQLKGGTLQ-RSTSFRQgpeesglgEGTKLSALECLEGMASGLYSELFTLLISLVNRALKS 483
Cdd:cd14884 295 KAA----AECLQIEEEDLENVIKYKNIRvSHEVIRT--------ERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 484 SQHSLCSM------------MIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIeLAFD 551
Cdd:cd14884 363 CKEKDESDnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCS 435
|
490
....*....|....*
gi 1907082239 552 DLEPVADDSVAAVDQ 566
Cdd:cd14884 436 DVAPSYSDTLIFIAK 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1619 |
1.42e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 116.31 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNELR-----LSSD--RLETRISELTSELTDERNTGESASQLLDAETAERLRTEKE 1029
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQkelyaLANEisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1030 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQeLEDKMEVEQQSRR 1109
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-LEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1110 QLERRLGDLQADSDESQRALQQLKkkCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEETQR----E 1181
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEAleelREELEEAEQALDAAERELAQLQARldslE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1182 KLQR--EKLQREKDMLLAEAF-------SLKQQME-----EKDLDIA--GFTQKVV--SLEAELQDISSQESKDE---AS 1240
Cdd:TIGR02168 496 RLQEnlEGFSEGVKALLKNQSglsgilgVLSELISvdegyEAAIEAAlgGRLQAVVveNLNAAKKAIAFLKQNELgrvTF 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1241 LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERM--------------RQTHSKEMESR--------- 1297
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddldnalELAKKLRPGYRivtldgdlv 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1298 ---------DEEVEEARQSCQKKLKQMEVQ---LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDL 1362
Cdd:TIGR02168 656 rpggvitggSAKTNSSILERRREIEELEEKieeLEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1363 KRTKALLADAQIMLDHL-KNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1441
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1442 QREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSL 1520
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALlRSE 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1521 VSRQEAKIRELETRlefektqVKRLENLasrLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARK--- 1597
Cdd:TIGR02168 896 LEELSEELRELESK-------RSELRRE---LEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKied 965
|
730 740
....*....|....*....|...
gi 1907082239 1598 -EAEASRKKHELEMDLESLEAAN 1619
Cdd:TIGR02168 966 dEEEARRRLKRLENKIKELGPVN 988
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
961-1659 |
4.79e-25 |
|
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: 114.39 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 961 RNKDEEIQQLRSKLEKVE------------KERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE-RLRTE 1027
Cdd:TIGR02169 207 REKAERYQALLKEKREYEgyellkekealeRQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1028 KEMKELQTQYDALKKQMEVMEMEVMEA--RLIRAAE--INGEVDDDDAGGEWRlKYERAVREVDFTKKRLQQELEDKmev 1103
Cdd:TIGR02169 287 EEQLRVKEKIGELEAEIASLERSIAEKerELEDAEErlAKLEAEIDKLLAEIE-ELEREIEEERKRRDKLTEEYAEL--- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1104 eQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQQVRnheLEKKQRRFDSELSQAHEETQREKL 1183
Cdd:TIGR02169 363 -KEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINE----LKRELDR---LQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1184 QREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV---KDQEE 1260
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggRAVEE 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1261 ELD------------------------EQAGS-----------------IQMLEQAKL-RLE-MEMERMRQTHS-KEMES 1296
Cdd:TIGR02169 515 VLKasiqgvhgtvaqlgsvgeryataiEVAAGnrlnnvvveddavakeaIELLKRRKAgRATfLPLNKMRDERRdLSILS 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1297 RD------------------------------EEVEEAR----------------------------------------- 1305
Cdd:TIGR02169 595 EDgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAARrlmgkyrmvtlegelfeksgamtggsraprggilfsrsepa 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1306 --QSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLDHLKNN- 1382
Cdd:TIGR02169 675 elQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEEDLSSLEQEi 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1383 APSKREIAQLKNQLEESEftcAAAVKARKAME-VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1461
Cdd:TIGR02169 754 ENVKSELKELEARIEELE---EDLHKLEEALNdLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1462 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT 1540
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlKKERDELEAQLRELERKIEELEA 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1541 QVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAEASRKKhELEMDLESLEAANQ 1620
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEAL--------------EEELSEIEDPKGEDEEIPEEELSLEDVQAELQ-RVEEEIRALEPVNM 975
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1907082239 1621 SLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSLQDM 1659
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEEYEKK 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
955-1650 |
8.60e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.08 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 955 LSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL--ETRISELTSELTDERNTgESASQLLDAETAERLRTEKEMKE 1032
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1033 LQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQELEDKMEVEQqSRRQLE 1112
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEA-VKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1113 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEETQREKLQREKLQR 1190
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1191 EKdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGSI 1269
Cdd:PTZ00121 1315 KK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1270 QMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1349
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1350 RDFESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLHLQI 1424
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1425 DDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1501
Cdd:PTZ00121 1549 DELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1502 QALQSQVEFLEQSMVDKslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ 1581
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1582 R-------------QLRDTKEE----MSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEM 1644
Cdd:PTZ00121 1706 ElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
....*.
gi 1907082239 1645 ESDENE 1650
Cdd:PTZ00121 1786 DEEDEK 1791
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1094-1670 |
1.02e-23 |
|
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: 109.34 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1094 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1171
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1172 SQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1251
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1252 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1328
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1329 ALREKrelESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAVK 1408
Cdd:TIGR04523 247 EISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1409 AR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDM-AQ 1479
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1480 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFEKTQVKR 1544
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1545 LENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQA 1624
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1625 DLKLAF--KRIGDLQAAIEDEMEsdENEDLINS---LQDMVTKYQKKKNKL 1670
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIEELKQ--TQKSLKKKqeeKQELIDQKEKEKKDL 601
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
952-1597 |
2.42e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 108.99 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD----AETAERL-RT 1026
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQAELeEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1027 EKEMKELQTQYDALKKQMEVMEMEVMEARLIR------AAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRL---QQEL 1097
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALdaaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLG-DLQA----DSDESQRALQQLKK--------------KCQRLTAELQDTKLHLEGQQVRNH 1158
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALGgRLQAvvveNLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1159 ELEKKQRRFDSELS------------QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAE 1226
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1227 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERmrqtHSKEMESRDEEVEEArq 1306
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTEL-- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1307 scQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1386
Cdd:TIGR02168 760 --EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1387 -REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1465
Cdd:TIGR02168 837 eRRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1466 HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQsQVEFleqsMVDKSLVSRQEAKIRELETRLEFEKTQVKRL 1545
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTL----EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1546 E--NLASrlketMEKLTEERdQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1597
Cdd:TIGR02168 985 GpvNLAA-----IEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
120-546 |
1.55e-22 |
|
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: 105.10 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 120 SSVLHTLRQRYGASLLHTYAGPSLLVLStrgaPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISIN----PYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLatIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 279
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS-NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 280 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISpEE 359
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR--SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 360 QKTCWLILASIYHLGAAgatkepleEQDEAAEAGRKQFAR-----HEWAQKAAYLLGCSLEELSSAIfkhqlkggTLQRS 434
Cdd:cd14937 231 KDDLFLTLSGLLLLGNV--------EYQEIEKGGKTNCSEldknnLELVNEISNLLGINYENLKDCL--------VFTEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 435 TSFRQGPEesglgegTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGA 511
Cdd:cd14937 295 TIANQKIE-------IPLSVEESVsicKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKN 361
|
410 420 430
....*....|....*....|....*....|....*
gi 1907082239 512 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI 546
Cdd:cd14937 362 SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDI 396
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
877-1666 |
1.91e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.38 E-value: 1.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 877 RAGTLARLEEQRDEQTSRHLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 949
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 950 LIQVQLSEEQIR----NKDEEIQQLRSKLEKVEKERNE---LRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1022
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1023 RLRTEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKME 1102
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1103 VEQQSRRQLERRLGDLQADSDESQRAlQQLKKKCQrltaelQDTKlhlEGQQVRNHELEKKQRrfdSELSQAHEETQREK 1182
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAE------EDKK---KADELKKAAAAKKKA---DEAKKKAEEKKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1183 LQREKLQREKdmllaEAFSLKQQMEEKDldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEEL 1262
Cdd:PTZ00121 1435 EAKKKAEEAK-----KADEAKKKAEEAK-------------KAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1263 DEQAGSIQMLEQAKLRLEmEMERMRQTHSKEMESRDEE---VEEARQSCQKKlKQMEVQLEEEY---EDKQKALREKREL 1336
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEakkADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAE 1573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1337 ESKLSTL-----SDQVNQRDFESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES-------- 1399
Cdd:PTZ00121 1574 EDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelk 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1400 ----EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVAQ 1472
Cdd:PTZ00121 1654 kaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1473 ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLAS-- 1550
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANii 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1551 --------RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSL 1622
Cdd:PTZ00121 1812 eggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1907082239 1623 QADLKlafkrigDLQAAIEDEMESDENEDLINSLQDmVTKYQKK 1666
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLD-KDEYIKR 1927
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
952-1581 |
2.01e-22 |
|
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: 105.10 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMK 1031
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1032 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQL 1111
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1112 E----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1174
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1175 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1254
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1255 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEE---EYED 1325
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1326 KQKALREK-RELESKLSTLsDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNNapSKREIAQLKNQLEESEFTca 1404
Cdd:TIGR04523 480 IKQNLEQKqKELKSKEKEL-KKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKE--KESKISDLEDELNKDDFE-- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1405 aavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQ 1484
Cdd:TIGR04523 554 -----------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1485 AQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFEKTQVKRLENLASRLKET 1555
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELSLHYKKY 696
|
650 660
....*....|....*....|....*...
gi 1907082239 1556 MEKLTEERDQRAAAENRE--KEQNKRLQ 1581
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKeiEKELKKLD 724
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
881-1566 |
4.06e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.63 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 881 LARLEEQRdEQTSRHLTLfQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKgvkdwpwwklfttvrplIQVQLSEEQI 960
Cdd:COG1196 202 LEPLERQA-EKAERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELE-----------------AELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 961 RNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDAL 1040
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1041 KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQELEDKMEVEQQSRRQLERRLGDLQA 1120
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1121 DSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1200
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1201 SLKQQMEEKDLDIAGftqkvvSLEAELQDISSQESKDEASLAKVKKQLRD-----LEAKVKDQEEELDEQAGS-IQMLEQ 1274
Cdd:COG1196 495 LLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAAALQNIVVEDDEVAAAaIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1275 AKL--RLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmevqLEEEYEDKQKALREKRELESKLSTLSDQvnqrdf 1352
Cdd:COG1196 569 AKAgrATFLPLDKIRARAALAAALARGAIGAAV-------------DLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1353 eseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKT 1432
Cdd:COG1196 630 ---ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------LEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1433 ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLE 1512
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1513 QsmVDksLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQR 1566
Cdd:COG1196 781 P--VN--LLAIEEYE--ELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1073-1641 |
8.39e-22 |
|
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: 103.72 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1073 GEWRLKYERAVREVDFTKKRLQQELE-----DKMEVEQQSRRQ-LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT 1146
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQeLEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1147 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMllaeafslkqqmeekdldiagftqkvvsLEAE 1226
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----------------------------LEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1227 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQ 1306
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1307 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLsdqvnQRDFESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1381
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1382 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE 1453
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1454 EDQEDMNELMKKHKAAvaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1533
Cdd:pfam01576 395 TLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1534 rlefektqvKRLENLASRLKETMEKLTEERDQRAAAENR----EKEQNKrLQRQLRDTKE-------EMSELARKEAEAS 1602
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEakrnverQLSTLQAQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082239 1603 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1641
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1057-1671 |
2.32e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.06 E-value: 2.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1057 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQELEDKMEVEQQSRRQlERRLGDLQA 1120
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1121 DSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDMLLA 1197
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1198 EAfslkQQMEEKDLDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGSIQMLEQ 1274
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1275 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdFES 1354
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1355 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1434
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1435 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS 1514
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1515 MVDKSlvsrqEAKIRELET---RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEM 1591
Cdd:PRK03918 586 SVEEL-----EERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1592 SElarkeaEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED----EMESDENEDLINSLQDMVTKYQKKK 1667
Cdd:PRK03918 661 YE------ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEErekaKKELEKLEKALERVEELREKVKKYK 734
|
....
gi 1907082239 1668 NKLE 1671
Cdd:PRK03918 735 ALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1078-1600 |
2.82e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.68 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1078 KYERAVREVDFTKKRLQqELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1157
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1158 HELEKKQR--RFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFtQKVVSLEAELQDISSQES 1235
Cdd:PRK03918 304 EYLDELREieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1236 kdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQKK 1311
Cdd:PRK03918 383 --GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1312 LKQMEVQLEEEYEDKQKALREKRELESKLstlsdqvnqrdfESEKRLRKDLKrtkalladaqiMLDHLKN--NAPSKREI 1389
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1390 AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMNE 1461
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1462 LMKKH------KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETRL 1535
Cdd:PRK03918 597 LEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSREL 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1536 EFEKTQVKRLENLASRLKETMEKLTEERDQRAAAE------NREKEQNKRLQRQLRDTKEEMSELARKEAE 1600
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
121-573 |
2.84e-20 |
|
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: 97.86 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 199
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 200 SSGSGKTTSFQHLVQYLAT--IAGTSGTKVFSVEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 277
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTtdLSRSKYLRDYILES----GIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 278 TMLLEKLRVARRPASEATFNVFYYLLAcgdatlrtelhlnhlaennvfGIVplskpeEKQKAAQQFSKLQaamkvlaisp 357
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLK---------------------GIT------DEEKAAYQLGDIN---------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 358 eeqktcwlilaSIYHLGAAGATKEPLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLE---ELSSAIF-----KHQLKGG 429
Cdd:cd14905 199 -----------SYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSfiiILGNVTFfqkngKTEVKDR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 430 TLQRSTSFRQGPEESGLgEGTKLS--------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLcSMMIVDTPGFQN 501
Cdd:cd14905 268 TLIESLSHNITFDSTKL-ENILISdrsmpvneAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQES 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 502 PEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI----ELAFDDLE---PVADDSVAAVDQASHLVRS 573
Cdd:cd14905 346 SQLNG------YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEesvEMMEKIINLLDQESKNINS 418
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1224-1682 |
3.07e-20 |
|
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: 98.71 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1224 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS----------KE 1293
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1294 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTK 1366
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1367 ALLADAQI----------MLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1436
Cdd:pfam01576 159 ERISEFTSnlaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1437 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE-FLEQSM 1515
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1516 VDKSLVSRQEAKIRELETRLEFE-KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSEL 1594
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1595 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIEdemesdenedlinSLQDMVTKYQKKKNKLEGD 1673
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELE-------------SVSSLLNEAEGKNIKLSKD 462
|
490
....*....|
gi 1907082239 1674 -SDVDSELED 1682
Cdd:pfam01576 463 vSSLESQLQD 472
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
958-1616 |
6.66e-20 |
|
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: 97.01 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqlLDAET---AERLRTEKEMK-EL 1033
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDKEQKnKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1034 QTQYDALKKQMEVMEMEVmearliraAEINGEV-DDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ------Q 1106
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNI--------DKFLTEIkKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkikN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1107 SRRQLERRLGDLQAdsdesqralqqLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFdSELSQAHEETQrEKLQRE 1186
Cdd:TIGR04523 195 KLLKLELLLSNLKK-----------KIQKNKSLESQISELK---KQNNQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1187 KLQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1261
Cdd:TIGR04523 259 KDEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1262 LDEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLS 1341
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1342 TLSDQVNQRD-----FESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkarkameve 1416
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE---------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1417 medlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASrdmaqmnDLQAQIEESNKEKQE 1496
Cdd:TIGR04523 454 -----LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK-------ELEEKVKDLTKKISS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1497 LQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE--KTQVKRLENLASRLKETMEKLTEERDQ-RAAAENRE 1573
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDL------EDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQKE 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1574 KEQNK-------------RLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1616
Cdd:TIGR04523 596 KEKKDlikeieekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
950-1590 |
7.44e-20 |
|
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: 97.35 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 950 LIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLE-----TRISELTSELTDERNTGESASQLLDAETAERl 1024
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1025 rtekeMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgeWRLKYERAVREVDFTKKrLQQELEDKMEVE 1104
Cdd:TIGR00618 324 -----AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS--IREISCQQHTLTQHIHT-LQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1105 QQSRRQLE--RRLGDLQADSDESQRALQQlkkkcqrltaelqdTKLHLEGQQVRNHELEKKQRRFDSElsQAHEETQREK 1182
Cdd:TIGR00618 396 QSLCKELDilQREQATIDTRTSAFRDLQG--------------QLAHAKKQQELQQRYAELCAAAITC--TAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1183 LQREKLQ--REKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS---QESKDEASLAKVKKQLRDLEAKVKD 1257
Cdd:TIGR00618 460 HLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1258 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1334
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1335 ELESKLSTLSDQVNQRDFESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM 1413
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1414 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1493
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1494 KQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENRE 1573
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
650
....*....|....*..
gi 1907082239 1574 KEQNKRLQRQLRDTKEE 1590
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLS 875
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
151-269 |
1.15e-19 |
|
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: 88.17 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 151 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTK---- 226
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 227 ---------VFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 269
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
948-1704 |
1.37e-19 |
|
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: 96.58 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 948 RPLIQVQLSEEQIRNKDEEIQqlRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTE 1027
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELK--LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1028 KEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQS 1107
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1108 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1187
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1188 LQREKDMLLAEAFSL--KQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1265
Cdd:pfam02463 414 ARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1266 AG-SIQMLEQ------AKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1338
Cdd:pfam02463 494 KLeERSQKESkarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1339 KLStlSDQVNQRDFESEKRLRKDLK------RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKA 1412
Cdd:pfam02463 574 PLG--ARKLRLLIPKLKLPLKSIAVleidpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKE-------SAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1413 MEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNK 1492
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1493 EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENR 1572
Cdd:pfam02463 725 DRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1573 E--KEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1650
Cdd:pfam02463 805 AleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKL 884
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1651 DLINS---------LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDD 1704
Cdd:pfam02463 885 KDELEskeekekeeKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
957-1684 |
7.11e-19 |
|
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: 94.03 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETRISELTSE---LTDERNTgESASQ----------LLDAE 1019
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1020 TAERLRtEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingeVDDDDAGGEWRLKYERA----VREVDFTKKRLQQ 1095
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL-------VDFEEASGKKIYEHDSMstmhFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1096 ELEDKMEVEQQSRRQLERRLGDLQADS-DESQRALQQLKKKCQRLTAE--LQDTKLHLEGQQVRNhELEKKQRRFDSELS 1172
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEheVEITGLTEKASSARS-QANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1173 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1252
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1253 AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEYEDKQKALRE 1332
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1333 KRELESKLSTLSDQVnqrdfESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEESE----FTCAAAVK 1408
Cdd:pfam15921 456 KNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKEraieATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1409 ARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDMAQMNDLQAQ 1486
Cdd:pfam15921 522 LRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1487 IE-ESNKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETR---LEFEKTqvkRLENLASRLKETMEKLTEE 1562
Cdd:pfam15921 595 LEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARvsdLELEKV---KLVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1563 RDQ-------RAAAENREKEQNKRLQRQLRDTKEEMSELARK-EAEASRKKHELEM---DLESLEAAN-------QSLQA 1624
Cdd:pfam15921 655 RDQllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamkvaMGMQK 734
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1625 DLKLAFKRIGDLQAAI---EDEMESDENEDLI-----NSLQDMVTKYQKKKNKLEGDSDVDSELEDRV 1684
Cdd:pfam15921 735 QITAKRGQIDALQSKIqflEEAMTNANKEKHFlkeekNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1212-1602 |
1.01e-18 |
|
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: 93.59 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1212 DIAG---FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLEMEmermrq 1288
Cdd:TIGR02169 161 EIAGvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-REREKAERYQALLKEKREYEGYELLKEKE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1289 thskEMESRDEEVEEARQSCQKKLKQMEVQLEEeyedkqkalREKR--ELESKLSTLSDQVNQRDFESEKRLRKDLKRTK 1366
Cdd:TIGR02169 234 ----ALERQKEAIERQLASLEEELEKLTEEISE---------LEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1367 ALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1446
Cdd:TIGR02169 301 AEIASLE-------------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1447 EIQNRLEEDQEDMNELMKKHKAAVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEA 1526
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1527 KIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRDTKeemSELARKEAEAS 1602
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQ---RELAEAEAQAR 500
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
957-1667 |
2.84e-18 |
|
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: 91.71 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLLD---AETAERL-RTEKE 1029
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKetcARSAEKTkKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1030 MKELQTQYDALKKQMEvmemevmeaRLIRAAEiNGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmevEQQSRR 1109
Cdd:pfam05483 178 REETRQVYMDLNNNIE---------KMILAFE-ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1110 QL------ERRLGDLQADSDESQRALQQLKKKcqrltAELQDTKLHlegqqvrnhELEKKQRRFDSELSQAHEETQREKL 1183
Cdd:pfam05483 245 LLiqitekENKMKDLTFLLEESRDKANQLEEK-----TKLQDENLK---------ELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1184 QREKLQREKDMLLAEAFSLKQ----QMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1259
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1260 EELDEQAG-----SIQMLEQAKLRLEMEM----ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1330
Cdd:pfam05483 391 SELEEMTKfknnkEVELEELKKILAEDEKlldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1331 REKRELESKLstlsdqvnqrdfESEKrlrkdLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKAR 1410
Cdd:pfam05483 471 KEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1411 KAMEvemEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQ 1486
Cdd:pfam05483 526 KKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1487 IEESNKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKE----TMEKLTEE 1562
Cdd:pfam05483 603 IENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1563 RDQRAA----AENREKEQNKRLQRQLRD---------------TKEEMSELA---RKEAEASRKKHELEMDLESLEAANQ 1620
Cdd:pfam05483 677 VEKAKAiadeAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiIEERDSELGlykNKEQEQSSAKAALEIELSNIKAELL 756
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082239 1621 SLQADLklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKK 1667
Cdd:pfam05483 757 SLKKQL----------------EIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1082-1663 |
5.20e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 5.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1082 AVREVDFTKKRLQQELEDkmEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1161
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1162 kkqrrfdsELSQAHEETQREKLQREklqREKDMLLAEAFSLKQQMEEkdldiagftqkvvsLEAELQDISSQESKDEASL 1241
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1242 AKVKKQLRDLEAKVKDQEEELDEQAGSIQML-EQAK------LRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQ 1314
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHnEEAEslredaDDLEERAEELR-EEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1315 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnAPskrEIAQlkn 1394
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALLEAGK--CP---ECGQ--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1395 QLEESEFTCAAAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKNeiqnRLEEDQEDMNELMKKHKAAVAQ 1472
Cdd:PRK02224 460 PVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIE----RLEERREDLEELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1473 ASRdmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsRQEAKirELETRLEFEKTQVKRLENLASRL 1552
Cdd:PRK02224 535 KRE----------RAEELRERAAELEAEAEEKREAAAEAEEEAEEA----REEVA--ELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1553 ------KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHE-----LEMDLESLEAANQS 1621
Cdd:PRK02224 599 aaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDD 678
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907082239 1622 LQadlklafKRIGDLQAAIEdEMES--DENEDLINSLQDMVTKY 1663
Cdd:PRK02224 679 LQ-------AEIGAVENELE-ELEElrERREALENRVEALEALY 714
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1022-1671 |
1.41e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.03 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1022 ERLRTEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1095
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1096 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1175
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1176 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1255
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1256 KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRE 1335
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1336 LESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM-- 1413
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLK--VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAis 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1414 ---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDMAQMNDLQAQ 1486
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1487 IEESNKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRLEfekTQVKRLENLASRLKETMEKLTEERDQR 1566
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELTKE---LLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1567 AAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigdLQAAIEDEMES 1646
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS---ELSLKEKELAE 778
|
650 660
....*....|....*....|....*
gi 1907082239 1647 DENEDLINSLQDMVTKYQKKKNKLE 1671
Cdd:pfam02463 779 EREKTEKLKVEEEKEEKLKAQEEEL 803
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1389-1651 |
1.83e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1389 IAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA 1468
Cdd:COG1196 195 LGELERQLEPLE---RQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1469 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSL-VSRQEAKIRELETRLEFEKTQVKRLEN 1547
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEeLAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1548 LASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1627
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260
....*....|....*....|....
gi 1907082239 1628 LAFKRIGDLQAAIEDEMESDENED 1651
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELE 455
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1089-1671 |
9.70e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 86.95 E-value: 9.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1089 TKKRLQQELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHELEKK 1163
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1164 QRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQ--MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1241
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1242 AKVKKQLRDLEAKVK---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQMEVQ 1318
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QCEKL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1319 LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR---E 1388
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1389 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKA 1468
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1469 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLEFEK 1539
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1540 TQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA--------SRKKHELEMD 1611
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAA 773
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1612 L------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQdMVTKYQKKKNKLE 1671
Cdd:TIGR00618 774 LqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCET-LVQEEEQFLSRLE 838
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
121-303 |
2.38e-16 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 85.27 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 198
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 199 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---------------------STLLEAFGNSPTIMNGSATRF 257
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907082239 258 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 303
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
121-850 |
1.23e-15 |
|
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: 82.85 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 121 SVLHTLRQRYGASLLHTYAGPSLLVLST---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVL 197
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 198 LGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQ 277
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 278 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN--------HLAENNVFgivplskpEEKQKAAQQFSKLQAA 349
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 350 MKVLAISpeeqktcWL----ILASIYHLGAAGATKEPLEEQDEAAEAGRKQfarhewaqkAAYLLGCSleelSSAIFKhq 425
Cdd:cd14881 224 LGILGIP-------FLdvvrVLAAVLLLGNVQFIDGGGLEVDVKGETELKS---------VAALLGVS----GAALFR-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 426 lkgGTLQRSTSFRQGPEESGLGEGTKLSALECLegmASGLYSElftLLISLVNRAlkSSQHSLCSMM----------IVD 495
Cdd:cd14881 282 ---GLTTRTHNARGQLVKSVCDANMSNMTRDAL---AKALYCR---TVATIVRRA--NSLKRLGSTLgthatdgfigILD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 496 TPGFQNPewggsaRGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafdDLEPVADDSVAAVDqashLVRSLa 575
Cdd:cd14881 351 MFGFEDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID----LISSL- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 576 hadeARGLLWLLEEEALVPGATEdalldrlfSYYGPQEGDKKGQSPLLRSSK--PRHFLLGHSHGTnwVEYNVAGWLnyt 653
Cdd:cd14881 417 ----RTGLLSMLDVECSPRGTAE--------SYVAKIKVQHRQNPRLFEAKPqdDRMFGIRHFAGR--VVYDASDFL--- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 654 kqnpatqnaprllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQIKLQV 733
Cdd:cd14881 480 --------------DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRL 514
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 734 DALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYR 813
Cdd:cd14881 515 DNLLRTLVHARPHFVRCIRSNTTETPN-----------------------------HFDRGTVVRQIRSLQVLETVNLMA 565
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907082239 814 QGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDEK 850
Cdd:cd14881 566 GGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
948-1677 |
1.46e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.56 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 948 RPLIQVQLSEEQIRNKDEEIQ--QLRSKLEKVEKE-------RNELRLSSDRLETR---ISELTSELTDERNTGESASQL 1015
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1016 LDAETAERLRT--------EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1084
Cdd:TIGR00606 431 IRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1085 -EVDFTKKRLQQELE-----------------DKMEVEQQSRRQLERRLGDLQA------DSDESQRALQQLKKKCQRLT 1140
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1141 AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-----------ETQREKLQR--EKLQREKDMLLAEAFSLKQQME 1207
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeESDLERLKEeiEKSSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1208 EKDLDIAG---FTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1284
Cdd:TIGR00606 671 QLTDENQSccpVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1285 RMRQTHSK------EMESRDEEVEEARQSCQKKLKQMEV---------QLEEEYEDKQKALREK-RELESKLSTLS-DQV 1347
Cdd:TIGR00606 748 ELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQaAKLQGSDLDRTvQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1348 NQRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAME-------VEM 1417
Cdd:TIGR00606 828 NQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsTEV 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1418 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED----QEDMNELMKKHKAAVA---------------QASRDMA 1478
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGymkdienkiqdgkddYLKQKET 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1479 QMNDLQAQIEESNKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLasRLKET 1555
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMKQE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1556 MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrKKHELEMDLESLEAANQSL--------QADLK 1627
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAIMK 1133
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1628 LAFKRIGDLQAAIED--------------EMESDENEDLinSLQDMVTKYQKKKNKLEGDSDVD 1677
Cdd:TIGR00606 1134 FHSMKMEEINKIIRDlwrstyrgqdieyiEIRSDADENV--SASDKRRNYNYRVVMLKGDTALD 1195
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
974-1445 |
3.20e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.74 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 974 LEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVME 1053
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1054 ARLI-RAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQRALQQL 1132
Cdd:COG4717 128 LPLYqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL----------SLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1133 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEtqreklqrEKLQREKDMLLAEA-----FSLKQQME 1207
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--------ERLKEARLLLLIAAallalLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1208 EKDLDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL-RLEMEMERM 1286
Cdd:COG4717 270 SLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1287 RQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR--------DFES 1354
Cdd:COG4717 347 EELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleellEALD 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1355 EKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKT 1432
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 1907082239 1433 ALEEQLSRLQREK 1445
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
913-1502 |
3.37e-15 |
|
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: 81.61 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 913 KKRKIQDLAIRCVQKNIKKNKgvkdwpwwKLFTTVRPLIQVQLS-EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL 991
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK--------SLESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 992 ETRISELTSELtderntgESASQLLDaetaerlRTEKEMKELQTQYDALKKQmevmemevmearliRAAEINGEVDDDDA 1071
Cdd:TIGR04523 266 KKQLSEKQKEL-------EQNNKKIK-------ELEKQLNQLKSEISDLNNQ--------------KEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1072 GGEWRL--------KYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKkcqrLTAEL 1143
Cdd:TIGR04523 318 NQEKKLeeiqnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1144 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSL 1223
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1224 EAELQDISSQESKDEASLAKVKKQLrdleakvKDQEEELDeqagsiqMLEQAKLRLEMEMermrqthsKEMESRdeevee 1303
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELK-------KLNEEKKELEEKV--------KDLTKK------ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1304 arqscQKKLKQMEVQLEeeyedkqkalREKRELESKLSTLSDQVNQRDFESEKRLRKD-----------LKRTKALLADA 1372
Cdd:TIGR04523 519 -----ISSLKEKIEKLE----------SEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeieeLKQTQKSLKKK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1373 QIMLDHLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR- 1451
Cdd:TIGR04523 584 QEEKQELIDQ--KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKw 661
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1452 ---------LEEDQEDMNELMKKHK----AAVAQASRDMAQMNDLQaQIEESNKEKQELQEKLQ 1502
Cdd:TIGR04523 662 peiikkikeSKTKIDDIIELMKDWLkelsLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLD 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1159-1639 |
3.52e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1159 ELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQ--DISSQESK 1236
Cdd:COG4717 57 ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1237 DEASLAKVKKQLRDLEAkvkdQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQME 1316
Cdd:COG4717 137 LEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1317 VQLEEEYEDKQKALREKRELESKLSTLSDQvnqrdfesekrlrKDLKRTKALLADAQIMLdhlknnapskrEIAQLKNQL 1396
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-----------ALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1397 EESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1476
Cdd:COG4717 269 LSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1477 MAQMNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFEKTQVKRLENLASRLKETM 1556
Cdd:COG4717 343 LDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1557 EKLTEERDQRAAAENREKEQnkRLQRQLRDTKEEMSELARKEAEASRKKHELEMD--LESLEAANQSLQADLKLAFKRIG 1634
Cdd:COG4717 416 GELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEEWA 493
|
....*
gi 1907082239 1635 DLQAA 1639
Cdd:COG4717 494 ALKLA 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1331-1687 |
5.91e-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: 81.27 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1331 REKRELESKLSTLS--DQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaAAVK 1408
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1409 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM-AQMNDLQAQI 1487
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1488 EESNKEKQELQEKLQ-------ALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFEKTQVKRLENLASRL 1552
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaeidKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1553 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1632
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1633 IGDLQA---AIEDEMESDENEdlinsLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGV 1687
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-----LAEAEAQARASEERVRGGRAVEEVLKASIQGV 523
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
951-1467 |
6.20e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET---------RISELTSELTDERNTGE-------SASQ 1014
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1015 LLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1094
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1095 QELEDKMEVEQQsRRQLERRLGDLQADSDESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1171
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1172 SQAHEETQREKLQREKLQREKDMLlaEAFSLKQQMEEKDLDIAgftQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1250
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA---EQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1251 LEAKVKDQEEELDEQagsiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1326
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1327 QKALREKRELESKLSTLSDQVnqRDFESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAA 1405
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE--KELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1406 AVKARKAMEV-----EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHK 1467
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
951-1297 |
7.59e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.87 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET-------RISELTSELTDERNTGESASQLLDAETAER 1023
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1024 LRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQELEDKME 1102
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1103 VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1182
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1183 LQREKLQREKDMLLaEAFSLKQQMeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1256
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSL-------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082239 1257 --------DQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthSKEMESR 1297
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
957-1438 |
8.88e-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: 80.60 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISEL---TSELTDERNTGESAsqlldaetaeRLRTEKEMKEL 1033
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1034 QTQYDAlkkqmevmemevmearliraaEINGEvddDDAGGEWRLKYERAVREvdftkkrLQQELEDKMEVEQQ---SRRQ 1110
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1111 LERRLGDLQADSDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL 1183
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1184 QREKLQREKDmllaeafslkqqmeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1263
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1264 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKALREKRELESKLST 1342
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1343 LSDQVNQrdfESEKRLR--KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKARKA 1412
Cdd:pfam01576 979 LEEQLEQ---ESRERQAanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAARRK 1055
|
490 500
....*....|....*....|....*.
gi 1907082239 1413 MEVEMEDLHLQIDDIAKAKTALEEQL 1438
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1349-1682 |
1.28e-14 |
|
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: 80.10 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1349 QRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkamevemedlhLQID 1425
Cdd:TIGR02168 172 ERRKETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRE-----------------------LELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1426 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasrdmaqmndlQAQIEESNKEKQELQEKLQALQ 1505
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQEL---------------------EEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1506 SqvEFLEQSmvdkslvsrqeAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLR 1585
Cdd:TIGR02168 288 K--ELYALA-----------NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1586 DTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQK 1665
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
330
....*....|....*..
gi 1907082239 1666 KKNKLEGDSDVDSELED 1682
Cdd:TIGR02168 435 LKELQAELEELEEELEE 451
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1230-1682 |
1.75e-14 |
|
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: 79.29 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1230 ISSQESKD---EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRD-------- 1298
Cdd:TIGR04523 28 ANKQDTEEkqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDkinklnsd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 -----EEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekrlrkDLKRTKALLA 1370
Cdd:TIGR04523 105 lskinSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN------------DLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1371 DAQIMLDHLKNNApsKREIAQLKNQLEESEFTCAAAVKARKamevEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1450
Cdd:TIGR04523 173 NELNLLEKEKLNI--QKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1451 RLEEDQEDMNELMKKHKaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD------KSLVSRQ 1524
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1525 EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLT---EERDQRAAAENRE----KEQNKRLQRQLRDTKEEMSELARK 1597
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsenSEKQRELEEKQNEieklKKENQSYKQEIKNLESQINDLESK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1598 EAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESD-ENEDLINSLQDMVTKYQKKKNKLEGD-SD 1675
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDsVKELIIKNLDNTRESLETQLKVLSRSiNK 479
|
....*..
gi 1907082239 1676 VDSELED 1682
Cdd:TIGR04523 480 IKQNLEQ 486
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1092-1597 |
1.82e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.57 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1092 RLQQELEDKMEVEQQSRRQLERR--LGDLQADSDESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1169
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEETQREKLQREKLQREKDMLLAEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1241
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1242 AKVKKQLR------------------DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKE---------- 1293
Cdd:COG4913 383 AALRAEAAallealeeelealeealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1294 ----MESRDEE-------------------VEEARQSC------QKKLKQmEVQLEEEYEDKQKALREK-------RELE 1337
Cdd:COG4913 463 vgelIEVRPEEerwrgaiervlggfaltllVPPEHYAAalrwvnRLHLRG-RLVYERVRTGLPDPERPRldpdslaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1338 SKLSTLSDQVNQ---RDF-----ESEKRLRKDlkrTKALLADAQImldhlKNNApSKREIaQLKNQLEESEFTCAAAVKA 1409
Cdd:COG4913 542 FKPHPFRAWLEAelgRRFdyvcvDSPEELRRH---PRAITRAGQV-----KGNG-TRHEK-DDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1410 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelmkkhkaaVAQASRDMAQMNDLQAQIEE 1489
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1490 SNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVK----RLENLASRLKETMEKLTEERDQ 1565
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFA 756
|
570 580 590
....*....|....*....|....*....|..
gi 1907082239 1566 RAAAENREKEQNKRLQRQLRDTKEEMSELARK 1597
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
954-1605 |
5.50e-14 |
|
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: 78.09 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 954 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaetaERLRTEKEMKEL 1033
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1034 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELE--DKMEVEQQSRRQL 1111
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1112 ERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQRE 1191
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQLDKAT 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1192 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1265
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1266 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1345
Cdd:pfam02463 693 EILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1346 QVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1425
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1426 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQ 1505
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKE 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1506 SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLEN---LASRLKETMEKLTEERDQRAAAENREKEQN----K 1578
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeELGKVNLMAIEEFEEKEERYNKDELEKERLeeekK 1005
|
650 660
....*....|....*....|....*..
gi 1907082239 1579 RLQRQLRDTKEEMSELARKEAEASRKK 1605
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1386-1602 |
7.52e-14 |
|
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: 75.57 E-value: 7.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1386 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1465
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1466 -------HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1538
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1539 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1602
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
961-1566 |
7.77e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.39 E-value: 7.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 961 RNKDEEIQQLRSKLEkvEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaETAERLrteKEMKELQTQYDAL 1040
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1041 KkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELED---KMEVEQQSRRQLERRLGD 1117
Cdd:PRK02224 257 E------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1118 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmlla 1197
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1198 eafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGSIQ 1270
Cdd:PRK02224 395 ---ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1271 MLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkaLREKRELESKLSTlsdqvNQR 1350
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEELIA-----ERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1351 DFESEKRLRKDLKRTKAlladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-------MEDLHLQ 1423
Cdd:PRK02224 530 ETIEEKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerIRTLLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1424 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEEsnkEKQELQEKLQ 1502
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREERD 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1503 ALQSQVEFLEQSMvdkslvsrqeAKIRELETRLEFEKTQVKRLENL---ASRLKETMEKLTEERDQR 1566
Cdd:PRK02224 678 DLQAEIGAVENEL----------EELEELRERREALENRVEALEALydeAEELESMYGDLRAELRQR 734
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
958-1594 |
3.19e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEEIQQLRSKLEKVEKERNELRLssDRLETRISELTSELTDERntgesasQLLDAETAERLRTEKEMKELQTQY 1037
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1038 DALKKQMevmemevmearliraaeingevddDDAGGEwRLkyERAVREVdftkKRLQQELEDKmeveQQSRRQLERRLGD 1117
Cdd:COG4913 326 DELEAQI------------------------RGNGGD-RL--EQLEREI----ERLERELEER----ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1118 LQADSDESQRALQQLKKKCQRLTAELQDtklHLEGQQVRNHELEKKQRRFDSELSQAHEE----TQREKLQREKLQREKD 1193
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1194 MLlAEAFSLKqqmeEKDLDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQL--RDLEA 1253
Cdd:COG4913 448 AL-AEALGLD----EAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVnrLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1254 KVKDQEEELDEQAGSIQMLEQAKL--RLEMEMERMRQTHSKEMESRD-----EEVEEARQ-------SCQKKL------K 1313
Cdd:COG4913 513 RLVYERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitrAGQVKGngtrheK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1314 QMEVQLEEEY------EDKQKALREKR-ELESKLSTLSDQVNQRdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1386
Cdd:COG4913 593 DDRRRIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1387 REIAQLKNQ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE----DQEDM 1459
Cdd:COG4913 668 REIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1460 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEfek 1539
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWPAETADLDADLESLPEYLALLD--- 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1540 tqvkRLENlaSRLKETMEKLteeRDQRAAAENREKEQ-NKRLQRQLRDTKEEMSEL 1594
Cdd:COG4913 823 ----RLEE--DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1069-1681 |
7.10e-13 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 74.70 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1069 DDAGGEWRLKYERAVREVDFTKKRLQQeledkmeveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTaELQDTKL 1148
Cdd:TIGR01612 1099 DDFGKEENIKYADEINKIKDDIKNLDQ--------------KIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1149 HLEGQQvrnhELEKKQRRFDSELSQA---HEETQreKLQREKLQREKDmllaeafslKQQMEE-KDLDIAgFTQKVVSLE 1224
Cdd:TIGR01612 1164 SNDDPE----EIEKKIENIVTKIDKKkniYDEIK--KLLNEIAEIEKD---------KTSLEEvKGINLS-YGKNLGKLF 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1225 aeLQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGsIQMLEQAklrlemEMERMRQTHSKEM------ESRD 1298
Cdd:TIGR01612 1228 --LEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMG-IEMDIKA------EMETFNISHDDDKdhhiisKKHD 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVEEARQscqKKLKQMEVQLEE-EYEDKQKAL--------REKRELESKLSTLSDQVNQRDFESEKRLRKDLKR-TKAL 1368
Cdd:TIGR01612 1298 ENISDIRE---KSLKIIEDFSEEsDINDIKKELqknlldaqKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEyTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1369 LADAQIMLDHLKNnapSKREIAQLKNQLeeSEFTCAAAVKArkamEVEMEDLHLQIDDIAKAKTALEEQLSRLQ------ 1442
Cdd:TIGR01612 1375 EENNKNIKDELDK---SEKLIKKIKDDI--NLEECKSKIES----TLDDKDIDECIKKIKELKNHILSEESNIDtyfkna 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1443 REKNE----IQNRLEEDQEDMNELMKKHKAavaQASRDMA-QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvd 1517
Cdd:TIGR01612 1446 DENNEnvllLFKNIEMADNKSQHILKIKKD---NATNDHDfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY--- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1518 KSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEErdqraaAENREKEQNKRLQRQLRDTKEemselARK 1597
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKDAHKKFILE------AEKSEQKIKEIKKEKFRIEDD-----AAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1598 EAEASRKKHELEMDLESLEaaNQSLQ-ADLKlafKRIGDLQAAIED-------------EMESDENEDLINSLQDMVTKY 1663
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFE--NKFLKiSDIK---KKINDCLKETESiekkissfsidsqDTELKENGDNLNSLQEFLESL 1662
|
650 660
....*....|....*....|..
gi 1907082239 1664 QKKKNKLEGDS----DVDSELE 1681
Cdd:TIGR01612 1663 KDQKKNIEDKKkeldELDSEIE 1684
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1107-1672 |
7.76e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.18 E-value: 7.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1107 SRRQLERRLGDLQADSDESQRALQqlkkkcQRLTAelqdtKLHLEGQQ--------------------VRNHELEKKQ-- 1164
Cdd:COG4913 156 DIRALKARLKKQGVEFFDSFSAYL------ARLRR-----RLGIGSEKalrllhktqsfkpigdlddfVREYMLEEPDtf 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 RRFDS------ELSQAHEETQREKLQREKLQREKDmlLAEAF-SLKQQMEEKDLDIAGFTQKVVSLEAELQdissqeskd 1237
Cdd:COG4913 225 EAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRLELL--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1238 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL--------RLEMEMERMRQTHskemesrdEEVEEARQSCQ 1309
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL--------EERERRRARLE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1310 KKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQImLDHLKNNAPskREI 1389
Cdd:COG4913 366 ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LERRKSNIP--ARL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1390 AQLKNQLEEseftcAAAVKARKA------MEVEMED--------------------------------------LHLQID 1425
Cdd:COG4913 443 LALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwvnrlhlrGRLVYE 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1426 DI------AKAKTALEEQLSR-LQREKNEIQNRLE------------EDQEDmnelMKKHKAAVAQA-----SRDMAQMN 1481
Cdd:COG4913 518 RVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEE----LRRHPRAITRAgqvkgNGTRHEKD 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1482 DL-------------QAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRleFEKTQVKRLENL 1548
Cdd:COG4913 594 DRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS--WDEIDVASAERE 669
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1549 ASRLKETMEKLTEERDQRAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA-ANQSLQA 1624
Cdd:COG4913 670 IAELEAELERLDASSDDLAALEEQLEELEAEleeLEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlARLELRA 749
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907082239 1625 DLKLAFkrigdlQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEG 1672
Cdd:COG4913 750 LLEERF------AAALGDAVERELRENLEERIDALRARLNRAEEELER 791
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1270-1671 |
8.17e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 73.65 E-value: 8.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1270 QMLEQaklRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1349
Cdd:COG4717 45 AMLLE---RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1350 -RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS----KREIAQLKNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQ 1423
Cdd:COG4717 121 lEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1424 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK-----------AAVA--------------------- 1471
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1472 ---------------QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQ----SQVEFLEQSMVDKSLVSRQEAKIRELE 1532
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1533 TRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrkkhELEMDL 1612
Cdd:COG4717 361 EELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1613 ESLEAANQSLQADLKLAFKRIGDLQAAIEdEMESDEnedlinSLQDMVTKYQKKKNKLE 1671
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELE-QLEEDG------ELAELLQELEELKAELR 486
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1428-1632 |
8.61e-13 |
|
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: 72.49 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1428 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1507
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1508 VEFLEQSMVD--------------KSLVSRQEAK-----IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAA 1568
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1569 AENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1632
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1171-1373 |
8.61e-13 |
|
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: 72.49 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1171 LSQAHEETQREKlQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1250
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1251 LEAKVKDQEEELDEQAGSIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1323
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1324 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQ 1373
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1130-1663 |
1.72e-12 |
|
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: 73.08 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1130 QQLKKKCQRLTAELQDTKLHLEGQQVRNHElekKQRRFDSELSQAHEETQREKLQREKLQREkDMLLAEAFSLKQQMEEK 1209
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1210 DLDIAGFT--QKVVSLEAELQDISSQESK---DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1284
Cdd:TIGR00618 266 RARIEELRaqEAVLEETQERINRARKAAPlaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1285 RMRQTHSKEMESRDE-EVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE--SEKRLRKD 1361
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1362 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaaAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1441
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1442 QREKNE-----------------IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQAL 1504
Cdd:TIGR00618 503 PCPLCGscihpnparqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1505 QSQVEFLEQSMVD------------KSLVSRQEAKIRELETRLE------FEKTQVKRLENLASRLKETMEKLTEERDQR 1566
Cdd:TIGR00618 583 KEDIPNLQNITVRlqdlteklseaeDMLACEQHALLRKLQPEQDlqdvrlHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1567 AAAENREKEQNKRLQRQLRDTKEE-------------------MSELARKEAEASRKKHELEMDLESLEaanQSLQADLK 1627
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQsekeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLG---SDLAARED 739
|
570 580 590
....*....|....*....|....*....|....*.
gi 1907082239 1628 LAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1663
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1280-1620 |
2.18e-12 |
|
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: 72.46 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1280 EMEMERMRQTH---SKEMESRD--EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTlsDQVNQRDFES 1354
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1355 EKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiakaktA 1433
Cdd:pfam17380 373 EISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE------A 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1434 LEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdmaQMNDLQAQIEESNKEKQELqEKLQALQSQVEFLEQ 1513
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1514 SMVDKSLVSRQEAKIRELETRLEFEKtqvkrlenlasRLKETMEKLTEERDQRAAAENREKEQN----KRLQRQLRDTKE 1589
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|...
gi 1907082239 1590 EMSEL--ARKEAEASRKKHELEMDLESLEAANQ 1620
Cdd:pfam17380 564 ERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1080-1618 |
4.09e-12 |
|
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: 72.18 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1080 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL----GDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQV 1155
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHG---AFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1156 RNHELEKKQRRFDSeLSQAHEETQREKLQREKL--QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1233
Cdd:pfam12128 352 WQSELENLEERLKA-LTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1234 eSKDEASLAKVKKQLRDLEAKVK-----DQEEELDEQAGSIQMLEQAKLRLEM---EMERMrQTHSKEMESRDEEVEEAR 1305
Cdd:pfam12128 431 -GKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAanaEVERL-QSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1306 QSCQKKLKQMEVQLEE-------------EYEDKQKALREK---RELESKLSTLSDQVNQRDFESEKR------LRKDLK 1363
Cdd:pfam12128 509 RQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSVGGelnlygVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1364 RTKALladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakAKTALEEQLSRLQR 1443
Cdd:pfam12128 589 RIDVP--------EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1444 EKNEIQNrleeDQEDMNELMKKHKAAVAQASRDMAQ-----MNDLQAQIEESNKEKQELQ-EKLQALQSQVEFLEQSM-- 1515
Cdd:pfam12128 658 LFDEKQS----EKDKKNKALAERKDSANERLNSLEAqlkqlDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLal 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1516 VDKSLVSRQEAKIRELETRLEFEKTQVKRL---ENLASRLKETMEKLTE-----ERDQRAAAENRE------KEQNKRLQ 1581
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERkieriAVRRQEVLRYFDwyqetwLQRRPRLA 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1907082239 1582 RQLRDTKEEMSE----LARKEAEASRKKHELEMDLESLEAA 1618
Cdd:pfam12128 814 TQLSNIERAISElqqqLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1716 |
4.17e-12 |
|
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: 71.59 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1287 RQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTK 1366
Cdd:TIGR04523 31 QDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK-LNSDLSKIN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1367 AlladaQIMLD-HLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREK 1445
Cdd:TIGR04523 110 S-----EIKNDkEQKNK--LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1446 NEIQN----------RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSm 1515
Cdd:TIGR04523 183 LNIQKnidkiknkllKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1516 vDKSLVSRQEAKIRELETrlefEKTQVKRLENLASRLKETMEKLteerdqraaaeNREKEQN--KRLQRQLRDTKEEMSE 1593
Cdd:TIGR04523 262 -QNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQLKSEISDL-----------NNQKEQDwnKELKSELKNQEKKLEE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1594 LarkeaeasrkkhelemdlesleaanqslqadlklafkrigdlqaaiedEMESDENEDLINSLQDMVTKYQKKKNKLEGD 1673
Cdd:TIGR04523 326 I------------------------------------------------QNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1907082239 1674 -SDVDSELEDRVDGVKSWLSKNKGPSKAPSddgSLKSSRTALNS 1716
Cdd:TIGR04523 358 nSEKQRELEEKQNEIEKLKKENQSYKQEIK---NLESQINDLES 398
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1077-1629 |
4.86e-12 |
|
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: 71.39 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1077 LKYERAVREVDFTKKRLqqeLEDKMEVEQQSRRQLERRLGDLQaDSDESQRALQQL----KKKCQRLTAELQDTKLHLEG 1152
Cdd:pfam10174 41 LKKERALRKEEAARISV---LKEQYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1153 QQVRNHELEKKQRRFDSELSQAHEE------TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLD--IAGFTQKVVS 1222
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1223 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1302
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1303 --EARQSCQKKLKQMEVQLEEEYEDKQKalrEKRELESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLK 1380
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1381 NNAPSKREIAQLKNQ----LEESEFTCAAA---------VKARKAMEVE--MEDLHLQIDDIAKAKTALEEQLSRLQREK 1445
Cdd:pfam10174 352 LRLEEKESFLNKKTKqlqdLTEEKSTLAGEirdlkdmldVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1446 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-----KSL 1520
Cdd:pfam10174 432 SNTDTALTTLEEALSEKERIIERLKEQREREDRERLE---ELESLKKENKDLKEKVSALQPELTEKESSLIDlkehaSSL 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1521 VSR---QEAKIRELETRLEFEKTQVKRLENLASRLKETmeklteERDQRAAAENREKEQNkrLQRqlrdtkeemsELARK 1597
Cdd:pfam10174 509 ASSglkKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA------EEAVRTNPEINDRIRL--LEQ----------EVARY 570
|
570 580 590
....*....|....*....|....*....|...
gi 1907082239 1598 EAEASRKKHELEMDLESL-EAANQSLQADLKLA 1629
Cdd:pfam10174 571 KEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1222-1696 |
5.76e-12 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 71.47 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1222 SLEAELQDISSQESKDEAS---LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMermrqthsKEMESRD 1298
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVeearqscqkklKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkDLKRTKALLADAQIMLDH 1378
Cdd:PRK01156 249 DMK-----------NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1379 LKNNAPSKREIAQLKNQLEE--SEFTcaaavkarkAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1456
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKdyNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1457 EDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM-----------------VDKS 1519
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1520 L---------VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENRekeQNKRLQRQLRDTKEE 1590
Cdd:PRK01156 468 NhiinhynekKSRLEEKIREIE-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIK 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1591 MSELARKEAEASRKKHELE-MDLESLEA------------------ANQSLQADLKLAFKRIGDLQAAIEDEMESDE--N 1649
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKsLKLEDLDSkrtswlnalavislidieTNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyI 617
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907082239 1650 EDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKG 1696
Cdd:PRK01156 618 DKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS 664
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
952-1532 |
1.94e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 69.76 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGEsasqlLDAETAERLRTEKE-M 1030
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QELEDKMEVEQQS 1107
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1108 RRQLERRLGDLQADS-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1169
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---------------------AELQ 1228
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1229 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGSIQMLEQAKLRLEM-------EMERMRQTHSKEM 1294
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1295 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLAD 1371
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1372 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1445
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1446 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmnDLQAQ-IEESNKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1521
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 1907082239 1522 SRQEAKIRELE 1532
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1334-1597 |
2.23e-11 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 68.89 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1334 RELESKLSTLSDQVN--------QRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseftca 1404
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqqqiktYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN------ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1405 aavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdmaQ 1479
Cdd:PHA02562 246 --------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD----------K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1480 MNDLQAQIEESNKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKL 1559
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907082239 1560 TEERDQRaaaenreKEQNKRLQRQLRDTKEEMSELARK 1597
Cdd:PHA02562 371 QAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1105-1329 |
2.87e-11 |
|
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: 67.87 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1105 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1184
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKLQREKDMLLAEAFSLKQQMEEKDL-DIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELD 1263
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLlSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1264 EQAGSIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKA 1329
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1415-1576 |
3.02e-11 |
|
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: 65.72 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1415 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDMAQMNDLQAQIeESN 1491
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1492 KEkqelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1571
Cdd:COG1579 89 KE-------YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 1907082239 1572 REKEQ 1576
Cdd:COG1579 156 AELEE 160
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1431-1639 |
3.55e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.55 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1431 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL--QALQSQV 1508
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1509 EFLEQSMVDKSLVSRQeakIRELETRLEFektqvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTK 1588
Cdd:COG3883 98 SGGSVSYLDVLLGSES---FSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1589 EEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA 1639
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
949-1595 |
4.03e-11 |
|
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: 68.71 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 949 PLIQVQLSeeqirNKDEEIQQLRSKLEKVEKERNELRLSSD-RLETRISELTSELTDERntgesasqlldaETAERLRTE 1027
Cdd:pfam12128 350 PSWQSELE-----NLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR------------EARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1028 KEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDftkkRLQQELEDKMEve 1104
Cdd:pfam12128 413 AE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANA-- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1105 QQSRRQLERRLgdLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdselSQAHEETQREKLQ 1184
Cdd:pfam12128 486 EVERLQSELRQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKLQREKDMLLAEAFSLKQQ-------MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1257
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1258 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR--- 1334
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtek 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1335 --ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHL----KNNAPSKREIAQLKNQLEESEFTCAAAVK 1408
Cdd:pfam12128 717 qaYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1409 ARKAME----VEMEDLHLQIDDIAKAKTALEEQLSRLQ------REKNEIQNRLEEDQED-MNELMKKHKAAVAQASRDM 1477
Cdd:pfam12128 797 YFDWYQetwlQRRPRLATQLSNIERAISELQQQLARLIadtklrRAKLEMERKASEKQQVrLSENLRGLRCEMSKLATLK 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1478 AQMNDLQAQ--IEESNKEKQELQEKLQ----ALQSQVEFLEQSMVDKS---------LVSRQEAKIRELETRLEFEKTQV 1542
Cdd:pfam12128 877 EDANSEQAQgsIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSgsglaetweSLREEDHYQNDKGIRLLDYRKLV 956
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1543 KRLENLASRLKETMEKLTEER------------DQRAAAENREKEQNKRLQRQLRDTK--EEMSELA 1595
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQvsilgvdltefyDVLADFDRRIASFSRELQREVGEEAffEGVSESA 1023
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
965-1282 |
4.16e-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: 68.56 E-value: 4.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 965 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTD-ERNTGE---SASQLLDAETAERLRTEKEMKELQTQYDAL 1040
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGEiekEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1041 -----KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRlKYERAVREVDFTKKRLQ----------QELEDKMEVEQ 1105
Cdd:TIGR02169 754 envksELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP-EIQAELSKLEEEVSRIEarlreieqklNRLTLEKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1106 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQR 1185
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1186 EKLQREKDMLLAEAFSLKQQMEE-------------KDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1252
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELK 992
|
330 340 350
....*....|....*....|....*....|
gi 1907082239 1253 AKVKDQEEELDEQAGSIQMLEQAKLRLEME 1282
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
965-1182 |
4.39e-11 |
|
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: 67.10 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 965 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQm 1044
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1045 eVMEMEVMEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDftKKRLQQELEDKMEVEQQSRRQLERR-- 1114
Cdd:COG4942 99 -LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALRAELEAERae 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1115 LGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1182
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
958-1453 |
5.59e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.14 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntGESASQLLDAETAERLRTEKEMKELQTQy 1037
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1038 DALKKQMevmemevmearlIRAAEINGEVddddaggewrlkyERAVREVDftkkrlqqELEDKMEVEQQSRRQLERRLGD 1117
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1118 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEetqREKLQREKLQREKDMlLA 1197
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1198 EAFSLK---------QQMEEKDL--DIAGFTQKVVSLEAELQDISSQESKDEA------SLAKVKKQLRDLEAKVK---- 1256
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdlee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1257 ---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------E 1321
Cdd:PRK02224 524 liaERRETIEEKRERAEELRERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1322 EYEDKQKALREKRElesKLSTLSDQvnQRDFESEKRLRKDlkrtkalladaqimldhlknnapskreiaQLKNQLEESEF 1401
Cdd:PRK02224 603 DAEDEIERLREKRE---ALAELNDE--RRERLAEKRERKR-----------------------------ELEAEFDEARI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1402 TCAAAVKARKA-----MEVEMEDLHLQIDDIAKAKTALE---EQLSRLQREKNEIQNRLE 1453
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVE 708
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
954-1395 |
6.70e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 67.84 E-value: 6.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 954 QLSEEQiRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1025
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1026 TEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1105
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1106 QSRRQLERRLGDLQADSDESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNHelekkqrrfdSELSQAHEET----Q 1179
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIENM----------TQLVGQHGRTagamQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1180 REKLQREKLQREKDMLLAEAFSLKqqmEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1259
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1260 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1308
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1309 QKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1388
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
....*..
gi 1907082239 1389 IAQLKNQ 1395
Cdd:pfam15921 826 IIQRQEQ 832
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
958-1574 |
6.74e-11 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 68.15 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEE-IQQLRSKLEKVEKERNELRLSSD--RLETRISELTSELTDERNTGESASQLLDaETAErlrTEKEmkelQ 1034
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1035 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQELEDKMEVEQQSRRQLEr 1113
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1114 rLGDLQADSDESQRALQQLKKKcqrltaELQDtklhlegqqVRNHELEKKQRRF-DSELSQAHEETQREKLQREKLQREK 1192
Cdd:TIGR01612 1278 -TFNISHDDDKDHHIISKKHDE------NISD---------IREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1193 DMLLAEAFSLKQQMEEKDL-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1265
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1266 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1338
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1339 KLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARKAMEV 1415
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1416 EMEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESn 1491
Cdd:TIGR01612 1575 KKEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDT- 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1492 kekqELQEKLQALQSQVEFLEqSMVDkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1571
Cdd:TIGR01612 1644 ----ELKENGDNLNSLQEFLE-SLKD------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
...
gi 1907082239 1572 REK 1574
Cdd:TIGR01612 1713 KEE 1715
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1101-1688 |
8.46e-11 |
|
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: 67.56 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1101 MEVEQQSRRQLERRLGDLQADsDESQRALQQLKKkcQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQA 1174
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILED-DGVVPPKSRLNR--QQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1175 HEETQREKLQREKLQREKDMLLAEafslkqqmeekdldiagFTQKVVSLEAELQdissqESKDEASLakvkkQLRDLEAK 1254
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQETSAE-----------------LNQLLRTLDDQWK-----EKRDELNG-----ELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1255 VKDQEEEL---DEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEE-------YE 1324
Cdd:pfam12128 317 VAKDRSELealEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiagIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 DKQKALREKRE------------LESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqL 1392
Cdd:pfam12128 397 DKLAKIREARDrqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE--------------L 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1393 KNQLEESEFTCAAAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1472
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1473 ASRDMAQMNDLQAQIEESNK-EKQELQEKLQALQSQVEF--------LEQSMVDKSLVSRQEAKIR--ELETRLEFEKTQ 1541
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELnlygvkldLKRIDVPEWAASEEELRERldKAEEALQSAREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1542 VKRLENLASRLKETMEKLT-EERDQRAAAENREKEQnKRL---QRQLRDTKEEMSELARKEAEASRKK--HELEMDLESL 1615
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRLfdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKH 698
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1616 EAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINslQDMVTKYQKKKNKLEG-DSDVDSELEDR-VDGVK 1688
Cdd:pfam12128 699 QAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLK--AAIAARRSGAKAELKAlETWYKRDLASLgVDPDV 769
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1219-1625 |
1.28e-10 |
|
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: 66.69 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1219 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgsiqmleQAKLRLEMEMERMRQTHSKEMESRD 1298
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVEEARQsCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFEsekrlrkdLKRTKALLADAQIMLDH 1378
Cdd:pfam05557 73 EQAELNRL-KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1379 LKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--------RLQREKNEIQN 1450
Cdd:pfam05557 144 LKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipelekelERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1451 RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ----------ALQSQVEFLEQSmvDKSL 1520
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQR--EIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1521 VSRQ-----------------EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD-QRAAAENREKEQN-KRLQ 1581
Cdd:pfam05557 296 KEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELTmSNYS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907082239 1582 RQLRDTKEEMSELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1625
Cdd:pfam05557 376 PQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1150-1536 |
1.33e-10 |
|
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: 66.07 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1150 LEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREkdmllaeafsLKQQMEEKDLDIAGFTQKVVSLEAELQD 1229
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----------LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1230 ISsqeskdeASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScQ 1309
Cdd:pfam07888 106 LS-------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-Q 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1310 KKLKQMEVQLeeeyedkqkalrekRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREI 1389
Cdd:pfam07888 178 AKLQQTEEEL--------------RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1390 AQLKNQLEESEFTCAA-------AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1458
Cdd:pfam07888 240 RSLQERLNASERKVEGlgeelssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1459 M----NELMKKHKAAVAQASR------DMAQMNDL-QAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE-- 1525
Cdd:pfam07888 320 IeklsAELQRLEERLQEERMEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEll 391
|
410
....*....|.
gi 1907082239 1526 AKIRELETRLE 1536
Cdd:pfam07888 392 EYIRQLEQRLE 402
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1423-1689 |
2.93e-10 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 65.42 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1423 QIDDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQAQIEESNKEKQELQEKL 1501
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1502 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeKTQVKRLENLASRLKE------TMEKLTEERDQRAAAENREKE 1575
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1576 QNKRLqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDemESDENEDLINS 1655
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD--NAEELAKLQDE 387
|
250 260 270
....*....|....*....|....*....|....
gi 1907082239 1656 LQDMVTKYQKKKNKLEGDSDVDSELEDrvDGVKS 1689
Cdd:PHA02562 388 LDKIVKTKSELVKEKYHRGIVTDLLKD--SGIKA 419
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
939-1370 |
3.02e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 3.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 939 PWWKLFTTVRPLiQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDA 1018
Cdd:PRK03918 359 ERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---KAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1019 E----TAERLRTEKEMKELQTQYDA-LKKQMEVMEMEVMEARLIRAAEIngEVDDDDAGGEWRLKYERAVREVDFTKKRL 1093
Cdd:PRK03918 435 KgkcpVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELR--ELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1094 QQELEDKMEVEQQSRRQLERRLGDLQADS---DESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSE 1170
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELA-------ELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1171 LSQAHEETQREklqREKLQREkdmlLAEAFSLKQQMEEKDldiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1250
Cdd:PRK03918 586 SVEELEERLKE---LEPFYNE----YLELKDAEKELEREE-------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1251 LEAKVKDQEEEldeqagsiqMLEQAKLRLEMEMERMRqthskemeSRDEEVEEARQSCQKKLKqmevQLEEEYEDKQKAL 1330
Cdd:PRK03918 652 LEKKYSEEEYE---------ELREEYLELSRELAGLR--------AELEELEKRREEIKKTLE----KLKEELEEREKAK 710
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082239 1331 REKRELESKLSTLsdqvnqrdfeseKRLRKDLKRTKALLA 1370
Cdd:PRK03918 711 KELEKLEKALERV------------EELREKVKKYKALLK 738
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
955-1503 |
3.39e-10 |
|
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: 65.15 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 955 LSEEQIRNKDEEIQQLRSKLEKVEKERNElrlsSDRLETRISELTSELTDErnTGESASQLLDAETAERlRTEKEMKELQ 1034
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADAREVISCLKNE--LSELRRQIQRAELELQ-STNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1035 TQYDALKKqmevmemevmearliRAAEINGEVDDDDAGGEWRLKYERAVREVDFtkkRLQQELEDKMEVEQQSRRQLerR 1114
Cdd:pfam05557 139 ERLDLLKA---------------KASEAEQLRQNLEKQQSSLAEAEQRIKELEF---EIQSQEQDSEIVKNSKSELA--R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1115 LGDLQadsdesqRALQQLKKKCQRLTaELQDTKLHLEGQQvrnHELEKKQRRfdselsqahEETQREKLQreKLQREKDM 1194
Cdd:pfam05557 199 IPELE-------KELERLREHNKHLN-ENIENKLLLKEEV---EDLKRKLER---------EEKYREEAA--TLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1195 LLAEAFSLKQQMEEKDLDIA---GFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK-------DQEEELDE 1264
Cdd:pfam05557 257 LEQELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1265 QAGSIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALRE 1332
Cdd:pfam05557 337 HKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLS-------VAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1333 KRELESKLSTLSDQVnqrdfesekrlrkDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLEESEFTCAAAVKARKA 1412
Cdd:pfam05557 410 LGGYKQQAQTLEREL-------------QALRQQESLADP----------SYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1413 MEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRdma 1478
Cdd:pfam05557 467 LEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK--- 543
|
570 580
....*....|....*....|....*
gi 1907082239 1479 QMNDLQAQIEESNKEKQELQEKLQA 1503
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1417-1671 |
4.87e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 63.01 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1417 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE 1496
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1497 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFE-KTQVKRLEN---LASRLKETMEKLteerdQRAAAENR 1572
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEEekeLVEKIKELEKEL-----EKAKKALE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1573 EKEQNKRLQRQLRDTKEEMSELARKEAEASRK--KHELEMDlESLEAANQsLQADLKLAFKRIGDLQAAIEDEMES-DEN 1649
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEaqELHEEMI-ELYKEADE-LRKEADELHKEIVEAQEKADELHEEiIEL 235
|
250 260
....*....|....*....|..
gi 1907082239 1650 EDLINSLQDMVTKYQKKKNKLE 1671
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1299-1524 |
5.02e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDH 1378
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1379 LKNNAPSKREIAQLKNQLEESEF-----TCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ---N 1450
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEallA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1451 RLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1524
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1296-1663 |
5.21e-10 |
|
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: 65.20 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1296 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIM 1375
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1376 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1434
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1435 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE--------------LQE 1499
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1500 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQ----VKRLENLASRLKETMEKLTEERDQRAAAEnreke 1575
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1576 qnkrlqRQLRDTKEEMSELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDENEdlins 1655
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHEAQ----- 346
|
....*...
gi 1907082239 1656 LQDMVTKY 1663
Cdd:pfam01576 347 LQEMRQKH 354
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1077-1671 |
5.75e-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: 65.07 E-value: 5.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1077 LKYERAVREVDFTKKRLQQ---ELEDKME-VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQdtklhLEG 1152
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1153 QQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS 1232
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1233 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKL 1312
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1313 KQMEVQLEEeyedkqkalrEKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1392
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1393 ------KNQLEEsefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL------EEDQEDMN 1460
Cdd:TIGR00606 566 lgyfpnKKQLED---WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1461 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ-ALQSQVEFLEqsmvdksLVSRQEAKIRELETRLEFEK 1539
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQE-------FISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1540 TQVKRLENlasRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMDLESLEA 1617
Cdd:TIGR00606 716 SELKKKEK---RRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDVT 792
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1618 ANQSLQADLKlafkrigDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLE 1671
Cdd:TIGR00606 793 IMERFQMELK-------DVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELD 839
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1272-1679 |
5.81e-10 |
|
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: 64.38 E-value: 5.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1272 LEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELesklstlsdqvNQRD 1351
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR-LLEKREAEAEEALREQAEL-----------NRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1352 FESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAK 1431
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKN------ELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1432 TALEEQLSRLQREKNEIQNrLE---EDQEDMNELMKKHKAAVAQasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1508
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKE-LEfeiQSQEQDSEIVKNSKSELAR----IPELEKELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1509 EFLEQSMvdkslvSRQE---AKIRELETRLEFEKTQVKRLENLASRLKETM---EKLTEERDQRAAAENREKEQNKRLQR 1582
Cdd:pfam05557 231 EDLKRKL------EREEkyrEEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1583 QLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE---DEME----SDENEDLINS 1655
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsydKELTmsnySPQLLERIEE 384
|
410 420
....*....|....*....|....
gi 1907082239 1656 LQDMVTKYQKKKNKLEGDSDVDSE 1679
Cdd:pfam05557 385 AEDMTQKMQAHNEEMEAQLSVAEE 408
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
952-1230 |
6.31e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE-----TAERLRT 1026
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1027 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmeveQQ 1106
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEL----EA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1107 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQrEKLQRE 1186
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLE 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1187 KLQREKDMLLAEAFSLK-------QQMEEKDLDIAGFTQKVVSLEAELQDI 1230
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1418-1623 |
9.74e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.88 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1418 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdmaQMNDLQAQIEESNKEKQEL 1497
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1498 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFEKTQV-----------KRLENLASRLKETM 1556
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1557 EKLTEE-RDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1623
Cdd:COG3206 312 QRILASlEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1169-1557 |
1.64e-09 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 62.93 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1169 SELSQAHEETQREKLQREKLQRE--KDmLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---LEAE--LQDISSQE 1234
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1235 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1306
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1307 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLR-------KDLKRTKALLADAQIM---- 1375
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqy 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1376 LDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE-- 1453
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEks 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1454 ------EDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM----------- 1515
Cdd:PRK04778 438 nlpglpEDYLEMFFEVSDEiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQLIqyanryrsdne 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 1516 -VDKSLVS--------RQEAKIRELETRLE-FEKTQVKRLENLASRLKETME 1557
Cdd:PRK04778 518 eVAEALNEaerlfreyDYKAALEIIATALEkVEPGVTKRIEDSYEKEKETIR 569
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1232-1671 |
1.67e-09 |
|
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: 63.45 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1232 SQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEmeSRDEEVEEARQSCQ 1309
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL--TQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1310 KKLKQMEVQLEE------EYEDKQKALREKRELEsKLSTLSDQVNQRDFESEkRLRKDLKRTKALLADAQIMLDHLKNNA 1383
Cdd:TIGR00618 260 QLLKQLRARIEElraqeaVLEETQERINRARKAA-PLAAHIKAVTQIEQQAQ-RIHTELQSKMRSRAKLLMKRAAHVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1384 PSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAKAKTALEEQ-------LSRLQREKNEIQNRL 1452
Cdd:TIGR00618 338 SSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQQKTTLTQKlqslckeLDILQREQATIDTRT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1453 EEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdKSLVSRQEAKIRELE 1532
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTK---EQIHLQETRKKAVVL 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1533 TRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDL 1612
Cdd:TIGR00618 494 ARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1613 ESLEAANQSLQADLKLAFKRIGDLQAAIedEMESDENEDLINSLQDMVTKYQKKKNKLE 1671
Cdd:TIGR00618 573 SILTQCDNRSKEDIPNLQNITVRLQDLT--EKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1185-1715 |
2.42e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 62.61 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKLQREKDmllaEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLakvkKQLRDLEAKVKDQEEELDE 1264
Cdd:PRK01156 189 EEKLKSSNL----ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL----NELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1265 QAGSIQMLEQAKLRL-EMEMERMRQTHSKEMESRDEEVEEARQSCQ-KKLKQMEVQLEEEYEDKQKALREKRELESKLSt 1342
Cdd:PRK01156 261 AESDLSMELEKNNYYkELEERHMKIINDPVYKNRNYINDYFKYKNDiENKKQILSNIDAEINKYHAIIKKLSVLQKDYN- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1343 lsdqvnqrDFESEKRLRKDLKRTKALLADaqimlDHLKNNApSKREIAQLKNQLEE----SEFTCAAAVKARKAMEVEME 1418
Cdd:PRK01156 340 --------DYIKKKSRYDDLNNQILELEG-----YEMDYNS-YLKSIESLKKKIEEysknIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1419 DLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLqaqIEESNKEKQELQ 1498
Cdd:PRK01156 406 AIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHI---INHYNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1499 EKLQALQSQVEFLEQSMVD-KSLVSRQEA-KIRELET---RLEFEKTQVKRLENLASRLKETMEKLT-----------EE 1562
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDlKKRKEYLESeEINKSINeynKIESARADLEDIKIKINELKDKHDKYEeiknrykslklED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1563 RDQR----------------AAAENREKEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMD--------LESLE 1616
Cdd:PRK01156 563 LDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSyiDKSIREIENEANnlnnkyneIQENK 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1617 AANQSLQADLKLAFKRIGDLQAAIEDEME-----SDENEDLINS---LQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVK 1688
Cdd:PRK01156 643 ILIEKLRGKIDNYKKQIAEIDSIIPDLKEitsriNDIEDNLKKSrkaLDDAKANRARLESTIEILRTRINELSDRINDIN 722
|
570 580
....*....|....*....|....*..
gi 1907082239 1689 SWLSKNKGPSKAPSDdgsLKSSRTALN 1715
Cdd:PRK01156 723 ETLESMKKIKKAIGD---LKRLREAFD 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
957-1402 |
4.48e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKD-EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDE-----------RNTGESASQLLDAETAERL 1024
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1025 RTEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1077
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1078 ---------KYERAVRE----------VDFTKKRLQQELEDKMEVEQQS----------------RRQLERRLGDLQADS 1122
Cdd:COG4913 487 faltllvppEHYAAALRwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1123 desqraLQQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEETQREKLQR 1185
Cdd:COG4913 567 ------PEELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1186 EKLQRekdmlLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1265
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1266 AGSIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKALREKRE-LESKLSTLS 1344
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1345 DQVN------QRDFESEKRlrkDLKRTKALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT 1402
Cdd:COG4913 787 EELEramrafNREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVA 849
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1081-1629 |
4.83e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 61.90 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1081 RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERR--LGDLQADSDES----QRALQQLKKKCQRLTA------ELQDTKL 1148
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERrmalRQQLEQLQARIQRLAArapawlAAQDALA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1149 HLEGQQvrNHELEKKQRRfdSELSQAHEETQRE-KLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKV--VSLEA 1225
Cdd:PRK04863 614 RLREQS--GEEFEDSQDV--TEYMQQLLERERElTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFggVLLSE 689
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1226 ELQDISSQESKD-EASLAKVKKQL--RDLEAkVKDQEEELDEQAGSIQMLEQAKLRL--------EMEMERMRQTHSKEM 1294
Cdd:PRK04863 690 IYDDVSLEDAPYfSALYGPARHAIvvPDLSD-AAEQLAGLEDCPEDLYLIEGDPDSFddsvfsveELEKAVVVKIADRQW 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1295 E-SRDEEV----EEARQscqKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR-------DFESE-KRLRKD 1361
Cdd:PRK04863 769 RySRFPEVplfgRAARE---KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeaDPEAElRQLNRR 845
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1362 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcaAAVKARKAMEVEMEDLHLQIDDIAKAK---------- 1431
Cdd:PRK04863 846 RVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR-----LNLLADETLADRVEEIREQLDEAEEAKrfvqqhgnal 920
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1432 TALEEQLSRLQREKNEI---QNRLEEDQEDMNELMKKHKA-----------AVAQASRDMAQMNDLQAQIEESNKEKQEL 1497
Cdd:PRK04863 921 AQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFAltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQE 1000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1498 QEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFEKtqvkRLENLASRLKETME-KLTEERDQRAAAENREK 1574
Cdd:PRK04863 1001 RTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLSANR 1073
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1575 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1629
Cdd:PRK04863 1074 SRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
957-1499 |
4.84e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.84 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIS-------ELTSELTDERNTGESASQLL---DAETAERLRT 1026
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdpvyknrNYINDYFKYKNDIENKKQILsniDAEINKYHAI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1027 EKEMKELQTQYDALKKQMEvmemevmearliRAAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1106
Cdd:PRK01156 328 IKKLSVLQKDYNDYIKKKS------------RYDDLNNQILELE---GYEMDYNSYLKSIESLKKKIEEYSKNIERMSAF 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1107 SRRQLERRLGD---LQADSDESQRALQQLKKKCQRLTA----------ELQDTKLHLEGQQV----RNHELEKKQRR--- 1166
Cdd:PRK01156 393 ISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEMLNGQSVcpvcGTTLGEEKSNHiin 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1167 -FDSELSQAHEETQREKLQREKLQREKDMLLaeafSLKQQMEEKDLD-IAGFTQKVVSLEAELQDissqeskDEASLAKV 1244
Cdd:PRK01156 473 hYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKIESARADLED-------IKIKINEL 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQlrdleakvKDQEEELDEQAGSIQmLEQAKLRLEMEMERMRQTHSKEME---SRDEEVEEARQSCQKKLKQMEVQLEE 1321
Cdd:PRK01156 542 KDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFPD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1322 EYEDKQKALrekRELESKLSTLSDQVNQrdFESEKRLRKDLKRTkalladaqimLDHLKNNAPSKREIAQLKNQLeesef 1401
Cdd:PRK01156 613 DKSYIDKSI---REIENEANNLNNKYNE--IQENKILIEKLRGK----------IDNYKKQIAEIDSIIPDLKEI----- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1402 tcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMnELMKKHKAAVAQAS--RDMAQ 1479
Cdd:PRK01156 673 ----TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKrlREAFD 746
|
570 580
....*....|....*....|....*.
gi 1907082239 1480 MNDLQAQIEES------NKEKQELQE 1499
Cdd:PRK01156 747 KSGVPAMIRKSasqamtSLTRKYLFE 772
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
957-1558 |
6.46e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 61.46 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKernELRLSSDRLEtRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTq 1036
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1037 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYeravrevDFTKKRlqqELEDKMEVEQQSRRQLERRLG 1116
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1117 DLQADSDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEETQREKLQREKLQREKDM 1194
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1195 LLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEELDEQAG 1267
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1268 SiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLeEEYEDKQKALREKrelESKLSTL 1343
Cdd:PRK01156 480 R---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADL-EDIKIKINELKDK---HDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1344 SDQVNQRDFESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVEMEDLHLQ 1423
Cdd:PRK01156 552 KNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1424 IDDIAKaktALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ- 1502
Cdd:PRK01156 617 IDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDd 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1503 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLaSRLKETMEK 1558
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1387-1568 |
8.93e-09 |
|
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: 58.40 E-value: 8.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1387 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1466
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1467 kaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKtqvKRLE 1546
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170 180
....*....|....*....|..
gi 1907082239 1547 NLASRLKETMEKLTEERDQRAA 1568
Cdd:COG1579 149 EELAELEAELEELEAEREELAA 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
881-1297 |
1.11e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 881 LARLEEQRDEQTSRHLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIQVQLSEEQ 959
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 960 IRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELT-SELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYD 1038
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1039 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEL 1097
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1174
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1175 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1252
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 1253 -------AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESR 1297
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1085-1585 |
1.16e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 60.14 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1085 EVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQ 1164
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR-----------IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 RrfdsELSQAHEETQREKLQREKLQREKDMLLAEA----FSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS--------- 1231
Cdd:pfam05557 72 R----EQAELNRLKKKYLEALNKKLNEKESQLADAreviSCLKNELSELRRQIQRAELELQSTNSELEELQerldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1232 -SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRL----EMEME----RMRQTHSKEMESRDEEVE 1302
Cdd:pfam05557 148 aSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripELEKElerlREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1303 EARQSCQKKLKQME------VQLEEEYEDKQKAL---------------------REKRELESKLSTLSDQV-------- 1347
Cdd:pfam05557 228 EEVEDLKRKLEREEkyreeaATLELEKEKLEQELqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENssltssar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1348 ----NQRDFESEKR--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAM 1413
Cdd:pfam05557 308 qlekARRELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1414 EVEMEDLhlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1493
Cdd:pfam05557 382 IEEAEDM---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1494 KQELQEKLQALQSQVEFLE----QSMVDKSLVSRQEAKIRELEtrlEFEKTQVKRLENLASRLKETMEKLTEERDQRAAA 1569
Cdd:pfam05557 457 RQRLREQKNELEMELERRClqgdYDPKKTKVLHLSMNPAAEAY---QQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRL 533
|
570
....*....|....*.
gi 1907082239 1570 ENREKEQNKRLQRQLR 1585
Cdd:pfam05557 534 PETTSTMNFKEVLDLR 549
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1158-1516 |
1.21e-08 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 59.87 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1158 HELEKKQRRFDSELSQ--AHEETQREKLQ--REKLQREKDMLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---L 1223
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1224 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1296
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1297 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ----------------------VNQRD 1351
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVRG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1352 FESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDD 1426
Cdd:pfam06160 334 LEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1427 IAKAKTALEEQLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDMAQ----MNDLQAQIEESNKEKQEL 1497
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTL 469
|
410
....*....|....*....
gi 1907082239 1498 QEKLQALQSQVEFLEQSMV 1516
Cdd:pfam06160 470 YEKTEELIDNATLAEQLIQ 488
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1093-1507 |
1.32e-08 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 60.04 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1093 LQQELEDKMEVEQQSrrqLERRLGDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1172
Cdd:pfam05667 216 LAAAQEWEEEWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1173 QAHEETQREKLQR-EKLQREKDMLLAEAFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDL 1251
Cdd:pfam05667 290 TDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1252 EAKVKDQEEELDEQagsiqmlEQAKLRLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKAL- 1330
Cdd:pfam05667 362 ESSIKQVEEELEEL-------KEQNEELEKQYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLi 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1331 REKRELESKLSTlsdqvnqRDFESEKRLR--KDLK-RTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------S 1399
Cdd:pfam05667 433 EEYRALKEAKSN-------KEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1400 EFTcaaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRD 1476
Cdd:pfam05667 495 AYT-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKY 562
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907082239 1477 MAQMNDLQAQ----IEESNK---EKQELQEKLQALQSQ 1507
Cdd:pfam05667 563 LAALHENCEQliqtVEETGTimrEIRDLEEQIETESGK 600
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1074-1415 |
1.38e-08 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.14 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1074 EWRLKYE-RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdeSQRALQQLKKKCQRltaELQDTKLHLEG 1152
Cdd:pfam17380 255 EYTVRYNgQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRQEKEEKAR---EVERRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1153 QQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLK-QQMEEKDLDIAGFTQKVVSLEAELQDI 1230
Cdd:pfam17380 322 EKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1231 SSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQagsIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQ 1306
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1307 SCQKKLKQMEVQLEEEY----------EDKQKALREKR-------ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALL 1369
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQrrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082239 1370 ADAQIMLDHLKNNAPSKREiAQLKNQLEESEftcaaavKARKAMEV 1415
Cdd:pfam17380 556 EQMRKATEERSRLEAMERE-REMMRQIVESE-------KARAEYEA 593
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1318-1705 |
1.38e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 59.15 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1318 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1397
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1398 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1477
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1478 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETME 1557
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1558 KLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1637
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1638 AAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDG 1705
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1444-1682 |
1.42e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 60.31 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1444 EKNEIQNRLEEDQEDMNELMKKHKAAVaQASRdmaQMNDLQaQIEESNKEKQELQEKLQALQSQVEFLEqsmvdkslVSR 1523
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALE-DARE---QIELLE-PIRELAERYAAARERLAELEYLRAALR--------LWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1524 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD----QRAAAENREKEQnkrLQRQLRDTKEEMSELARKEA 1599
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDeleaQIRGNGGDRLEQ---LEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1600 EASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMesDENEDLINSLQDMVTKYQKKKNKLE-GDSDVDS 1678
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEAL--AEAEAALRDLRRELRELEAEIASLErRKSNIPA 440
|
....
gi 1907082239 1679 ELED 1682
Cdd:COG4913 441 RLLA 444
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1074-1513 |
1.89e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1074 EWRLKYERAV--REVDFTKKRLQQELEDKM-----EVEQQSRRQ--LERrlgDLQADSDESQRALQ--QLKKKCQRLTAE 1142
Cdd:COG3096 279 ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAREsdLEQ---DYQAASDHLNLVQTalRQQEKIERYQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1143 LQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDML-------------LAEAfslKQQMEEK 1209
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKA---RALCGLP 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1210 DLDIAGFTQKVVSLEAELQDISSQeskdeaslakvkkqLRDLEAKVKDQEEELDEQAGSIQMLEqaklRLEMEMERmrqt 1289
Cdd:COG3096 433 DLTPENAEDYLAAFRAKEQQATEE--------------VLELEQKLSVADAARRQFEKAYELVC----KIAGEVER---- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1290 hSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSdqvnqrdfeseKRLRKDLkrtkall 1369
Cdd:COG3096 491 -SQAWQTARELLRRYRS--QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC-----------QRIGQQL------- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1370 aDAQIMLDHLKnnapskreiAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID---DIAKAKTALEEQLSRLQREKN 1446
Cdd:COG3096 550 -DAAEELEELL---------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaARAPAWLAAQDALERLREQSG 619
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1447 EiqnrleedqedmnelmkkhkaAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1513
Cdd:COG3096 620 E---------------------ALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ 665
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1089-1508 |
1.97e-08 |
|
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: 59.53 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1089 TKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQR---ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQ 1164
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSL----------AEAQQRessAYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 RRFDSEL-SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1243
Cdd:pfam15964 370 ERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1244 VKKQLRDLEAKVKDQEEELdeqagsiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQscqkKLKQMEVQLEEEY 1323
Cdd:pfam15964 450 VCGEMRYQLNQTKMKKDEA-----------------EKEHREYRTKTGRQLEIKDQEIEKLGL----ELSESKQRLEQAQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1324 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEESEFTC 1403
Cdd:pfam15964 509 QDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELT------QKMQQMEAQHDKTVNEQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1404 AAAVKARKAMEVEMED----LHLQIDDIAKAKTALEEQLSR----LQREKNEIQNRLEEDQED------MNELMK----- 1464
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQcvqhgrMHERMKqrlrq 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082239 1465 --KHKAAVAQasrdmaQMNDLQAQIEESNKEKQELQEKLQALQSQV 1508
Cdd:pfam15964 663 ldKHCQATAQ------QLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1333-1598 |
2.51e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.54 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1333 KRELESKLSTLSDQvnqRDFESEKrlrkdlkrtKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaAAVKARKA 1412
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAED---------KLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1413 MEvEMEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESN 1491
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1492 K---------------EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEfekTQVKRLENLAS-- 1550
Cdd:PRK11281 177 NllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1551 RLKETMEKLTEERDQRAAAEN-------REKEQNKRLQRQLRDTKEEMSELARKE 1598
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
950-1353 |
4.95e-08 |
|
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: 57.98 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 950 LIQVQLsEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDAETaerlRTEKE 1029
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1030 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQ 1106
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1107 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETqreklqre 1186
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1187 klqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1266
Cdd:pfam07888 230 ----------AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1267 GSIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKALRE-KRELESKLSTLs 1344
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL- 373
|
....*....
gi 1907082239 1345 dQVNQRDFE 1353
Cdd:pfam07888 374 -RVAQKEKE 381
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1390-1654 |
5.65e-08 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 56.85 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1390 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1468
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1469 AvaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTQVK----R 1544
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1545 LENLASRLKETMEKLTEE-RDQRAAAENREKEQNKRLQRQ-------LRDTKEEMSELarkeaeaSRKKHELEMDLESLE 1616
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIaAKNREEAEEWYQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1617 AANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1654
Cdd:pfam00038 238 KQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1383-1578 |
6.22e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1383 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1462
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1463 ---MKKHKAAV-----------------------AQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV 1516
Cdd:COG3883 92 araLYRSGGSVsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1517 D-KSLVSRQEAKIRELETRlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNK 1578
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1386-1602 |
6.68e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.72 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1386 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1465
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1466 HKAAVAQASRDmAQMNDLQAQIEESNKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1538
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1539 KTQVKRLENLASRLKETMEKLTEERDQRAaaenrekeqnkRLQRQLRDTKEEMSELARKEAEAS 1602
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1388-1685 |
1.05e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1388 EIAQLKNQLEESEFTCAAAVKARKAMEV---EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMK 1464
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEvleEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1465 KHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL-QALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFEKTQVK 1543
Cdd:PRK02224 294 ERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLeECRVAAQAHNEE-------AESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1544 RLEnlaSRLKETMEKLTEERDQRAAAENREKEQNKRLQR---QLRDTKEEMSELARKEAEASRKKHELEMDLESLE---A 1617
Cdd:PRK02224 367 ELE---SELEEAREAVEDRREEIEELEEEIEELRERFGDapvDLGNAEDFLEELREERDELREREAELEATLRTARervE 443
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1618 ANQSLQADLKLA-----FKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEDRVD 1685
Cdd:PRK02224 444 EAEALLEAGKCPecgqpVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEE 516
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
964-1585 |
1.24e-07 |
|
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: 57.14 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 964 DEEIQQLRSKLEKVEKERNELRLSSDRLETRIS--ELTSELTDE-----------RNTGESASQLLDAETAERLRTEKEM 1030
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGARDEsikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYD-------ALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgewrlKYERAVREVDFTKKRLQQELEDKMEV 1103
Cdd:pfam10174 195 GHLEVLLDqkekeniHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERNIRDLEDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1104 EQQSRRQLE----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRRFD----- 1168
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQRAAilqte 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1169 -SELSQAHEETQR------EKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDissqesKDeasl 1241
Cdd:pfam10174 347 vDALRLRLEEKESflnkktKQLQD--LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1242 akvkKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEE 1321
Cdd:pfam10174 415 ----KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1322 EYEDKQKALREKRE-----------LESKLSTLSDQVNQRdFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA 1390
Cdd:pfam10174 490 ELTEKESSLIDLKEhasslassglkKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVA 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1391 QLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakaktaLEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAV 1470
Cdd:pfam10174 569 RYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE-------LESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1471 AQASR---DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS--LVSRQEAKIRELETRLEF-------- 1537
Cdd:pfam10174 638 LEEARrreDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMkqeallaa 717
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1538 --EK-TQVKRLENLASRLKETMEKLteerdqraAAENREKEqnkRLQRQLR 1585
Cdd:pfam10174 718 isEKdANIALLELSSSKKKKTQEEV--------MALKREKD---RLVHQLK 757
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
956-1629 |
2.15e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 956 SEEQIRNKDEEIQQLRSKLEKVEKERNEL----RLSSDRL------------ETRISELTSELTDERNTGESASQLLDAE 1019
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLeqdyQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1020 TAER----LRTEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAvREVDF 1088
Cdd:PRK04863 378 QEENearaEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA-KEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1089 TKKRLQqeLEDKMEVEQQSRRQLERRLGDLQ--ADSDESQRALQQLKKKCQRLTAE-LQDTKLhlegQQVRNHElekkqr 1165
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQFEQAYQLVRkiAGEVSRSEAWDVARELLRRLREQrHLAEQL----QQLRMRL------ 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1166 rfdSELSQAHEETQR-EKLQREKLQREKDMLLAEAFsLKQQMEEkdldiagftqkvvsLEAELQDISSQeskdeaslakv 1244
Cdd:PRK04863 523 ---SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES----------- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQMEVQlEEEYE 1324
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVE-RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 dkqkalREKRELESKLSTLSdqvnQRDFESEKRLRKDLKRTKA-LLAD--AQIMLDhlknNAP----------------- 1384
Cdd:PRK04863 652 ------ARKQALDEEIERLS----QPGGSEDPRLNALAERFGGvLLSEiyDDVSLE----DAPyfsalygparhaivvpd 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1385 ---SKREIAQLKNQLEE------------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDD 1426
Cdd:PRK04863 718 lsdAAEQLAGLEDCPEDlyliegdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1427 IAkaktaleEQLSRLQREKNEIQnRLeedQEDMNELMKKHkAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1506
Cdd:PRK04863 798 LA-------ERYATLSFDVQKLQ-RL---HQAFSRFIGSH-LAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1507 QVEFLEQSMV-------------DKSLVSRQEAkIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnRE 1573
Cdd:PRK04863 866 QLEQAKEGLSalnrllprlnllaDETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLK-QD 943
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1574 KEQNKRLQRQLRDTKEEMSEL-ARKEAEASrkkHELEMDLESLEAANQSLQADLKLA 1629
Cdd:PRK04863 944 YQQAQQTQRDAKQQAFALTEVvQRRAHFSY---EDAAEMLAKNSDLNEKLRQRLEQA 997
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1327-1503 |
3.30e-07 |
|
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: 53.39 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1327 QKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAA 1406
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1407 VKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQ 1484
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 1907082239 1485 AQIEESNKEKQELQEKLQA 1503
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1225-1408 |
4.03e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 55.02 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1225 AELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMER------MRQTH------SK 1292
Cdd:PHA02562 216 ARKQNKYDELVEEAKTI---KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGgvcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1293 EMESRDEEVEEARQS---CQKKLKQMEVQLEEEYE---DKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTK 1366
Cdd:PHA02562 293 QISEGPDRITKIKDKlkeLQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQ 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907082239 1367 ALLADaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVK 1408
Cdd:PHA02562 372 AEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1123-1337 |
5.35e-07 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 52.36 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1123 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKqrrfdselSQAHEETQREKlqreklQREKDMLLAE 1198
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRR--------IQTLEESLEQH------ERMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1199 AFSLKQQMEEKDL-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGSIQMLEQAK 1276
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1277 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKALREkRELE 1337
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1238-1600 |
5.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1238 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1313
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1314 QMEVQLEEEYEDKQKALREKRELESKLSTLSDQVnqrdfesekrlrkdlKRTKALLADAQIMLDHLKnnapsKREIA--Q 1391
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1392 LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQreknEIQNRLEEdqedmneLMKKHKAAVA 1471
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ----AAHSQFEQ-------AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1472 QASRDMAQmNDLQAQIEESNKEKQELQeKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASR 1551
Cdd:PRK04863 488 EVSRSEAW-DVARELLRRLREQRHLAE-QLQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082239 1552 LKETMEKLTEErdQRAAAENREkeqnkRLQRQLRDTKEEMSELARKEAE 1600
Cdd:PRK04863 563 LEARLESLSES--VSEARERRM-----ALRQQLEQLQARIQRLAARAPA 604
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1200-1584 |
6.41e-07 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 54.46 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1200 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ-------EEELDEQAGSIQML 1272
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1273 -------------EQAK---LRLEMEMERMRQThskeMesrdEEVEEARQSCQKKLKQmevQLEEEYEDKQKALREKREL 1336
Cdd:PRK04778 181 fsqfveltesgdyVEAReilDQLEEELAALEQI----M----EEIPELLKELQTELPD---QLQELKAGYRELVEEGYHL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1337 ESKlstlsdqvnqrDFESE-KRLRKDLKRTKALLADAQimLDHLK-NNAPSKREIAQLKNQLEeseftcaAAVKARKAME 1414
Cdd:PRK04778 250 DHL-----------DIEKEiQDLKEQIDENLALLEELD--LDEAEeKNEEIQERIDQLYDILE-------REVKARKYVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1415 VEMEDLHLQIDDIAKAKTALEEQLSRLQ-----------------REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1477
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1478 AQMNDLQAQIEESN-------KEKQELQEKLQALQSQVE----FLEQS---------MVDKSLVSRQeakIRELETRLE- 1536
Cdd:PRK04778 390 KQLEEIEKEQEKLSemlqglrKDELEAREKLERYRNKLHeikrYLEKSnlpglpedyLEMFFEVSDE---IEALAEELEe 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1537 --FEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAE------NREKEQNKRLQRQL 1584
Cdd:PRK04778 467 kpINMEAVNRLLEEATEDVETLEEETEElVENATLTEqliqyaNRYRSDNEEVAEAL 523
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1387-1671 |
7.80e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 54.36 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1387 REIAQlKNQLEESEFTCAAAVKARKAMEVEMEDLHLQiddiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1466
Cdd:pfam17380 310 REVER-RRKLEEAEKARQAEMDRQAAIYAEQERMAME----------RERELERIRQEERKRELERIRQEEIAMEISRMR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1467 KAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1546
Cdd:pfam17380 379 ELERLQMER---QQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1547 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE-EMSELARKEAEASRKKHELEMDLESLEAANQSLQAd 1625
Cdd:pfam17380 456 QERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEkELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER- 534
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907082239 1626 lklafKRIGDLQAAIEDEMESDENedlinsLQDMVTKYQKKKNKLE 1671
Cdd:pfam17380 535 -----RREAEEERRKQQEMEERRR------IQEQMRKATEERSRLE 569
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1243-1591 |
8.63e-07 |
|
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: 54.09 E-value: 8.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1243 KVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsKEMESRdEEVEEAR---QSCQKKLKQMEVQL 1319
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLE-----------------SEEKNR-EEVEELKdkyRELRKTLLANRFSY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1320 EEEYEDKQKALrekRELESKLSTLSDQVNQRDFESEK----RLRKDLKRTKALLADAQIMLDHLKNNAPskREIAQLKN- 1394
Cdd:pfam06160 145 GPAIDELEKQL---AEIEEEFSQFEELTESGDYLEARevleKLEEETDALEELMEDIPPLYEELKTELP--DQLEELKEg 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1395 --QLEESEFtcaaaVKARKAMEVEMEDLHlqiDDIAKAKTALEE-QLSRLQREKNEIQNRLEEDQEDM-------NELMK 1464
Cdd:pfam06160 220 yrEMEEEGY-----ALEHLNVDKEIQQLE---EQLEENLALLENlELDEAEEALEEIEERIDQLYDLLekevdakKYVEK 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1465 KHKAAVAQASRDMAQMNDLQAQIEESNK----------EKQELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKIRELET 1533
Cdd:pfam06160 292 NLPEIEDYLEHAEEQNKELKEELERVQQsytlneneleRVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEELEEILE 371
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1534 RLE-FEKTQVKrlenlasrLKETMEKLTEErdqraaaENREKEQNKRLQRQLRDTKEEM 1591
Cdd:pfam06160 372 QLEeIEEEQEE--------FKESLQSLRKD-------ELEAREKLDEFKLELREIKRLV 415
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1277-1627 |
1.01e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 54.09 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1277 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKALrekrELESKLSTLSDqvnqrdfESEK 1356
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLRE-------EFSK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1357 RLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1436
Cdd:PLN03229 498 ANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1437 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDMAQMNDLQAQIEESNKEKQ-ELQEKLQALQSQVEFL 1511
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1512 EQsmvdKSLVSRQEAKIRELETRLEFEKTQV-KRLENL--ASRLKETMEKLTEERDQRAAAEN-REKEQNKRLQRQLRDT 1587
Cdd:PLN03229 632 TK----KNKDTAEQTPPPNLQEKIESLNEEInKKIERVirSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQK 707
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907082239 1588 -KEEMSELARKEaeasrKKHELEMDLESLEAANQSLQADLK 1627
Cdd:PLN03229 708 iAEALNSSELKE-----KFEELEAELAAARETAAESNGSLK 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1294-1507 |
1.31e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1294 MESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKALREKRElESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQ 1373
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1374 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVK-------ARKAMEVEMEDLHLQIDD-IAKAKTALE 1435
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 1436 EQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1507
Cdd:COG3206 320 AELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1309-1683 |
1.38e-06 |
|
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: 53.42 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1309 QKKLKQMEVQ-LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLR--KDLKRTKALLadaQIMLDHLKNNAPS 1385
Cdd:COG5185 165 FGKLTQELNQnLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGseSTLLEKAKEI---INIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1386 KREIAQLKNQLEESEFtcaaAVKARKamEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE-----DQEDMN 1460
Cdd:COG5185 242 ESELEDLAQTSDKLEK----LVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSidikkATESLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1461 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQEAKIRELETRLEFEKT 1540
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1541 ----QVKRLENLASRLKETMEKLTEERDQraaaenrekeQNKRLQRQLRDTKEEMSELARK--EAEASRKKHELEMDLES 1614
Cdd:COG5185 392 sldeIPQNQRGYAQEILATLEDTLKAADR----------QIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEES 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1615 LE-------AANQSLQADLKLAFKRIGDLQAAI-----EDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELED 1682
Cdd:COG5185 462 QSrleeaydEINRSVRSKKEDLNEELTQIESRVstlkaTLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
.
gi 1907082239 1683 R 1683
Cdd:COG5185 542 E 542
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
958-1688 |
1.46e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 54.07 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEEIQQLRSKLEKVEKER------NELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAeRLRTEKEMK 1031
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1032 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQELEDKMEVEQQSRRQ 1110
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1111 LERRLGDLQADSDesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EET 1178
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1179 QREKLQREKLQREKDML------LAEAFSLKQQMEEKDLDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1250
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1251 LEAKVKDQEEELDEQAGSIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1324
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 DKQKA---LREKRELESKLSTLSDQVNQRDFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES- 1399
Cdd:PTZ00440 1553 IKDEIetiLNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1400 --------EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1464
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1465 KhkaavaqASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFEKTQVKR 1544
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1545 LENLASRLKETMEKLTEErDQRAAAENREKEQNKRLQRQLRDT-KEE-------------------MSELARKE--AEAS 1602
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDE-NNLSDSLNQAEDKNKEVANLTHYTnKNEaknllghvvksanfigikiMTGLQPTEltPDAS 1863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1603 RKK-------HELEMDLESLEAANQSLQAD---------------LKLAF---KRIGDLQAAIEDEMESDENEDLINSLQ 1657
Cdd:PTZ00440 1864 LETapeltfeSENNSDLELDHLSSNKNELDvykniqdayksslqiLKYSDdidKKQRDCNKLVEDGNEIYLKSTAINELK 1943
|
810 820 830
....*....|....*....|....*....|.
gi 1907082239 1658 DMVTKYQKKKNKLEGDSDVDSELEDRVDGVK 1688
Cdd:PTZ00440 1944 NMINSVKNKESAISNKIDNVSNKLSELNKIT 1974
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
957-1397 |
2.40e-06 |
|
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: 52.90 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNE-------LRLSSDRLETRISELTSELTderntgesasqlldaetaerlRTEKE 1029
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1030 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERAVREVDFTKKRLQQELEDKmev 1103
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEEKESFLNKKTKQLQDLTEEK--- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1104 eqqsrRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE---ETQR 1180
Cdd:pfam10174 376 -----STLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEalsEKER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1181 --EKLQREKlQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ 1258
Cdd:pfam10174 451 iiERLKEQR-EREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1259 EEEldeqagSIQMLEQAKLRLEMEM-ERMRQTHSKEMESRDEEV----EEARQsCQKKLKQM-----EVQLEEEYEDKQK 1328
Cdd:pfam10174 530 KEE------CSKLENQLKKAHNAEEaVRTNPEINDRIRLLEQEVarykEESGK-AQAEVERLlgilrEVENEKNDKDKKI 602
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1329 ALREKRELESKLSTLSDQVNQRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNApSKREIAQLKNQLE 1397
Cdd:pfam10174 603 AELESLTLRQMKEQNKKVANIKHGQQEMK-----KKGAQLLEEARRREDNLADNS-QQLQLEELMGALE 665
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1248-1598 |
2.59e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.84 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1248 LRDLEAKV------KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEE-VEEARQSCQKKLKQMEVQLE 1320
Cdd:pfam13868 8 LRELNSKLlaakcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1321 EEYEDKQKALREKRELesklstLSDQVNQRDFESEKRLRKDLKRTKAlladaqimldhlknnapsKREIAQLKNQLEese 1400
Cdd:pfam13868 88 KRQEEYEEKLQEREQM------DEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQA--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1401 ftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQ----REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1476
Cdd:pfam13868 141 -------EWKELEKEEEREEDERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1477 MAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-----DKSLVSRQEAKIRELEtRLEFEKTQVKRLENLasR 1551
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaerEEEEFERMLRKQAEDE-EIEQEEAEKRRMKRL--E 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907082239 1552 LKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1598
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
952-1645 |
3.33e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNEL------------RLSSDRLETRISELTSELTDERNtgESASQLLDAE 1019
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDYL--AAFRAKEQQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1020 TAERLRTEKEM---KELQTQYDAlkkqmevmemevmEARLIRAaeINGEVDDDDAggewrlkYERAvREVdftkkrLQQE 1096
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEK-------------AYELVCK--IAGEVERSQA-------WQTA-REL------LRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1097 LEDKMEVEQQSrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhlegqqvrNHELEKKQRRFDSELSQAHE 1176
Cdd:COG3096 505 RSQQALAQRLQ--QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----------AEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1177 ETQREKLQREKLQREKDMLLAEAFSLKQQmeekdldiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1256
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAAR--------APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1257 DQEEEldeqagsiqmLEQAKLRLEMEMERMRQTHSkemesrdeeVEEARqscqkkLKQME-----VQLEEEYEDkqKALR 1331
Cdd:COG3096 644 VERDE----------LAARKQALESQIERLSQPGG---------AEDPR------LLALAerlggVLLSEIYDD--VTLE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1332 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-----IAQLKN-QLEESEFTcAA 1405
Cdd:COG3096 697 DAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEEledavVVKLSDrQWRYSRFP-EV 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1406 AVKARKAMEVEMEDLHLQIDDIAK--AKTAL----------------------------EEQLSRLQREKNEIQNRLEED 1455
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEqyAKASFdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQH 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1456 QEDmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL 1535
Cdd:COG3096 856 RAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1536 ----------EFEKTQVKRLENLASRLKETMEKLTEERDQRAA----------AENRekEQNKRLQRQLRDTKEEMSElA 1595
Cdd:COG3096 927 avlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEARRE-A 1003
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1596 RKEAEASRKKH-ELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1645
Cdd:COG3096 1004 REQLRQAQAQYsQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAEAE 1054
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
964-1265 |
3.78e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 964 DEEIQQLRSKLEKVEKERNELRLSSDRLEtrisELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1043
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1044 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMeveqqsrRQLERRLGDLQADSD 1123
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM-------RAFNREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1124 ESQRALQQLKKKCQRLTAElqdtklHLEGQQVRNHELEKKQ-----RRFDSELSQAHEETqreklqREKLQREKDMLLAE 1198
Cdd:COG4913 809 ADLESLPEYLALLDRLEED------GLPEYEERFKELLNENsiefvADLLSKLRRAIREI------KERIDPLNDSLKRI 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1199 AFS----LKQQMEE-KDLDIAGFTQkvvsleaELQDISSQESKDEASLAKVK-KQLRDLEAKVKDQEEELDEQ 1265
Cdd:COG4913 877 PFGpgryLRLEARPrPDPEVREFRQ-------ELRAVTSGASLFDEELSEARfAALKRLIERLRSEEEESDRR 942
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
958-1363 |
4.17e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 958 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQY 1037
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRERE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1038 DALKKQMEVMEMEVMEARLIRAA----EINGEVDDD---DAGGEWRLKYEravrevdftkkRLQQELEDkMEVEQQSRRQ 1110
Cdd:PRK02224 429 AELEATLRTARERVEEAEALLEAgkcpECGQPVEGSphvETIEEDRERVE-----------ELEAELED-LEEEVEEVEE 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1111 LERRLGDLQADSDESQRALQQLKKKCQRLT---AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1187
Cdd:PRK02224 497 RLERAEDLVEAEDRIERLEERREDLEELIAerrETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1188 LQREKDMLLAEAFSLkQQMEEKDLDIAGFTQKVVSLEAELQDIssQESKDEAslakvKKQLRDLEAKVKDQEEELDEQAg 1267
Cdd:PRK02224 577 LNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL--AELNDER-----RERLAEKRERKRELEAEFDEAR- 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1268 sIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKALREKRElesKLSTLSD 1345
Cdd:PRK02224 648 -IEEAREDKERAEEYLE--------QVEEKLDELREERDDLQAEIGAVENELEelEELRERREALENRVE---ALEALYD 715
|
410
....*....|....*...
gi 1907082239 1346 QVNQRDfESEKRLRKDLK 1363
Cdd:PRK02224 716 EAEELE-SMYGDLRAELR 732
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1159-1696 |
4.78e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 52.36 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1159 ELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLKQQME---EKDLD--IAGFTQKVVSLEAELQDISS 1232
Cdd:TIGR01612 697 KLDDLKSKIDKEYDKIQNmETATVELHLSNIENKKNELLDIIVEIKKHIHgeiNKDLNkiLEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1233 ---QESKDEASLAKVKKQLRDLEA--KVKDQE-----EELDEQAGSIQMLEQAKLRLEMEMERMRQthskEMESRDEEVE 1302
Cdd:TIGR01612 777 ekdELNKYKSKISEIKNHYNDQINidNIKDEDakqnyDKSKEYIKTISIKEDEIFKIINEMKFMKD----DFLNKVDKFI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1303 EARQSCQKKLKQMEVQLEE-------EYEDKQKALREKRELESKlsTLSDQVNqRDFESEKRLRKDLKRTKALLADAqim 1375
Cdd:TIGR01612 853 NFENNCKEKIDSEHEQFAEltnkikaEISDDKLNDYEKKFNDSK--SLINEIN-KSIEEEYQNINTLKKVDEYIKIC--- 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1376 ldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDD-IAKAKTALEEQLSRLQREKNEIQNrlee 1454
Cdd:TIGR01612 927 ----ENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD---KFDNtLIDKINELDKAFKDASLNDYEAKN---- 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1455 dqedmNELMKKHKAAVAQASRDmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmVDKSLVSRQEAKIRELETR 1534
Cdd:TIGR01612 996 -----NELIKYFNDLKANLGKN--KENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIA-IHTSIYNIIDEIEKEIGKN 1067
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1535 LEFEKTQV-KRLENLASRLKETMEKLT---------EERDQRAAAENREKEQNKRLQRQLRDTKEEMSELarkeaeasRK 1604
Cdd:TIGR01612 1068 IELLNKEIlEEAEINITNFNEIKEKLKhynfddfgkEENIKYADEINKIKDDIKNLDQKIDHHIKALEEI--------KK 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1605 KHELEMDleslEAANQslqadlklafkrIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSDVDSELEdRV 1684
Cdd:TIGR01612 1140 KSENYID----EIKAQ------------INDLEDVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA-EI 1202
|
570
....*....|..
gi 1907082239 1685 DGVKSWLSKNKG 1696
Cdd:TIGR01612 1203 EKDKTSLEEVKG 1214
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1235-1360 |
4.80e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.07 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1235 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1314
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907082239 1315 MEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRK 1360
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEKLEKPKKKAKP 628
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
239-525 |
4.94e-06 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 52.05 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 239 LLEAFGNSPTIMNGSATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 307
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 308 A-----TLRTELHLNHL----------AENNVFGIVplSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYH 372
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 373 LGAAgatkePLEEQDEAAEAGRKQFARHEWAQKAAYLLGC-SLEELSSAIFKhqlKGGTLQRSTSFRQGPEESGLGEGTK 451
Cdd:cd14894 413 LGNI-----ELDYREVSGKLVMSSTGALNAPQKVVELLELgSVEKLERMLMT---KSVSLQSTSETFEVTLEKGQVNHVR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 452 lsaleclEGMASGLYSELFTLLISLVNRALKSS-------QHSLCS----------MMIVDTPGFQNpewggsARGASFE 514
Cdd:cd14894 485 -------DTLARLLYQLAFNYVVFVMNEATKMSalstdgnKHQMDSnasapeavslLKIVDVFGFED------LTHNSLD 551
|
330
....*....|.
gi 1907082239 515 ELCHNYAQDRL 525
Cdd:cd14894 552 QLCINYLSEKL 562
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1098-1520 |
5.33e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1174
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1175 HEETQREKLQREKLQREKDML--LAEAFSLkqqmeekdLDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1252
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1253 akvkdqeEELDEQAGSIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1324
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 DKQKALREKRELESKLSTLSDQVNQ-RDfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1402
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQeRT-----RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1403 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDMAQM 1480
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082239 1481 NDLqaqieesnkEKQELQEKLQALQSQVeflEQSMVDKSL 1520
Cdd:PRK04863 1128 NGV---------ERRLHRRELAYLSADE---LRSMSDKAL 1155
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1179-1369 |
5.70e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1179 QREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1256
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1257 DQEEELDE---------QAGSIQMLEQAKLRLEMEMERMRQTHSKE---MESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1324
Cdd:COG3206 244 ALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082239 1325 DKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALL 1369
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEVARELY 367
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1109-1265 |
5.82e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1109 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLhlegqQVRNHELEKKQrrfdselSQAHEETQREKLQREKL 1188
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-----EIKRLELEIEE-------VEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082239 1189 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1265
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1170-1360 |
6.09e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.92 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1249
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1250 DLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEMERMRqthskemesrdEEVEEARQSCQKKLKQMEvQLEEEYEDKQKA 1329
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIEELE-----------EELAELEAELAELEAELE-EKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|..
gi 1907082239 1330 LREKRE-LESKLSTLSDQVNQRDFESEKRLRK 1360
Cdd:COG1579 154 LEAELEeLEAEREELAAKIPPELLALYERIRK 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1243-1398 |
7.33e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1243 KVKKQLRDLEAKVKDQEEELDEQAGSIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1322
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1323 YEDKQKALREKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQLE 1397
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 1907082239 1398 E 1398
Cdd:PRK12704 180 E 180
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1018-1266 |
7.92e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1018 AETAERLRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEL 1097
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1177
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1178 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1257
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1907082239 1258 QEEELDEQA 1266
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1218-1503 |
9.69e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.91 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1218 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQmleqaKLRLEMemermrQTHSKEMESR 1297
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK-----ELREEA------QELREKRDEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1298 DEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ---------RDFESEKRLRKDLKRTKAL 1368
Cdd:COG1340 70 NEKVKELKEERDELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevLSPEEEKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1369 LADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI 1448
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADEL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1449 QNRLEEDQEDMNELMKKHKAAvaqasRDMAQMNDLQAQIEESNKEKQELQEKLQA 1503
Cdd:COG1340 229 HEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1238-1598 |
1.04e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1238 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscQKKLK 1313
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL----TERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1314 QMEVQLEEEYEDKQKAlREKRElesklstlsdqvnqrdfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1393
Cdd:COG3096 365 EQEEVVEEAAEQLAEA-EARLE---------------------AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1394 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAVaqa 1473
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEV--- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1474 srDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELEtrlEFEKTQVKRLENlASRLK 1553
Cdd:COG3096 489 --ERSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLE---EFCQRIGQQLDA-AEELE 556
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907082239 1554 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1598
Cdd:COG3096 557 ELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1353-1652 |
1.18e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 49.81 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1353 ESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAKT 1432
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1433 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1506
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1507 QVEFLEQSMVDkslvsrqeakireletrlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD 1586
Cdd:pfam15905 206 KLVSTEKEKIE--------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1587 TKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1652
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1096-1471 |
1.24e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1096 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1171
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1172 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1251
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1252 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEearqscqKKLKQMEVQLEEEYEDKQKALR 1331
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-------KLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1332 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARK 1411
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1412 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1471
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1105-1438 |
1.30e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1105 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1184
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR-----DLEAKVKDQE 1259
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1260 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELE 1337
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1338 SKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1417
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 1907082239 1418 EDLHLQIDDIAKAKTALEEQL 1438
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1392-1626 |
1.86e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1392 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1471
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1472 QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLENLAS 1550
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERmKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1551 RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD----------TKEEMSELARKEAEASRKKHELEMDLESLEAANQ 1620
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTahrkeaeneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRD 268
|
....*.
gi 1907082239 1621 SLQADL 1626
Cdd:pfam07888 269 RTQAEL 274
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
957-1626 |
1.89e-05 |
|
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: 50.34 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 957 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQ 1036
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1037 YDALKKQMEVMEMEVmeARLIRAAEINGE-VDDDDAGGEWRLKYERAVREVDFTKKRLQQEledKMEVEQQSRRQLerrl 1115
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEaLADSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS---- 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1116 gdlQADSDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ-------------- 1164
Cdd:COG3096 665 ---QPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpedlyli 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 ----RRFDSELSQAHEETQREKLQREKLQ----------------REK--DMLLAEAFSLKQQMEEKDLDIagftQKVVS 1222
Cdd:COG3096 738 egdpDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKrlEELRAERDELAEQYAKASFDV----QKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1223 LEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKEMES 1296
Cdd:COG3096 814 LHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKLLPQANLLADET 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1297 RDEEVEEARqscqkklkqmevqleEEYEDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQI 1374
Cdd:COG3096 891 LADRLEELR---------------EELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1375 MLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAKaktaleeqlsrlqrekneiqnRLEE 1454
Cdd:COG3096 956 QIFALSE-------------------------VVQRRP--------HFSYEDAVG---------------------LLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1455 DQeDMNELMKkHKAAVAQASRDMA--QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA 1526
Cdd:COG3096 982 NS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqADAEAEERARI 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1527 KIRELETRL--------EFEKTQVKR---LENLASRLKETMEKLTEERDQRAAAenreKEQNKRLQRQLRDTKEE----M 1591
Cdd:COG3096 1060 RRDELHEELsqnrsrrsQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVErrlhR 1135
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082239 1592 SELARKEAEASRkkhelEMDLESLEAANQSlQADL 1626
Cdd:COG3096 1136 RELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1163-1570 |
1.90e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1163 KQRRFDSElsqaheETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD-IAGFTQKVVSLEAELQDISSQesKDEASL 1241
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1242 AKVKKQLRdleaKVKDQEEELDEQAGS-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1320
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1321 EEYEDKQKALREKRELEsklsTLSDQVNQRDFESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1396
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1397 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIqnrLEEDQEDMNELMKKHKAAVAQASRD 1476
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDC---WWEKVENLQDLLDRATNQVEKAALV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1477 MAQMNDLQAQI---EESNKEKQELQEKLQalqsQVEFLEQSMvdKSLVSRQEAKIRELETrlefektQVKRLENLASRLK 1553
Cdd:PLN02939 323 LDQNQDLRDKVdklEASLKEANVSKFSSY----KVELLQQKL--KLLEERLQASDHEIHS-------YIQLYQESIKEFQ 389
|
410
....*....|....*..
gi 1907082239 1554 ETMEKLTEERDQRAAAE 1570
Cdd:PLN02939 390 DTLSKLKEESKKRSLEH 406
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1299-1617 |
2.62e-05 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 49.29 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDF----------ESEKRLRKDLKRTKAL 1368
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAeeeqppagpsEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1369 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKT---ALEEQLSRLQ-- 1442
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAERWGEQAEDRKQILEDMQSDRATISRALSqnrELKEQLAELQng 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1443 -----REKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDlqaQIEESNKEKQELQEK----LQALQSQVEFLEQ 1513
Cdd:pfam15070 178 fvkltNENMELTSALQSEQHVKKELAKK----LGQLQEELGELKE---TLELKSQEAQSLQEQrdqyLAHLQQYVAAYQQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1514 SMVDKSLVSRQEAKIRELETRLEFEKTQVK-RLENLASRLKETMEKLTeerdqrAAAenrekEQNKRLQRQLRDTKEEMS 1592
Cdd:pfam15070 251 LASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLE------ALT-----QQNQQLQAQLSLLANPGE 319
|
330 340
....*....|....*....|....*....
gi 1907082239 1593 ----ELARKEAEASRKKHELEMDLESLEA 1617
Cdd:pfam15070 320 gdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1309-1680 |
2.81e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1309 QKKLKQMEVQLEEEYEDKQKALREKRelesklsTLSDQVNQrdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1388
Cdd:TIGR01612 458 KSKLKALEKRFFEIFEEEWGSYDIKK-------DIDENSKQ-----DNTVKLILMRMKDFKDIIDFMELYKPDEVPSKNI 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1389 IAqlknqleeseFTCAAAVKARKAMEVEmedlhlqiddiAKAKTALEeQLSRLQREKNEIQNRLEEDQEDMNELMKkhka 1468
Cdd:TIGR01612 526 IG----------FDIDQNIKAKLYKEIE-----------AGLKESYE-LAKNWKKLIHEIKKELEEENEDSIHLEK---- 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1469 avaqasrdmaQMNDLQAQ----IEES---NKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQ 1541
Cdd:TIGR01612 580 ----------EIKDLFDKyleiDDEIiyiNKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYIDELAKISPYQVPE 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1542 -VKRLENLASRLKETMEKLTEerDQRAAAENrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE-MDLESLEAAN 1619
Cdd:TIGR01612 650 hLKNKDKIYSTIKSELSKIYE--DDIDALYN---ELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQnMETATVELHL 724
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1620 QSLQADLKLAFKRIGDLQAAIEDEMesdeNEDLINSLQDMVTKYQKKKNKLEGDSDVDSEL 1680
Cdd:TIGR01612 725 SNIENKKNELLDIIVEIKKHIHGEI----NKDLNKILEDFKNKEKELSNKINDYAKEKDEL 781
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1299-1607 |
2.87e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1299 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRtkallA 1370
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS-----I 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1371 DAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaAAVKARKA-MEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNE 1447
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELEESKRETE----TGIQNLTAeIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1448 IQNRLE----EDQEDMNELMKKHKAAVAQASRDMA----QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS 1519
Cdd:COG5185 382 FKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1520 LVSRQEAK---IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELAR 1596
Cdd:COG5185 462 QSRLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330
....*....|.
gi 1907082239 1597 KEAEASRKKHE 1607
Cdd:COG5185 542 ENLIPASELIQ 552
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1191-1513 |
3.20e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 3.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1191 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1250
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1251 LEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1314
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1315 MEVQLEEeYEDKQKALREK-RELESKLSTLSDQVNQRD------------------FESEKRLRKDLKRTKALLADAQIM 1375
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1376 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE- 1454
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRl 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1455 ---------DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1513
Cdd:PRK04863 599 aarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1201-1399 |
3.26e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1201 SLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLE 1280
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1281 M---------------EMERMRQTHSKEMesrdEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1345
Cdd:COG3883 107 VllgsesfsdfldrlsALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1346 QVNQrdfesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES 1399
Cdd:COG3883 183 LLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1108-1532 |
4.01e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.87 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1108 RRQLERRLGDLQADSDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1173
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1174 ---AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1249
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1250 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKA 1329
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1330 LREKREL----ESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1404
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1405 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDLQ 1484
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLA 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1907082239 1485 AQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1532
Cdd:pfam05701 401 QAAREELRKAKEEAEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1216-1283 |
4.39e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 46.08 E-value: 4.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1216 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML--EQAKLRLEMEM 1283
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1297-1638 |
4.68e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1297 RDEEVEEArQSCQKKLKQMEVQLEEEyedkQKALREkreLESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIML 1376
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAE----QYRLVE---MARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1377 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1452
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1453 EEDQEdMNELMKkhkAAVAQASRDMAQmndLQAQIEESNKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1526
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1527 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaAENREKEQNKRLQRQLRDtkEEMSELARKEAEASRK 1604
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE 568
|
330 340 350
....*....|....*....|....*....|....
gi 1907082239 1605 KHELEmdLESLEAANQSLQADLKLAFKRIGDLQA 1638
Cdd:PRK04863 569 SLSES--VSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
962-1287 |
4.68e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 962 NKDEEIQQLRSKL----EKVEkernELRLSSDRLETRISELTSELTDERN--------TGESASQLLDAETAERLRTEKE 1029
Cdd:pfam00038 1 NEKEQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1030 MKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQELedkmeveq 1105
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEEV-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1106 qsrRQLERRLGDlqadsdeSQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQAhEETQREKLQ 1184
Cdd:pfam00038 145 ---RELQAQVSD-------TQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQA-AARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKlqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1264
Cdd:pfam00038 214 SAK---------EEITELRRTIQSLEIELQSLKKQKASLERQLAET---EERYELQLADYQELISELEAELQETRQEMAR 281
|
330 340
....*....|....*....|...
gi 1907082239 1265 QAGSIQMLEQAKLRLEMEMERMR 1287
Cdd:pfam00038 282 QLREYQELLNVKLALDIEIATYR 304
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1098-1651 |
5.86e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 48.64 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLE----RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1164
Cdd:PRK10246 231 EEKQLLTAQQQQQQSlnwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHweriqeqsaALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDlDIAGFTQKVVSLEAELqdisSQESKDEASLAKV 1244
Cdd:PRK10246 311 QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQF----SQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQLRDLEAKVKDQEE-----ELDEQAGSI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQME 1316
Cdd:PRK10246 386 QQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQRN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1317 VQLEEeyedKQKALREKRELESKLSTLSDQvnqrdfesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnqL 1396
Cdd:PRK10246 461 AALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE--P 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1397 EESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLsrlQREKNEIQNRLEEDQEdmneLMKKHKAAVAQASRD 1476
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQL---QRDESEAQSLRQEEQA----LTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1477 MAQMNDLQAQIEESNKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVK-RLENLASRLK 1553
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTLP 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1554 ETMEKLT--EERDQRAAAENREKEQNKRLQRQ------LRDTKEEMSELARKEAEAS----RKKHElemDLESLEAANQS 1621
Cdd:PRK10246 659 QEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQT 735
|
570 580 590
....*....|....*....|....*....|
gi 1907082239 1622 LQADLKLAFKRIGDLQAAIEDEMESDENED 1651
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1309-1624 |
8.08e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.83 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1309 QKKLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS 1385
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1386 KREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1461
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1462 lmkKHKAAVAQASRDMAQmndLQAQIEEsnKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFEK 1539
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1540 TQVKRLENLASRLKETMEKLTEERDQRaaAENREKEQNKRLQRQ-LRDTKEEMSE----LARKEAEASRKKHELEMDLES 1614
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEH--LKDVLVEQEIELQREfLQDIKEKVEEeragRLLKLNELLANLKGLEKATSS 431
|
330
....*....|.
gi 1907082239 1615 -LEAANQSLQA 1624
Cdd:pfam09731 432 hSEVEDENRKA 442
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1493-1650 |
8.46e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1493 EKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdQRAAAEN 1571
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKElPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEV-----EARIKKY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1572 REKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1650
Cdd:COG1579 79 EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1283-1629 |
8.62e-05 |
|
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: 47.82 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1283 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE----- 1353
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1354 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1425
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1426 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1502
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1503 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEerdQRAAAENREKEQNKR 1579
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1580 LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1629
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1098-1307 |
9.07e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1177
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1178 TQREKLQREKLqrekDMLL-AEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1248
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1249 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1307
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1094-1593 |
9.48e-05 |
|
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: 47.59 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1094 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSELSQ 1173
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAVLAQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1174 AHEETQREKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QLRDL 1251
Cdd:pfam15964 293 THTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQCEQL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1252 EAKVKDQEEELDEQAGSiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALR 1331
Cdd:pfam15964 362 KSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------KVTR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1332 EKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEESef 1401
Cdd:pfam15964 425 EKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSES-- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1402 tcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqnrleedqedmneLMKKHKAAVAQASRDMAQMN 1481
Cdd:pfam15964 501 --------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEAKAQ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1482 DLQAQIEEsnkekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTE 1561
Cdd:pfam15964 554 ALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQ 612
|
490 500 510
....*....|....*....|....*....|..
gi 1907082239 1562 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSE 1593
Cdd:pfam15964 613 KSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1138-1503 |
9.61e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1138 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT 1217
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1218 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMErMRQTHSKEMESR 1297
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1298 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLD 1377
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1378 HLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1457
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1458 DM----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQA 1503
Cdd:COG4372 316 ALlaalLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1388-1657 |
9.68e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.98 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1388 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1467
Cdd:pfam19220 91 RLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1468 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT-QVKRL 1545
Cdd:pfam19220 171 LLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHRAERAsLRMKL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1546 ENLASRLKETMEKLTEERDQ--RAAAENREKEQN--------KRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESL 1615
Cdd:pfam19220 251 EALTARAAATEQLLAEARNQlrDRDEAIRAAERRlkeasierDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1616 EAANQSLQADLKLAFKRIGDLQAAIE---DEMESDE------NEDLINSLQ 1657
Cdd:pfam19220 331 TKALAAKDAALERAEERIASLSDRIAeltKRFEVERaaleqaNRRLKEELQ 381
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1123-1500 |
1.03e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 46.73 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1123 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMllaeafs 1201
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDKRL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1202 lkQQMEEKdldiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDqeeeldeqagsiqmLEQAKLRLEM 1281
Cdd:pfam15905 97 --QALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNE--------------LLKAKFSEDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1282 EMERMRQTHSKEMESRDEeVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkd 1361
Cdd:pfam15905 150 TQKKMSSLSMELMKLRNK-LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1362 lkrtkalladaqimldhlknnapskrEIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1441
Cdd:pfam15905 227 --------------------------YITELSCVSEQVE-------KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1442 QREKNEIQNRLEEDQEDMNELMKKHKAavaQASRDMAQMNDLQAQIEESNKEKQELQEK 1500
Cdd:pfam15905 274 SKQIKDLNEKCKLLESEKEELLREYEE---KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1080-1629 |
1.19e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1080 ERAVREVDFTKKRLQQELEDKMEVE------QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTA------ELQDTK 1147
Cdd:COG3096 532 QNAERLLEEFCQRIGQQLDAAEELEellaelEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArapawlAAQDAL 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1148 LHLEGQQvrNHELEKKQrrfdsELSQAHEETqrekLQREK-LQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLeAE 1226
Cdd:COG3096 612 ERLREQS--GEALADSQ-----EVTAAMQQL----LEREReATVERDELAARKQALESQIERLSQPGGAEDPRLLAL-AE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1227 ------LQDISSQESKDEA-----------------SLAKVKKQLRDLEAKVKD------QEEELDEQAGSIQMLEQAKL 1277
Cdd:COG3096 680 rlggvlLSEIYDDVTLEDApyfsalygparhaivvpDLSAVKEQLAGLEDCPEDlyliegDPDSFDDSVFDAEELEDAVV 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1278 RLEMEME--------------RMRQTHSKEM-ESRDEEVEE------ARQSCQKKL--------KQMEVQLEEEYEDKQK 1328
Cdd:COG3096 760 VKLSDRQwrysrfpevplfgrAAREKRLEELrAERDELAEQyakasfDVQKLQRLHqafsqfvgGHLAVAFAPDPEAELA 839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1329 ALREKR-ELESKLSTLSDQvnqrdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPskreiAQLKNQLEESEFTCAAAV 1407
Cdd:COG3096 840 ALRQRRsELERELAQHRAQ--------EQQLRQQLDQLKEQLQLLNKLLPQANLLAD-----ETLADRLEELREELDAAQ 906
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1408 KARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELM-KKHKAAVAQASRDMAQ---M 1480
Cdd:COG3096 907 EAQAFIQQHGKALA-QLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKqqiFALSEVVqRRPHFSYEDAVGLLGEnsdL 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1481 ND-LQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVdkSLVSRQEAKIRELEtrlEFEktqvKRLENLASRLKETME-K 1558
Cdd:COG3096 986 NEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA--SLKSSRDAKQQTLQ---ELE----QELEELGVQADAEAEeR 1056
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1559 LTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1629
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER---EQVVQAKAGWCAVLRLA 1124
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1449-1642 |
1.26e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 45.76 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1449 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1528
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1529 RELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQR------QLRDTKEEMSELARKEAEAS 1602
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082239 1603 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1642
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1521-1638 |
1.29e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.16 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1521 VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAE 1600
Cdd:COG2433 408 LTEEEEEIRRLE-------EQVERLEAEVEELEAELEEK--------------DERIERLERELSEARSEERREIRKDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907082239 1601 ASRKKHE---LEMDLESLEAANQSLQADLKLaFKRIGDLQA 1638
Cdd:COG2433 467 ISRLDREierLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
944-1319 |
1.59e-04 |
|
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: 46.82 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 944 FTTVRPLIQV-QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRlssdrletriSELTSELTDERNTGESASQLLDAETAE 1022
Cdd:pfam15964 349 FEKTKALIQCeQLKSELERQKERLEKELASQQEKRAQEKEALR----------KEMKKEREELGATMLALSQNVAQLEAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1023 RLRTEKEMKELQTQYDALKKQMEVMemevmearliraaeingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQ 1095
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ-----------------EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1096 ELEDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-S 1172
Cdd:pfam15964 482 QLEIK----DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1173 QAHEETQREK----------LQREKLQREKDMLLAEAFSLkqqmeekdldIAGFTQKVVSLEAELQDISSQESKDEASLA 1242
Cdd:pfam15964 553 QALQAQQREQeltqkmqqmeAQHDKTVNEQYSLLTSQNTF----------IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1243 KVKKQLRDLEAKVKDQEEELDEQAgsIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQME 1316
Cdd:pfam15964 623 QEKEYLQDRLEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLR 699
|
...
gi 1907082239 1317 VQL 1319
Cdd:pfam15964 700 SQV 702
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1353-1626 |
1.71e-04 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 46.11 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1353 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1431
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1432 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFL 1511
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1512 EQSMVDKSLVSRQEAKiRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEM 1591
Cdd:pfam09311 167 EEKLKAEILFLKEQIQ-AEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKI-RQLEDLQTTK 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1907082239 1592 SELARKEAEASRKKHELEMDLESLEAANQSLQADL 1626
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1442-1621 |
1.78e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1442 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE----FLEQSMVD 1517
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAqeraRQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1518 KSLVSRQEAKIRELETRLEFEKTQVKRLE-NLASRLKETMEKLTEERDQraaaenrekeqnkrLQRQlrdtKEEMSELAR 1596
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEQKRLMEMAEEERLE--------------YQRQ----KQEAEEKAR 491
|
170 180
....*....|....*....|....*
gi 1907082239 1597 KEAEASRKKHELEMDLESLEAANQS 1621
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQA 516
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1429-1801 |
1.84e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.96 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1429 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLqaLQS 1506
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1507 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFEKTQVKR--LENLAsRLKETMEKlTEERDQRAAAENREKEQNKRL-QRQ 1583
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEE-QEEVEEKEIAKEQRLKSKTKGkASK 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1584 LRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKY 1663
Cdd:PTZ00108 1169 LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1664 QKKKNKLEGDSDVDSELED-----RVDGVKSWLSKNKGPSKAPSDDGSLKSSRTalNSLPKEGKGPEERPSSVLSSLSYR 1738
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKegkpkNAPKRVSAVQYSPPPPSKRPDGESNGGSKP--SSPTKKKVKKRLEGSLAALKKKKK 1326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1739 KRLTlkdsiggTGDQDSLLTTLSERATSPERPPRKARggPREEPDQaqgrrcEELDDCSSIFS 1801
Cdd:PTZ00108 1327 SEKK-------TARKKKSKTRVKQASASQSSRLLRRP--RKKKSDS------SSEDDDDSEVD 1374
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1090-1288 |
1.95e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1090 KKRLQQELEDKMEVEQ-QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfd 1168
Cdd:pfam09787 23 KEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1169 SELSQAHEETQREKLQREKLQrekdmllAEAFSLKQQM----EEKDLDIAGFTQKVVSLEAELQDISSQ-ESKDEASLAK 1243
Cdd:pfam09787 93 EQLQELEEQLATERSARREAE-------AELERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082239 1244 vkkqlRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ 1288
Cdd:pfam09787 166 -----SELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1123-1266 |
1.97e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1123 DESQRALQQLKKKCQrLTA--ELQDTKLHLEGQ-QVRNHELEKKQRRFdselsQAHEETQREKLqrEKLQREKDMLLAEA 1199
Cdd:PRK12704 45 EEAKKEAEAIKKEAL-LEAkeEIHKLRNEFEKElRERRNELQKLEKRL-----LQKEENLDRKL--ELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1200 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeSKDEAS---LAKVKKQLR-DLEAKVKDQEEELDEQA 1266
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEAKeilLEKVEEEARhEAAVLIKEIEEEAKEEA 186
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1098-1502 |
2.07e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 46.54 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1098 EDKMEVEQQSRRQLERRLGDLQADSDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1169
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEETQREKLQREKLQREKDMLLAEA-FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1248
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1249 RDLEAKVKDQEEELDEQAGSIQMLEQAKlrlememermrqthskemESRDEEVEEARQSCQKKLKQ-MEVQLEEEYEDKQ 1327
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------------TDREKAEEEAKRRADAKLKEaVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1328 KAlREKRELESKLSTlsdqvnqrdfesekrlrKDLKRTKALLADAQIMLDHLKNnaPSKREiaqlKNQLEESEFTCAAAV 1407
Cdd:NF033838 262 KR-RAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPS--PSLKP----EKKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1408 KARKAMEVE---------MEDLHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASRdM 1477
Cdd:NF033838 318 KKAKDQKEEdrrnyptntYKTLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR-L 388
|
410 420
....*....|....*....|....*
gi 1907082239 1478 AQMNDLQAQIEESNKEKQELQEKLQ 1502
Cdd:NF033838 389 EKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1386-1596 |
2.18e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1386 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1465
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1466 HKAAVAQASRDMAQ-------------------MNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKSLVSRQEA 1526
Cdd:PRK11637 139 HTGLQLILSGEESQrgerilayfgylnqarqetIAELKQTREELAAQKAELEEK-QSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082239 1527 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD-------TKEEMSELAR 1596
Cdd:PRK11637 218 KktLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRkgstykpTESERSLMSR 296
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1208-1367 |
2.28e-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: 44.92 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1208 EKDLDIAGFTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMR 1287
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1288 QTHS-KEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKALRE-KRELESKLSTLSDQVNQRDfESEKRLRKDLKRT 1365
Cdd:COG1579 84 NVRNnKEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAElEAELAELEAELEEKKAELD-EELAELEAELEEL 161
|
..
gi 1907082239 1366 KA 1367
Cdd:COG1579 162 EA 163
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1262-1614 |
2.47e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 45.59 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1262 LDEQAGSIQMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKREleskls 1341
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYK-LRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1342 TLSDQVNQRdfesEKRLRKDLKRTkalladaqimLDHLKnnapskREIAQLKNQLEeseftcaaavkarKAMEVEMEDLH 1421
Cdd:pfam09755 96 TLAMNYEQE----EEFLTNDLSRK----------LTQLR------QEKVELEQTLE-------------QEQEYQVNKLM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1422 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM-NELMKKhkaavaqasrdmaqMNDLQAqieesnkEKQELQEK 1500
Cdd:pfam09755 143 RKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEALvNRLWKR--------------MDKLEA-------EKRLLQEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1501 LQALQSQVEFLEQSMVDKSLVSRQEAKIRELEtrlefektqvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRL 1580
Cdd:pfam09755 202 LDQPVSAPPSPRDSTSEGDTAQNLTAHIQYLR----------KEVERLRRQLATAQQEHTEKMAQYAQEERHIREENLRL 271
|
330 340 350
....*....|....*....|....*....|....
gi 1907082239 1581 QRQLRDTKEEMSELARKEAEAsrkKHELEMDLES 1614
Cdd:pfam09755 272 QRKLQLEMERREALCRHLSES---ESSLEMDEER 302
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1432-1617 |
2.67e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1432 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1507
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1508 VEFLEQSMVdKSLVSRQEaKIRELETRLEFEKTQVK--------------RLENLASRL--KETM-EKLTEERDQRAAAE 1570
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLTsksqssssqselenRLHQLTETLiqKQTMlEALSTEKNSLVLQL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907082239 1571 NREKEQNKRLQ-RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1617
Cdd:pfam09787 201 ERMEQQIKELQgEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1528-1693 |
2.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1528 IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEMSELARKEAEASRKKHE 1607
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL-EKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1608 LEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSLQDMVTKYQKKKNKLEGDSdvdSELEDRVDGV 1687
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---SRLEEEINGI 326
|
....*.
gi 1907082239 1688 KSWLSK 1693
Cdd:PRK03918 327 EERIKE 332
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1478-1658 |
3.03e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.63 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1478 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFEKTQvKRLENLASRLKEtME 1557
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1558 KLTEERDQ-RAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1626
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180 190
....*....|....*....|....*....|...
gi 1907082239 1627 KLAFKRIGDLQAAIEDEMES-DENEDLINSLQD 1658
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQIRFLTE 183
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
951-1265 |
3.29e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1030
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYDALKKQmevmemevmearlirAAEINGEVDDddaggewrlkyeravrevdftKKRLQQELEDKMEVEQQSRRQ 1110
Cdd:COG4372 104 ESLQEEAEELQEE---------------LEELQKERQD---------------------LEQQRKQLEAQIAELQSEIAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1111 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1190
Cdd:COG4372 148 REEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1191 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1265
Cdd:COG4372 228 EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1429-1680 |
3.31e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.09 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1429 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA----QASRDMAQMND------LQAQIEEsnKEKQELQ 1498
Cdd:pfam15818 21 EAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAvfkkQLQMKMCALEEekgkyqLATEIKE--KEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1499 EKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKTQVKRLEN----LASR---LKETMEKLtEERDQRAAAEN 1571
Cdd:pfam15818 99 ETLKALQVSKYSLQKK------VSEMEQKLQLHLLAKEDHHKQLNEIEKyyatITGQfglVKENHGKL-EQNVQEAIQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1572 -REKEQNKRLQRQLRDTKEEM----SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFkrigDLQAAIEDEME- 1645
Cdd:pfam15818 172 kRLSALNKKQESEICSLKKELkkvtSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMEL----ELNKKINEEITh 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907082239 1646 -SDENEDLINSLQDMVTKYQKkknKLEGDSDVDSEL 1680
Cdd:pfam15818 248 iQEEKQDIIISFQHMQQLLQQ---QTQANTEMEAEL 280
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
952-1173 |
3.45e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNElRLSSDRLETRISELTSELTDERNT-GESASQLLDAETAERlRTEKEM 1030
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQQELEDKMEVEQQsrrQ 1110
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1111 LERRLGDLQADSdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1173
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
954-1325 |
3.45e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.72 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 954 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSsdrletriseltseltDERNTGESASQLldAETAERLRteKEMKEL 1033
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLE----------------KLGENAESSKRL--NENANNLI--KQFENT 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1034 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewrlkYERAVREVDFTKKRLQQELEdkmeveqQSRRQLER 1113
Cdd:COG5185 295 KEKIAEYTKSIDIKKATESLEEQLAAAEAEQE-------------LEESKRETETGIQNLTAEIE-------QGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1114 RLGDLQADSDESQRALQQlkkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL-QREKLQREK 1192
Cdd:COG5185 355 NLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1193 DmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK--VKKQLRDLEAKVKDQEEELDEQAGSiq 1270
Cdd:COG5185 430 E-------QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKAT-- 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1271 mLEQAKLRLEMEMERMRQTHSKEMESRDEEvEEARQSCQKKLKQMEVQLEEEYED 1325
Cdd:COG5185 501 -LEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPASELIQA 553
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1121-1612 |
3.53e-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: 45.45 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1121 DSDESQRALQQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEETQREKLQREKLQ 1189
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1190 REKDmllAEAFSLKQQMEEKD-LDIAGFTQKVVSLEAElqdisSQESKDE-----ASLAKVKKqlrdLEAKV---KDQEE 1260
Cdd:pfam05622 78 LETA---RDDYRIKCEELEKEvLELQHRNEELTSLAEE-----AQALKDEmdilrESSDKVKK----LEATVetyKKKLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1261 ELDEQAGSIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKALREKRELESK 1339
Cdd:pfam05622 146 DLGDLRRQVKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKKLEEK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1340 LSTLsdqvnQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKN------------------QLEESEF 1401
Cdd:pfam05622 220 LEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDnlaaeimpaeireklirlQHENKML 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1402 TCaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLsRLQREK-NEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqm 1480
Cdd:pfam05622 295 RL----GQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRiLELQQQVEELQKALQEQGSKAEDSSL--------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1481 ndLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIRELETRLefektQVKRLENLA--SRLKETMEK 1558
Cdd:pfam05622 361 --LKQKLEEHLEKLHEAQSELQKKKEQIEELEP-----KQDSNLAQKIDELQEAL-----RKKDEDMKAmeERYKKYVEK 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1559 LTEE-RDQRAAAENREKEQNKRLQRQLRDtKEEMSELARKEAEASRKKHELEMDL 1612
Cdd:pfam05622 429 AKSViKTLDPKQNPASPPEIQALKNQLLE-KDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1245-1425 |
3.62e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQLRDLEAKVKDQEEELDEQAgsiqMLEQAKLRLEMEMERMRqtHSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYE 1324
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEE----KLEAALLEAKELLLRER--NQQRQEARREREELQRE--EERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 DKQKALREKRELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEsEFTCA 1404
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEEL----EKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLE 173
|
170 180
....*....|....*....|.
gi 1907082239 1405 AAVKARKAMEVEMEDLHLQID 1425
Cdd:PRK12705 174 AERKAQNILAQAMQRIASETA 194
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1356-1642 |
3.85e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1356 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKA 1430
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1431 KtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQE-KLQALQSQVE 1509
Cdd:pfam13868 89 R---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1510 FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKR-----LQRQL 1584
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1585 RDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigDLQAAIED 1642
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR--ELEKQIEE 301
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
964-1143 |
4.15e-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: 44.15 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 964 DEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT--QYDALK 1041
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1042 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQAD 1121
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1907082239 1122 SDESQRALQQLKKKCQRLTAEL 1143
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
951-1261 |
4.43e-04 |
|
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: 45.48 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 951 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1030
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1031 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDK---MEVEQQS 1107
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1108 RRQLERRlgdlqadSDESQRALQQLKKKCQRLTAELQDTKLHLeGQQVRNHELEKKQRRFDSElsQAHEETQREKLQRE- 1186
Cdd:pfam05483 617 NKALKKK-------GSAENKQLNAYEIKVNKLELELASAKQKF-EEIIDNYQKEIEDKKISEE--KLLEEVEKAKAIADe 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1187 --KLQREKDML----LAEAFSLKQQ--------MEEKDLDIAGFTQK-------VVSLEAELQDIssqeskdEASLAKVK 1245
Cdd:pfam05483 687 avKLQKEIDKRcqhkIAEMVALMEKhkhqydkiIEERDSELGLYKNKeqeqssaKAALEIELSNI-------KAELLSLK 759
|
330
....*....|....*....
gi 1907082239 1246 KQL---RDLEAKVKDQEEE 1261
Cdd:pfam05483 760 KQLeieKEEKEKLKMEAKE 778
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1245-1441 |
4.47e-04 |
|
Protein of unknown function (DUF1633); This family contains sequences derived from a group of hypothetical proteins expressed by Arabidopsis thaliana. These sequences are highly similar and the region concerned is about 100 residues long.
Pssm-ID: 116408 [Multi-domain] Cd Length: 698 Bit Score: 45.26 E-value: 4.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQLRDLEAKVK-DQEEELDEQAgsiQMLEQAKLRLEMEMermrqTHSKEMESRDEEveearqscqkKLKQMEVQLEEEY 1323
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1324 EDKQKALREKRELESKLSTLSDQVnqRDFESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQLEESEF 1401
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQAAEVES 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907082239 1402 TCA---AAVKARKAMEVEMEDLHLQIDDIaKAKTALEE----QLSRL 1441
Cdd:pfam07794 597 NLAlidQITKAAIDLTLEKPRFQAEIDDL-EARCKLKEvsdfTLSKL 642
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1080-1337 |
4.96e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1080 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHE 1159
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEER---------EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1160 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvsLEAELQDIssqeskdEA 1239
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE-------------REAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1240 SLAKVKKQLRDLEAKVKDQEEELDEQagsiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQM 1315
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRL 252
|
250 260
....*....|....*....|..
gi 1907082239 1316 EVQLEEEYEDKQKALREKRELE 1337
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDE 274
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1393-1567 |
5.41e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1393 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1470
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1471 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFEKtqvkrlen 1547
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180
....*....|....*....|
gi 1907082239 1548 lASRLKETMEKLTEERDQRA 1567
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADKKA 190
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
1475-1651 |
5.56e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 45.05 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1475 RDMAQMNDLQAQIEESNKEKQELQEKLqALQSQVEFLEQSMVDKSLvsrqeaKIRELETRLEFEKTQVKRLENLASRL-K 1553
Cdd:PRK12903 741 VQYSQKNPYQVYTEEGTKKFNILLQEI-AYDVIVSLFNNPNAEKIL------IITEILSDGINNSDINDRPQELIDQIiE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1554 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFK-R 1632
Cdd:PRK12903 814 SEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKdV 893
|
170
....*....|....*....
gi 1907082239 1633 IGDLQAAIEDEMESDENED 1651
Cdd:PRK12903 894 LIKLVISSDEIKQDEKTTK 912
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1255-1589 |
6.11e-04 |
|
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: 44.67 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1255 VKDQEEELDEQAGSIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1318
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1319 LEEEYEDKQKALREkRELESKLSTLSDQvnqrdfeSEKRLRKDLKRTKALLADAQIMldhlknnapskreIAQLKNQLEE 1398
Cdd:pfam15742 81 LTAEWKHCQQKIRE-LELEVLKQAQSIK-------SQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1399 SEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA 1473
Cdd:pfam15742 140 AHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1474 SRDMAQMNDLQAQI---EESNKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRLEFE 1538
Cdd:pfam15742 217 QQQEAQLKQLENEKrksDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRLVHE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1539 KTQ----VKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE 1589
Cdd:pfam15742 297 VEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEE 351
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1213-1474 |
6.59e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1213 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsk 1292
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1293 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAlrekreleSKLSTLSDQVNQRDFesekrLRKDLKRTKALLADA 1372
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSV--------SYLDVLLGSESFSDF-----LDRLSALSKIADADA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1373 QIMLDHlknnapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL 1452
Cdd:COG3883 133 DLLEEL-------KADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
250 260
....*....|....*....|..
gi 1907082239 1453 EEDQEDMNELMKKHKAAVAQAS 1474
Cdd:COG3883 206 AAAEAAAAAAAAAAAAAAAAAA 227
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1526-1651 |
7.98e-04 |
|
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular transport factor, Transcytosis associate protein (TAP) and Vesicle docking protein, this myosin-shaped molecule consists of an N-terminal globular head region, a coiled-coil tail which mediates dimerization, and a short C-terminal acidic region. p115 tethers COP1 vesicles to the Golgi by binding the coiled coil proteins giantin (on the vesicles) and GM130 (on the Golgi), via its C-terminal acidic region. It is required for intercisternal transport in the golgi stack. This family consists of the acidic C-terminus, which binds to the golgins giantin and GM130. p115 is thought to juxtapose two membranes by binding giantin with one acidic region, and GM130 with another.
Pssm-ID: 461461 [Multi-domain] Cd Length: 121 Bit Score: 41.23 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1526 AKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnrekEQNKRLQRQLRDTKEEMSELARKEAEASRKK 1605
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082239 1606 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1651
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
952-1321 |
8.03e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.44 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 952 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIseltseLTDERNTGESASQLldaetaerlrtEKEMK 1031
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1032 ELQTQYDalkkqmevmemevmearliRAAEINGEVDDDDAggewRLKYERAVREVDFTK----------KRLQQELEDKM 1101
Cdd:PRK04778 176 NLEEEFS-------------------QFVELTESGDYVEA----REILDQLEEELAALEqimeeipellKELQTELPDQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1102 EVEQQSRRQLER---RLGDLQADSDesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK--------QRRFDSE 1170
Cdd:PRK04778 233 QELKAGYRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydilEREVKAR 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1171 lSQAHEETQREKLQREKLQREKDMLLAEAFSLKQ--QMEEKDLDIA-GFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1247
Cdd:PRK04778 306 -KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1248 LRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKKLKQMEVQL 1319
Cdd:PRK04778 385 LEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEEL 464
|
..
gi 1907082239 1320 EE 1321
Cdd:PRK04778 465 EE 466
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1333-1507 |
8.25e-04 |
|
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: 43.85 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1333 KRELESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1412
Cdd:smart00787 146 KEGLDENLEGLK--------EDYKLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1413 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEE--- 1489
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrg 267
|
170
....*....|....*....
gi 1907082239 1490 -SNKEKQELQEKLQALQSQ 1507
Cdd:smart00787 268 fTFKEIEKLKEQLKLLQSL 286
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1247-1561 |
8.27e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1247 QLRDLeaKVKDQEEELDEQAGSIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1324
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1325 DKQKALR----EKRELESKLSTLSdqvNQRDFESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLEESE 1400
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1401 F----TCAAAVKARKAMEV--EMEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1474
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1475 rdmaqmNDLQAQIEESNKEKQELQEKLQALQS----QVE-FLEQSMVD--KSLVSRQEAK---IRELETRLEFEKTQVKr 1544
Cdd:PRK05771 247 ------EELLALYEYLEIELERAEALSKFLKTdktfAIEgWVPEDRVKklKELIDKATGGsayVEFVEPDEEEEEVPTK- 319
|
330
....*....|....*..
gi 1907082239 1545 LENlaSRLKETMEKLTE 1561
Cdd:PRK05771 320 LKN--PKFIKPFESLTE 334
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
956-1042 |
9.94e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 956 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldAETAERLRTEKEMKELQT 1035
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDR 472
|
....*..
gi 1907082239 1036 QYDALKK 1042
Cdd:COG2433 473 EIERLER 479
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1417-1508 |
1.11e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.90 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1417 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRDMAQMNDLQA 1485
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 1907082239 1486 QIEESNKEKQELQEKLQALQSQV 1508
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1108-1325 |
1.14e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1108 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEETQREK 1182
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1183 LQREKLQREKDMLLAEAFSLKQqmeekDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1258
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1259 ----EEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1325
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1405-1596 |
1.15e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1405 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------ 1478
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1479 ------QMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVKRLENLAS-- 1550
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGid 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907082239 1551 -----RLKETMEKLTEERDQRAAAEnREKEQNKRLQRQLRDTKEEMS---ELAR 1596
Cdd:COG1842 160 sddatSALERMEEKIEEMEARAEAA-AELAAGDSLDDELAELEADSEvedELAA 212
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1129-1346 |
1.19e-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: 43.97 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1129 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEetqreklqrEKLQREKDMLLaeafSLKQQME 1207
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1208 EKDLDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGSIQMLEQAKLRLEMEM 1283
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1284 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ 1346
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1153-1627 |
1.24e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.05 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1153 QQVRNHELEKKQRRFDSE--LSQAHEETQR----EKLQREKLQREkdmLLAEAFSLKQQMEEK------------DLDIA 1214
Cdd:NF041483 76 QLLRNAQIQADQLRADAEreLRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQLDQElaerrqtveshvNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1215 GFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM-------- 1283
Cdd:NF041483 153 WAEQLRARTESQarrLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLnaastqaq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1284 ------ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesEKR 1357
Cdd:NF041483 233 eatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN------EQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1358 LRKdlkrtkalladaqimldhlknnapSKREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1436
Cdd:NF041483 307 TRT------------------------AKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1437 --QLSRLQREKNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQ--------ELQEKL 1501
Cdd:NF041483 363 aaQLAKAARTAEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1502 QALQSQVEFLEQSMVDKSLVSRQEAKireletrlefeKTQVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQNKR 1579
Cdd:NF041483 443 RRLRGEAEQLRAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1580 LQR--QLRDTKEEMSELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1627
Cdd:NF041483 512 IERatTLRRQAEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1546-1655 |
1.27e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1546 ENLASRLKETMEKLTEERDQRAaaenREKEQNKRLQRQLRDTKEEMSELArKEAEAsrKKHELEMDLESLEAANQSLQAD 1625
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQA----REKAQSQALAEAQQQELVALEGLA-AELEE--KQQELEAQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|
gi 1907082239 1626 LKLAFKRIGDlQAAIEDEMESDENEDLINS 1655
Cdd:PRK11448 214 RKQKRKEITD-QAAKRLELSEEETRILIDQ 242
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1429-1554 |
1.28e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1429 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1508
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082239 1509 EFLEQSMVDKslvsrqEAKIRELETRLEFEKTQVKRLENLASRLKE 1554
Cdd:pfam10473 83 ENLTKELQKK------QERVSELESLNSSLENLLEEKEQEKVQMKE 122
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
964-1144 |
1.43e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 964 DEEIQQLRSKLEKVEKERNELRLSSDrletriseltseLTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1043
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1044 MEVMEMEVMEAR--------LIRAAEINGEVDdddaggEWRLKY-------ERAVREVDFTKKRLQQELEDKMEVEQQSR 1108
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907082239 1109 RQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQ 1144
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1434-1623 |
1.44e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 43.51 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1434 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkKHKAAVAQASRDM------AQMNDLQAQIEESNKEKQELQEKLQAlqsQ 1507
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAEL--KNQAAVPPAEEEQppagpsEEEQRLQEEAEQLQKELEALAGQLQA---Q 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1508 VEFLEQSmvdKSLVSRQEAKIRELETRLEFEKTQVKRLEnlasRLKETME--KLTeerDQRAAAENRE-KEQNKRLQRQ- 1583
Cdd:pfam15070 109 VQDNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGf 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082239 1584 LRDTKEEM-------------SELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1623
Cdd:pfam15070 179 VKLTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1284-1609 |
1.47e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1284 ERMRQTHSKEMESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKalrekrelesklstLSDQVNQRDFESEKRLRKDL 1362
Cdd:pfam02029 18 ERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEA--------------FLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1363 KRTKALLadaqimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaktalEEQLSRlq 1442
Cdd:pfam02029 84 ERQKEFD----------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYK----------------EEETEI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1443 REKNEIQNRLEEDQEDMNELMKKHKAAVAQASR-DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS------M 1515
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEvPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngeeE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1516 VDKSLVS--RQEAKIRELETRLEFEKTQV---KRLENLASRLKET----MEKLtEERDQRAAAE----NREKEQNKRL-- 1580
Cdd:pfam02029 216 VTKLKVTtkRRQGGLSQSQEREEEAEVFLeaeQKLEELRRRRQEKeseeFEKL-RQKQQEAELEleelKKKREERRKLle 294
|
330 340
....*....|....*....|....*....
gi 1907082239 1581 QRQLRDTKEEMSELARKEAEASRKKHELE 1609
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1106-1349 |
1.58e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1106 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheetqrEKLq 1184
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1185 REKLQREKDML----------LAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK- 1246
Cdd:COG0497 225 REALQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1247 --QLRDLEAKVKDQEEELdeqagsIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYE 1324
Cdd:COG0497 305 laLLRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELL 358
|
250 260
....*....|....*....|....*
gi 1907082239 1325 DKQKALREKRELESKlsTLSDQVNQ 1349
Cdd:COG0497 359 EAAEKLSAARKKAAK--KLEKAVTA 381
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1181-1332 |
1.60e-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: 41.82 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1181 EKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1260
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082239 1261 ELDeqagsiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKALRE 1332
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1459-1675 |
1.70e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1459 MNELMKKHKAAVAQASRDMAqMNDLQAQIEESNKEKQELQEKLQALQSQV-EFLEQSMVDKSlvsrqeaKIRELETRLEf 1537
Cdd:cd22656 96 ILELIDDLADATDDEELEEA-KKTIKALLDDLLKEAKKYQDKAAKVVDKLtDFENQTEKDQT-------ALETLEKALK- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1538 ektqvkrlenlasrlketmEKLTEErdqraaAENREKEQNKRLQRQLrdtKEEMSELARKEAEASRKKHELEMDLESLEA 1617
Cdd:cd22656 167 -------------------DLLTDE------GGAIARKEIKDLQKEL---EKLNEEYAAKLKAKIDELKALIADDEAKLA 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1618 ANQSLQADLKLAFKRIGDLQAAIEDEMESDENedLINSLQDMVTKYQKKKNKLEGDSD 1675
Cdd:cd22656 219 AALRLIADLTAADTDLDNLLALIGPAIPALEK--LQGAWQAIATDLDSLKDLLEDDIS 274
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
963-1268 |
1.76e-03 |
|
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: 43.41 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 963 KDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE---TAERLRTEKEMKELQTQYDA 1039
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaeqELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1040 LKKQMEVMEmevmearliRAAEINGEVDDDDAGGEWRLKYER---AVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLG 1116
Cdd:COG5185 346 EQGQESLTE---------NLEAIKEEIENIVGEVELSKSSEEldsFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1117 DLQADSDESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDSELSQAHEETQREKLQR-----EKLQRE 1191
Cdd:COG5185 417 AADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADEESQSRLEEAYDEINRSvrskkEDLNEE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1192 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---AELQDISSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGS 1268
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1524-1632 |
1.94e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1524 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEklteERDQRAAaenREKEQNKRLQRQLRDTKEEMSELARKEAEASR 1603
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1907082239 1604 KKHELE---MDLESLEAANQSLQADLKLAFKR 1632
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1016-1282 |
2.05e-03 |
|
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: 43.14 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1016 LDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDAGGEWRLKYERAVR 1084
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1085 EV---DFTKKRLQQELEDKMEVEQQSrRQLERRLGDLQADSDESQRALQ----QLKKKCQR---LTAELQDTKLHLEGQQ 1154
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNeletQNRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1155 VRNHELEKKQRRFDS---ELSQAHEETQREKLQREKLQREKDMLLAE-AFSLKQQMEEKDLDIAGFTQK----------- 1219
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1220 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagsiqmLEQAKLRLEME 1282
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1464-1611 |
2.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1464 KKHKAAVAQASRDMAQMndlqaqIEESNKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFEKTQV 1542
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1543 KRLENLASRLKETMEKLTEERDQR--------AAAENREKEQNKRLQRQLRDTKEE-----MSELARK-EAEASRKKHEL 1608
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKqqelekkeEELEELIEEQLQELERISGLTAEEakeilLEKVEEEaRHEAAVLIKEI 178
|
...
gi 1907082239 1609 EMD 1611
Cdd:PRK12704 179 EEE 181
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1453-1603 |
2.23e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.92 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1453 EEDQEDMNELMKKHKAAVAQASRDMAQ-MNDLQAQIEESNKEKQELQEKLQalqsqvefleqsmvdkslvsRQEAKIREL 1531
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEeIRRLEEQVERLEAEVEELEAELE--------------------EKDERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082239 1532 ETRLEFEKTQVKRlenlasrlketmekltEERDQRaAAENREKEqNKRLQRQLRDTKEEMSELARKEAEASR 1603
Cdd:COG2433 447 ERELSEARSEERR----------------EIRKDR-EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1348-1619 |
2.32e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.90 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1348 NQRDFESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1427
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1428 AKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKkhkaavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQS 1506
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1507 QvefLEQSMVDKSLVSrqEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRD 1586
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLL-------TLRIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 1907082239 1587 TKEEMSELARKEAEASRKkhELEMDLESLEAAN 1619
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1578-1672 |
2.57e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 40.25 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1578 KRLQRQLRDTKEEM-SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEdLINSL 1656
Cdd:pfam03938 18 KAAQAQLEKKFKKRqAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQE-LLQPI 96
|
90
....*....|....*.
gi 1907082239 1657 QDMVTKYQKKKNKLEG 1672
Cdd:pfam03938 97 QDKINKAIKEVAKEKG 112
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1144-1665 |
2.58e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1144 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQreKLQREKLQREK-DMLLAEAFSLKQQMEEKDLDIagFTQKVVS 1222
Cdd:PTZ00440 617 EKNDLQEKVKYILNKFYKGDLQELLDELSHFLDDHK--YLYHEAKSKEDlQTLLNTSKNEYEKLEFMKSDN--IDNIIKN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1223 LEAELQDISSQesKDEAslakVKKQLRDLEAKVKDQEEELDEQAGSIQM-LEQAKlrlemEMERMRQTHSKEMESRDEEV 1301
Cdd:PTZ00440 693 LKKELQNLLSL--KENI----IKKQLNNIEQDISNSLNQYTIKYNDLKSsIEEYK-----EEEEKLEVYKHQIINRKNEF 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1302 EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQV--NQRDFESEKRLRKDLK--------RTKALL-- 1369
Cdd:PTZ00440 762 ILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKknNQDLLNSYNILIQKLEahtekndeELKQLLqk 841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1370 ---ADAQIMLDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLqIDDIAKAKTALEEQLS------ 1439
Cdd:PTZ00440 842 fptEDENLNLKELEKEFNENNQIVDnIIKDIENMNKNINIIKTLNIAINRSNSNKQL-VEHLLNNKIDLKNKLEqhmkii 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1440 ----------------RLQREKNEIQNRLeeDQEDMNEL-MKKHKA-AVAQASRDMAQMND--LQAQIEESNKEKQELQE 1499
Cdd:PTZ00440 921 ntdniiqkneklnllnNLNKEKEKIEKQL--SDTKINNLkMQIEKTlEYYDKSKENINGNDgtHLEKLDKEKDEWEHFKS 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1500 KLQALQSQVEFLEQSMVDksLVSRQEAKIRELETRLEFEKTQ-----VKRLENLASRLKETMEKLTeerdqraAAENREK 1574
Cdd:PTZ00440 999 EIDKLNVNYNILNKKIDD--LIKKQHDDIIELIDKLIKEKGKeieekVDQYISLLEKMKTKLSSFH-------FNIDIKK 1069
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1575 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAF----KRIGDLQAAIE---DEMESD 1647
Cdd:PTZ00440 1070 YKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEHYnkkkKSLEKIYKQMEktlKELENM 1149
|
570
....*....|....*....
gi 1907082239 1648 ENEDL-INSLQDMVTKYQK 1665
Cdd:PTZ00440 1150 NLEDItLNEVNEIEIEYER 1168
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1093-1230 |
3.07e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1093 LQQELEDKmEVEQQSRRQLERRLgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDSELS 1172
Cdd:pfam02841 178 LQEFLQSK-EAVEEAILQTDQAL-------TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM---MEAQERSYQEHVK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1173 QAHEETQREklqREKLQREKDMLLAeafslKQQMEEKDLDIAGFTQKVVSLEAELQDI 1230
Cdd:pfam02841 247 QLIEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1488-1606 |
3.54e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1488 EESNKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKL------TE 1561
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907082239 1562 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKH 1606
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1384-1584 |
3.75e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1384 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREKNEIQNRLE 1453
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1454 EdqedmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQvefleqsmvdksLVSRQEAKIReLET 1533
Cdd:PRK11281 105 A--------LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQTQPER-AQA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1534 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1584
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKS 214
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1245-1332 |
3.94e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1245 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1324
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
|
....*....
gi 1907082239 1325 DK-QKALRE 1332
Cdd:pfam03938 98 DKiNKAIKE 106
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1222-1523 |
3.98e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1222 SLEAeLQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEqagsiqmLEQaklRLEMEMERMRQThSKEMES-RDEE 1300
Cdd:PRK11281 44 QLDA-LNKQKLLEAEDKLVQQDLEQTLALL-DKIDRQKEETEQ-------LKQ---QLAQAPAKLRQA-QAELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1301 VEEARQSCQK-KLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDLKRT----KALL 1369
Cdd:PRK11281 111 DEETRETLSTlSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLqqiRNLLKGGkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1370 ADAQIMLdhlknNApskrEIAQLKNQLEESEFTCAAAVKarkameveMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNei 1448
Cdd:PRK11281 191 PSQRVLL-----QA----EQALLNAQNDLQRKSLEGNTQ--------LQDLLQKQRDYLTARIQrLEHQLQLLQEAIN-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1449 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQI--------EESNK-EKQELQEKLQ---ALQSQVEFLEQSMV 1516
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISV 331
|
....*....
gi 1907082239 1517 DK-SLV-SR 1523
Cdd:PRK11281 332 LKgSLLlSR 340
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1233-1597 |
4.59e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.97 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1233 QESKD-EASLAKVKKQLRDLEAKVKDQEEELdeqagsiqmlEQAKLRLEMEMERMRQTHSKEMESR-DEEVEEARQSCQK 1310
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEANL----------QKLDKEKEKLEADFLDECWKKIKRKkNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1311 KLKQMEVQLEE--EYEDKQKALREKRELESKLSTLSDQ---------VNQRDFESEKRLRKDLKRTKALLADAQIMLDHL 1379
Cdd:pfam13166 159 EANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1380 KNNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------S 1439
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1440 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR---------DMAQMNDLQAQIEES----NKEKQELQEKLQALQS 1506
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKsieldsvdaKIESINDLVASINELiakhNEITDNFEEEKNKAKK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1507 QVEfleqsmvdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRD 1586
Cdd:pfam13166 398 KLR--------LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKL--------------REEIKELEAQLRD 455
|
410
....*....|....
gi 1907082239 1587 TK---EEMSELARK 1597
Cdd:pfam13166 456 HKpgaDEINKLLKA 469
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1361-1617 |
4.98e-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: 41.82 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1361 DLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS 1439
Cdd:pfam15964 348 NFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1440 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDMA-QMNDLQAQIEESNKEKQELQEKlqaLQSQVEFLEQsmvdk 1518
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1519 slvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaaenrEKEQNKRLQRQLRDTKEE-MSELARK 1597
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 1907082239 1598 EA-EASRKKHELEMDLESLEA 1617
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1393-1617 |
5.20e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 41.74 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1393 KNQLEESEFTCAAAVKARKAMEVEMEDLHLQ--IDDIAKAKTALEEQLS---RLQREKNEIQNRLEEDQEdmnelmkkhk 1467
Cdd:pfam15066 329 KQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfVDIINKLKENVEELIEdkyNVILEKNDINKTLQNLQE---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1468 aavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQ-SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1546
Cdd:pfam15066 399 -----------ILANTQKHLQESRKEKETLQLELKKIKvNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQ 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082239 1547 nlasRLKETMEKLTEerdqrAAAENREKEQNKRLQRQLRDTKeemsELARKEAEASRKKHELEMDLESLEA 1617
Cdd:pfam15066 468 ----QLKGELEKATT-----SALDLLKREKETREQEFLSLQE----EFQKHEKENLEERQKLKSRLEKLVA 525
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1467-1609 |
5.66e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.37 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1467 KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTqvKRLE 1546
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA---------EQARQKELEQRAAAEKA--AKQA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082239 1547 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE 1609
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEE 170
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
956-1174 |
5.72e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 956 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDerntgesasqlldaetaerlrTEKEMKELQT 1035
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1036 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1106
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1107 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1174
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1387-1630 |
6.37e-03 |
|
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: 40.40 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1387 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1466
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1467 KAAVAQASRDMAQMNDLQAQI-------EESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEK 1539
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1540 TQVKRLENLAsrlketmekltEERDQRaaaENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAAN 1619
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKY 220
|
250
....*....|.
gi 1907082239 1620 QSLQADLKLAF 1630
Cdd:pfam00261 221 KAISEELDQTL 231
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1093-1254 |
6.77e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.89 E-value: 6.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1093 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1169
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1170 ELSQAHEEtqreKLQR-EKLQREKDMLLAE----AFSLKQQMEEKDLDIAgftQKVVSL-------EAELQDISSQESKD 1237
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQALgetlekkEAQLNEVLAAANLD 175
|
170
....*....|....*...
gi 1907082239 1238 EASLAKVKKQLRD-LEAK 1254
Cdd:pfam13851 176 PDALQAVTEKLEDvLESK 193
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1437-1626 |
6.91e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1437 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQvefleQ 1513
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1514 SMVDKSLVSRQEAKIRE-----LETRLEFEKTQVK-RLENLASRL----KETMEKLTEERDQrAAAENREKEQNKRLQRQ 1583
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082239 1584 LRDTKEEmSELARKEAEASRKKhelemDLESLEAANQSLQADL 1626
Cdd:PRK11637 199 LLYEQQA-QQQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
1478-1562 |
8.23e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.97 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1478 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS--------MVDKSLVSR-QEAKIRELETRLEFEKTQVKRLENL 1548
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLdedtkvykLIGDVLVKQdKEEVKEQLEERKETLEKEIKTLEKQ 81
|
90
....*....|....
gi 1907082239 1549 ASRLKETMEKLTEE 1562
Cdd:pfam01920 82 LEKLEKELEELKEE 95
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1282-1455 |
8.55e-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: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1282 EMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQV-NQRDFES-EKRLr 1359
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEAlQKEI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1360 KDLKRTKALLADaqimldhlknnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLS 1439
Cdd:COG1579 99 ESLKRRISDLED----------------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELE 159
|
170
....*....|....*.
gi 1907082239 1440 RLQREKNEIQNRLEED 1455
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1409-1513 |
8.59e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.32 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1409 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIE 1488
Cdd:pfam13863 11 VQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|....*
gi 1907082239 1489 ESNKEKQELQEKLQALQSQVEFLEQ 1513
Cdd:pfam13863 91 ELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1011-1270 |
8.94e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.44 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1011 SASQLLDAETAERLRTEKEmkeLQTQYDALKKQMEVmemevmearliraaeingEVDDddaggewrlkyeravrevdftk 1090
Cdd:PRK11281 22 LSSAFARAASNGDLPTEAD---VQAQLDALNKQKLL------------------EAED---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1091 KRLQQELE------DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKcqrltaELQDTKLHLEGQQVRnhELEKKQ 1164
Cdd:PRK11281 59 KLVQQDLEqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD------NDEETRETLSTLSLR--QLESRL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1165 RRFDSELSQAHEE------------TQREKLQRE---KLQR---------------------EKDMLLAEAFSLKQQMEE 1208
Cdd:PRK11281 131 AQTLDQLQNAQNDlaeynsqlvslqTQPERAQAAlyaNSQRlqqirnllkggkvggkalrpsQRVLLQAEQALLNAQNDL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082239 1209 KDLDIAGFTQkvvsleaeLQDIsSQESKDEASL--AKVKKQLRDLE----AKVKDQEEELDEQAGSIQ 1270
Cdd:PRK11281 211 QRKSLEGNTQ--------LQDL-LQKQRDYLTAriQRLEHQLQLLQeainSKRLTLSEKTVQEAQSQD 269
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
1445-1540 |
9.38e-03 |
|
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of polymorphic toxin proteins in bacteria. It is predicted to use Type VII secretion pathway to mediate export of bacterial toxins.
Pssm-ID: 428100 [Multi-domain] Cd Length: 202 Bit Score: 39.54 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1445 KNEIQNRLEEDQEDMNELMKKHKAAVAQASR----DMAQMNDLQAQIEESNKEKQELQEKLQAL-QSQVEFLEQSmvdKS 1519
Cdd:pfam04740 101 EHELENGLKKAKEKTEELTDEINSILASVSDivslPKLSDSEVQDSLQKAKKKVKDTIEKLYDFdQEQTSELSEL---EA 177
|
90 100
....*....|....*....|.
gi 1907082239 1520 LVSRQEAKIRELETRLEFEKT 1540
Cdd:pfam04740 178 DLQALKTYVSELEEMTSNGKI 198
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1417-1584 |
9.57e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.11 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1417 MEDLHLQIDDIAKAKTALEEQ----LSRL----QRE----------KNEIQN----------RLEEDQEDMNELMKKHKA 1468
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQsqnlLSKLeiaqQKEskflenlaslKHENDNlssmlnrkerRLKDLEDQLSELKNSYEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082239 1469 AVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQ--EAKIRELETRLE-FEKTQVKRL 1545
Cdd:pfam17078 85 LT-------ESNKQLKKRLENSSASETTLEAELERLQIQYD----ALVDSQNEYKDhyQQEINTLQESLEdLKLENEKQL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082239 1546 ENLASRL----KETMEKLTEERDQRAAAENREKEQNKRLQRQL 1584
Cdd:pfam17078 154 ENYQQRIssndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| |
