|
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 ... |
467-1224 |
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: 1128.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGtKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVG-GVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 706
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 707 QKTCWLILASIYHLGAAGATKEPleeqdeaaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFRQ 786
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAA--------SAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 787 GPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGSARGASFEELCHN 866
Cdd:cd01386 312 ESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 867 YAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASH--LVRSLAHADEARGLLWLLEEEALVPGAT 944
Cdd:cd01386 392 YAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQqaLVRSDLRDEDRRGLLWLLDEEALYPGSS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 945 EDALLDRLFSYYGPQEGDkKGQSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWLNYTKQNPATQNAPRLLQDSQKKiisnl 1024
Cdd:cd01386 472 DDTFLERLFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE----- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1025 flgragsatvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEG 1104
Cdd:cd01386 546 ---------------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNA 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1105 WPGEPRsassrrvsssseldlppGDPCEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLT 1184
Cdd:cd01386 587 GKDERS-----------------TSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLT 649
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907082217 1185 KKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd01386 650 KKLGLNSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
468-1224 |
1.64e-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: 462.83 E-value: 1.64e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS-----VEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEN---NVFGIVPLSKPEEKQKAAQQFSKLQAAMK 698
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 699 VLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGGTl 778
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVAD------DESLKAAAKLLGVDAEDLEEALTTRTIKVGG- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 779 qrstsfrqgpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSS--QHSLCSMMIVDTPGFQNPEWggsar 856
Cdd:cd00124 315 -----------ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV----- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 857 gASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVAD------DSV-AAVDQASHLvrslahade 926
Cdd:cd00124 379 -NSFEQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSfidFPDNQDCLDliegkpLGIlSLLDEECLF--------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 927 argllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFllGHSHGTNWVEYNVAGWLNYTKQNpat 1006
Cdd:cd00124 449 --------------PKGTDATFLEKLYSAHGSHPRFFSK-----KRKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1007 qnaprllqdsqkkiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqiklQVDALIDT 1086
Cdd:cd00124 505 ----------------------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDT 529
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1087 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1166
Cdd:cd00124 530 LNSTQPHFVRCIKPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVR 580
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1167 MVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd00124 581 LPFDEFLKRYRILAPGATEKA-----SDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
448-1236 |
7.25e-113 |
|
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: 376.12 E-value: 7.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 448 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 527
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 528 TAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFS 605
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 606 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFgivpLSKPEEKQK 685
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 686 A----AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSL 761
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGN-------IEFEEGRNDNAASTVKDKEELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 762 EELSSAIfkhqlkggtLQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIV 841
Cdd:smart00242 307 EELEKAL---------TKRKIKTGGEVITKPL---NVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 842 DTPGFQ----NpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqa 914
Cdd:smart00242 375 DIYGFEifevN----------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDwtfIDFFDNQDCID--------- 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 915 shLVRS-----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGT 986
Cdd:smart00242 436 --LIEKkppgiLSLLDEE----------CRFPKGTDQTFLEKLNQHH--------KKHPHFSKPKKKgrtEFIIKHYAGD 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 987 nwVEYNVAGWLnytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGM 1064
Cdd:smart00242 496 --VTYDVTGFL---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1065 aavkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLR 1144
Cdd:smart00242 550 ----------QFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPG-----------------------------DFDSSLVL 590
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1145 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:smart00242 591 HQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLR 665
|
810
....*....|..
gi 1907082217 1225 AGTLARLEEQRD 1236
Cdd:smart00242 666 PGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
429-1950 |
2.36e-109 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 385.20 E-value: 2.36e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 429 KLDHDGAILDVDEDDIEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVM 507
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPyRDLG-IYTDDII 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 508 HMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST-- 585
Cdd:COG5022 121 QSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnp 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 586 LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-- 663
Cdd:COG5022 200 ILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqn 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 664 ----NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAgatkEPLEEQDEAAea 739
Cdd:COG5022 280 pkdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGNI----EFKEDRNGAA-- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 740 grkQFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGG--TLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELF 817
Cdd:COG5022 347 ---IFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ--------------ALAIRDSLAKALYSNLF 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 818 TLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE--- 894
Cdd:COG5022 410 DWIVDRINKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsf 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 895 LAFDDLEPVADDSvaavdQASHLVRSLAHADEArgllwlleeeALVPGATEDALLDRLFSYYgPQEGDKKGQSPLLRSSK 974
Cdd:COG5022 484 IDYFDNQPCIDLI-----EKKNPLGILSLLDEE----------CVMPHATDESFTSKLAQRL-NKNSNPKFKKSRFRDNK 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 975 prhFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLALRRAT 1054
Cdd:COG5022 548 ---FVVKHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGRFPTLG 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1055 SMrktfttgmaavkkkslciqIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceag 1134
Cdd:COG5022 609 SR-------------------FKESLNSLMSTLNSTQPHYIRCIKPNEEKSPW--------------------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1135 llQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDEKRAVEELLESLDLEKSSC 1214
Cdd:COG5022 643 --TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEELVIDSSKY 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1215 CLGLSRVFFRAGTLARLEEQRDEQTSRHLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWPWWKLFTT 1293
Cdd:COG5022 720 QIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYELKWRLFIK 798
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1294 VRPLIQVQLSEEQIRNKDEEIQQLRSKLEKV----EKERNELRLSSDRLETRISEltSELTDERNTGESASQLLDAETAE 1369
Cdd:COG5022 799 LQPLLSLLGSRKEYRSYLACIIKLQKTIKREkklrETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETIYLQSAQR 876
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1370 RLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKKRLQQELE 1445
Cdd:COG5022 877 VELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIEYVKLPEL 956
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1446 DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsELSQAHEET 1525
Cdd:COG5022 957 NKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EVAELQSAS 1032
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1526 QREKLQREKLQREKDMLLAEAFSLKQQME-EKDLdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAK--- 1601
Cdd:COG5022 1033 KIISSESTELSILKPLQKLKGLLLLENNQlQARY-------KALKLRRENSLL---DDKQLYQLESTENLLKTINVKdle 1102
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1602 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEvqlEEEYEDKQKALRE 1679
Cdd:COG5022 1103 VTNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLE---ALPSPPPFAALSE 1179
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1680 KRELESKL----STLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLknqleESEFTCAA 1752
Cdd:COG5022 1180 KRLYQSALydekSKLSSSEVNdlkNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNL-----NKKFDTPA 1254
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1753 AVKarkameveMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLeeDQEDMNEL-MKKHKAAVAQASRDmaqmnDLQ 1831
Cdd:COG5022 1255 SMS--------NEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI--NVGLFNALrTKASSLRWKSATEV-----NYN 1319
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1832 AQIEESNKEKQELQEklqaLQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKT-QVKRLENlasrlketmeklteeR 1910
Cdd:COG5022 1320 SEELDDWCREFEISD----VDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKS---------------R 1380
|
1530 1540 1550 1560
....*....|....*....|....*....|....*....|.
gi 1907082217 1911 DQRAAAENR-EKEQNKRLQRQLRDTKEEMSELARKEAEASR 1950
Cdd:COG5022 1381 YDPADKENNlPKEILKKIEALLIKQELQLSLEGKDETEVHL 1421
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
456-1224 |
2.74e-108 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 362.75 E-value: 2.74e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 456 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGT-SGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDF 612
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 613 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL---------NHLAENNVFGIvplskpeek 683
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 684 qKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEaaeagrkqFARHEWAQKAAYLLGCSLEE 763
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV--------PDDTENLQKAASLLGIDSTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 764 LSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVD 842
Cdd:pfam00063 303 LEKALCKRRIKTGRETVSKPQ------------NVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLD 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 843 TPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVR 919
Cdd:pfam00063 371 IYGFEIFEKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEwtfIDFGDNQPCID-----------LIE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 920 S-----LAHADEArgllwlleeeALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEY 991
Cdd:pfam00063 434 KkplgiLSLLDEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEY 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 992 NVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkks 1071
Cdd:pfam00063 494 NVEGFLEKNK-DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS------- 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1072 lciQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSR 1151
Cdd:pfam00063 559 ---QFKESLGELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNG 606
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1152 LLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:pfam00063 607 VLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
468-1224 |
2.76e-100 |
|
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: 338.67 E-value: 2.76e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFgIVPLSKPEEKQKAAQQFSKLQAAMKV 699
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 700 LAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT-- 777
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDG--------TEEADKAAHLLGVNSSDLLKALLKPRIKVGRew 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 778 LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----Npewgg 853
Cdd:cd01377 312 VTKGQNKEQ--------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 854 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----DDLEPVADdsvaavdqashLVRS-----LAHA 924
Cdd:cd01377 373 -----SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-----------LIEKpnmgiLSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 925 DEargllwlleeEALVPGATEDALLDRLFSYygpQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLnyTK-QN 1003
Cdd:cd01377 437 DE----------ECVFPKATDKTFVEKLYSN---HLGKSKNFKKPKPKKSEAHFILKHYAGD--VEYNIDGWL--EKnKD 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1004 PATQNAPRLLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDAL 1083
Cdd:cd01377 500 PLNENVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NKL 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1084 IDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGY 1163
Cdd:cd01377 556 MTTLRSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKGF 606
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1164 PDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
2.04e-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: 310.40 E-value: 2.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVAsshkgRKDHNIPGELER-QLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF--GIVPLSkpeeKQKAAQQFSKLQAAM 697
Cdd:cd14920 160 GANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 698 KVLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGT 777
Cdd:cd14920 236 HIMGFSHEEILSMLKVVSSVLQFGNISFKKE--RNTDQAS------MPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 778 --LQRSTsfrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgs 854
Cdd:cd14920 308 dyVQKAQ--------------TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 855 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaAVDQASHLVRSLAHADEargl 930
Cdd:cd14920 372 ----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIdfglDLQPCID----LIERPANPPGVLALLDE---- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 931 lwlleeEALVPGATEDALLDRLfsyygpqEGDKKGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYTKQNPATQ 1007
Cdd:cd14920 440 ------ECWFPKATDKTFVEKL-------VQEQGSHSKFQKPRQLKdkaDFCIIHYAGK--VDYKADEWL-MKNMDPLND 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1008 NAPRLLQDSQKKIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqiklqvDALIDTI 1087
Cdd:cd14920 504 NVATLLHQSSDRFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATL 570
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1088 KRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHM 1167
Cdd:cd14920 571 RNTNPNFVRCIIPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 621
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1168 VFSEFRRRFDVLAPHLTKKhgrnyIVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14920 622 VFQEFRQRYEILTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
467-1224 |
2.81e-84 |
|
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: 292.31 E-value: 2.81e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIA----GTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNV--FGIVPLSkpeeKQKAAQQFSKLQAAMK 698
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 699 VLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtl 778
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKE--RNTDQAS------MPDNTAAQKVCHLMGINVTDFTRSILTPRIKVG-- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 779 qrsTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsarg 857
Cdd:cd14921 307 ---RDVVQKAQ-------TKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 858 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeE 937
Cdd:cd14921 372 -SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDE----------E 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 938 ALVPGATEDALLDRLFSyygPQEGDKKGQSPLLRSSKPRHFLLghsHGTNWVEYNVAGWLNyTKQNPATQNAPRLLQDSQ 1017
Cdd:cd14921 441 CWFPKATDKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASS 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1018 KKIISNLFLGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQIKLQVDALIDTIKRSKMHFVHC 1097
Cdd:cd14921 514 DKFVADLWKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRC 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1098 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1177
Cdd:cd14921 581 IIPNHEKRSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYE 631
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082217 1178 VLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
1.38e-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: 290.34 E-value: 1.38e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIA-----GTSGTKVFSV-------EKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLD 611
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAaskpkGSGAVPHPAVnpavligELEQQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 612 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVF---GIVPLSKPEEkqkaAQ 688
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 689 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAI 768
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQE--RNNDQAT------LPDNTVAQKIAHLLGLSVTDMTRAF 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 769 FKHQLKGGtlqrstsfRQGPEESGLGEGTKLSalecLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQ 847
Cdd:cd14911 308 LTPRIKVG--------RDFVTKAQTKEQVEFA----VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 848 NPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFD----DLEPVADdsvaavdqashLVrslah 923
Cdd:cd14911 376 IFELN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-----------LI----- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 924 aDEARGLLWLLEEEALVPGATEDALLDRLFSYYgpqegdkkGQSPLLRSSKPR---HFLLGHSHGTnwVEYNVAGWLnYT 1000
Cdd:cd14911 434 -DKPGGIMALLDEECWFPKATDKTFVDKLVSAH--------SMHPKFMKTDFRgvaDFAIVHYAGR--VDYSAAKWL-MK 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1001 KQNPATQNAPRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQV 1080
Cdd:cd14911 502 NMDPLNENIVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQL 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1081 DALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYR 1160
Cdd:cd14911 565 AKLMDTLRNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICR 615
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1161 QGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
7.23e-82 |
|
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: 285.38 E-value: 7.23e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTK------VFS---VEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQA 615
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKkdqssiALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 616 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQA 695
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQ----DEAAeagrkqfarhewAQKAAYLLGCSLEELSSAIFKH 771
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQasmpDDTA------------AQKVCHLLGMNVTDFTRAILSP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 772 QLKGGtlqrsTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPE 850
Cdd:cd14932 306 RIKVG-----RDYVQKAQ-------TQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 851 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargl 930
Cdd:cd14932 374 LN------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDE---- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 931 lwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPlLRSSKPRHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAP 1010
Cdd:cd14932 444 ------ECWFPKATDKSFVEKVVQEQG---NNPKFQKP-KKLKDDADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1011 RLLQDSQKKIISNLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQIKLQVDALIDTIKRS 1090
Cdd:cd14932 511 TLLNQSTDKFVSELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNT 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1091 KMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFS 1170
Cdd:cd14932 577 NPNFVRCIIPNHEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 627
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1171 EFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
9.91e-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: 9.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKvfsvEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALedqimqaNPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDATLRTELHLN------HLAENNVFGIvplskpeEKQKAAQQFSKL 693
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 694 QAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQL 773
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGT--------ENADKAAFLMGINSSELVKGLIHPRI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 774 KGGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEW 851
Cdd:cd14929 301 KVGNeyVTRSQNIEQVTYAVG--------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDY 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 852 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaddsvAAVDQASHLVRSLAHADEARGLL 931
Cdd:cd14929 367 N------SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDW-------------VSIDFGLDLQACIDLIEKPMGIF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 932 WLLEEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKPR------HFLLGHSHGTnwVEYNVAGWLNYTKqNPA 1005
Cdd:cd14929 428 SILEEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKNK-DLL 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1006 TQNAPRLLQDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqiklqvDALID 1085
Cdd:cd14929 498 NETVVAVFQKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL--------NKLMT 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1086 TIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPD 1165
Cdd:cd14929 557 NLKSTAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICREGFPN 607
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1166 HMVFSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
4.44e-80 |
|
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: 280.06 E-value: 4.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 623
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLlqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 624 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAAMKVLAIS 703
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 704 PEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqrsTS 783
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKE--RNTDQAS------MPDNTAAQKVSHLLGINVTDFTRGILTPRIKVG-----RD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 784 FRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaSFEE 862
Cdd:cd14919 306 YVQKAQ-------TKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 863 LCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEALVPG 942
Cdd:cd14919 373 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDE----------ECWFPK 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 943 ATEDALLDRLFSYYGPQegdKKGQSPLLRSSKPrHFLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLLQDSQKKIIS 1022
Cdd:cd14919 443 ATDKSFVEKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1023 NLFlgRAGSATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDTIKRSKMHFVHCFLPVA 1102
Cdd:cd14919 516 ELW--KDVDRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNH 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1103 EGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1182
Cdd:cd14919 583 EKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPN 633
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082217 1183 LTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14919 634 SIPKG-----FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
467-1224 |
6.49e-76 |
|
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: 268.09 E-value: 6.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNSLALSHGELekqllqanpiLEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKaaQQFSKLQAA 696
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETMEA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEagrkqfarHEWAQKAAYLLGCSLEELSSAIFKHQLKGG 776
Cdd:cd15896 239 FRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPD--------NTAAQKVCHLMGMNVTDFTRAILSPRIKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 777 T--LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGg 853
Cdd:cd15896 311 RdyVQKAQTQEQ--------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 854 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwl 933
Cdd:cd15896 376 -----SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDE------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 leeEALVPGATEDALLDRLFSyygpqegdKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQ 1007
Cdd:cd15896 444 ---ECWFPKATDKSFVEKVLQ--------EQGTHP--KFFKPKKlkdeadFCIIHYAGK--VDYKADEWL-MKNMDPLND 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1008 NAPRLLQDSQKKIISNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqiklQVDALIDT 1086
Cdd:cd15896 508 NVATLLNQSTDKFVSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMAT 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1087 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1166
Cdd:cd15896 572 LRNTNPNFVRCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNR 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1167 MVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd15896 623 IVFQEFRQRYEILTPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
467-1224 |
3.94e-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: 262.58 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQ 614
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATKTGGTLedqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 615 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN------HLAENNVFGIVPLSKPEEkqkaaq 688
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 689 qFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAI 768
Cdd:cd14927 235 -LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGT--------ESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 769 FKHQLKGGtlQRSTSFRQGPEESGLGEGtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQN 848
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVYAVG----------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGFEI 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 849 PEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDqashLVrslahaDEAR 928
Cdd:cd14927 374 FEFN------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDF---GLDLQACID----LI------EKPL 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 929 GLLWLLEEEALVPGATEDALLDRLFSYYgpqegdkKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTK 1001
Cdd:cd14927 435 GILSILEEECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPdkkrkyeAHFEVVHYAGV--VPYNIVGWLDKNK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1002 qNPATQNAPRLLQDSQKKIISNLFLGRAGSATVlsgsiAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqiklqvD 1081
Cdd:cd14927 506 -DPLNETVVAIFQKSQNKLLATLYENYVGSDST-----EDPKSGVKEKRKKAAS----FQT-VSQLHKENL--------N 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1082 ALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQ 1161
Cdd:cd14927 567 KLMTNLRATQPHFVRCIIPNETKTPG-----------------------------VMDPFLVLHQLRCNGVLEGIRICRK 617
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1162 GYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
3.77e-72 |
|
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: 256.69 E-value: 3.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaeNNVFGIVPLSKPE---EKQKAAQQFSKLQAAM 697
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQAF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 698 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEA--AEAGrkqfarhewaQKAAYLLGCSLEELSSAIFKHQLKG 775
Cdd:cd14909 237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQdgEEEG----------GRVSKLFGCDTAELYKNLLKPRIKV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GTlQRSTSFRQgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGGsa 855
Cdd:cd14909 307 GN-EFVTQGRN-----------VQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG-- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 856 rgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQASHLVRSLAHADEargllwlle 935
Cdd:cd14909 373 ----FEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDF---GMDLLACIDLIEKPMGILSILEE--------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 936 eEALVPGATEDALLDRLFSyygpqegDKKGQSPLLRSSKP-------RHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQN 1008
Cdd:cd14909 437 -ESMFPKATDQTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDT 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1009 APRLLQDSQKKIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQIKLQVDALIDTIK 1088
Cdd:cd14909 506 VVDQFKKSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLR 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1089 RSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPpgdpceaGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMV 1168
Cdd:cd14909 566 STQPHFVRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMM 616
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1169 FSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14909 617 YPDFKMRYKILNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
468-1224 |
4.41e-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: 253.43 E-value: 4.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAGT------SGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdlakkKDSKMKGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---A 696
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGG 776
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKTAYLMGLNSSDLLKALCFPRVKVG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 777 TlqrstsfrqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsar 856
Cdd:cd14913 310 N-----------EYVTKGQ-TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 857 gaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEE 936
Cdd:cd14913 374 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 937 EALVPGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQD 1015
Cdd:cd14913 439 ECMFPKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLYQK 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1016 SQKKIISNLFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqiklqvDALIDTIKRSKMHF 1094
Cdd:cd14913 514 SSNRLLAHLYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHPHF 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1095 VHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1174
Cdd:cd14913 572 VRCIIPNETKTPGA-----------------------------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQ 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1175 RFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
467-1224 |
1.69e-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: 251.94 E-value: 1.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGT-SGTKVFSV-----EKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSpKGRKEPGVpgeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQkaaQQFSKLQAAMKVL 700
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESLRVL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 701 AISPEEQKTCWLILASIYHLGAAGATKEplEEQDEAAeagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQLKGGtlqr 780
Cdd:cd14930 238 GFSHEEITSMLRMVSAVLQFGNIVLKRE--RNTDQAT------MPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 781 sTSFRQGPEesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQNPEWGgsargaS 859
Cdd:cd14930 306 -RDYVQKAQ-------TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 860 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEPVADDSVAAVDQASHLVRSLAHADEargllwlleeEAL 939
Cdd:cd14930 372 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDE----------ECW 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 940 VPGATEDALLDRLfsyygpqeGDKKGQSPllRSSKPRH------FLLGHSHGTnwVEYNVAGWLnYTKQNPATQNAPRLL 1013
Cdd:cd14930 442 FPKATDKSFVEKV--------AQEQGGHP--KFQRPRHlrdqadFSVLHYAGK--VDYKANEWL-MKNMDPLNDNVAALL 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1014 QDSQKKIISNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqiklqvDALIDTIKRSK 1091
Cdd:cd14930 509 HQSTDRLTAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTN 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1092 MHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1171
Cdd:cd14930 572 PSFVRCIVPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1172 FRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14930 623 FRQRYEILTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
468-1181 |
2.33e-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: 244.92 E-value: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQAAMKV 699
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGVDD-------AKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 700 LAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQ 779
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVAD--------EAVSTAASLLGCNANDLMLALSTRKIQAGGDK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 780 RSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQH-SLCSMMIVDTPGFQnpewggSARGA 858
Cdd:cd01383 300 IVKKL------------TLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE------SFQKN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 859 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLEpvadDSVAAVDqashLVRS-----LAHADEargllwl 933
Cdd:cd01383 362 SFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLD----LIEKkplglISLLDE------- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 leeEALVPGATEDALLDRLFSYYGPQEGDKKGQSpllrsskpRHFLLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLL 1013
Cdd:cd01383 427 ---ESNFPKATDLTFANKLKQHLKSNSCFKGERG--------GAFTIRHYAGE--VTYDTSGFLE--------KNRDLLH 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1014 QDsqkkiISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMH 1093
Cdd:cd01383 486 SD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLENTTPH 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1094 FVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1173
Cdd:cd01383 552 FIRCIKPNNKQLPGV-----------------------------FDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFA 602
|
....*...
gi 1907082217 1174 RRFDVLAP 1181
Cdd:cd01383 603 RRYGFLLP 610
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
467-1224 |
7.66e-68 |
|
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: 243.78 E-value: 7.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEKQKAaqqfsklQA 695
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvpnpkeYHWVSQGVTVVDNMDDGEELQIT-------DV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 775
Cdd:cd14934 233 AFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTT--------EVADKVAHLMGLNSGELQKGITRPRVKV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 853
Cdd:cd14934 305 GNefVQKGQNMEQCNNSIG--------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 854 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQashlvrslahADEARGLLWL 933
Cdd:cd14934 370 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDF---GLDLQACIDL----------LEKPMGIFSI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 LEEEALVPGATE--------DALLDRLFSYYGPQEGDKKGQSPllrsskprHFLLGHSHGTnwVEYNVAGWLNYTKqNPA 1005
Cdd:cd14934 432 LEEQCVFPKATDatfkaalyDNHLGKSSNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK-DPL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1006 TQNAPRLLQDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQIKLQVDALID 1085
Cdd:cd14934 501 NETVVGLFQKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNKLMT 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1086 TIKRSKMHFVHCFLpvaegwpgeprsassrrvsssseldlpPGDPCEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPD 1165
Cdd:cd14934 555 TLHSTAPHFVRCIV---------------------------PNEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKGFPN 605
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1166 HMVFSEFRRRFDVLAPHLTKKHgrnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
468-1224 |
1.59e-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: 243.09 E-value: 1.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAG---------TSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 618
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAigdrskkdqTPGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 619 ASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 695
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDML----LITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAagaTKEPLEEQDEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 775
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGN---MKFKQKQREEQAEPDGT-----EEADKSAYLMGLNSADLLKGLCHPRVKV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 853
Cdd:cd14917 309 GNeyVTKGQNVQQVIYATG--------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 854 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWL 933
Cdd:cd14917 374 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---GMDLQACIDLI----------EKPMGIMSI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 LEEEALVPGATEDALLDRLFSYYGPQEGDKkgQSPLLRSSKPR-HFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 1012
Cdd:cd14917 436 LEEECMFPKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGL 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1013 LQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqiklqvDALIDTIKRSKM 1092
Cdd:cd14917 511 YQKSSLKLLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1093 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1172
Cdd:cd14917 570 HFVRCIIPNETKSPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1173 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14917 621 RQRYRILNPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
467-1224 |
4.20e-66 |
|
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: 238.38 E-value: 4.20e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTG-SILV-------AVnpykelpiYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 539 DQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTkvFSVEKwQAL--STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14883 73 NQSVIISGESGAGKTETTKLILQYLC--AVTNNH--SWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACG--DATLRTELHL---NHLAENNVFGIVPLSKPEEKQKaaqqFS 691
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 692 KLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSA-IFK 770
Cdd:cd14883 224 HLRLAMNVLGIPEEMQEGIFSVLSAILHLGN-------LTFEDIDGETGALTVEDKEILKIVAKLLGVDPDKLKKAlTIR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 771 HQLKGGTLqrsTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPE 850
Cdd:cd14883 297 QINVRGNV---TEIPLKVQE----------ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 851 WGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDLEPVADdsvaAVDQASHLVRSLAhADEA 927
Cdd:cd14883 364 VN------SFEQLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDNQECLD----LIEKPPLGILKLL-DEEC 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 928 RgllwlleeealVPGATEDALLDRLFSYYGPQEGDKKgqsPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNytkQNPATQ 1007
Cdd:cd14883 433 R-----------FPKGTDLTYLEKLHAAHEKHPYYEK---PDRRRWKTE-FGVKHYAGE--VTYTVQGFLD---KNKDTQ 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1008 --NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALI 1084
Cdd:cd14883 493 qdDLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLV 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1085 DTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYP 1164
Cdd:cd14883 556 DVLSATQPWYVRCIKPNSLKEPN-----------------------------VFDDELVLAQLRYAGMLEIIRIRKEGFP 606
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1165 DHMVFSEFRRRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14883 607 IHLTFKEFVDRYLCLDPRARSADHK-----ETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
468-1224 |
2.66e-65 |
|
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: 236.55 E-value: 2.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLK 774
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQNLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 775 GGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 852
Cdd:cd14910 310 VGNeyVTKGQTVQQVYNAVG--------------ALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 853 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLW 932
Cdd:cd14910 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 933 LLEEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 1012
Cdd:cd14910 437 ILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKVEAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETVVGL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1013 LQDSQKKIISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 1092
Cdd:cd14910 513 YQKSSMKTLALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHP 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1093 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1172
Cdd:cd14910 573 HFVRCIIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1173 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14910 624 KQRYKVLNASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
468-1224 |
2.80e-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: 236.50 E-value: 2.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAgTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTLedqiiqanplLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLL----LISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELssaifkhqLK 774
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAGYLMGLNSAEM--------LK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 775 GGTLQRstsFRQGPEESGLGEGTKlSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgs 854
Cdd:cd14923 301 GLCCPR---VKVGNEYVTKGQNVQ-QVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 855 argaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLL 934
Cdd:cd14923 375 ----SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIFSIL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 935 EEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQ 1014
Cdd:cd14923 438 EEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQ 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1015 DSQKKIISNLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKMHF 1094
Cdd:cd14923 514 KSSLKLLSFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1095 VHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1174
Cdd:cd14923 575 VRCLIPNETKTPG-----------------------------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1175 RFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14923 626 RYRILNASAIPE-GQ---FIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
469-1186 |
8.66e-65 |
|
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: 234.49 E-value: 8.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 469 VLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIaVNPFKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKPEEkqkaaqqFSKLQAAMKV 699
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 700 LAISPEEQKTCWLILASIYHLG----AAGATKEPLEEQDEAAEagrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQlkg 775
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniefSKGEEDDSSVPKDEKSE---------FHLKAAAELLMCDEKALEDALCKRV--- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 gtlqrstsfRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSA 855
Cdd:cd01384 303 ---------IVTPDGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 856 RGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF----------DDLEPVADDSVAAVDQASHLVRSlahad 925
Cdd:cd01384 368 KTNSFEQFCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSYiefvdnqdvlDLIEKKPGGIIALLDEACMFPRS----- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 926 eargllwlleeealvpgaTEDALLDRLFSYYgpqeGDKKgqspllRSSKPR----HFLLGHSHGTnwVEYNVAGWLNYTK 1001
Cdd:cd01384 443 ------------------THETFAQKLYQTL----KDHK------RFSKPKlsrtDFTIDHYAGD--VTYQTDLFLDKNK 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1002 QN--PATQNaprLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQIKLQ 1079
Cdd:cd01384 493 DYvvAEHQA---LLNASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQ 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1080 VDALIDTIKRSKMHFVHCFLPVAEgwpgeprsassrrvsssseldLPPGDPCEAGLLQldvsllraQLRGSRLLDAMRMY 1159
Cdd:cd01384 540 LQELMETLNTTEPHYIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRIS 590
|
730 740
....*....|....*....|....*..
gi 1907082217 1160 RQGYPDHMVFSEFRRRFDVLAPHLTKK 1186
Cdd:cd01384 591 CAGYPTRKPFEEFLDRFGLLAPEVLKG 617
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
468-1224 |
9.84e-65 |
|
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: 234.62 E-value: 9.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIA---------GTSGTKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAvtgekkkeeAASGKMQGTLED-QIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA- 695
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 --AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQL 773
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLTSLNSADLLKALCYPRV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 774 KGGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEW 851
Cdd:cd14915 309 KVGNeyVTKGQTVQQVYNSVG--------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 852 GgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLL 931
Cdd:cd14915 375 N------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEF-------------IDFGMDLAACIELIEKPMGIF 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 932 WLLEEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPR 1011
Cdd:cd14915 436 SILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPA-KGKAEAHFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVG 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1012 LLQDSQKKIISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSK 1091
Cdd:cd14915 512 LYQKSGMKTLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTH 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1092 MHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSE 1171
Cdd:cd14915 572 PHFVRCLIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1172 FRRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
469-1224 |
2.38e-64 |
|
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: 233.47 E-value: 2.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 469 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSS 548
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 549 GSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQ--------ALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQgtledqiiSANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnhLAENNVFGIVPLSKPEEKQKAAQQFSKLQA---AM 697
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 698 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGT 777
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKALCYPRVKVGN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 778 lqrstsfrqgpEESGLGEgTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 857
Cdd:cd14918 311 -----------EYVTKGQ-TVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN----- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 858 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLWLLEEE 937
Cdd:cd14918 374 -SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPLGIFSILEEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 938 ALVPGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQ 1017
Cdd:cd14918 440 CMFPKATDTSFKNKLYDQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1018 KKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqiklQVDALIDTIKRSKMHFVHC 1097
Cdd:cd14918 516 MKTLASLFSTYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRC 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1098 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1177
Cdd:cd14918 575 IIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYK 625
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1907082217 1178 VLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
468-1224 |
1.28e-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: 231.54 E-value: 1.28e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL----------LEAFGNSPTIMNGSATRFSQILSLDFDQAGQ 617
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQGTLedqiisanplLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 618 VASASIQTMLLEKLRVARRPASEATFNVFYYLlacgDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA-- 695
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQI----TSNKKPELIEMLLITTNPYDYPFVSQGEISVASIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 -AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLK 774
Cdd:cd14912 238 sAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGT--------EVADKAAYLQSLNSADLLKALCYPRVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 775 GGT--LQRSTSFRQGPEESGlgegtklsalecleGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWG 852
Cdd:cd14912 310 VGNeyVTKGQTVEQVTNAVG--------------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 853 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFddlepvaddsvaaVDQASHLVRSLAHADEARGLLW 932
Cdd:cd14912 376 ------SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTF-------------IDFGMDLAACIELIEKPMGIFS 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 933 LLEEEALVPGATEDALLDRLFSYYGPQEGDKKgQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 1012
Cdd:cd14912 437 ILEEECMFPKATDTSFKNKLYEQHLGKSANFQ-KPKVVKGKAEAHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGL 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1013 LQDSQKKIISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 1092
Cdd:cd14912 513 YQKSAMKTLAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHP 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1093 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1172
Cdd:cd14912 575 HFVRCIIPNETKTPG-----------------------------AMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1173 RRRFDVLAPHLTKKhGRnyiVVDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
468-1181 |
1.63e-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: 228.02 E-value: 1.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLATIA--GTSGTKVFSVEKWQAL-------STLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQV 618
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAaiGDRSKKENPNANKGTLedqiiqaNPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 619 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdaTLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQA--- 695
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKG 775
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGT--------EDADKSAYLMGLNSADLLKGLCHPRVKV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GT--LQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGg 853
Cdd:cd14916 310 GNeyVTKGQSVQQ--------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 854 sargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDSVAAVDQAshlvrslahaDEARGLLWL 933
Cdd:cd14916 375 -----SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---GMDLQACIDLI----------EKPMGIMSI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 LEEEALVPGATEDALLDRLF-SYYGPQEGDKKGQSplLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRL 1012
Cdd:cd14916 437 LEEECMFPKASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGL 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1013 LQDSQKKIISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqiklqvDALIDTIKRSKM 1092
Cdd:cd14916 512 YQKSSLKLMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHP 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1093 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1172
Cdd:cd14916 572 HFVRCIIPNERKAPG-----------------------------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDF 622
|
....*....
gi 1907082217 1173 RRRFDVLAP 1181
Cdd:cd14916 623 RQRYRILNP 631
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
467-1181 |
5.28e-62 |
|
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: 226.58 E-value: 5.28e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 541
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 542 IVLLGSSGSGKTTSFQHLVQYLATIagTSGTKVFSVEKWQALST------------------LLEAFGNSPTIMNGSATR 603
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARI--TSGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 604 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLnhlaENNVFGIVPLSK--PE 681
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 682 EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAG--ATKEPLEEQDEAAeagrkqfarHEWAQKAAYLLGC 759
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDfeSENDTTVLEDATT---------LQSLKLAAELLGV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 760 SLEELSSAIFKHQL--KGGTLQRstsfrqgPEESGLGEgTKLSALeclegmASGLYSELFTLLISLVNRALKSSQHSLCS 837
Cdd:cd14890 306 NEDALEKALLTRQLfvGGKTIVQ-------PQNVEQAR-DKRDAL------AKALYSSLFLWLVSELNRTISSPDDKWGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 838 MMIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADDSVAAVDQA 914
Cdd:cd14890 372 IGVLDIYGFEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFNDNQACLELIEGKVNGK 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 915 SHLVRSLahaDEARGLLWLLEEEALVpgatedALLDRLF--SYYGPQEGDKKGQSPLLRSSK---PRHFLLGHSHGTnwV 989
Cdd:cd14890 446 PGIFITL---DDCWRFKGEEANKKFV------SQLHASFgrKSGSGGTRRGSSQHPHFVHPKfdaDKQFGIKHYAGD--V 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 990 EYNVAGwlnYTKQNPATqnaprlLQDSQKKIIsnlflgragsatvlsgsiagleggsqlalrrATSMRktfttgmaAVKK 1069
Cdd:cd14890 515 IYDASG---FNEKNNET------LNAEMKELI-------------------------------KQSRR--------SIRE 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1070 KSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagLLQLDVSLlraQLRG 1149
Cdd:cd14890 547 VSVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGK--------------------------FDGLDCLR---QLKY 597
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082217 1150 SRLLDAMRMYRQGYP---DHMVFseFrRRFDVLAP 1181
Cdd:cd14890 598 SGMMEAIQIRQQGFAlreEHDSF--F-YDFQVLLP 629
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
467-1181 |
9.92e-62 |
|
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: 225.43 E-value: 9.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAennVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 706 EQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRkqfarhEWAQKAAYLLGCSLEELSSAIFKHQLKGGTLQRSTSFR 785
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGD------QGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 786 qgpeesglgegtKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsargaSFEELCH 865
Cdd:cd14903 310 ------------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 866 NYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLepvADDS-VAAVDQASHLVRSLAHADEARgllwlleeealvPGAT 944
Cdd:cd14903 372 NYANEKLQQKFTQDVFKTVQIEYEEEGIRWAHIDF---ADNQdVLAVIEDRLGIISLLNDEVMR------------PKGN 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 945 EDALLDRLFSYYgpqeGDKKGQSPLLRSSKPRhFLLGHSHGTnwVEYNVAGWLNYTKQNpatqnaprLLQD-------SQ 1017
Cdd:cd14903 437 EESFVSKLSSIH----KDEQDVIEFPRTSRTQ-FTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1018 KKIISNLFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHC 1097
Cdd:cd14903 502 KPFLRMLFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRC 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1098 FLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1177
Cdd:cd14903 566 IKPNSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFW 616
|
....
gi 1907082217 1178 VLAP 1181
Cdd:cd14903 617 LFLP 620
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
467-1100 |
2.89e-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: 220.88 E-value: 2.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPslLVLST---RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 543
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGH--VLISVnpfKDLG-IYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 544 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVeKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASA 621
Cdd:cd01378 78 ISGESGAGKTEASKRIMQYIAAVSGGSESEVERV-KDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 622 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL------NHLAENNVFGIVPLSKpeekqkaAQQFSKLQA 695
Cdd:cd01378 157 HITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFDVDGIDD-------AADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKeplEEQDEAAEAGRKQfarhewAQKAAYLLGCSLEELSSAIFKHQLKG 775
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQFAE---DEEGNAAISDTSV------LDFVAYLLGVDPDQLEKALTHRTIET 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GTLQRST-SFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGF----QNp 849
Cdd:cd01378 301 GGGGRSVyEVPLNVEQ----------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFeifeKN- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 850 ewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDlEPVADdsvaavdqashLVRS----- 920
Cdd:cd01378 370 ---------SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNN-KIICD-----------LIEEkppgi 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 921 LAHADEArgllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPllRSSKPRHFLLGHSHGTnwVEYNVAGwlnYT 1000
Cdd:cd01378 429 FAILDDA---------CLTAGDATDQTFLQKLNQLFSNHPHFECPSGH--FELRRGEFRIKHYAGD--VTYNVEG---FL 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1001 KQNPAT--QNAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkkslciQIKL 1078
Cdd:cd01378 493 DKNKDLlfKDLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT----------KFKN 540
|
650 660
....*....|....*....|..
gi 1907082217 1079 QVDALIDTIKRSKMHFVHCFLP 1100
Cdd:cd01378 541 SANALVETLMKKQPSYIRCIKP 562
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
467-1181 |
3.13e-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: 214.81 E-value: 3.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGpSLLVlstrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTG-SILV-------AVnpyqilpiYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 539 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGtsgtKVFSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01381 73 DQCVVISGESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH------LAENNVFGIvplskpeEKQKAAQQF 690
Cdd:cd01381 148 VIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 691 SKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGaTKEPLEEQDEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFK 770
Cdd:cd01381 221 ADIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIK-FEATVVDNLDASE-----VRDPPNLERAAKLLEVPKQDLVDALTT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 771 HQL--KGGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLCSMMIVDTPG 845
Cdd:cd01381 295 RTIftRGETVVSPLSAEQ--------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 846 FQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsVAAVDQAShlvrSLA 922
Cdd:cd01381 361 FENFEVN------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMN----IMS 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 923 HADEargllwlleeEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLLRSSKPRHFLlghshGTnwVEYNVAGWLNytKQ 1002
Cdd:cd01381 429 LIDE----------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KN 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1003 NPA-TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQIKLQVD 1081
Cdd:cd01381 490 RDTfSADLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLD 539
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1082 ALIDTIKRSKMHFVHCFLPVAEGWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQ 1161
Cdd:cd01381 540 QLMKTLSACQPFFVRCIKPNEYKKPML-----------------------------FDRELCVRQLRYSGMMETIRIRKA 590
|
730 740
....*....|....*....|
gi 1907082217 1162 GYPDHMVFSEFRRRFDVLAP 1181
Cdd:cd01381 591 GYPIRHTFEEFVERYRVLVP 610
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
468-1026 |
2.28e-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: 211.86 E-value: 2.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTkvFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLSPSDDS--DLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNH----------LAENNVFGIVplskpEEKQKAAQQFSKLQAA 696
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDpdchrilrddNRNRPVFNDS-----EELEYYRQMFHDLTNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISPEEQKTCWLILASIYHLgaAGATKEPLEEQDEAaeagrkQFARHEWAQKAAYLLGCSLEELSSAIF--KHQLK 774
Cdd:cd14897 235 MKLIGFSEEDISVIFTILAAILHL--TNIVFIPDEDTDGV------TVADEYPLHAVAKLLGIDEVELTEALIsnVNTIR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 775 GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-----HSLCSMMIVDTPGFQNp 849
Cdd:cd14897 307 GERIQSWKSLRQ--------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFEN- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 850 ewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAfdDLEPVADDSV------------AAVDQASHL 917
Cdd:cd14897 372 -----FKINSFDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVlelffkkplgilPLLDEESTF 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 918 vrslahadeargllwlleeealvPGATEDALLDRLFSYYGPqegdkkgqSPLLRSSKPRHFLLGHSHGTNWVEYNVAGWL 997
Cdd:cd14897 445 -----------------------PQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFL 493
|
570 580
....*....|....*....|....*....
gi 1907082217 998 NYTKQNpATQNAPRLLQDSQKKIISNLFL 1026
Cdd:cd14897 494 EKNRDN-LSSDIVGCLLNSNNEFISDLFT 521
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
468-899 |
4.38e-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: 210.86 E-value: 4.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYG-ASLLHTYAGpslLVLStrgapAV--------YSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQ 538
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCG---IVLV-----AInpyedlpiYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 539 DQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01380 74 NQSIIVSGESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAA 696
Cdd:cd01380 152 RIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISPEEQKTCWLILASIYHLG-----AAGATKEPLEEQDEAaeagrkqfarhewAQKAAYLLGCSLEELSSAIFKH 771
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGnveikATRNDSASISPDDEH-------------LQIACELLGIDESQLAKWLCKR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 772 QLK--GGTLQRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQ-HSLCSMM-IVDTPGFQ 847
Cdd:cd01380 298 KIVtrSEVIVKPLTLQQ--------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFE 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 848 NPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDD 899
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 ... |
468-1184 |
1.93e-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: 209.65 E-value: 1.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGpSLL--VLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIG-SILasVNPYQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATIAGTS-----GTKVFSVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVA 619
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVEQAILESSpIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 620 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhLAEN----NVFGIVPLSKPEEKqkaaQQFSKLQA 695
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLS-TPENyhylNQSGCVEDKTISDQ----ESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAgatkepleeqdEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkg 775
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNI-----------EFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL------- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 gtLQRSTSFRqGPEESglgegTKLS---ALECLEGMASGLYSELFTLLISLVNRALKSSQHsLCSMMIVDTPGFQNPEWG 852
Cdd:cd14873 298 --TQRSMFLR-GEEIL-----TPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 853 gsargaSFEELCHNYAQDRLQRLFHERTF-LQELERYKEDnieLAFDDLEPVadDSVAAVDQASHLVRSLAHADEargll 931
Cdd:cd14873 369 ------HFEQFNINYANEKLQEYFNKHIFsLEQLEYSREG---LVWEDIDWI--DNGECLDLIEKKLGLLALINE----- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 932 wlleeEALVPGATEDALLDRLFSyygpqeGDKKGQSPLlrssKPR--HFLLGHSHGTNWVEYNVAGWLnytKQNPAT--Q 1007
Cdd:cd14873 433 -----ESHFPQATDSTLLEKLHS------QHANNHFYV----KPRvaVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrD 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1008 NAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQIKLQVDALIDT 1086
Cdd:cd14873 495 DLLNLLRESRFDFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMAT 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1087 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1166
Cdd:cd14873 550 LSSSNPFFVRCIKPNMQKMPD-----------------------------QFDQAVVLNQLRYSGMLETVRIRKAGYAVR 600
|
730
....*....|....*...
gi 1907082217 1167 MVFSEFRRRFDVLAPHLT 1184
Cdd:cd14873 601 RPFQDFYKRYKVLMRNLA 618
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
467-1224 |
4.50e-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: 208.45 E-value: 4.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQTM 626
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTE---------LHLNHLAENNVFGivplskpeekQKAAQQFSKLQAAM 697
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 698 KVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKqfARHEWaqkAAYLLGCSLEELSSAIfkhqlkggt 777
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGQEGVSVGSD--AEIQW---VAHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 778 LQRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarg 857
Cdd:cd01387 294 TFKVTETRRERIFTPL---TIDQALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN----- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 858 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVAddsvaavdqasHLVrslahADEARGLLWLL 934
Cdd:cd01387 366 -SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQPVI-----------NLI-----SKKPVGILHIL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 935 EEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllRSSKPR----HFLLGHSHGTNWveYNVAGWLNYTKqNPATQNAP 1010
Cdd:cd01387 429 DDECNFPQATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQLRQDVL 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1011 RLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQIKLQ--VDALIDTIK 1088
Cdd:cd01387 496 ELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQLLEKME 555
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1089 RSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMV 1168
Cdd:cd01387 556 RCNPWFVRC---------------------------LKPNHKKEPMLFDMDVVM--AQLRYSGMLETIRIRKEGYPVRLP 606
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1169 FSEFRRRFDvlapHLTKKHGRNYIVVDEKRAVeELLESLDLEKSSCCLGLSRVFFR 1224
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 ... |
468-905 |
4.62e-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: 207.90 E-value: 4.62e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLaTIAGTSGTKVFSvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTML 627
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 628 LEKLRVARRPASEATFNVFYYLLA-------CGDATLRTELHLNHLAEnnvFGIVPLSKpEEKQKAAQQFSKLQAAMKVL 700
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQN---DGLTVQDI-VNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 701 AISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAaeagRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQL--KGGTL 778
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDIEFTEVESNHQTDK----SSRISNPEALNNVAKLLGIEADELQEALTSHSVvtRGETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 779 QRSTSFRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNpewggsA 855
Cdd:cd01379 312 IRNNTVEE--------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFEN------F 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 856 RGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL---AFDDLEPVAD 905
Cdd:cd01379 372 QKNSFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
467-1180 |
2.60e-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: 203.09 E-value: 2.60e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIagtsGTKVFSVEKWQALSTL--LEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 624
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSL----YQDQTEDRLRQPEDVLpiLESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAEN----NVFGIVPLSKPEEkqkaAQQFSKLQAAMKVL 700
Cdd:cd14896 156 HYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 701 AISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAgrkqfarhEWA--QKAAYLLGCSLEELSSAIFKHQLKGGTL 778
Cdd:cd14896 231 GLCAEELTAIWAVLAAILQLGNICFSSSERESQEVAAVS--------SWAeiHTAARLLQVPPERLEGAVTHRVTETPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 779 QRSTSFrqgPEEsglgegtklSALECLEGMASGLYSELFTLLISLVNRAL--KSSQHSLCSMMIVDTPGFQnpewggSAR 856
Cdd:cd14896 303 RVSRPL---PVE---------GAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 857 GASFEELCHNYAQDRLQRLFHERTFLQELERYKEDniELAFDDLEPVADDSVA--AVDQASHLVRSLahadeargllwll 934
Cdd:cd14896 365 VNGLEQLCINLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLdlLVDQPHSLLSIL------------- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 935 EEEALVPGATEDALLDRLFSYYGPQEGDKKGQSPLlrsskPRhFLLGHSHGTnwVEYNVAGWLNYTKQ--NPATQNaprL 1012
Cdd:cd14896 430 DDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----PV-FTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---M 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1013 LQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRatsmrktfttgmaavKKKSLCIQIKLQVDALIDTIKRSKM 1092
Cdd:cd14896 499 LAQSQLQLVGSLF----------------QEAEPQYGLGQ---------------GKPTLASRFQQSLGDLTARLGRSHV 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1093 HFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEF 1172
Cdd:cd14896 548 YFIHCLNPNPGKLPG-----------------------------LFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAF 598
|
....*...
gi 1907082217 1173 RRRFDVLA 1180
Cdd:cd14896 599 LARFGALG 606
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
464-903 |
8.33e-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: 201.62 E-value: 8.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 464 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLSTRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTS--GTKVfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFD 613
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 614 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF---GIVPL-SKPEEKQkaAQQ 689
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 690 FSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagatkepLEEQDEAAeagrkqfARHEWA--------QKAAYLLGCSL 761
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHLGN-------LEFTYDHE-------GGEESAvvkntdvlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 762 EELSSAI-FKHQLKGGtlQRSTSFrqgpeesgLG-EGTKLSALEclegMASGLYSELFTLLISLVNRALKSSQHSLCSMM 839
Cdd:cd14879 303 EDLETSLtYKTKLVRK--ELCTVF--------LDpEGAAAQRDE----LARTLYSLLFAWVVETINQKLCAPEDDFATFI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 840 -IVDTPGFQNPewgGSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA----FDDLEPV 903
Cdd:cd14879 369 sLLDFPGFQNR---SSTGGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPatsyFDNSDCV 434
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
469-1179 |
2.14e-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: 200.52 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 469 VLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIVL 544
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 545 LGSSGSGKTTSFQHLVQYLATIAgtSGTKVFSVEKWQaLSTLLEAFGNSPTIMNGSATRFSQILSLDFdQAGQVASASIQ 624
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL----NHLAENNVFGivplsKPEEKQKAAQQFSKLQAAMKVL 700
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLldpgKYRYLNNGAG-----CKREVQYWKKKYDEVCNAMDMV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 701 AISPEEQKTCWLILASIYHLGAAgatkePLEEQDEaaEAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqlkgGTLQR 780
Cdd:cd14889 234 GFTEQEEVDMFTILAGILSLGNI-----TFEMDDD--EALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTC 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 781 STSFRQGpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHS---LCSMMIVDTPGFQNPEWGgsarg 857
Cdd:cd14889 297 TVTFTRG--EQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 858 aSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD-------DSVAAVDQASHLvrslahadea 927
Cdd:cd14889 370 -RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDlflnkpiGILSLLDEQSHF---------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 928 rgllwlleeealvPGATEDALLDRLFSYYGPQEGDKKGQspllrsSKPRHFLLGHSHGTnwVEYNVAGWLNYTKQN-PAT 1006
Cdd:cd14889 439 -------------PQATDESFVDKLNIHFKGNSYYGKSR------SKSPKFTVNHYAGK--VTYNASGFLEKNRDTiPAS 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1007 QNAprLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQIKLQVDALIDT 1086
Cdd:cd14889 498 IRT--LFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEK 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1087 IKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDH 1166
Cdd:cd14889 561 MFAASPHFVRCIKPNHVKVPG-----------------------------QLDSKYIQDQLRYNGLLETIRIRREGFSWR 611
|
730
....*....|...
gi 1907082217 1167 MVFSEFRRRFDVL 1179
Cdd:cd14889 612 PSFAEFAERYKIL 624
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
468-1181 |
5.20e-53 |
|
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: 200.29 E-value: 5.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGS 547
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLaTIAGTSGTKVfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd01385 82 SGSGKTESTNFLLHHL-TALSQKGYGS-GVEQ-TILGAgpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd01385 159 YLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQ-PEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 706 EQKTCWLILASIYHLGAAgATKEPLEEQDEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIF--KHQLKGGTLQRSTS 783
Cdd:cd01385 238 TQRQIFSVLSAVLHLGNI-EYKKKAYHRDESVTVGNP-----EVLDIISELLRVKEETLLEALTtkKTVTVGETLILPYK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 784 FrqgPEesglgegtklsALECLEGMASGLYSELFTLLISLVNRAL---KSSQHSLC-SMMIVDTPGFQNPEWGgsargaS 859
Cdd:cd01385 312 L---PE-----------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDFGNN------S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 860 FEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVadDSVAAVdqasHLVRSLAHadearGLLWLLEEEAL 939
Cdd:cd01385 372 FEQFCINYANEHLQYYFNQHIFKLEQEEYKKEGIS--WHNIEYT--DNTGCL----QLISKKPT-----GLLCLLDEESN 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 940 VPGATEDALLDRLFS-------YYGPQEgdkkgqspllrssKPRHFLLGHSHGTnwVEYNVAGW----LNYTKQNPATqn 1008
Cdd:cd01385 439 FPGATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQIKDFreknLDLMRPDIVA-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1009 aprLLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRRATSMRktfttGMAAVKKKS 1071
Cdd:cd01385 502 ---VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDRTTKSL-----LHLHKKKKP 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1072 LCIQIKLQV--DALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRG 1149
Cdd:cd01385 574 PSVSAQFQTslSKLMETLGQAEPFFIRCIKSNAEKKP-----------------------------LRFDDELVLRQLRY 624
|
730 740 750
....*....|....*....|....*....|..
gi 1907082217 1150 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1181
Cdd:cd01385 625 TGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
468-1181 |
4.46e-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: 196.70 E-value: 4.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGtsGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEE 706
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 707 QKTCWLILASIYHLGAAgatkePLEEQDEAAEAgrkqFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRQ 786
Cdd:cd14904 240 QRTLFKILSGVLHLGEV-----MFDKSDENGSR----ISNGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 787 gpeESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRALkSSQHSLCSMMI--VDTPGFQNPEWGGsargasFEELC 864
Cdd:cd14904 302 ---ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFC 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 865 HNYAQDRLQRLFHERTFLQELERYKEDNieLAFDDLEPVADDSVAAVDQASHLVRSLAHaDEARGllwlleeealvPGAT 944
Cdd:cd14904 372 INYANEKLQQKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEVIDGKMGIIALMN-DHLRQ-----------PRGT 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 945 EDALLDRLFSYYGPQEGDKKGQSPllrSSKPRHFLLGHSHGTnwVEYNVAGWLNytKQNPATQN-APRLLQDSQKKIISN 1023
Cdd:cd14904 438 EEALVNKIRTNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1024 LFlgraGSATVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAE 1103
Cdd:cd14904 511 LF----GSSEAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNAN 567
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1104 GWPGEprsassrrvsssseldlppgdpceagllqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1181
Cdd:cd14904 568 KSPTE-----------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
468-1181 |
5.52e-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: 5.52e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLL-VLSTRGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIVL 544
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIaVNPFKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 545 LGSSGSGKTTSFQHLVQYLATiAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQ-------- 614
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 615 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIV--PLSKPEEKQKAAQQFS 691
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADakPISIDMSSFEPHLKFR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 692 KLQ--------------------AAMKVLAISPEEQKTCWLILASIYHLGAAgatkepLEEQDEAAEAGRKQFA-RHEWA 750
Cdd:cd14888 238 YLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNI------LFENNEACSEGAVVSAsCTDDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 751 QKAAYLLGCSLEELSSAifkhqLKGGTLQRSTSFRQGPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNRAL-K 829
Cdd:cd14888 312 EKVASLLGVDAEDLLNA-----LCYRTIKTAHEFYTKPLRVDEAEDVR-------DALARALYSCLFDKVVERTNESIgY 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 830 SSQHSLCSMMIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLE-PVADDSV 908
Cdd:cd14888 380 SKDNSLLFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDfPDNQDCV 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 909 AAVDQASHLVrsLAHADEargllwlleeEALVPGATEDALLDRLFSYYGpqeGDKKGQSPllrSSKPRHFLLGHSHGTnw 988
Cdd:cd14888 452 DLLQEKPLGI--FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP-- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 989 VEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVK 1068
Cdd:cd14888 512 VKYCSDGFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKK 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1069 KKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPgeprsassrrvsssSELDlppgdpceagllQLDVSllrAQLR 1148
Cdd:cd14888 564 FVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFD------------RISVN---EQLK 614
|
730 740 750
....*....|....*....|....*....|...
gi 1907082217 1149 GSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1181
Cdd:cd14888 615 YGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
468-1186 |
6.81e-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: 197.42 E-value: 6.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 537
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATI-----AGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQILSL 610
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 611 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAE---NNVFGIVPLSKPEEKQKAA 687
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 688 QQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEA-AEAGRKQFArhewaqKAAYLLGCSLEELSS 766
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAvTAASRFHLA------KCAELMGVDVDKLET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 767 AIFKHQLKGGtlQRSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN---------RALKSSQHSLCS 837
Cdd:cd14902 316 LLSSREIKAG--VEVMVLKLTPEQ----------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELAT 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 838 MMIVDTPGFQNPEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVaddsVAAVDqa 914
Cdd:cd14902 384 IGILDIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDwknISYPSNAAC----LALFD-- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 915 shlvrslahaDEARGLLWLLEEEALVPGATEDALLDRLFSYYGPQEgdkkgqspllrsskprHFLLGHSHGTnwVEYNVA 994
Cdd:cd14902 452 ----------DKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVE 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 995 GWLNyTKQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLC 1073
Cdd:cd14902 504 QFVE-KNTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVS 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1074 IQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLL 1153
Cdd:cd14902 563 AQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPG-----------------------------IFDRERMVEQMRSVGVL 613
|
730 740 750
....*....|....*....|....*....|...
gi 1907082217 1154 DAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1186
Cdd:cd14902 614 EAVRIARHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
470-1180 |
1.10e-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: 195.36 E-value: 1.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 470 LHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 540
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 541 SIVLLGSSGSGKTTSFQHLVQYLATI----AGTSGTKVF-----SVEKWQALS-TLLEAFGNSPTIMNGSATRFSQILSL 610
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATAsklaKGASTSKGAanaheSIEECVLLSnLILEAFGNAKTIRNDNSSRFGKYIQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 611 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAEnnvFGIVPLSKPEEKQKA--AQ 688
Cdd:cd14892 162 HYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 689 QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagATKEPLEEQDEAAeagrKQFARHEWAQKAAYLLGCSLEELSSAI 768
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVF----AQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 769 FKHQLKGGtlqRSTSFRQ--GPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRAlkSSQHSLCSMMIVDTP-- 844
Cdd:cd14892 313 VTQTTSTA---RGSVLEIklTARE----------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtf 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 845 ----------GFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaaV 911
Cdd:cd14892 378 spfigildifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----L 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 912 DQASHLvrslahadeargllwlleeeALVPGATEDALLDR-------LFSYYgpQEGDKKGQSpllrSSKPR----HFLL 980
Cdd:cd14892 447 IQKKPL--------------------GLLPLLEEQMLLKRkttdkqlLTIYH--QTHLDKHPH----YAKPRfecdEFVL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 981 GHSHGTnwVEYNVAGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktF 1060
Cdd:cd14892 501 RHYAGD--VTYDVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------F 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1061 TTgmaavkkkslciqiklQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvsssSELDLPPGDPCEagllqldv 1140
Cdd:cd14892 537 RT----------------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE-------- 572
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907082217 1141 sLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1180
Cdd:cd14892 573 -LVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
220-308 |
1.47e-51 |
|
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MYO18 protein and related domains. MYO18 (also known as myosin XVIIIA, KIAA0216, MysPDZ), a member of the myosin superfamily, is involved in regulating cell protrusion and migration, and Golgi trafficking and morphology, and is required for myoblast adhesion and muscle integrity. The MYO18A/MRCK/LRAP35a complex regulates actomyosin retrograde flow in cell protrusion and migration; the PtdIns(4)P/GOLPH3/MYO18A/F-actin complex is a hub for signals that regulate Golgi trafficking function. The MYO18A PDZ domain binds p190Rho-guanine nucleotide exchange factor (p190RhoGEF), Golgin45, and leucine repeat adaptor protein 1 (Lurap1, also known as Lrap35a). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MYO18-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467229 [Multi-domain] Cd Length: 90 Bit Score: 176.73 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRTTMLDRAPE-GQAYRRVVHFAEPGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 1907082217 299 SGDSVRLKVQ 308
Cdd:cd06747 81 SGDTVTLKVQ 90
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
468-1224 |
3.72e-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: 193.45 E-value: 3.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATIAGTSGtkvfSVEKwQALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASI 623
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTN----GVEQ-RVLLAnpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGAST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 624 QTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlaenNVFGIVPLSKPEEKQKA--AQQFSKLQAAMKVLA 701
Cdd:cd14872 155 ENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSS-----AAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 702 ISPEEQKTCWLILASIYHLGAAGatkepLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGgtlQ 779
Cdd:cd14872 230 FDDADINNVMSLIAAILKLGNIE-----FASGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTSRlmEIKG---C 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 780 RSTSFRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVNRALKSSQHSL-CSMMIVDTPGFQNPEWGgsarga 858
Cdd:cd14872 302 DPTRIPLTPAQ----------ATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 859 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEPVADdsvaavdqashLVrslahadEAR--GLLWL 933
Cdd:cd14872 366 SFEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-----------LI-------EKKqpGLMLA 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 934 LEEEALVPGATEDALLDRLfsyyGPQEGDKKGQSPLLRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLL 1013
Cdd:cd14872 428 LDDQVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLL 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1014 QDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMH 1093
Cdd:cd14872 501 SSSKNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPH 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1094 FVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQLDVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1173
Cdd:cd14872 548 YIRC---------------------------VKPNQEKRARLFDGFMSL--EQLRYAGVFEAVKIRKTGYPFRYSHERFL 598
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1174 RRFDVLAPHLTKKHGRnyivvDEKRAVEELLESLDLEKSSCCLGLSRVFFR 1224
Cdd:cd14872 599 KRYRFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
468-1222 |
4.80e-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: 187.69 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 537
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW----QALST--LLEAFGNSPTIMNGSATRFSQILSLD 611
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 612 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSKPEEKQKAAQQFS 691
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 692 KLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKepleeqdEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH 771
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-------KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 772 QLKGGTLQRSTSFRqgPEESGLGEgtklsaleclEGMASGLYSELFTLLISLVNRALK--SSQHSLCSMMIVDTPGF--- 846
Cdd:cd14901 315 EIRAGGEYITMPLS--VEQALLTR----------DVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFeif 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 847 -QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAFDDLePVADDSVAAVDQASHLVRSLahAD 925
Cdd:cd14901 383 aTN----------SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-PNNDACVAMFEARPTGLFSL--LD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 926 EargllwlleeEALVPGATEDALLDrlfSYYgpqegDKKGQSPLLRSSK----PRHFLLGHSHGTnwVEYNVAGWLNYTK 1001
Cdd:cd14901 450 E----------QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKlqqgKRQFVIHHYAGA--VCYATDGFCDKNK 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1002 QNPATqNAPRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQIKLQVD 1081
Cdd:cd14901 510 DHVHS-EALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLS 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1082 ALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDpcEAGLLQLDVSLLRAQLRGSRLLDAMRMYRQ 1161
Cdd:cd14901 542 SLLEVLNATEPHFIRC---------------------------IKPND--VLSPSEFDAKRVLEQLRCSGVLEAVKISRS 592
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1162 GYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDEKRAVEELLESLDLEKSSCCLGLSRVF 1222
Cdd:cd14901 593 GYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
467-1179 |
8.74e-49 |
|
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: 187.16 E-value: 8.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 537
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAG----------------TSGTKVFSVEKwQALST--LLEAFGNSPTIMNG 599
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQqeqnseevltltssirATSKSTKSIEQ-KILSCnpILEAFGNAKTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 600 SATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHL-NHLAENNVFgivPL 677
Cdd:cd14907 160 NSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD---YL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 678 SKPE----EKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEqDEAAEAGRKQFarhewAQKA 753
Cdd:cd14907 237 KKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDD-NSPCCVKNKET-----LQII 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 754 AYLLGCSLEELSSAIFKHQLKGGTlQRSTSfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRAL-- 828
Cdd:cd14907 311 AKLLGIDEEELKEALTTKIRKVGN-QVITS--------------PLSKKECinnRDSLSKELYDRLFNWLVERLNDTImp 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 829 ------KSSQHSLCSMMIVDTPGFQNPEwggsarGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-----LAF 897
Cdd:cd14907 376 kdekdqQLFQNKYLSIGLLDIFGFEVFQ------NNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdylnqLSY 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 898 DDLEPVAD--DS-----VAAVDQASHLvrslahadeargllwlleeealvPGATEDALLDRLFSYYGpqeGDKKGQSPll 970
Cdd:cd14907 450 TDNQDVIDllDKppigiFNLLDDSCKL-----------------------ATGTDEKLLNKIKKQHK---NNSKLIFP-- 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 971 RSSKPRHFLLGHSHGTnwVEYNVAGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsql 1048
Cdd:cd14907 502 NKINKDTFTIRHTAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1049 alrratsmrktfttgmAAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppg 1128
Cdd:cd14907 570 ----------------SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK------------------------ 609
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1129 dpcEAGLLQLDVSLLraQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1179
Cdd:cd14907 610 ---KADLFIQGYVLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
468-1180 |
6.41e-46 |
|
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: 178.99 E-value: 6.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 535
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 536 --SRQDQSIVLLGSSGSGKTTSFQHLVQYLA-----TIAGTSGTKVFSVEKWQALST--LLEAFGNSPTIMNGSATRFSQ 606
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 607 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvFGIVPLSKPE 681
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 682 EKQKAAQ---QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAA--GATKEPLEEQDEAAEAGRKQFARHEWAQKAAY- 755
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEDNGAASAPCRLASASPSSLTVQq 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 756 -------LLGCSLEELSSAIFKHQLKGGtlqrstsfrqgpEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVNRAL 828
Cdd:cd14895 314 hldivskLFAVDQDELVSALTTRKISVG------------GETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 829 KSSQHSLCS-----------MMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 897
Cdd:cd14895 382 PQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 898 DDLEpvaDDSVA--AVDQASHLVRSLAhaDEargllwlleeEALVPGATEDALLDRLFSYYGpqegDKKGQSPLLRSSKP 975
Cdd:cd14895 456 VDYE---DNSVCleMLEQRPSGIFSLL--DE----------ECVVPKGSDAGFARKLYQRLQ----EHSNFSASRTDQAD 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 976 RHFLLGHSHGTnwVEYNVAGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQLALRRATS 1055
Cdd:cd14895 517 VAFQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQPKLRRRSS 586
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1056 MRKTFTTGMaavkkkslciQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGl 1135
Cdd:cd14895 587 VLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRC---------------------------IKPNDESASD- 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082217 1136 lQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1180
Cdd:cd14895 629 -QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
468-889 |
2.71e-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: 172.82 E-value: 2.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIAGTSGTKVFS--VEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 624
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENnvfgivplskpeekqkaAQQFSKLQAAMKVLAISP 704
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 705 EEQKTCWLILASIYHLGAAgatkePLEEQDEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAI---FKHQLKGGTlqR 780
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGNI-----EFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSLttrVMQTTRGGA--K 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 781 STSFRQG--PEESGlgegtklSALECLegmASGLYSELFTLLISLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npewg 852
Cdd:cd01382 294 GTVIKVPlkVEEAN-------NARDAL---AKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN---- 356
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907082217 853 gsargaSFEELCHNYAQDRLQRLFHERTFLQELERYK 889
Cdd:cd01382 357 ------SFEQFCINYCNEKLQQFFNERILKEEQELYE 387
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
507-894 |
3.77e-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: 172.54 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 507 MHMFKGCRREDMAPHIYAVAQTAYRAMLMSR---QDQSIVLLGSSGSGKTTSFQHLVQYLAT-----IAGTSGTKVFSVE 578
Cdd:cd14891 40 KSDYINTPLDPCPPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 579 KWQALST-----------LLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVF 646
Cdd:cd14891 120 KRKLSVTslderlmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 647 YYLLACGDATLRTELHlnhlaennvfgivpLSKPEEKQKAAQ-------------QFSKLQAAMKVLAISPEEQKTCWLI 713
Cdd:cd14891 200 YQLLAGASAELLKELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 714 LASIYHLGAAGATKEPLEEQD--EAAEAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqlkggtLQRSTSFRqgpees 791
Cdd:cd14891 266 LAGLLHLGNIEFDEEDTSEGEaeIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR------ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 792 GLGEGTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEwggsaRGASFEELCHNYA 868
Cdd:cd14891 325 GETFTIKRNAREAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYA 399
|
410 420
....*....|....*....|....*.
gi 1907082217 869 QDRLQRLFHERTFLQELERYKEDNIE 894
Cdd:cd14891 400 NEALQATFNQQVFIAEQELYKSEGID 425
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1275-1969 |
7.77e-44 |
|
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: 175.75 E-value: 7.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1275 NIKKNKGVKDWPWWKLFTTVRPLIQVQLSEEQIRNKDE-EIQQLRSKLEKVEKERNELrlssdrlETRISELTSELtder 1353
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1354 ntgESASQLLDAETAERLRTEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1430
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1431 REVDF----TKKRLQQELEdKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1506
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1507 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSqeSKDEA 1586
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1587 --SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1664
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1665 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrKDLKRTKALLADAQIMLDHLKNN-----APSKREIAQL 1739
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 KN------QLEESeftCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1813
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1814 KAAVAQ---------ASRDMAQMND-LQAQIEESNKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1883
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1884 FEKTQ----VKRLENLASRLKETMEKLTEER---DQRAAAENREKEQNKRLQRQLRDTKEEMSelarkEAEASRKKheLE 1956
Cdd:pfam01576 985 QESRErqaaNKLVRRTEKKLKEVLLQVEDERrhaDQYKDQAEKGNSRMKQLKRQLEEAEEEAS-----RANAARRK--LQ 1057
|
730
....*....|...
gi 1907082217 1957 MDLESLEAANQSL 1969
Cdd:pfam01576 1058 RELDDATESNESM 1070
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
468-1195 |
1.60e-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: 170.10 E-value: 1.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 533
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 534 LMSR----QDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGS 600
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQT-NILLESFGNARTLRNDN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 601 ATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDAtlrtelhlnhlaennvfgivplskp 680
Cdd:cd14900 159 SSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAI-GAS------------------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 681 eEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGA---AGATKEPLEEQDEAAEAGRKQFARhewaQKAAYLL 757
Cdd:cd14900 213 -EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNltfEHDENSDRLGQLKSDLAPSSIWSR----DAAATLL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 758 GCSLEELSSAIFKHQLKGGTLQRSTsfrqgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALK----- 829
Cdd:cd14900 288 SVDATKLEKALSVRRIRAGTDFVSM---------------KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddss 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 830 SSQHSLCSMMIVDTPGF----QNpewggsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE---LAFDDLEp 902
Cdd:cd14900 353 KSHGGLHFIGILDIFGFevfpKN----------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDwkyVEFCDNQ- 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 903 vadDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSyygpqegdKKGQSPLLRSSKPRH----F 978
Cdd:cd14900 422 ---DCVNLISQRPTGILSL--IDE----------ECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglF 478
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 979 LLGHSHGTnwVEYNVAGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrk 1058
Cdd:cd14900 479 TIVHYAGH--VEYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------- 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1059 tfttgmaavkkkslCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCEAGLLQL 1138
Cdd:cd14900 513 --------------GLQFKEQLTTLLETLQQTNPHYVRC---------------------------LKPNDLCKAGIYER 551
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1139 DVSLlrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA----PHLTKKHGrnYIVVD 1195
Cdd:cd14900 552 ERVL--NQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSLAraknRLLAKKQG--TSLPD 608
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
468-1192 |
1.94e-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: 165.15 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATiagTSGTKVF----------SVEKWQALST-LLEAFGNSPTIMNGSATRFSQILSLDFDQ 614
Cdd:cd14906 82 GESGSGKTEASKTILQYLIN---TSSSNQQqnnnnnnnnnSIEKDILTSNpILEAFGNSRTTKNHNSSRFGKFLKIEFRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 615 A-GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDATLRTELHLNH--------LAENNVFGIV------PLS 678
Cdd:cd14906 159 SdGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 679 KPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagaTKEPLEEQDEAAEAGRKQFARHEWAQkAAYLLG 758
Cdd:cd14906 239 NHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLG----NIEFEEDSDFSKYAYQKDKVTASLES-VSKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 759 CSLEELSSAIFKHQLKGGTlqRSTSFRQgPEESGLGEGTKlsaleclEGMASGLYSELFTLLISLVNR-----------A 827
Cdd:cd14906 314 YIESVFKQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTR-------DALSKSLYVRLFKYIVEKINRkfnqntqsndlA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 828 LKSSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELA---FDDlepvA 904
Cdd:cd14906 384 GGSNKKNNLFIGVLDIFGFEN------LSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----N 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 905 DDSVAAVDQASHLVRSLAHaDEArgllwlleeeaLVPGATEDALLDRLFSYYgpqegdKKGQSPLLRSSKPRHFLLGHSH 984
Cdd:cd14906 454 KECIELIEKKSDGILSLLD-DEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 985 GTnwVEYNVAGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGM 1064
Cdd:cd14906 516 GD--VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTV 573
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1065 AAvkkkslciQIKLQVDALIDTIKRSKMHFVHCFLPvaegwpgeprsassrrvssssELDLPPGDpceagllqLDVSLLR 1144
Cdd:cd14906 574 SG--------QFLEQLNQLIQTINSTSVHYIRCIKP---------------------NQTMDCNN--------FNNVHVL 616
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1907082217 1145 AQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1192
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
467-1180 |
7.16e-39 |
|
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: 156.51 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIV 543
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 544 LLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSveKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDF-DQAGQVASAS 622
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 623 IQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgiVPLSKPEEKQKAA-----QQFSKLQAAM 697
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 698 KVLAISPEEQKTCWLILASIYHLGAAGATKepLEEQDEAAEAGRKQFarhewaQKAAYLLGCSLEELSSAIFK--HQLKG 775
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTA--LTEADSAFVSDLQLL------EQVAGMLQVSTDELASALTTdiQYFKG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GTLQRSTSFRQGPEESGLgegtklsaleclegMASGLYSELFTLLISLVNRALKsSQHSLCSMM-----IVDTPGFQNpe 850
Cdd:cd14878 308 DMIIRRHTIQIAEFYRDL--------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEE-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 851 wggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE-------------LAFDDLEPVADDSVaaVDQASHL 917
Cdd:cd14878 371 ----FQKNEFEQLCVNMTNEKMHHYINEVLFLQEQTECVQEGVTmetayspgnqtgvLDFFFQKPSGFLSL--LDEESQM 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 918 VRSLAHADEARgllwlleeealVPGATEDALLDRLFSYYGPQEGD--KKGQSPLlrsskprhFLLGHSHGTnwVEYNVAG 995
Cdd:cd14878 445 IWSVEPNLPKK-----------LQSLLESSNTNAVYSPMKDGNGNvaLKDQGTA--------FTVMHYAGR--VMYEIVG 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 996 WLNYTKqNPATQNAPRLLQDSQKKIISNLFlgRAGSATVlsgsiaglegGSQLalrratsmrktfttgmaavkKKSLC-I 1074
Cdd:cd14878 504 AIEKNK-DSLSQNLLFVMKTSENVVINHLF--QSKLVTI----------ASQL--------------------RKSLAdI 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1075 QIKLQvdalidtikRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLD 1154
Cdd:cd14878 551 IGKLQ---------KCTPHFIHCIKPNNSKLPD-----------------------------TFDNFYVSAQLQYIGVLE 592
|
730 740
....*....|....*....|....*.
gi 1907082217 1155 AMRMYRQGYPDHMVFSEFRRRFDVLA 1180
Cdd:cd14878 593 MVKIFRYGYPVRLSFSDFLSRYKPLA 618
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
470-1224 |
4.42e-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: 155.19 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 470 LHTLRQRYGA--------SLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 541
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 542 IVLLGSSGSGKTTSFQHLVQYLATI------AGTSGTKvfsvEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQA 615
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVsdrrhgADSQGLE----ARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 616 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDATLRTELHlnhlaennvfgivplSKPEEKQKAAQQFSKLQA 695
Cdd:cd14887 160 GKLTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQK---------------SSAGEGDPESTDLRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKQFARHEWAQKAAYLLgcSLEELSSAIFKHQLKG 775
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSVSVGCEETAADRSHSS--EVKCLSSGLKVTEASR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 776 GTLQRSTSFRQGPEESGLGEGTKLS-----------------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSM 838
Cdd:cd14887 301 KHLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsffdldgAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 839 MIVDTP--------------GFQNPEWGGSARgasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL-----AFDD 899
Cdd:cd14887 381 SDEDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQnqdcsAFPF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 900 LEPVADDSVAAVDQASHLvrSLAHADEARGLLWLLEEEALVPGATEDALLdrlfsyygpqegdkkgQSPLLRSSKPRHFL 979
Cdd:cd14887 458 SFPLASTLTSSPSSTSPF--SPTPSFRSSSAFATSPSLPSSLSSLSSSLS----------------SSPPVWEGRDNSDL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 980 LGHShgtnwVEYNVAGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLAL 1050
Cdd:cd14887 520 FYEK-----LNKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYT 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1051 RRATSMRKTFTTGMAAvKKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGwpgeprsassrrvsssseldlppgdp 1130
Cdd:cd14887 588 RLVGSKKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ-------------------------- 640
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1131 cEAGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDEKRAVEELLESLDLE 1210
Cdd:cd14887 641 -EAGI--FEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEIN 711
|
810
....*....|....
gi 1907082217 1211 KSSCCLGLSRVFFR 1224
Cdd:cd14887 712 SNSYTFGKTKIFFR 725
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
468-897 |
2.33e-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: 152.37 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 537
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 538 QDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALSTL---------LEAFGNSPTIMNGSATRFSQIL 608
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGKLSIMdrvlqsnpiLEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 609 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNvfgivpLSKPEEKQKAAQ 688
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGG------LQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 689 -------------QFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAagATKEPLEEqDEAAEAGrkQFARHEWAQKAAY 755
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQ--LEFESKEE-DGAAEIA--EEGNEKCLARVAK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 756 LLGCSLEELSSAIFKHQLKGGTLQRSTSFrqgpeesglgegTKLSALECLEGMASGLYSELFTLLISLVNRALK--SSQH 833
Cdd:cd14908 311 LLGVDVDKLLRALTSKIIVVRGKEITTKL------------TPHKAYDARDALAKTIYGALFLWVVATVNSSINweNDKD 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 834 SLCSMMIVDTPGFQNPEWGgsargaSFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 897
Cdd:cd14908 379 IRSSVGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF 436
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
467-897 |
2.66e-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: 151.93 E-value: 2.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 542
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 543 VLLGSSGSGKTTSFQHLVQYLATIAG--TSGTKVFSVEKWQAL----STLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAspTSWESHKIAERIEQRilnsNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 617 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELhlnHLAENNVFGIVPLSkpeEKQKAAQQFSKLQAA 696
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQW---HLPEGAAFSWLPNP---ERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRKQFARhewaqKAAYLLGCSLEELSSAIFKHQLKGG 776
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTKESVR-----TSALLLKLPEDHLLETLQIRTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 777 TLQRstSFRQgpeesglgegtKLSALEC---LEGMASGLYSELFTLLISLVNRALKSSQHSLCSMM-IVDTPGFQN-PEw 851
Cdd:cd14880 310 KQQQ--VFKK-----------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPE- 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082217 852 ggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELAF 897
Cdd:cd14880 376 ------NSLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
467-1176 |
4.15e-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: 151.79 E-value: 4.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 535
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 536 SRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKW-------------QALST--LLEAFGNSPTIMNGS 600
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESIsppaspsrttieeQVLQSnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 601 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDATLRTELHLNHLAEN-NVFGI 674
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 675 VPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEA----AEAGRKQFARHEWA 750
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVfadeARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 751 QKAAYLLGCSLEELSSAIFKHQLKGGtlqrSTSFRQGPEESGLGEGTKLSALEClegmasglYSELFTLLISLVNRALK- 829
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRWLHAS----NETLVVGVDVAHARNTRNALTMEC--------YRLLFEWLVARVNNKLQr 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 830 --------------SSQHSLCSMMIVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIEL 895
Cdd:cd14899 389 qasapwgadesdvdDEEDATDFIGLLDIFGFED------MAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 896 AFDDLEpvadDSVAAVDQASHlvrslahadEARGLLWLLEEEALVPGATEDALLDRlfsYYgpQEGDKKGQSPLLRSS-- 973
Cdd:cd14899 463 SFVDFP----NNRACLELFEH---------RPIGIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFRSApl 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 974 --KPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQLALR 1051
Cdd:cd14899 525 iqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGGRTRR 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1052 RATSmrktfttgmaAVKKKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPC 1131
Cdd:cd14899 599 RAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRC---------------------------IKPNDSH 641
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1907082217 1132 EAGLLQldVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1176
Cdd:cd14899 642 VGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
402-1280 |
1.72e-36 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 150.95 E-value: 1.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 402 LVHRDgfSLASQLKSEELSLPEGKarvkldhdgaILDVDEDDIEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGAS 480
Cdd:PTZ00014 56 LVLPG--STGEKLTLKQIDPPTNS----------TFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 481 LLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHL 559
Cdd:PTZ00014 124 QIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 560 VQYLAtiAGTSGTKVFSVEK--WQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRP 637
Cdd:PTZ00014 204 MRYFA--SSKSGNMDLKIQNaiMAA-NPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 638 ASEATFNVFYYLLACGDATLRTELHLNHLAENNVfgIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASI 717
Cdd:PTZ00014 281 DDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKY--INPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 718 YHLGAAGATKEPLEEQDEAAEAGRKQFarhEWAQKAAYLLGCSLEELS-SAIFKHQLKGGTLQRStsfRQGPEESglgEG 796
Cdd:PTZ00014 359 LLLGNVEIEGKEEGGLTDAAAISDESL---EVFNEACELLFLDYESLKkELTVKVTYAGNQKIEG---PWSKDES---EM 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 797 TKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQ----NpewggsargaSFEELCHNYAQDRL 872
Cdd:PTZ00014 430 LKDS-------LSKAVYEKLFLWIIRNLNATIEPPGGFKVFIGMLDIFGFEvfknN----------SLEQLFINITNEML 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 873 QRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV--DQashlvrSLAhadeargllwlleeealvP 941
Cdd:PTZ00014 493 QKNFVDIVFERESKLYKDEGIsteELEYTSNESVIDllcgkgKSVLSIleDQ------CLA------------------P 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 942 GATEDALLDRLFSYYGPQEGDKKGqspllRSSKPRHFLLGHSHGTnwVEYNVAGWLNYTKqNPATQNAPRLLQDSQKKII 1021
Cdd:PTZ00014 549 GGTDEKFVSSCNTNLKNNPKYKPA-----KVDSNKNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLV 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1022 SNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkkkslciqiklQVDALIDTIKRSKMHFVHCFLP 1100
Cdd:PTZ00014 621 RDLFEG----VEVEKGKLAkGQLIGSQF-------LN---------------------QLDSLMSLINSTEPHFIRCIKP 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1101 vaegwpgeprsassrrvssssELDLPPGDPCEAGLLqldvsllrAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1180
Cdd:PTZ00014 669 ---------------------NENKKPLDWNSSKVL--------IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLD 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1181 PHLTKKHGrnyivVDEKRAVEELLESLDLEKSSCCLGLSRVFFR---AGTLARLEEQRDEQTSRHLTLFQAACRGYLARQ 1257
Cdd:PTZ00014 720 LAVSNDSS-----LDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKR 794
|
890 900
....*....|....*....|...
gi 1907082217 1258 HFKKRkIQDLAIrcVQKNIKKNK 1280
Cdd:PTZ00014 795 KVRKN-IKSLVR--IQAHLRRHL 814
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
468-1191 |
9.32e-36 |
|
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: 145.81 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGpsLLVLSTRGAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIVLLGS 547
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSG--LVFLALNPYETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 548 SGSGKTTSFQHLVQYLatIAGTSGTKvfSVEK-WQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDqaGQVASASIQTM 626
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVFGIVPLSkpeekqkaaQQFSKLQAAMKVLAI-SPE 705
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQLS---------EKYKMTCSAMKSLGIaNFK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 706 EQKTCwliLASIYHLGAAGATKEpleeqdeaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QLKGGTLQRSTS 783
Cdd:cd14898 223 SIEDC---LLGILYLGSIQFVND-----------GILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 784 FRQgpeesglgegtklsALECLEGMASGLYSELFTLLISLVNRALK-SSQHSLCsmmIVDTPGFQNPEWGGsargasFEE 862
Cdd:cd14898 289 LKQ--------------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 863 LCHNYAQDRLQRLFHERTFLQELERYKEDNIElaFDDLEPVADDSVaavdqashlvrsLAHADEARGLLWLLEEEALVPG 942
Cdd:cd14898 346 LCINWTNEKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC------------IRDFEKPCGLMDLISEESFNAW 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 943 ATEDALLDRLFSYYGPQEGDKKGQSPLLrsskprhfllghSHGTNWVEYNVAGWLNYTKQNpatqnaprllqdSQKKIIS 1022
Cdd:cd14898 412 GNVKNLLVKIKKYLNGFINTKARDKIKV------------SHYAGDVEYDLRDFLDKNREK------------GQLLIFK 467
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1023 NLFLGRAGSatvlsgsiagleggsqlalrratsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVA 1102
Cdd:cd14898 468 NLLINDEGS-------------------------------------KEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNE 510
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1103 EGWPgeprsassrrvsssseldlppgdpceaglLQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1182
Cdd:cd14898 511 ECRP-----------------------------WCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGIT 561
|
730
....*....|...
gi 1907082217 1183 LTK----KHGRNY 1191
Cdd:cd14898 562 LFEvvdyRKGRTR 574
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
467-1182 |
1.57e-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: 137.80 E-value: 1.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 536
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 537 RQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQALS----------TLLEAFGNSPTIMNGSATRFSQ 606
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHpigqqilhafTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 607 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDATLRTELHLNHLAENnvFGIVPLSKPEEKQ 684
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 685 KA--AQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPleEQDEAAEAGRKQFARHEWA----QKAAYLLG 758
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDP--EGGKSVGGANSTTVSDAQScalkDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 759 CSLEELSSAIFKHQLKggtLQRSTSFRQGPEESGLGEGTKLSALECLEGMASGLYSELFTLLISLVN--------RALKS 830
Cdd:cd14893 317 AKLLEVEPVVLDNYFR---TRQFFSKDGNKTVSSLKVVTVHQARKARDTFVRSLYESLFNFLVETLNgilggifdRYEKS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 831 -----SQhslcSMMIVDTPGFQNPEwggsARGASFEELCHNYAQDRLQRLFHERTfLQELERYKEDNIELAFDDLepvAD 905
Cdd:cd14893 394 nivinSQ----GVHVLDMVGFENLT----PSQNSFDQLCFNYWSEKVHHFYVQNT-LAINFSFLEDESQQVENRL---TV 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 906 DSVAAVDQASHLVRSLAHaDEARGLLWLLEEEALVPGATEDALLDRLFS-------YYGPQEGDKKGQSPLLRSSKPR-H 977
Cdd:cd14893 462 NSNVDITSEQEKCLQLFE-DKPFGIFDLLTENCKVRLPNDEDFVNKLFSgneavggLSRPNMGADTTNEYLAPSKDWRlL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 978 FLLGHSHGTnwVEYNVAGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLSGSIAglEGGSQLALRRATS 1055
Cdd:cd14893 541 FIVQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAAASSE--KAAKQTEERGSTS 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1056 --MRKTFTTGMAAVK-KKSLCIQIKLQVDALIDTIKRSKMHFVHCflpvaegwpgeprsassrrvsssseldLPPGDPCE 1132
Cdd:cd14893 609 skFRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVC---------------------------IKPNETLE 661
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1133 AGLlqLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1182
Cdd:cd14893 662 EGV--FDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1314-2002 |
1.08e-31 |
|
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: 136.35 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1314 IQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLL----DAETAERLR----TEKEMKELQT 1382
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1383 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQELEDKMEVEQQSR 1455
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1456 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKL 1535
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1536 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1608
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1609 LDEQAGSIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1655
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1656 QKKLKQME----------------------------------VQLEEEYEDKQK----------ALREKREL--ESKLST 1689
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyvfgdtlvveDIEAARRLmgKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1690 L-------------------SDQVNQR-DFESEKRLRKDLKRTKALLADAQIMLDHLKNNA--------PSKREIAQLKN 1741
Cdd:TIGR02169 644 LegelfeksgamtggsraprGGILFSRsEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1742 QLEESEFTcAAAVKAR--------KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1808
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1809 LMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1884
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1885 EKTQVKRLENLAS---RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS------------ 1949
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelsledv 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1950 -RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINS 2002
Cdd:TIGR02169 957 qAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEE 1011
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1312-1989 |
3.14e-31 |
|
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: 134.92 E-value: 3.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1312 EEI-QQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDErntgESASQLLDAEtaeRLRTEKEMKELQTQYDALKKQ 1390
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1391 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQELEDKMEVEQqSRRQLERRLGDLQ 1466
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1467 ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEA 1546
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1547 FSLKQQMEEkdldiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQags 1615
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1616 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS- 1691
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1692 --DQVNQRDFESEK---RLRKDLKRTKALLADAQIML-------------------------DHLKNNAPSKREI----- 1736
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1737 ------AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1800
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1801 EDQEDMNELMKKHKAAVAQAS--RDMAQMN---------DLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1867
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1868 VSRQEAKiRELETRLEFEKTQVKRL-------ENLASRLKETME--KLTEERDQRAAAENREkEQNKRLQRQLRDTKEEM 1938
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELedelqatEDAKLRLEVNMQalKAQFERDLQARDEQGE-EKRRQLVKQVRELEAEL 758
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1939 SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1989
Cdd:pfam01576 759 EDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD 809
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
468-913 |
6.58e-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: 131.79 E-value: 6.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLATIA-GTSGTkvfsVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLGdGNRGA----TGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRteLHLNHLAENNVFGIVPLSKPEEKQKA----------AQQFSKLQA 695
Cdd:cd14882 157 YQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 696 AMKVLAISPEEQKTCWLILASIYHLGAAgatkePLEEQDEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQL-K 774
Cdd:cd14882 235 ILKDLDFNEEQLETVRKVLAAILNLGEI-----RFRQNGGYAE-----LENTEIASRVAELLRLDEKKFMWALTNYCLiK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 775 GGTLQRStsfRQGPEEsglgegtklsALECLEGMASGLYSELFTLLISLVN------RALKSSQHSLcsmMIVDTPGFQN 848
Cdd:cd14882 305 GGSAERR---KHTTEE----------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFEC 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 849 PEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIelafddlePVAD----DSVAAVDQ 913
Cdd:cd14882 369 FHRNR------LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDI--------PTINlrfyDNKTAVDQ 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1438-2017 |
1.33e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 132.37 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1438 KRLQQELED-KMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1516
Cdd:COG1196 216 RELKEELKElEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1596
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLE-------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1597 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKA 1676
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1677 LREKRELESKLSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcAAAVKA 1756
Cdd:COG1196 448 AEEEAELEEEEEALLELL--------AELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG----VKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1757 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQReknEIQNRLEEDQEDMNELMKKHKAAVA-------QASRDMAQMND 1829
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ---NIVVEDDEVAAAAIEYLKAAKAGRAtflpldkIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1830 LQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE 1909
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYV--LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1910 RDQRAAAENREKEQNKRLQRQLRDTKEEmsELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAfkrigDLQAAIED 1989
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEA--LLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE-----ELLEELLE 743
|
570 580
....*....|....*....|....*...
gi 1907082217 1990 EMESDENEDLINSEGDSDVDsELEDRVD 2017
Cdd:COG1196 744 EEELLEEEALEELPEPPDLE-ELERELE 770
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
469-894 |
1.77e-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: 127.31 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 469 VLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 542
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 543 VLLGSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVekwqALST--LLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVAS 620
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSL----ILGSnpLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 621 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENNVF-GIVPLSKPE-EKQKaaqQFSKLQAAMK 698
Cdd:cd14886 159 GKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnASKCYDAPGiDDQK---EFAPVRSQLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 699 VLaISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAeagrkQFARHEWAQKAAYLLGCSLEELSSAIfkhqlkggtL 778
Cdd:cd14886 236 KL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMGVINAA-----KISNDEDFGKMCELLGIESSKAAQAI---------I 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 779 QRSTSFRQGPEESGLgegTKLSALECLEGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQNPEWGgsarga 858
Cdd:cd14886 301 TKVVVINNETIISPV---TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN------ 371
|
410 420 430
....*....|....*....|....*....|....*.
gi 1907082217 859 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIE 894
Cdd:cd14886 372 TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
520-1186 |
2.19e-29 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 127.23 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 520 PHIYAVAQTAYRAMLM-SRQDQSIVLLGSSGSGKTTSFQHLVQYLA---------TIAGTSGTKVFSVEKWQalSTLLEA 589
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGqlsymhssnTSQRSIADKIDENLKWS--NPVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 590 FGNSPTIMNGSATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDAT-------LRTEL 661
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEekkelggLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 662 HLNHLAENNVF---GI--VPLSKPEEkqkaaqqFSKLQAAMKVLAISPEEQKTCWLILASIYHLgaagatkepLEEQDEA 736
Cdd:cd14875 214 DYKCLNGGNTFvrrGVdgKTLDDAHE-------FQNVRHALSMIGVELETQNSIFRVLASILHL---------MEVEFES 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 737 AEAGRKQFARHEwaqkaAYLLGCSLEELSSAifkhQLKGGTLQRS-----TSFRQGPEESGLgegtklsalecLEGMASG 811
Cdd:cd14875 278 DQNDKAQIADET-----PFLTACRLLQLDPA----KLRECFLVKSktslvTILANKTEAEGF-----------RNAFCKA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 812 LYSELFTLLISLVNRALKSSQH-SLCSMM-IVDTPGFQNpewggsARGASFEELCHNYAQDRLQRLFHERTFLQELERYK 889
Cdd:cd14875 338 IYVGLFDRLVEFVNASITPQGDcSGCKYIgLLDIFGFEN------FTRNSFEQLCINYANESLQNHYNKYTFINDEEECR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 890 EDNIE---LAFDDlepvADDSVAAVDQASHLVRSLahADEargllwlleeEALVPGATEDALLDRLFSYYGpqegdkkGQ 966
Cdd:cd14875 412 REGIQipkIEFPD----NSECVNMFDQKRTGIFSM--LDE----------ECNFKGGTTERFTTNLWDQWA-------NK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 967 SPLL---RSSKPRHFllGHSHGTNWVEYNVAGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagl 1042
Cdd:cd14875 469 SPYFvlpKSTIPNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA---------- 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1043 eggsqlalRRatsmrktfttgmaavkKKSLCIQIKLQVDALIDTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssse 1122
Cdd:cd14875 535 --------RR----------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPS--------------- 575
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1123 ldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1186
Cdd:cd14875 576 --------------FLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1323-2002 |
8.22e-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: 8.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1323 KVEKERNELRLSS--DRLEtRISELTSELtdERNTGESASQlldAETAERLRtekemkELQTQYDALKKQMEVMEMEVME 1400
Cdd:COG1196 171 KERKEEAERKLEAteENLE-RLEDILGEL--ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1401 ARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQL 1479
Cdd:COG1196 239 AELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1480 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD 1559
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1560 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK 1639
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1640 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLrkdlkrtkALLADA 1719
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL--------EAALAA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1720 QIMLDHLKNNAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR 1798
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1799 LEEDQEDM-NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvSRQEAKIRE 1877
Cdd:COG1196 627 LVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA------------ERLAEEELE 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1878 LETRLEFEKTQVKRLEnlasrlketmekltEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEM 1957
Cdd:COG1196 695 LEEALLAEEEEERELA--------------EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP 760
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1958 DLESLEAANQSLQADLklafKRIGDL-QAAIE--DEME------SDENEDLINS 2002
Cdd:COG1196 761 DLEELERELERLEREI----EALGPVnLLAIEeyEELEerydflSEQREDLEEA 810
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1298-1990 |
1.23e-28 |
|
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: 126.44 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSE--EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD--AETAERLRT 1373
Cdd:pfam01576 227 LQAQIAElrAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRdlGEELEALKT 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1374 EKEmkelQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgEWRLKYERAVRE--------------VDFTKKR 1439
Cdd:pfam01576 307 ELE----DTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQ-EMRQKHTQALEElteqleqakrnkanLEKAKQA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1440 LQQELED-----------KMEVEQQsRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1508
Cdd:pfam01576 382 LESENAElqaelrtlqqaKQDSEHK-RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1509 KKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1588
Cdd:pfam01576 461 KDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME--RMRQTHSKEMESRDEEVeearqscQKKLKQMevqL 1666
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdlLVDLDHQRQLVSNLEKK-------QKKFDQM---L 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1667 EEE-------YEDKQKALREKRELESKLSTLSdqvnqRDFESEKRLRKDLKRT-KALLADAQIML---DHLKNNA----P 1731
Cdd:pfam01576 611 AEEkaisaryAEERDRAEAEAREKETRALSLA-----RALEEALEAKEELERTnKQLRAEMEDLVsskDDVGKNVheleR 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1732 SKR----EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID-DIAKAKTALEEQLSRLQREKNEIQNRLEEDQedm 1806
Cdd:pfam01576 686 SKRaleqQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFErDLQARDEQGEEKRRQLVKQVRELEAELEDER--- 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1807 nelmKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeQSMVDKSLVSRQEAKIRELETRlefek 1886
Cdd:pfam01576 763 ----KQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDL-QRELEEARASRDEILAQSKESE----- 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 tqvKRLENLASRLKETMEKLteerdqrAAAEnrekeqnkrlqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAan 1966
Cdd:pfam01576 833 ---KKLKNLEAELLQLQEDL-------AASE-----------RARRQAQQERDELADEIASGASGKSALQDEKRRLEA-- 889
|
730 740
....*....|....*....|....
gi 1907082217 1967 qslqadlklafkRIGDLQAAIEDE 1990
Cdd:pfam01576 890 ------------RIAQLEEELEEE 901
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1298-2004 |
1.93e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 125.94 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldaetAERLRTEKEM 1377
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--------------LEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQ------ELEDKMEVE 1451
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEElkeeleSLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1452 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEETQREKLQ 1531
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 R--EKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeskdEASLAKVKKQLRDLEAKVKDQEEEL 1609
Cdd:TIGR02168 440 AelEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR----LDSLERLQENLEGFSEGVKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1610 DEQAGSIQMLEQ-----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1681
Cdd:TIGR02168 516 SGLSGILGVLSElisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1682 ELESKLSTLSDQVnqrdfESEKRLRKDLkrtKALLA------DAQIMLDHLKNNAPS----------------------- 1732
Cdd:TIGR02168 596 NIEGFLGVAKDLV-----KFDPKLRKAL---SYLLGgvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggvitggsak 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 --------KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1804
Cdd:TIGR02168 668 tnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1805 DMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLE 1883
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1884 FEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1963
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 1907082217 1964 AANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSEG 2004
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEY 949
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
469-1100 |
2.32e-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: 123.94 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 469 VLHTLRQRYGASLLHTYAGPSLLVLST---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 533
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 534 LMSRQDQSIVLLGSSGSGKTTSFQHLVQYLAtiAGTSGTKVFSVEKW-QALSTLLEAFGNSPTIMNGSATRFSQILSLDF 612
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 613 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLAENN--------VFGIVPLskpeekq 684
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDV------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 685 kaaQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGAAGATKEPLEEQDEAAEAGRkqfARHEWAQKAAYLLGCSLEEL 764
Cdd:cd14876 220 ---ADFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQGVDDAAAISN---ESLEVFKEACSLLFLDPEAL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 765 SSAIF-KHQLKGGtlQRSTSFRQGPEesglGEGTKLSaleclegMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDT 843
Cdd:cd14876 294 KRELTvKVTKAGG--QEIEGRWTKDD----AEMLKLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 844 PGF---QNpewggsargASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI---ELAFDDLEPVAD------DSVAAV 911
Cdd:cd14876 361 FGFevfKN---------NSLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 912 --DQAshlvrsLAhadeargllwlleeealvPGATEDALLDRLFSyygpQEGDKKGQSPLLRSSKpRHFLLGHSHGTnwV 989
Cdd:cd14876 432 leDQC------LA------------------PGGSDEKFVSACVS----KLKSNGKFKPAKVDSN-INFIVVHTIGD--I 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 990 EYNVAGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavk 1068
Cdd:cd14876 481 QYNAEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK----------- 537
|
650 660 670
....*....|....*....|....*....|..
gi 1907082217 1069 kkslciqiklQVDALIDTIKRSKMHFVHCFLP 1100
Cdd:cd14876 538 ----------QLESLMGLINSTEPHFIRCIKP 559
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
467-1181 |
2.54e-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: 123.44 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIVLL 545
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSvekwQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQT 625
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHS----SAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 626 MLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNHLaeNNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISPE 705
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 706 EQKTCWLILASIYHLGAA--GATKEPLEEQDeAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQLKGGTLQRSts 783
Cdd:cd14874 225 HCISIYKIISTILHIGNIyfRTKRNPNVEQD-VVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN-- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 784 frqgpeesglgegtklSALECLEGMASGLYSELFTLLISLVNRALKSSQHSlCSMMIVDTPGFQNPEWGGsargasFEEL 863
Cdd:cd14874 297 ----------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEEF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 864 CHNYAQDRLQRLFHERTFLQELERYKEDNIELafddlepvaDDSVAAVDQASHLVRSLAHADEarGLLWLLEEEALVPGA 943
Cdd:cd14874 354 LINSVNERIENLFVKHSFHDQLVDYAKDGISV---------DYKVPNSIENGKTVELLFKKPY--GLLPLLTDECKFPKG 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 944 TEDALLDRL------FSYYGPQegdkkgqspllRSSKPRHFLLGHSHGTNWveYNVAGWLNYTKQNpATQNAPRLLQDSQ 1017
Cdd:cd14874 423 SHESYLEHCnlnhtdRSSYGKA-----------RNKERLEFGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLRSSK 488
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1018 KKIISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqiklqvdaLIDTIKRSKMHFVHC 1097
Cdd:cd14874 489 NPIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHFVRC 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1098 FLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1177
Cdd:cd14874 536 IKSNNERQPK-----------------------------KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
....
gi 1907082217 1178 VLAP 1181
Cdd:cd14874 587 CLLP 590
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1304-1997 |
9.50e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 123.63 E-value: 9.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELR-----LSSD--RLETRISELTSELTDERNTGESASQLLDAETAERLRTEKE 1376
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQkelyaLANEisRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1377 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewrlkYERAVREVDftkkrlqqELEDKMEVEQQSRR 1456
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-------LETLRSKVA--------QLELQIASLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1457 QLERRLGDLQADSDESQRALQQLKKKCQRltAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQ 1536
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1537 REKDMLLAEAFSLKQQMEEKDldiaGFTQKVVSLEAE----------LQDISSQESKDEASLAKVkkqlrdLEAKVKDQE 1606
Cdd:TIGR02168 482 RELAQLQARLDSLERLQENLE----GFSEGVKALLKNqsglsgilgvLSELISVDEGYEAAIEAA------LGGRLQAVV 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1607 EELDEQAGS-IQMLEQAKLRLEMEMErMRQTHSKEMESRDEEVEEARQSCQKKLKQMeVQLEEEY--------------E 1671
Cdd:TIGR02168 552 VENLNAAKKaIAFLKQNELGRVTFLP-LDSIKGTEIQGNDREILKNIEGFLGVAKDL-VKFDPKLrkalsyllggvlvvD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKALREKRELESKLS--TL--------------SDQVNQRDFESE---KRLRKDLKRTKALLADAQIMLDHLKNNAPS 1732
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRivTLdgdlvrpggvitggSAKTNSSILERRreiEELEEKIEELEEKIAELEKALAELRKELEE 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KR-EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMk 1811
Cdd:TIGR02168 710 LEeELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE- 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1812 khkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLEFEKTQVK 1890
Cdd:TIGR02168 789 ------AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATErRLEDLEEQIEELSEDIESLAAEIE 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1891 RLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1970
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
|
730 740
....*....|....*....|....*..
gi 1907082217 1971 ADLKLAFKRIGDLQAAIEDEMESDENE 1997
Cdd:TIGR02168 943 ERLSEEYSLTLEEAEALENKIEDDEEE 969
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
468-913 |
3.69e-27 |
|
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: 120.40 E-value: 3.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 539
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 540 QSIVLLGSSGSGKTTSFQHLVQYLATIAGTSgTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQ----- 614
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 615 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDATLRT-----ELHLNHLAENNVFGIVPLSK----- 679
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSDEDLARrnlvrNCGVYGLLNPDESHQKRSVKgtlrl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 680 --------PEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYHLGaagatkepleeqdeaaeagrkqfarhEWAQ 751
Cdd:cd14884 241 gsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLG--------------------------NRAY 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 752 KAAyllgCSLEELSSAIFKHQLKGGTLQ-RSTSFRQgpeesglgEGTKLSALECLEGMASGLYSELFTLLISLVNRALKS 830
Cdd:cd14884 295 KAA----AECLQIEEEDLENVIKYKNIRvSHEVIRT--------ERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLK 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 831 SQHSLCSM------------MIVDTPGFQnpewggSARGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIeLAFD 898
Cdd:cd14884 363 CKEKDESDnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCS 435
|
490
....*....|....*
gi 1907082217 899 DLEPVADDSVAAVDQ 913
Cdd:cd14884 436 DVAPSYSDTLIFIAK 450
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1302-2020 |
9.23e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 120.63 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1302 LSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL--ETRISELTSELTDERNTgESASQLLDAETAERLRTEKEMKE 1379
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAEDAKK 1177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1380 LQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQELEDKMEVEQqSRRQLE 1459
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEA-VKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1460 RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEETQREKLQREKLQR 1537
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1538 EKdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGSI 1616
Cdd:PTZ00121 1315 KK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1617 QMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1696
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1697 RDFESEKRLRKDLKR----TKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEMEDLHLQI 1771
Cdd:PTZ00121 1469 AKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEKKKA 1548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1772 DDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1848
Cdd:PTZ00121 1549 DELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1849 QALQSQVEFLEQSMVDKSlvsRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ 1928
Cdd:PTZ00121 1629 EEEKKKVEQLKKKEAEEK---KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1929 R-------------QLRDTKEE----MSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEM 1991
Cdd:PTZ00121 1706 ElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
730 740 750
....*....|....*....|....*....|
gi 1907082217 1992 -ESDENEDLINSEGDSDVDSELEDRVDGVK 2020
Cdd:PTZ00121 1786 dEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1442-2013 |
1.19e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1442 QELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1521
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1522 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEA--------------S 1587
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqlelQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1588 LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMEsrdEEVEEARQSCQKKLKQMEVQLE 1667
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEL---EELQEELERLEEALEELREELE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1668 EEYEDKQKALREKRELESKLSTLSDQVNQRDFESE--------------------KRLRKDLKRTKALLADAQIMLDHL- 1726
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEgvkallknqsglsgilgvlsELISVDEGYEAAIEAALGGRLQAVv 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1727 -KNNAPSKREIAQLK-------------------------NQLEESEFTCAAAV-------KARKAM------------- 1760
Cdd:TIGR02168 552 vENLNAAKKAIAFLKqnelgrvtflpldsikgteiqgndrEILKNIEGFLGVAKdlvkfdpKLRKALsyllggvlvvddl 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1761 --------------------------------------------EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ 1796
Cdd:TIGR02168 632 dnalelakklrpgyrivtldgdlvrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELE 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1797 NRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKI 1875
Cdd:TIGR02168 712 EELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQI 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1876 RELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHEL 1955
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1956 EMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINSEGDSDVDSELE 2013
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRElESKRSELRRELEELREKLAQLELR 930
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1441-2026 |
8.44e-26 |
|
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: 116.27 E-value: 8.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1441 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1518
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1519 SQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1598
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1599 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1675
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1676 ALREKrelESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESeftCAAAVK 1755
Cdd:TIGR04523 247 EISNT---QTQLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1756 AR-KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDM-AQ 1826
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1827 MNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFEKTQVKR 1891
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1892 LENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQA 1971
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1972 DLKLAF--KRIGDLQAAIEDEMESDENEDLINSEGDSDVDsELEDRVDGVKSWLSKN 2026
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEK 608
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1299-1941 |
4.16e-25 |
|
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: 113.96 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMK 1378
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1379 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQL 1458
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1459 E----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1521
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1522 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1601
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1602 VKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS------KEMESRD-------EEVEEARQSCQKKLKQMEVQ--- 1665
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRSink 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1666 LEEEYEDKQKALREKrelESKLSTLSDQVNQrdfeSEKRLrKDLKRTKALLADAQIMLDHLKNNApsKREIAQLKNQLEE 1745
Cdd:TIGR04523 480 IKQNLEQKQKELKSK---EKELKKLNEEKKE----LEEKV-KDLTKKISSLKEKIEKLESEKKEK--ESKISDLEDELNK 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1746 SEFTcaaavkarkamevemedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMA 1825
Cdd:TIGR04523 550 DDFE-------------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1826 QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFEKTQVKRLENLA 1896
Cdd:TIGR04523 611 KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELS 690
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1907082217 1897 SRLKETMEKLTEERDqraaaENREKEQNKRLQRQLRDTKEEMSEL 1941
Cdd:TIGR04523 691 LHYKKYITRMIRIKD-----LPKLEEKYKEIEKELKKLDEFSKEL 730
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1299-1944 |
1.87e-24 |
|
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: 112.84 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLD----AETAERL-RT 1373
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaelKELQAELeEL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1374 EKEMKELQTQYDALKKQMEVMEMEVMEARLIR------AAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRL---QQEL 1444
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAEQALdaaereLAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgiLGVL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLG-DLQA----DSDESQRALQQLKK--------------KCQRLTAELQDTKLHLEGQQVRNH 1505
Cdd:TIGR02168 526 SELISVDEGYEAAIEAALGgRLQAvvveNLNAAKKAIAFLKQnelgrvtflpldsiKGTEIQGNDREILKNIEGFLGVAK 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1506 ELEKKQRRFDSELS------------QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAE 1573
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEK 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1574 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERmrqtHSKEMESRDEEVEEArq 1653
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTEL-- 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1654 scQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1733
Cdd:TIGR02168 760 --EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-EALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1734 -REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1812
Cdd:TIGR02168 837 eRRLEDLEEQIEELS-------EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1813 HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQsQVEFleqsMVDKSLVSRQEAKIRELETRLEFEKTQVKRL 1892
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY-SLTL----EEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1893 E--NLASrlketMEKLTEERdQRAAAENREKEQNKRLQRQLRDTKEEMSELARK 1944
Cdd:TIGR02168 985 GpvNLAA-----IEEYEELK-ERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1224-2007 |
5.85e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.39 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1224 RAGTLARLEEQRDEQTSRHLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1296
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1297 LIQVQLSEEQIR----NKDEEIQQLRSKLEKVEKERNE---LRLSSDRLETRISELTSELTDERNTGESASQLLDAETAE 1369
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1370 RLRTEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKME 1449
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1450 VEQQSRRQLERRLGDLQADSDESQRAlQQLKKKCQrltaelQDTKlhlEGQQVRNHELEKKQRrfdSELSQAHEETQREK 1529
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAE------EDKK---KADELKKAAAAKKKA---DEAKKKAEEKKKAD 1434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1530 LQREKLQREKdmllaEAFSLKQQMEEKDldiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEEL 1609
Cdd:PTZ00121 1435 EAKKKAEEAK-----KADEAKKKAEEAK-------------KAEEAKKKAEEAKKADEAKKKAEEAKKAD-EAKKKAEEA 1495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1610 DEQAGSIQMLEQAKLRLEmEMERMRQTHSKEMESRDEE---VEEARQSCQKKlKQMEVQLEEEY---EDKQKALREKREL 1683
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEakkADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAE 1573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1684 ESKLSTL-----SDQVNQRDFESEKRLRKDLKRTKALLA----DAQIMLDHLKNNAPSKREIAQLKNQLEES-------- 1746
Cdd:PTZ00121 1574 EDKNMALrkaeeAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelk 1653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1747 ----EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVAQ 1819
Cdd:PTZ00121 1654 kaeeENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA--AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1820 ASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLAS-- 1897
Cdd:PTZ00121 1732 AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANii 1811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1898 --------RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSL 1969
Cdd:PTZ00121 1812 eggkegnlVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIE 1891
|
810 820 830
....*....|....*....|....*....|....*...
gi 1907082217 1970 QADLKlafkrigDLQAAIEDEMESDENEDLINSEGDSD 2007
Cdd:PTZ00121 1892 KIDKD-------DIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1420-1988 |
1.26e-23 |
|
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: 109.88 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1420 GEWRLKYERAVREVDFTKKRLQQELE-----DKMEVEQQSRRQ-LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT 1493
Cdd:pfam01576 29 KELEKKHQQLCEEKNALQEQLQAETElcaeaEEMRARLAARKQeLEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1494 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMllaeafslkqqmeekdldiagftqkvvsLEAE 1573
Cdd:pfam01576 109 EEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKL----------------------------LEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1574 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQ 1653
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1654 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLsdqvnQRDFESEKRLRKDLKRTK-----ALLADAQIMLDHLKN 1728
Cdd:pfam01576 240 KKEEELQAALARLEEETAQKNNALKKIRELEAQISEL-----QEDLESERAARNKAEKQRrdlgeELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1729 NAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE 1800
Cdd:pfam01576 315 TAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1801 EDQEDMNELMKKHKAAvaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEt 1880
Cdd:pfam01576 395 TLQQAKQDSEHKRKKL-------EGQLQELQARLSESERQRAELAEKLSKLQSELESV------SSLLNEAEGKNIKLS- 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1881 rlefektqvKRLENLASRLKETMEKLTEERDQRAAAENR----EKEQNKrLQRQLRDTKE-------EMSELARKEAEAS 1949
Cdd:pfam01576 461 ---------KDVSSLESQLQDTQELLQEETRQKLNLSTRlrqlEDERNS-LQEQLEEEEEakrnverQLSTLQAQLSDMK 530
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082217 1950 RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1988
Cdd:pfam01576 531 KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1295-2013 |
2.21e-23 |
|
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: 109.29 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1295 RPLIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTseLTDERNTGESASQLLDAETAERLRTE 1374
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1375 KEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQS 1454
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1455 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREK 1534
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1535 LQREKDMLLAEAFSL--KQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1612
Cdd:pfam02463 414 ARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1613 AG--SIQMLEQAKLRLEMEMERMRQTHSKEM----------------------------ESRDEEVEEARQSCQK---KL 1659
Cdd:pfam02463 494 KLeeRSQKESKARSGLKVLLALIKDGVGGRIisahgrlgdlgvavenykvaistaviveVSATADEVEERQKLVRaltEL 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1660 KQMEVQLEEEYEDKQKALREKRELESKLST-------------------------LSDQVNQRDFESEKRLRKDLKRTKA 1714
Cdd:pfam02463 574 PLGARKLRLLIPKLKLPLKSIAVLEIDPILnlaqldkatleadeddkrakvvegiLKDTELTKLKESAKAKESGLRKGVS 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1715 LLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNE 1794
Cdd:pfam02463 654 LEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1795 IQ-----NRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVS 1869
Cdd:pfam02463 734 INeelklLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEE 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1870 RQEAKIRELETRLEfEKTQVKRLENLASRLKETM--EKLTEERDQRAAAENREKEQNKRLQRQLRDTKEE--MSELARKE 1945
Cdd:pfam02463 814 AELLEEEQLLIEQE-EKIKEEELEELALELKEEQklEKLAEEELERLEEEITKEELLQELLLKEEELEEQklKDELESKE 892
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1946 AEASRKKHELEMDLESLEAAN-QSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 2013
Cdd:pfam02463 893 EKEKEEKKELEEESQKLNLLEeKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1228-1913 |
4.99e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.72 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1228 LARLEEQRdEQTSRHLTLfQAACRGYLARQHFKKRKIQDLAIRCVQKNIKKNKgvkdwpwwklfttvrplIQVQLSEEQI 1307
Cdd:COG1196 202 LEPLERQA-EKAERYREL-KEELKELEAELLLLKLRELEAELEELEAELEELE-----------------AELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1308 RNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDAL 1387
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1388 KKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQELEDKMEVEQQSRRQLERRLGDLQA 1467
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEELEEAEEALLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1468 DSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1547
Cdd:COG1196 415 RLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1548 SLKQQMEEKDLDIAGftqkvvSLEAELQDISSQESKDEASLAKVKKQLRD-----LEAKVKDQEEELDEQAGS-IQMLEQ 1621
Cdd:COG1196 495 LLLEAEADYEGFLEG------VKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAAALQNIVVEDDEVAAAaIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1622 AKL--RLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmevqLEEEYEDKQKALREKRELESKLSTLSDQvnqrdf 1699
Cdd:COG1196 569 AKAgrATFLPLDKIRARAALAAALARGAIGAAV-------------DLVASDLREADARYYVLGDTLLGRTLVA------ 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1700 eseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaaVKARKAMEVEMEDLHLQIDDIAKAKT 1779
Cdd:COG1196 630 ---ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAAL------LEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1780 ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLE 1859
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1860 QsmVDksLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQR 1913
Cdd:COG1196 781 P--VN--LLAIEEYE--ELEERYDFLSEQREDLEEARETLEEAIEEIDRETRER 828
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1305-1963 |
6.27e-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: 107.03 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqlLDAET---AERLRTEKEMK-EL 1380
Cdd:TIGR04523 47 NELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDKEQKnKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1381 QTQYDALKKQMEVMEMEVmearliraAEINGEV-DDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ------Q 1453
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNI--------DKFLTEIkKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKnidkikN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1454 SRRQLERRLGDLQAdsdesqralqqLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFdSELSQAHEETQrEKLQRE 1533
Cdd:TIGR04523 195 KLLKLELLLSNLKK-----------KIQKNKSLESQISELK---KQNNQLKDNIEKKQQEI-NEKTTEISNTQ-TQLNQL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1534 KLQREKDmllaeafslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1608
Cdd:TIGR04523 259 KDEQNKI---------KKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1609 LDEQAGSIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLS 1688
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1689 TLSDQVNQRD-----FESEKRLRkdLKRTKALLADaqimldhlknNAPSKREIAQLKNQLEESEftcaaavkarkameve 1763
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKELL--EKEIERLKET----------IIKNNSEIKDLTNQDSVKE---------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1764 medlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASrdmaqmnDLQAQIEESNKEKQE 1843
Cdd:TIGR04523 454 -----LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK-------ELEEKVKDLTKKISS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1844 LQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE--KTQVKRLENLASRLKETMEKLTEERDQ-RAAAENRE 1920
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDL------EDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEEkQELIDQKE 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1921 KEQNK-------------RLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1963
Cdd:TIGR04523 596 KEKKDlikeieekekkisSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1425-1947 |
1.06e-22 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 106.69 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1425 KYERAVREVDFTKKRLQqELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1504
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1505 HELEKKQR--RFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFtQKVVSLEAELQDISSQES 1582
Cdd:PRK03918 304 EYLDELREieKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1583 kdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQKK 1658
Cdd:PRK03918 383 --GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1659 LKQMEVQLEEEYEDKQKALREKRELESKLstlsdqvnqrdfESEKRLRKDLKrtkalladaqiMLDHLKN--NAPSKREI 1736
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYNL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1737 AQLKNQLEESEFTCAAAVKARKAMEVEMEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMNE 1808
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLKE 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1809 LMKKH------KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETRL 1882
Cdd:PRK03918 597 LEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSREL 675
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1883 EFEKTQVKRLENLASRLKETMEKLTEERDQRAAAE------NREKEQNKRLQRQLRDTKEEMSELARKEAE 1947
Cdd:PRK03918 676 AGLRAELEELEKRREEIKKTLEKLKEELEEREKAKkeleklEKALERVEELREKVKKYKALLKERALSKVG 746
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
467-893 |
1.85e-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: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 467 SSVLHTLRQRYGASLLHTYAGPSLLVLStrgaPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISIN----PYQVIDVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLatIAGTSGTKVFSVEKWQAlSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQTM 626
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDS-NFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 627 LLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLNhlAENNVFGIVPLSKPEEKQKAAQQFSKLQAAMKVLAISpEE 706
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIR--SENEYKYIVNKNVVIPEIDDAKDFGNLMISFDKMNMH-DM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 707 QKTCWLILASIYHLGAAgatkepleEQDEAAEAGRKQFAR-----HEWAQKAAYLLGCSLEELSSAIfkhqlkggTLQRS 781
Cdd:cd14937 231 KDDLFLTLSGLLLLGNV--------EYQEIEKGGKTNCSEldknnLELVNEISNLLGINYENLKDCL--------VFTEK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 782 TSFRQGPEesglgegTKLSALECL---EGMASGLYSELFTLLISLVNRALKSSQHSLCSMMIVDTPGFQnpewggSARGA 858
Cdd:cd14937 295 TIANQKIE-------IPLSVEESVsicKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFE------IFSKN 361
|
410 420 430
....*....|....*....|....*....|....*
gi 1907082217 859 SFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI 893
Cdd:cd14937 362 SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDI 396
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1571-2014 |
8.83e-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: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1571 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGSIQMLEQAKLRLEMEMERMRQTHS----------KE 1640
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1641 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTK 1713
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1714 ALLADAQI----------MLDHLKNNAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1783
Cdd:pfam01576 159 ERISEFTSnlaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1784 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE-FLEQSM 1862
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1863 VDKSLVSRQEAKIRELETRLEFE-KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSEL 1941
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1942 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIED---EMESDENEDLINSEGDSDVDSELED 2014
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQD 472
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1404-1989 |
1.63e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 102.83 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1404 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQELEDKMEVEQQSRRQlERRLGDLQA 1467
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1468 DSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDMLLA 1544
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1545 EAfslkQQMEEKDLDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGSIQMLEQ 1621
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1622 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdFES 1701
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1702 EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEMEDLHLQidDIAKAKTAL 1781
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1782 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS 1861
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1862 MVDKSlvsrqEAKIRELET---RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQ---------- 1928
Cdd:PRK03918 586 SVEEL-----EERLKELEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEelekkyseee 660
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1929 -RQLRDTKEEMS-ELARKEAE---ASRKKHELEMDLESLEAAnqslQADLKLAFKRIGDLQAAIED 1989
Cdd:PRK03918 661 yEELREEYLELSrELAGLRAEleeLEKRREEIKKTLEKLKEE----LEEREKAKKELEKLEKALER 722
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1297-1937 |
2.06e-21 |
|
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: 102.74 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1297 LIQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLE-----TRISELTSELTDERNTGESASQLLDAETAERl 1371
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQSKMRSR- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1372 rtekeMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgeWRLKYERAVREVDFTKKrLQQELEDKMEVE 1451
Cdd:TIGR00618 324 -----AKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATS--IREISCQQHTLTQHIHT-LQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1452 QQSRRQLE--RRLGDLQADSDESQRALQQlkkkcqrltaelqdTKLHLEGQQVRNHELEKKQRRFDSElsQAHEETQREK 1529
Cdd:TIGR00618 396 QSLCKELDilQREQATIDTRTSAFRDLQG--------------QLAHAKKQQELQQRYAELCAAAITC--TAQCEKLEKI 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1530 LQREKLQ--REKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS---QESKDEASLAKVKKQLRDLEAKVKD 1604
Cdd:TIGR00618 460 HLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1605 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR 1681
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLR 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1682 ELESKLSTLSDQVNQRDFESEKRLRK-DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM 1760
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1761 EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1840
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1841 KQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENRE 1920
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSATLGEITHQLLKYEECS 858
|
650
....*....|....*..
gi 1907082217 1921 KEQNKRLQRQLRDTKEE 1937
Cdd:TIGR00618 859 KQLAQLTQEQAKIIQLS 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1523-1993 |
4.09e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 101.29 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1523 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftQKVVSLEAELQD-ISSQESKDEASLAKVKK---QLRDL 1598
Cdd:PRK03918 148 EKVVRQILGLDDYENAYKNLGEVIKEIKRRIERL--------EKFIKRTENIEElIKEKEKELEEVLREINEissELPEL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1599 EAKVKDQE---EELDEQAGSIQMLEQAKLRLEMEM----ERMRQTHS--KEMESRDEEVEEARqscqKKLKQMEvQLEEE 1669
Cdd:PRK03918 220 REELEKLEkevKELEELKEEIEELEKELESLEGSKrkleEKIRELEEriEELKKEIEELEEKV----KELKELK-EKAEE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1670 Y----EDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL 1743
Cdd:PRK03918 295 YiklsEFYEEYLDELREIEKRLSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1744 EEseftcaaaVKARKAMEvEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmKKHKAAVAQASRD 1823
Cdd:PRK03918 375 ER--------LKKRLTGL-TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 MAQ------MNDLQAQIEESNKEKQELQEKLQALqsqvefleqsmvdkslvsrqEAKIRELETRLEFEKTqVKRLENLAS 1897
Cdd:PRK03918 445 LTEehrkelLEEYTAELKRIEKELKEIEEKERKL--------------------RKELRELEKVLKKESE-LIKLKELAE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1898 RLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRdtkeemSELARKEAEASRKKhELEMDLESLEAANQSLQADLKLAF 1977
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLK------GEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELL 576
|
490
....*....|....*.
gi 1907082217 1978 KRIGDLQAAIEDEMES 1993
Cdd:PRK03918 577 KELEELGFESVEELEE 592
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1304-1975 |
1.54e-20 |
|
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: 99.41 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSE---LTDERNTGESASQLLD---AETAERL-RTEKE 1376
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKetcARSAEKTkKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1377 MKELQTQYDALKKQMEvmemevmeaRLIRAAEiNGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKmevEQQSRR 1456
Cdd:pfam05483 178 REETRQVYMDLNNNIE---------KMILAFE-ELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1457 QL------ERRLGDLQADSDESQRALQQLKKKcqrltAELQDTKLHlegqqvrnhELEKKQRRFDSELSQAHEETQREKL 1530
Cdd:pfam05483 245 LLiqitekENKMKDLTFLLEESRDKANQLEEK-----TKLQDENLK---------ELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1531 QREKLQREKDMLLAEAFSLKQ----QMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1606
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEekeaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1607 EELDEQAG-----SIQMLEQAKLRLEMEM----ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1677
Cdd:pfam05483 391 SELEEMTKfknnkEVELEELKKILAEDEKlldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1678 REKRELESKLstlsdqvnqrdfESEKrlrkdLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaaVKAR 1757
Cdd:pfam05483 471 KEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED--------IINC 525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1758 KAMEvemEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQ 1833
Cdd:pfam05483 526 KKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQ 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1834 IEESNKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKE----TMEKLTEE 1909
Cdd:pfam05483 603 IENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEdkkiSEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1910 RDQRAA----AENREKEQNKRLQRQLRD---------------TKEEMSELA---RKEAEASRKKHELEMDLESLEAANQ 1967
Cdd:pfam05483 677 VEKAKAiadeAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiIEERDSELGlykNKEQEQSSAKAALEIELSNIKAELL 756
|
....*...
gi 1907082217 1968 SLQADLKL 1975
Cdd:pfam05483 757 SLKKQLEI 764
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
468-920 |
3.38e-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: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLG 546
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 547 SSGSGKTTSFQHLVQYLAT--IAGTSGTKVFSVEKwqalSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAGQVASASIQ 624
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTtdLSRSKYLRDYILES----GIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 625 TMLLEKLRVARRPASEATFNVFYYLLAcgdatlrtelhlnhlaennvfGIVplskpeEKQKAAQQFSKLQaamkvlaisp 704
Cdd:cd14905 156 SYFLDENRVTYQNKGERNFHIFYQFLK---------------------GIT------DEEKAAYQLGDIN---------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 705 eeqktcwlilaSIYHLGAAGATKEPLEEQDEAAEAGRKQFARHEWAQKAAYLLGCSLE---ELSSAIF-----KHQLKGG 776
Cdd:cd14905 199 -----------SYHYLNQGGSISVESIDDNRVFDRLKMSFVFFDFPSEKIDLIFKTLSfiiILGNVTFfqkngKTEVKDR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 777 TLQRSTSFRQGPEESGLgEGTKLS--------ALECLEGMASGLYSELFTLLISLVNRALKSSQHSLcSMMIVDTPGFQN 848
Cdd:cd14905 268 TLIESLSHNITFDSTKL-ENILISdrsmpvneAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQES 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 849 PEWGGsargasFEELCHNYAQDRLQRLFHERTFLQELERYKEDNI----ELAFDDLE---PVADDSVAAVDQASHLVRS 920
Cdd:cd14905 346 SQLNG------YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNEesvEMMEKIINLLDQESKNINS 418
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1559-1949 |
1.31e-19 |
|
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: 96.68 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1559 DIAG---FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLEMEmermrq 1635
Cdd:TIGR02169 161 EIAGvaeFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLR-REREKAERYQALLKEKREYEGYELLKEKE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1636 thskEMESRDEEVEEARQSCQKKLKQMEVQLEEeyedkqkalREKR--ELESKLSTLSDQVNQRDFESEKRLRKDLKRTK 1713
Cdd:TIGR02169 234 ----ALERQKEAIERQLASLEEELEKLTEEISE---------LEKRleEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1714 ALLADAQimldhlknnapskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKN 1793
Cdd:TIGR02169 301 AEIASLE-------------RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1794 EIQNRLEEDQEDMNELMKKHKAAVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEA 1873
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EA 434
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1874 KIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRDTKeemSELARKEAEAS 1949
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQ---RELAEAEAQAR 500
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
498-616 |
1.34e-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: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 498 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIVLLGSSGSGKTTSFQHLVQYLATIAGTSGTK---- 573
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 574 ---------VFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQAG 616
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1304-2012 |
5.59e-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: 94.80 E-value: 5.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKL----EKVEKERNELRLSSDRLETRISELTSE---LTDERNTgESASQ----------LLDAE 1366
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLnesnELHEKQKFYLRQSVIDLQTKLQEMQMErdaMADIRRR-ESQSQedlrnqlqntVHELE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1367 TAERLRtEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingeVDDDDAGGEWRLKYERA----VREVDFTKKRLQQ 1442
Cdd:pfam15921 156 AAKCLK-EDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL-------VDFEEASGKKIYEHDSMstmhFRSLGSAISKILR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1443 ELEDKMEVEQQSRRQLERRLGDLQADS-DESQRALQQLKKKCQRLTAE--LQDTKLHLEGQQVRNhELEKKQRRFDSELS 1519
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESqNKIELLLQQHQDRIEQLISEheVEITGLTEKASSARS-QANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE 1599
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1600 AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEYEDKQKALRE 1679
Cdd:pfam15921 384 ADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQMERQMAAIQG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1680 KRELESKLSTLSDQVnqrdfESEKRLrkdLKRTKALLADAQIMLDHlknnapSKREIAQLKNQLEESE----FTCAAAVK 1755
Cdd:pfam15921 456 KNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKEraieATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1756 ARKAMEVEMEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDMAQMNDLQAQ 1833
Cdd:pfam15921 522 LRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTAGAMQVEKAQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1834 IE-ESNKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETR---LEFEKTqvkRLENLASRLKETMEKLTEE 1909
Cdd:pfam15921 595 LEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARvsdLELEKV---KLVNAGSERLRAVKDIKQE 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1910 RDQ-------RAAAENREKEQNKRLQRQLRDTKEEMSELARK-EAEASRKKHELEM---DLESLEAAN-------QSLQA 1971
Cdd:pfam15921 655 RDQllnevktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamkvaMGMQK 734
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907082217 1972 DLKLAFKRIGDLQAAI---EDEMESDENEDLINSEGDSDVDSEL 2012
Cdd:pfam15921 735 QITAKRGQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQEL 778
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1369-2007 |
2.47e-18 |
|
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: 92.73 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1369 ERLRTEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1442
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1443 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1522
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1523 EETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1602
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1603 KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRE 1682
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1683 LESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAM-- 1760
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLK--VLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAis 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1761 ---EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDMAQMNDLQAQ 1833
Cdd:pfam02463 547 tavIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1834 IEESNKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRLEfekTQVKRLENLASRLKETMEKLTEERDQR 1913
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELTKE---LLEIQELQEKAESELAKEEILRRQLEI 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1914 AAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES 1993
Cdd:pfam02463 702 KKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEERE 781
|
650
....*....|....
gi 1907082217 1994 DENEDLINSEGDSD 2007
Cdd:pfam02463 782 KTEKLKVEEEKEEK 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1429-2001 |
3.27e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.03 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1429 AVREVDFTKKRLQQELEDkmEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1508
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1509 kkqrrfdsELSQAHEETQREKLQREklqREKDMLLAEAFSLKQQMEEkdldiagftqkvvsLEAELQDISSQESKDEASL 1588
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLRDLEAKVKDQEEELDEQAGSIQML-EQAK------LRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQ 1661
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHnEEAEslredaDDLEERAEELR-EEAAELESELEEAREAVEDRREEIEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1662 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnAPskrEIAQlkn 1741
Cdd:PRK02224 389 LEEEIEELRERFGDAPVDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALLEAGK--CP---ECGQ--- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1742 QLEESEFTCAAAVK--ARKAMEVEMEDLHLQIDDIAKAKTALEEqLSRLQREKNeiqnRLEEDQEDMNELMKKHKAAVAQ 1819
Cdd:PRK02224 460 PVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIE----RLEERREDLEELIAERRETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1820 ASRdmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKslvsRQEAKirELETRLEFEKTQVKRLENLASRL 1899
Cdd:PRK02224 535 KRE----------RAEELRERAAELEAEAEEKREAAAEAEEEAEEA----REEVA--ELNSKLAELKERIESLERIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1900 ------KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHE-----LEMDLESLEAANQS 1968
Cdd:PRK02224 599 aaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDD 678
|
570 580 590
....*....|....*....|....*....|....*
gi 1907082217 1969 LQadlklafKRIGDLQAAIEdEMES--DENEDLIN 2001
Cdd:PRK02224 679 LQ-------AEIGAVENELE-ELEElrERREALEN 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1571-1996 |
4.09e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.04 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1571 EAELQDISSQESKD--EASLAKVKKQLRDLEAKVKDQEE--ELDEQagsiqmLEQAKLRLememermrqtHSKEMESRDE 1646
Cdd:TIGR02168 176 ETERKLERTRENLDrlEDILNELERQLKSLERQAEKAERykELKAE------LRELELAL----------LVLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1647 EVEEARQScqkkLKQMEVQLEEeyedkqkALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHL 1726
Cdd:TIGR02168 240 ELEELQEE----LKEAEEELEE-------LTAELQELEEKLEELRLEVSELE-EEIEELQKELYALANEISRLEQQKQIL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1727 KNnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM 1806
Cdd:TIGR02168 308 RE------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1807 NELmkkhKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdkslvsrQEAKIRELETRLEfek 1886
Cdd:TIGR02168 382 ETL----RSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--------EEAELKELQAELE--- 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 tqvkrlenlasRLKETMEKLTEERDQRAAAEnrekeqnKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAAN 1966
Cdd:TIGR02168 444 -----------ELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS 505
|
410 420 430
....*....|....*....|....*....|
gi 1907082217 1967 QSLQAdLKLAFKRIGDLQAAIEDEMESDEN 1996
Cdd:TIGR02168 506 EGVKA-LLKNQSGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1409-1808 |
6.41e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 91.27 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1409 INGEVDDDDAGgewRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQR 1485
Cdd:TIGR02168 661 ITGGSAKTNSS---ILERRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1486 LTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1565
Cdd:TIGR02168 738 LEAEVE--------------QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1566 KVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1645
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 eEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekRLRKDLKRTK-ALLADAQIMLD 1724
Cdd:TIGR02168 884 -SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE--------GLEVRIDNLQeRLSEEYSLTLE 954
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1725 HLKNN--------APSKREIAQLKNQLEE---------SEFtcaAAVKARKamevemEDLHLQIDDIAKAKTALEEQLSR 1787
Cdd:TIGR02168 955 EAEALenkieddeEEARRRLKRLENKIKElgpvnlaaiEEY---EELKERY------DFLTAQKEDLTEAKETLEEAIEE 1025
|
410 420
....*....|....*....|.
gi 1907082217 1788 LQReknEIQNRLEEDQEDMNE 1808
Cdd:TIGR02168 1026 IDR---EARERFKDTFDQVNE 1043
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1260-1849 |
7.88e-18 |
|
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: 90.46 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1260 KKRKIQDLAIRCVQKNIKKNKgvkdwpwwKLFTTVRPLIQVQLS-EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRL 1338
Cdd:TIGR04523 194 NKLLKLELLLSNLKKKIQKNK--------SLESQISELKKQNNQlKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1339 ETRISELTSELtderntgESASQLLDaetaerlRTEKEMKELQTQYDALKKQmevmemevmearliRAAEINGEVDDDDA 1418
Cdd:TIGR04523 266 KKQLSEKQKEL-------EQNNKKIK-------ELEKQLNQLKSEISDLNNQ--------------KEQDWNKELKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1419 GGEWRL--------KYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKkcqrLTAEL 1490
Cdd:TIGR04523 318 NQEKKLeeiqnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKN----LESQI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1491 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmllaeafSLKQQMEEKDLDIAGFTQKVVSL 1570
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-------DLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1571 EAELQDISSQESKDEASLAKVKKQLrdleakvKDQEEELDeqagsiqMLEQAKLRLEMEMermrqthsKEMESRdeevee 1650
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKEL-------KSKEKELK-------KLNEEKKELEEKV--------KDLTKK------ 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1651 arqscQKKLKQMEVQLEeeyedkqkalREKRELESKLSTLSDQVNQRDFESEKRLRKD-----------LKRTKALLADA 1719
Cdd:TIGR04523 519 -----ISSLKEKIEKLE----------SEKKEKESKISDLEDELNKDDFELKKENLEKeideknkeieeLKQTQKSLKKK 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1720 QIMLDHLKNNapSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR- 1798
Cdd:TIGR04523 584 QEEKQELIDQ--KEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKw 661
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1799 ---------LEEDQEDMNELMKKHK----AAVAQASRDMAQMNDLQaQIEESNKEKQELQEKLQ 1849
Cdd:TIGR04523 662 peiikkikeSKTKIDDIIELMKDWLkelsLHYKKYITRMIRIKDLP-KLEEKYKEIEKELKKLD 724
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1295-2011 |
1.30e-17 |
|
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: 90.49 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1295 RPLIQVQLSEEQIRNKDEEIQ--QLRSKLEKVEKE-------RNELRLSSDRLETR---ISELTSELTDERNTGESASQL 1362
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQslATRLELDGFERGpfserqiKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1363 LDAETAERLRT--------EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1431
Cdd:TIGR00606 431 IRDEKKGLGRTielkkeilEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1432 -EVDFTKKRLQQELE-----------------DKMEVEQQSRRQLERRLGDLQA------DSDESQRALQQLKKKCQRLT 1487
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQIRKIKSRHSDELTSllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1488 AELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-----------ETQREKLQR--EKLQREKDMLLAEAFSLKQQME 1554
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeESDLERLKEeiEKSSKQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1555 EKDLDIAG---FTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1631
Cdd:TIGR00606 671 QLTDENQSccpVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1632 RMRQTHSK------EMESRDEEVEEARQSCQKKLKQMEV---------QLEEEYEDKQKALREK-RELESKLSTLS-DQV 1694
Cdd:TIGR00606 748 ELRNKLQKvnrdiqRLKNDIEEQETLLGTIMPEEESAKVcltdvtimeRFQMELKDVERKIAQQaAKLQGSDLDRTvQQV 827
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1695 NQRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNApskreiaqlkNQLEESEFTCAAAVKARKAME-------VEM 1764
Cdd:TIGR00606 828 NQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsTEV 897
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1765 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEED----QEDMNELMKKHKAAVA---------------QASRDMA 1825
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSnkkaQDKVNDIKEKVKNIHGymkdienkiqdgkddYLKQKET 977
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1826 QMNDLQAQIEESNKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLasRLKET 1902
Cdd:TIGR00606 978 ELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMKQE 1055
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1903 MEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrKKHELEMDLESLEAANQSL--------QADLK 1974
Cdd:TIGR00606 1056 HQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAIMK 1133
|
810 820 830
....*....|....*....|....*....|....*...
gi 1907082217 1975 LAFKRIGDLQAAIEDEMESDEN-EDLINSEGDSDVDSE 2011
Cdd:TIGR00606 1134 FHSMKMEEINKIIRDLWRSTYRgQDIEYIEIRSDADEN 1171
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
1.39e-17 |
|
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467153 [Multi-domain] Cd Length: 81 Bit Score: 79.51 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRTTMLDRAPegqayrrVVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 1907082217 300 GDSVRLKVQ 308
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1436-2003 |
2.16e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 89.64 E-value: 2.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1436 TKKRLQQELEDKMEVEQQSRRQLeRRLGDLQADSDESQRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHELEKK 1510
Cdd:TIGR00618 223 VLEKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1511 QRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQ--MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1588
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLRDLEAKVK---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQMEVQ 1665
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QCEKL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1666 LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL-------RKDLKRTKALLADAQIMLDHLKNNAPSKR---E 1735
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRgeqT 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1736 IAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKA 1815
Cdd:TIGR00618 537 YAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDMLACE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1816 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ---------EAKIRELETRLEFEK 1886
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrQLALQKMQSEKEQLT 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 TQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA--------SRKKHELEMD 1958
Cdd:TIGR00618 694 YWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkarteahFNNNEEVTAA 773
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1959 L------ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 2003
Cdd:TIGR00618 774 LqtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE 824
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1305-1792 |
1.54e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.97 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELrlssDRLETRISELTSELTDERNTGESASQLLDAET--AERLRTEKEMKELQT 1382
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEEL----EELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1383 QYDALKKQMEVMEmevmearliraaeingevddddaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL 1462
Cdd:COG4717 147 RLEELEERLEELR-------------------------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1463 GDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQvrnhelekkqrrfdselsqaheetqreklQREKLQREKDML 1542
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-----------------------------LEERLKEARLLL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1543 LAEA-----FSLKQQMEEKDLDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1617
Cdd:COG4717 253 LIAAallalLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1618 MLEQAKL-RLEMEMERMRQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1692
Cdd:COG4717 330 LPPDLSPeELLELLDRIEELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1693 QVNQR--------DFESEKRLRKDLKRTKALLADAQIMLDHLknnapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEV 1762
Cdd:COG4717 410 QLEELlgeleellEALDEEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKA 483
|
490 500 510
....*....|....*....|....*....|
gi 1907082217 1763 EMEDLHLQIDDIAKAKTALEEQLSRLQREK 1792
Cdd:COG4717 484 ELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1305-1912 |
1.58e-16 |
|
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: 86.66 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQY 1384
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1385 DALKKQMEVMEMEVMEAR-------------------LIR-------AAEINGE-------VDDDDAGGEW--RLKYERA 1429
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRaveevlkasiqgvhgtvaqLGSvgeryatAIEVAAGnrlnnvvVEDDAVAKEAieLLKRRKA 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1430 VREVDFTKKRLQQELEDK---------------MEVEQQSRRQLERRLGD-LQADSDESQRALQqLKKKCQRLTAELQDT 1493
Cdd:TIGR02169 573 GRATFLPLNKMRDERRDLsilsedgvigfavdlVEFDPKYEPAFKYVFGDtLVVEDIEAARRLM-GKYRMVTLEGELFEK 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1494 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagfTQKVVSLEAE 1573
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA-------SRKIGEIEKE 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1574 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ--AKLRLEMEMERMRQTHSKEMESRDE--EVE 1649
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEdlHKLEEALNDLEARLSHSRIPEIQAElsKLE 804
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1650 EARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRdfesekrlrkdlkrtkalladaqimldhlknn 1729
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-------------------------------- 852
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1730 apsKREIAQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDDiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNEL 1809
Cdd:TIGR02169 853 ---EKEIENLNGKKEE--------------LEEELEELEAALRD-------LESRLGDLKKERDELEAQLRELERKIEEL 908
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1810 MkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELE-----TRLEF 1884
Cdd:TIGR02169 909 E-------AQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlAIQEY 981
|
650 660
....*....|....*....|....*...
gi 1907082217 1885 EKTQVKRLEnlasrLKETMEKLTEERDQ 1912
Cdd:TIGR02169 982 EEVLKRLDE-----LKEKRAKLEEERKA 1004
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
468-650 |
1.59e-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: 86.04 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLSTRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIVLL 545
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 546 GSSGSGKTTSFQHLVQYLATIAGTSGTKVFSVEKWQAL---------------------STLLEAFGNSPTIMNGSATRF 604
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1907082217 605 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 650
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1304-1785 |
2.08e-16 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 86.38 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISEL---TSELTDERNTGESAsqlldaetaeRLRTEKEMKEL 1380
Cdd:pfam01576 656 ERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMktqLEELEDELQATEDA----------KLRLEVNMQAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1381 QTQYDAlkkqmevmemevmearliraaEINGEvddDDAGGEWRLKYERAVREvdftkkrLQQELEDKMEVEQQ---SRRQ 1457
Cdd:pfam01576 726 KAQFER---------------------DLQAR---DEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQavaAKKK 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1458 LERRLGDLQADSDESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL 1530
Cdd:pfam01576 775 LELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1531 QREKLQREKDmllaeafslkqqmeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQEEELD 1610
Cdd:pfam01576 855 ARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELE 899
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1611 EQAGSIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKALREKRELESKLST 1689
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALEAKIAQ 978
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1690 LSDQVNQrdfESEKRLR--KDLKRTKALLADAQIMLDHLKNNAPSKREIA--------QLKNQLEESEFTCAAAVKARKA 1759
Cdd:pfam01576 979 LEEQLEQ---ESRERQAanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASRANAARRK 1055
|
490 500
....*....|....*....|....*.
gi 1907082217 1760 MEVEMEDLHLQIDDIAKAKTALEEQL 1785
Cdd:pfam01576 1056 LQRELDDATESNESMNREVSTLKSKL 1081
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1486-1986 |
2.19e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 85.59 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1486 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQ 1565
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1566 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1645
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQvnqrdfesekrlrKDLKRTKALLADAQIMLdh 1725
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1726 lknnapskrEIAQLKNQLEESEFTCAAAVKARKAMevemedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1805
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1806 MNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1885
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1886 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnkRLQRQLRDTKEEMSELARKEAEASRKKHELEMD--LESLE 1963
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 1907082217 1964 AANQSLQADLKLAFKRIGDLQAA 1986
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1298-1814 |
2.44e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.89 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET---------RISELTSELTDERNTGE-------SASQ 1361
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1362 LLDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1441
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1442 QELEDKMEVEQQsRRQLERRLGDLQADSDESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1518
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1519 SQAHEETQREKLQREKLQREKDMLlaEAFSLKQQMEEKDLDIAgftQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1597
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELREL--EKVLKKESELIKLKELA---EQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LEAKVKDQEEELDEQagsiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1673
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1674 QKALREKRELESKLSTLSDQVnqRDFESEKRLRKDLKRTkalLADAQIMLDHLKNNAPSKR-EIAQLKNQLEESEFTCAA 1752
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDAE--KELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1753 AVKARKAMEV-----EMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHK 1814
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEK-LEKALERVEELREKVK 731
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
222-307 |
3.80e-16 |
|
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467249 [Multi-domain] Cd Length: 80 Bit Score: 75.17 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 222 ELQRRPTGdFGFSLRRttmlDRAPEGQaYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06768 4 HLVKGPEG-YGFNLHA----EKGRPGH-FIREV---DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKASGN 72
|
....*.
gi 1907082217 302 SVRLKV 307
Cdd:cd06768 73 QVTLLV 78
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1678-2019 |
1.33e-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: 83.58 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1678 REKRELESKLSTLS--DQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaAAVK 1755
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1756 ARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM-AQMNDLQAQI 1834
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELeAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1835 EESNKEKQELQEKLQ-------ALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFEKTQVKRLENLASRL 1899
Cdd:TIGR02169 311 AEKERELEDAEERLAkleaeidKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1900 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1979
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1980 IGDLQA---AIEDEMESDENEdLINSE-----------GDSDVDSELEDRVDGV 2019
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-LAEAEaqaraseervrGGRAVEEVLKASIQGV 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1298-1644 |
1.40e-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: 83.57 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLET-------RISELTSELTDERNTGESASQLLDAETAER 1370
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveqleeRIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1371 LRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQELEDKME 1449
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1450 VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1529
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1530 LQREKLQREKDMLLaEAFSLKQQMeekdldiagftqkvvsleaELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1603
Cdd:TIGR02168 929 LRLEGLEVRIDNLQ-ERLSEEYSL-------------------TLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082217 1604 --------DQEEELDEQAGSIQMLEQAKLRLEMEMERMrqthSKEMESR 1644
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
468-1197 |
2.05e-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: 82.47 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 468 SVLHTLRQRYGASLLHTYAGPSLLVLST---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIVL 544
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 545 LGSSGSGKTTSFQHLVQYLATIAGtSGTKVFSVEKWQALSTLLEAFGNSPTIMNGSATRFSQILSLDFDQaGQVASASIQ 624
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 625 TMLLEKLRVARRPASEATFNVFYYLLACGDATLRTELHLN--------HLAENNVFgivplskpEEKQKAAQQFSKLQAA 696
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 697 MKVLAISpeeqktcWL----ILASIYHLGAAGATKEPLEEQDEAAEAGRKQfarhewaqkAAYLLGCSleelSSAIFKhq 772
Cdd:cd14881 224 LGILGIP-------FLdvvrVLAAVLLLGNVQFIDGGGLEVDVKGETELKS---------VAALLGVS----GAALFR-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 773 lkgGTLQRSTSFRQGPEESGLGEGTKLSALECLegmASGLYSELFTLLISLVNrALKSSQHSLC------SMMIVDTPGF 846
Cdd:cd14881 282 ---GLTTRTHNARGQLVKSVCDANMSNMTRDAL---AKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFGF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 847 QNPewggsaRGASFEELCHNYAQDRLQRLFHERTFLQELERYKEDNIELafdDLEPVADDSVAAVDqashLVRSLahade 926
Cdd:cd14881 355 EDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID----LISSL----- 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 927 ARGLLWLLEEEALVPGATEdalldrlfSYYGPQEGDKKGQSPLLRSSK--PRHFLLGHSHGTnwVEYNVAGWLnytkqnp 1004
Cdd:cd14881 417 RTGLLSMLDVECSPRGTAE--------SYVAKIKVQHRQNPRLFEAKPqdDRMFGIRHFAGR--VVYDASDFL------- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1005 atqnaprllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQIKLQVDALI 1084
Cdd:cd14881 480 ----------DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLDNLL 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1085 DTIKRSKMHFVHCFLPVAEGWPGeprsassrrvsssseldlppgdpceagllQLDVSLLRAQLRGSRLLDAMRMYRQGYP 1164
Cdd:cd14881 519 RTLVHARPHFVRCIRSNTTETPN-----------------------------HFDRGTVVRQIRSLQVLETVNLMAGGYP 569
|
730 740 750
....*....|....*....|....*....|...
gi 1907082217 1165 DHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDEK 1197
Cdd:cd14881 570 HRMRFKAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1301-1952 |
2.28e-15 |
|
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: 83.10 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1301 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaetaERLRTEKEMKEL 1380
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKLTEEKEELEK 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1381 QTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELE--DKMEVEQQSRRQL 1458
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRLGDLG 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1459 ERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQRE 1538
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQLDKAT 612
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1539 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1612
Cdd:pfam02463 613 LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESELAKE 692
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1613 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSD 1692
Cdd:pfam02463 693 EILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1693 QVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQID 1772
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKL 851
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1773 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdMAQMNDLQAQIEESNKEKQELQEKLQALQ 1852
Cdd:pfam02463 852 AEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK------EEKKELEEESQKLNLLEEKENEIEERIKE 925
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1853 SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLEN---LASRLKETMEKLTEERDQRAAAENREKEQN----K 1925
Cdd:pfam02463 926 EAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLakeELGKVNLMAIEEFEEKEERYNKDELEKERLeeekK 1005
|
650 660
....*....|....*....|....*..
gi 1907082217 1926 RLQRQLRDTKEEMSELARKEAEASRKK 1952
Cdd:pfam02463 1006 KLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1443-1919 |
2.58e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1443 ELEDKMEVEQQSRRQLERRLGDLQ---ADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1519
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT---------------------QKVVSLEAELQDIS 1578
Cdd:PRK02224 297 DLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNeeaeslredaddleeraeelrEEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1579 SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThskeMESRDEEVEEARQ----- 1653
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT----LRTARERVEEAEAlleag 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1654 ---SCQKKLKQME-VQLEEEYEDKQKALREKRE-LESKLSTLSDQVNQRD--FESEKRLRKDLKRTKA---LLADAQIML 1723
Cdd:PRK02224 453 kcpECGQPVEGSPhVETIEEDRERVEELEAELEdLEEEVEEVEERLERAEdlVEAEDRIERLEERREDleeLIAERRETI 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1724 DHLKNNAPSKREIAQ-LKNQLEESEftcAAAVKARKAMEVEMEdlhlQIDDIAKAKTALEEQLSRLQREKnEIQNRLEED 1802
Cdd:PRK02224 533 EEKRERAEELRERAAeLEAEAEEKR---EAAAEAEEEAEEARE----EVAELNSKLAELKERIESLERIR-TLLAAIADA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1803 QEDMNELMKKHKaavaqasrDMAQMNDL-QAQIEESNKEKQELQEKLQAlqsqvEFLEQSMVDKslvSRQEAKIRELETR 1881
Cdd:PRK02224 605 EDEIERLREKRE--------ALAELNDErRERLAEKRERKRELEAEFDE-----ARIEEAREDK---ERAEEYLEQVEEK 668
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907082217 1882 LEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENR 1919
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERREALENR 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1439-1944 |
3.84e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 82.27 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1439 RLQQELEDKMEVEQQSRRQLERR--LGDLQADSDESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1516
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEETQREKLQREKLQREKDMLLAEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASL 1588
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLR------------------DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKE---------- 1640
Cdd:COG4913 383 AALRAEAAallealeeelealeealaEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlgldeaelpf 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1641 ----MESRDEE-------------------VEEARQSC------QKKLKQmEVQLEEEYEDKQKALREK-------RELE 1684
Cdd:COG4913 463 vgelIEVRPEEerwrgaiervlggfaltllVPPEHYAAalrwvnRLHLRG-RLVYERVRTGLPDPERPRldpdslaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1685 SKLSTLSDQVNQ---RDF-----ESEKRLRKDlkrTKALLADAQImldhlKNNApSKREIaQLKNQLEESEFTCAAAVKA 1756
Cdd:COG4913 542 FKPHPFRAWLEAelgRRFdyvcvDSPEELRRH---PRAITRAGQV-----KGNG-TRHEK-DDRRRIRSRYVLGFDNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1757 RKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelmkkhkaaVAQASRDMAQMNDLQAQIEE 1836
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID---------VASAEREIAELEAELERLDA 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1837 SNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVK----RLENLASRLKETMEKLTEERDQ 1912
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFA 756
|
570 580 590
....*....|....*....|....*....|..
gi 1907082217 1913 RAAAENREKEQNKRLQRQLRDTKEEMSELARK 1944
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1577-2001 |
3.86e-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: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1577 ISSQESKD---EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRD-------- 1645
Cdd:TIGR04523 28 ANKQDTEEkqlEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE---QQIKDLNDKLKKNKDkinklnsd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 -----EEVEEARQSCQKK---LKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesekrlrkDLKRTKALLA 1717
Cdd:TIGR04523 105 lskinSEIKNDKEQKNKLeveLNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYN------------DLKKQKEELE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1718 DAQIMLDHLKNNApsKREIAQLKNQLEESEFTCAAAVKARKamevEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1797
Cdd:TIGR04523 173 NELNLLEKEKLNI--QKNIDKIKNKLLKLELLLSNLKKKIQ----KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1798 RLEEDQEDMNELMKKHKaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD------KSLVSRQ 1871
Cdd:TIGR04523 247 EISNTQTQLNQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1872 EAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRK 1951
Cdd:TIGR04523 320 EKKLEEIQ-------NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1952 KHELEMDLESLEAANQSLQADLK-------LAFKRIGDLQAAIEDemESDENEDLIN 2001
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKklqqekeLLEKEIERLKETIIK--NNSEIKDLTN 447
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1308-1913 |
1.14e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1308 RNKDEEIQQLRSKLEkvEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDaETAERLrteKEMKELQTQYDAL 1387
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1388 KkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELED---KMEVEQQSRRQLERRLGD 1464
Cdd:PRK02224 257 E------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1465 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDmlla 1544
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE---- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1545 eafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGSIQ 1617
Cdd:PRK02224 395 ---ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1618 MLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkaLREKRELESKLSTlsdqvNQR 1697
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEELIA-----ERR 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1698 DFESEKRLRKDLKRTKAlladaqimlDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE----MEDLHLQIDD 1773
Cdd:PRK02224 530 ETIEEKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKEriesLERIRTLLAA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1774 IAKAKTALE---EQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEEsnkEKQELQEKLQ 1849
Cdd:PRK02224 601 IADAEDEIErlrEKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREERD 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1850 ALQSQVefleqSMVDKSLvsrqeAKIRELETRLEFEKTQVKRLENL---ASRLKETMEKLTEERDQR 1913
Cdd:PRK02224 678 DLQAEI-----GAVENEL-----EELEELRERREALENRVEALEALydeAEELESMYGDLRAELRQR 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1696-2003 |
2.20e-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: 79.72 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1696 QRDFESEKRLRK---DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaaavkarkamevemedlhLQID 1772
Cdd:TIGR02168 172 ERRKETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRE-----------------------LELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1773 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasrdmaqmndlQAQIEESNKEKQELQEKLQALQ 1852
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQEL---------------------EEKLEELRLEVSELEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1853 SqvEFLEQSmvdkslvsrqeAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLR 1932
Cdd:TIGR02168 288 K--ELYALA-----------NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1933 DTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 2003
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1733-1949 |
2.42e-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: 77.50 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1812
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1813 -------HKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLEFE 1885
Cdd:COG4942 113 lyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA---------ELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1886 KTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1949
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1305-1941 |
5.01e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.42 E-value: 5.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELRLssDRLETRISELTSELTDERntgesasQLLDAETAERLRTEKEMKELQTQY 1384
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRL--WFAQRRLELLEAELEELR-------AELARLEAELERLEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1385 DALKKQMevmemevmearliraaeingevddDDAGGEwRLkyERAVREVdftkKRLQQELEDKmeveQQSRRQLERRLGD 1464
Cdd:COG4913 326 DELEAQI------------------------RGNGGD-RL--EQLEREI----ERLERELEER----ERRRARLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1465 LQADSDESQRALQQLKKKCQRLTAELQDtklHLEGQQVRNHELEKKQRRFDSELSQAHEE----TQREKLQREKLQREKD 1540
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEE---ELEALEEALAEAEAALRDLRRELRELEAEiaslERRKSNIPARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1541 MLlAEAFSLKqqmeEKDLDIAGftqkvvsleaELQDISSQESK------------------DEASLAKVKKQL--RDLEA 1600
Cdd:COG4913 448 AL-AEALGLD----EAELPFVG----------ELIEVRPEEERwrgaiervlggfaltllvPPEHYAAALRWVnrLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1601 KVKDQEEELDEQAGSIQMLEQAKL--RLEMEMERMRQTHSKEMESRD-----EEVEEARQ-------SCQKKL------K 1660
Cdd:COG4913 513 RLVYERVRTGLPDPERPRLDPDSLagKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRhpraitrAGQVKGngtrheK 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1661 QMEVQLEEEY------EDKQKALREKR-ELESKLSTLSDQVNQRdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSK 1733
Cdd:COG4913 593 DDRRRIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAE 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1734 REIAQLKNQ---LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE----DQEDM 1806
Cdd:COG4913 668 REIAELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAaedlARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1807 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQveFLEQSMVDKSLVSRQEAKIRELETRLEfek 1886
Cdd:COG4913 748 RALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA--FNREWPAETADLDADLESLPEYLALLD--- 822
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1887 tqvkRLENlaSRLKETMEKLteeRDQRAAAENREKEQ-NKRLQRQLRDTKEEMSEL 1941
Cdd:COG4913 823 ----RLEE--DGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1477-2003 |
1.47e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1477 QQLKKKCQRLTAELQDTKLHLEGQQVRNHElekKQRRFDSELSQAHEETQREKLQREKLQREkDMLLAEAFSLKQQMEEK 1556
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHE---RKQVLEKELKHLREALQQTQQSHAYLTQK-REAQEEQLKKQQLLKQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1557 DLDIAGFT--QKVVSLEAELQDISSQESK---DEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEME 1631
Cdd:TIGR00618 266 RARIEELRaqEAVLEETQERINRARKAAPlaaHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1632 RMRQTHSKEMESRDE-EVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE--SEKRLRKD 1708
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRtsAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1709 LKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcaaAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1788
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ---SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1789 QREKNE-----------------IQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQAL 1851
Cdd:TIGR00618 503 PCPLCGscihpnparqdidnpgpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRS 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1852 QSQVEFLEQSMVD------------KSLVSRQEAKIRELETRLE------FEKTQVKRLENLASRLKETMEKLTEERDQR 1913
Cdd:TIGR00618 583 KEDIPNLQNITVRlqdlteklseaeDMLACEQHALLRKLQPEQDlqdvrlHLQQCSQELALKLTALHALQLTLTQERVRE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1914 AAAENREKEQNKRLQRQLRDTKEE-------------------MSELARKEAEASRKKHELEMDLESLEaanQSLQADLK 1974
Cdd:TIGR00618 663 HALSIRVLPKELLASRQLALQKMQsekeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLG---SDLAARED 739
|
570 580
....*....|....*....|....*....
gi 1907082217 1975 LAFKRIGDLQAAIEDEMESDENEDLINSE 2003
Cdd:TIGR00618 740 ALNQSLKELMHQARTVLKARTEAHFNNNE 768
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1424-1976 |
2.25e-13 |
|
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: 76.01 E-value: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1424 LKYERAVREVDFTKKRLqqeLEDKMEVEQQSRRQLERRLGDLQaDSDESQRALQQL----KKKCQRLTAELQDTKLHLEG 1499
Cdd:pfam10174 41 LKKERALRKEEAARISV---LKEQYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1500 QQVRNHELEKKQRRFDSELSQAHEE------TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLD--IAGFTQKVVS 1569
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1570 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1649
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1650 --EARQSCQKKLKQMEVQLEEEYEDKQKalrEKRELESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLK 1727
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDALR 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1728 NNAPSKREIAQLKNQ----LEESEFTCAAA---------VKARKAMEVE--MEDLHLQIDDIAKAKTALEEQLSRLQREK 1792
Cdd:pfam10174 352 LRLEEKESFLNKKTKqlqdLTEEKSTLAGEirdlkdmldVKERKINVLQkkIENLQEQLRDKDKQLAGLKERVKSLQTDS 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1793 NEIQNRL---EE---DQEDMNELMKKHKAAVAQASRDmaqmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-- 1864
Cdd:pfam10174 432 SNTDTALttlEEalsEKERIIERLKEQREREDRERLE---------ELESLKKENKDLKEKVSALQPELTEKESSLIDlk 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1865 ---KSLVSR---QEAKIRELETRLEFEKTQVKRLENlasRLKETMEKlteERDQRAAAENREKEQNkrLQRqlrdtkeem 1938
Cdd:pfam10174 503 ehaSSLASSglkKDSKLKSLEIAVEQKKEECSKLEN---QLKKAHNA---EEAVRTNPEINDRIRL--LEQ--------- 565
|
570 580 590
....*....|....*....|....*....|....*....
gi 1907082217 1939 sELARKEAEASRKKHELEMDLESL-EAANQSLQADLKLA 1976
Cdd:pfam10174 566 -EVARYKEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1518-1720 |
2.41e-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: 74.42 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1518 LSQAHEETQREKlQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1597
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LEAKVKDQEEELDEQAGSIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1670
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1671 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQ 1720
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1617-1999 |
2.52e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1617 QMLEQaklRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQVNQ 1696
Cdd:COG4717 45 AMLLE---RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1697 -RDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS----KREIAQLKNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQ 1770
Cdd:COG4717 121 lEKLLQLLPLYQELEALEAELAELPERLEELEERLEElrelEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1771 IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK-----------AAVA--------------------- 1818
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLallglggsllsliltiagvlf 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1819 ---------------QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQ----SQVEFLEQSMVDKSLVSRQEAKIRELE 1879
Cdd:COG4717 281 lvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGlppdLSPEELLELLDRIEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1880 TRLEFEKTQvKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAsrkkhELEMDL 1959
Cdd:COG4717 361 EELQLEELE-QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEEL 434
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082217 1960 ESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDL 1999
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGELAEL 474
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1775-1979 |
2.71e-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: 74.03 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1775 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1854
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1855 VEFLEQSMVD--------------KSLVSRQEAK-----IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAA 1915
Cdd:COG4942 99 LEAQKEELAEllralyrlgrqpplALLLSPEDFLdavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1916 AENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1979
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1748-2004 |
3.92e-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: 73.64 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1748 FTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQM 1827
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1828 NDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKirELETRLEFEKTQVKRLENLASRLKETMEKLT 1907
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1908 EERDQRAaaenrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAI 1987
Cdd:COG4942 164 ALRAELE-------AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*..
gi 1907082217 1988 EDEMESDENEDLINSEG 2004
Cdd:COG4942 237 AAAAERTPAAGFAALKG 253
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1427-1965 |
6.81e-13 |
|
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: 74.87 E-value: 6.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1427 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRL----GDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQV 1502
Cdd:pfam12128 275 ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadAAVAKDRSELEALEDQHG---AFLDADIETAAADQEQLPS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1503 RNHELEKKQRRFDSeLSQAHEETQREKLQREKL--QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1580
Cdd:pfam12128 352 WQSELENLEERLKA-LTGKHQDVTAKYNRRRSKikEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEA 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1581 eSKDEASLAKVKKQLRDLEAKVK-----DQEEELDEQAGSIQMLEQAKLRLEM---EMERMrQTHSKEMESRDEEVEEAR 1652
Cdd:pfam12128 431 -GKLEFNEEEYRLKSRLGELKLRlnqatATPELLLQLENFDERIERAREEQEAanaEVERL-QSELRQARKRRDQASEAL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1653 QSCQKKLKQMEVQLEE-------------EYEDKQKALREK---RELESKLSTLSDQVNQRDFESEKR------LRKDLK 1710
Cdd:pfam12128 509 RQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQsigKVISPELLHRTDLDPEVWDGSVGGelnlygVKLDLK 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1711 RTkallaDAQIMLDHlknNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDiakAKTALEEQLSRLQR 1790
Cdd:pfam12128 589 RI-----DVPEWAAS---EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETF---ARTALKNARLDLRR 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1791 EKNEIQNrleeDQEDMNELMKKHKAAVAQASRDMAQ-----MNDLQAQIEESNKEKQELQ-EKLQALQSQVEFLEQSM-- 1862
Cdd:pfam12128 658 LFDEKQS----EKDKKNKALAERKDSANERLNSLEAqlkqlDKKHQAWLEEQKEQKREARtEKQAYWQVVEGALDAQLal 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1863 VDKSLVSRQEAKIRELETRLEFEKTQVKRL---ENLASRLKETMEKLTE-----ERDQRAAAENRE------KEQNKRLQ 1928
Cdd:pfam12128 734 LKAAIAARRSGAKAELKALETWYKRDLASLgvdPDVIAKLKREIRTLERkieriAVRRQEVLRYFDwyqetwLQRRPRLA 813
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1907082217 1929 RQLRDTKEEMSE----LARKEAEASRKKHELEMDLESLEAA 1965
Cdd:pfam12128 814 TQLSNIERAISElqqqLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1627-1967 |
8.63e-13 |
|
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: 74.00 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1627 EMEMERMRQTH---SKEMESRD--EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTlsDQVNQRDFES 1701
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1702 EKRLRKDLKRtkalladaqIMLDHLKNNAPSKREI-AQLKNQLEESEFTcaaavKARKAMEVEMEDLHLQIDDiakaktA 1780
Cdd:pfam17380 373 EISRMRELER---------LQMERQQKNERVRQELeAARKVKILEEERQ-----RKIQQQKVEMEQIRAEQEE------A 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1781 LEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdmaQMNDLQAQIEESNKEKQELqEKLQALQSQVEFLEQ 1860
Cdd:pfam17380 433 RQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQRR 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1861 SMVDKSLVSRQEAKIRELETRLEFEKtqvkrlenlasRLKETMEKLTEERDQRAAAENREKEQN----KRLQRQLRDTKE 1936
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKATE 563
|
330 340 350
....*....|....*....|....*....|...
gi 1907082217 1937 EMSEL--ARKEAEASRKKHELEMDLESLEAANQ 1967
Cdd:pfam17380 564 ERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1416-2021 |
2.17e-12 |
|
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: 73.55 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1416 DDAGGEWRLKYERAVREVDFTKKRLQQeledkmeveqqsrrQLERRLGDLQADSDESQRALQQLKKKCQRLTaELQDTKL 1495
Cdd:TIGR01612 1099 DDFGKEENIKYADEINKIKDDIKNLDQ--------------KIDHHIKALEEIKKKSENYIDEIKAQINDLE-DVADKAI 1163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1496 HLEGQQvrnhELEKKQRRFDSELSQA---HEETQreKLQREKLQREKDmllaeafslKQQMEE-KDLDIAgFTQKVVSLE 1571
Cdd:TIGR01612 1164 SNDDPE----EIEKKIENIVTKIDKKkniYDEIK--KLLNEIAEIEKD---------KTSLEEvKGINLS-YGKNLGKLF 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1572 aeLQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEELDEQAGsIQMLEQAklrlemEMERMRQTHSKEM------ESRD 1645
Cdd:TIGR01612 1228 --LEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMG-IEMDIKA------EMETFNISHDDDKdhhiisKKHD 1297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQscqKKLKQMEVQLEE-EYEDKQKAL--------REKRELESKLSTLSDQVNQRDFESEKRLRKDLKR-TKAL 1715
Cdd:TIGR01612 1298 ENISDIRE---KSLKIIEDFSEEsDINDIKKELqknlldaqKHNSDINLYLNEIANIYNILKLNKIKKIIDEVKEyTKEI 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1716 LADAQIMLDHLKNnapSKREIAQLKNQLeeSEFTCAAAVKArkamEVEMEDLHLQIDDIAKAKTALEEQLSRLQ------ 1789
Cdd:TIGR01612 1375 EENNKNIKDELDK---SEKLIKKIKDDI--NLEECKSKIES----TLDDKDIDECIKKIKELKNHILSEESNIDtyfkna 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1790 REKNE----IQNRLEEDQEDMNELMKKHKAavaQASRDMA-QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvd 1864
Cdd:TIGR01612 1446 DENNEnvllLFKNIEMADNKSQHILKIKKD---NATNDHDfNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQY--- 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1865 KSLVSRQEAKIRELETRLEFEKTQvKRLENLASRLKETMEKLTEErdqraaAENREKEQNKRLQRQLRDTKEemselARK 1944
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAKTK-KDSEIIIKEIKDAHKKFILE------AEKSEQKIKEIKKEKFRIEDD-----AAK 1587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1945 EAEASRKKHELEMDLESLEAanqslqadlklAFKRIGDLQAAIED---EMESDENEdlINSEGDSDVDSELEDRVDGVKS 2021
Cdd:TIGR01612 1588 NDKSNKAAIDIQLSLENFEN-----------KFLKISDIKKKINDclkETESIEKK--ISSFSIDSQDTELKENGDNLNS 1654
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1299-1879 |
2.98e-12 |
|
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: 72.84 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGEsasqlLDAETAERLRTEKE-M 1377
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QELEDKMEVEQQS 1454
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1455 RRQLERRLGDLQADS-------DESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1516
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---------------------AELQ 1575
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1576 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGSIQMLEQAKLRLEM-------EMERMRQTHSKEM 1641
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1642 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLAD 1718
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALD 939
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1719 AQIMLDHLKNNAPSK---REIAQLKNQLEESEFTCAAAVKARKAMevEMEDLHLQIDDIAKAKTALEEQLSR---LQREK 1792
Cdd:pfam15921 940 DRVRDCIIESSLRSDichSSSNSLQTEGSKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPKK 1017
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1793 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmnDLQAQ-IEESNKEKQELQEKLQALQSQVEFLE---QSMvdKSLV 1868
Cdd:pfam15921 1018 SPVHSLLTSSAEGSIGSSSQYRSAKTIHSPDSVK--DSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSMI 1093
|
650
....*....|.
gi 1907082217 1869 SRQEAKIRELE 1879
Cdd:pfam15921 1094 RNQEKRIQKVK 1104
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1304-1818 |
3.41e-12 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 72.06 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELtderntgESASQLLDAETAERLRTEKEMKELQTQ 1383
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDL-------QIATKTICQLTEEKEAQMEELNKAKAA 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1384 YDALKKQMEVMEMEVMeaRLIRAAEINGEVDDDdaggewRLKyeraVREVDFTKKRLQQE----LEDKMEVEQQsrrQLE 1459
Cdd:pfam05483 347 HSFVVTEFEATTCSLE--ELLRTEQQRLEKNED------QLK----IITMELQKKSSELEemtkFKNNKEVELE---ELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1460 RRLGDLQADSDES---QRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQ 1536
Cdd:pfam05483 412 KILAEDEKLLDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELT 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1537 REKDMLLAEAFSLKQqmEEKDLdiagftqkVVSLEAELQDISSQESKDEASLAKVkKQLRDLEAKVKDQEEELDEQAgsI 1616
Cdd:pfam05483 492 AHCDKLLLENKELTQ--EASDM--------TLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELESVREEF--I 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1617 QMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKALREKRELESK-LSTLSDQ 1693
Cdd:pfam05483 559 QKGDEVKCKLDKSEENARSI-EYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENKqLNAYEIK 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1694 VNQRDFEsekrlrkdlkrtkalLADAQIMLDHLKNNAPSKREIAQ-----LKNQLEESEFTCAAAVKARKAMEVE----- 1763
Cdd:pfam05483 638 VNKLELE---------------LASAKQKFEEIIDNYQKEIEDKKiseekLLEEVEKAKAIADEAVKLQKEIDKRcqhki 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1764 ------MEDLHLQIDDI------------------AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1818
Cdd:pfam05483 703 aemvalMEKHKHQYDKIieerdselglyknkeqeqSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1502-2021 |
3.48e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1502 VRNHELEKKQ--RRFDS------ELSQAHEETQREKLQREKLQREKDmlLAEAF-SLKQQMEEKDLDIAGFTQKVVSLEA 1572
Cdd:COG4913 213 VREYMLEEPDtfEAADAlvehfdDLERAHEALEDAREQIELLEPIRE--LAERYaAARERLAELEYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1573 ELQdissqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKL--------RLEMEMERMRQTHskemesr 1644
Cdd:COG4913 291 ELL---------EAELEELRAELARLEAELERLEARLDALREELDELEAQIRgnggdrleQLEREIERLEREL------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1645 dEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQImLD 1724
Cdd:COG4913 355 -EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS-LE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1725 HLKNNAPskREIAQLKNQLEEseftcAAAVKARKA------MEVEMED-------------------------------- 1766
Cdd:COG4913 433 RRKSNIP--ARLLALRDALAE-----ALGLDEAELpfvgelIEVRPEEerwrgaiervlggfaltllvppehyaaalrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1767 ------LHLQIDDI------AKAKTALEEQLSR-LQREKNEIQNRLE------------EDQEDMnelmKKHKAAVAQA- 1820
Cdd:COG4913 506 nrlhlrGRLVYERVrtglpdPERPRLDPDSLAGkLDFKPHPFRAWLEaelgrrfdyvcvDSPEEL----RRHPRAITRAg 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1821 ----SRDMAQMNDL-------------QAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdKSLVSRQEAKIRELETRle 1883
Cdd:COG4913 582 qvkgNGTRHEKDDRrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL--DALQERREALQRLAEYS-- 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1884 FEKTQVKRLENLASRLKETMEKLTEERDQRAAaenrekeqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1963
Cdd:COG4913 658 WDEIDVASAEREIAELEAELERLDASSDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1964 AANQSLQADLKLAFKRIGDLQAAIEDEMesdeNEDLINSEGDSDVDSELEDRVDGVKS 2021
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALLEER----FAAALGDAVERELRENLEERIDALRA 780
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1448-2022 |
3.50e-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: 72.56 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1448 MEVEQQSRRQLERRLGDLQADsDESQRALQQLKKkcQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQA 1521
Cdd:pfam12128 188 MHSKEGKFRDVKSMIVAILED-DGVVPPKSRLNR--QQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1522 HEETQREKLQREKLQREKDMLLAEafslkqqmeekdldiagFTQKVVSLEAELQdissqESKDEASLakvkkQLRDLEAK 1601
Cdd:pfam12128 264 HFGYKSDETLIASRQEERQETSAE-----------------LNQLLRTLDDQWK-----EKRDELNG-----ELSAADAA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1602 VKDQEEEL---DEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEE-------YE 1671
Cdd:pfam12128 317 VAKDRSELealEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiagIK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKALREKRE------------LESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDhlknnapskreiaqL 1739
Cdd:pfam12128 397 DKLAKIREARDrqlavaeddlqaLESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE--------------L 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 KNQLEESEFTCAAAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1819
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1820 ASRDMAQMNDLQAQIEESNK-EKQELQEKLQALQSQVEF--------LEQSMVDKSLVSRQEAKIR--ELETRLEFEKTQ 1888
Cdd:pfam12128 540 LRKEAPDWEQSIGKVISPELlHRTDLDPEVWDGSVGGELnlygvkldLKRIDVPEWAASEEELRERldKAEEALQSAREK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1889 VKRLENLASRLKETMEKLT-EERDQRAAAENREKEQnKRL---QRQLRDTKEEMSELARKEAEASRKK--HELEMDLESL 1962
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRLfdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKH 698
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1963 EAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINSEGDSdVDSELEDRVDGVKSW 2022
Cdd:pfam12128 699 QAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLKAAIAA-RRSGAKAELKALETW 755
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1762-1923 |
4.00e-12 |
|
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: 68.41 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1762 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDMAQMNDLQAQIeESN 1838
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1839 KEkqelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1918
Cdd:COG1579 89 KE-------YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 1907082217 1919 REKEQ 1923
Cdd:COG1579 156 AELEE 160
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1296-1942 |
6.32e-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: 71.79 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1296 PLIQVQLSeeqirNKDEEIQQLRSKLEKVEKERNELRLSSD-RLETRISELTSELTDERntgesasqlldaETAERLRTE 1374
Cdd:pfam12128 350 PSWQSELE-----NLEERLKALTGKHQDVTAKYNRRRSKIKeQNNRDIAGIKDKLAKIR------------EARDRQLAV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1375 KEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDftkkRLQQELEDKMEve 1451
Cdd:pfam12128 413 AE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANA-- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1452 QQSRRQLERRLgdLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdselSQAHEETQREKLQ 1531
Cdd:pfam12128 486 EVERLQSELRQ--ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKE-------APDWEQSIGKVIS 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 REKLQREKDMLLAEAFSLKQQ-------MEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1604
Cdd:pfam12128 557 PELLHRTDLDPEVWDGSVGGElnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1605 QEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKR-EL 1683
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1684 ESKL----STLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHL----KNNAPSKREIAQLKNQLEESEFTCAAAVK 1755
Cdd:pfam12128 717 QAYWqvveGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1756 ARKAME----VEMEDLHLQIDDIAKAKTALEEQLSRLQ------REKNEIQNRLEEDQED-MNELMKKHKAAVAQASRDM 1824
Cdd:pfam12128 797 YFDWYQetwlQRRPRLATQLSNIERAISELQQQLARLIadtklrRAKLEMERKASEKQQVrLSENLRGLRCEMSKLATLK 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1825 AQMNDLQAQ--IEESNKEKQELQEKLQ----ALQSQVEFLEQSMVDKS---------LVSRQEAKIRELETRLEFEKTQV 1889
Cdd:pfam12128 877 EDANSEQAQgsIGERLAQLEDLKLKRDylseSVKKYVEHFKNVIADHSgsglaetweSLREEDHYQNDKGIRLLDYRKLV 956
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1890 KRLENLASRLKETMEKLTEER------------DQRAAAENREKEQNKRLQRQLRDTK--EEMSELA 1942
Cdd:pfam12128 957 PYLEQWFDVRVPQSIMVLREQvsilgvdltefyDVLADFDRRIASFSRELQREVGEEAffEGVSESA 1023
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1305-1921 |
6.62e-12 |
|
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: 71.62 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEE-IQQLRSKLEKVEKERNELRLSSD--RLETRISELTSELTDERNTGESASQLLDaETAErlrTEKEmkelQ 1381
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1382 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQELEDKMEVEQQSRRQLEr 1460
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1461 rLGDLQADSDESQRALQQLKKKcqrltaELQDtklhlegqqVRNHELEKKQRRF-DSELSQAHEETQREKLQREKLQREK 1539
Cdd:TIGR01612 1278 -TFNISHDDDKDHHIISKKHDE------NISD---------IREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1540 DMLLAEAFSLKQQMEEKDL-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1612
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1613 AGSIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELES 1685
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1686 KLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDhLKNN-APSKREIAQLKNQLEE--SEFTCAAAVKARKAMEV 1762
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALA-IKNKfAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEI 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1763 EMEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESn 1838
Cdd:TIGR01612 1575 KKEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSIDSQDT- 1643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1839 kekqELQEKLQALQSQVEFLEqSMVDkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1918
Cdd:TIGR01612 1644 ----ELKENGDNLNSLQEFLE-SLKD------QKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIAN 1712
|
...
gi 1907082217 1919 REK 1921
Cdd:TIGR01612 1713 KEE 1715
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1778-1986 |
7.05e-12 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 69.86 E-value: 7.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1778 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL--QALQSQV 1855
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1856 EFLEQSMVDKSLVSRQeakIRELETRLEFektqvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTK 1935
Cdd:COG3883 98 SGGSVSYLDVLLGSES---FSDFLDRLSA-------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1936 EEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA 1986
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1305-1800 |
7.60e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.22 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntGESASQLLDAETAERLRTEKEMKELQTQy 1384
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELR- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1385 DALKKQMevmemevmearlIRAAEINGEVddddaggewrlkyERAVREVDftkkrlqqELEDKMEVEQQSRRQLERRLGD 1464
Cdd:PRK02224 328 DRLEECR------------VAAQAHNEEA-------------ESLREDAD--------DLEERAEELREEAAELESELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1465 LQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEkkqrrfdSELSQAHEetqREKLQREKLQREKDMlLA 1544
Cdd:PRK02224 375 AREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR-------EERDELRE---REAELEATLRTARER-VE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1545 EAFSLK---------QQMEEKDL--DIAGFTQKVVSLEAELQDISSQESKDEA------SLAKVKKQLRDLEAKVK---- 1603
Cdd:PRK02224 444 EAEALLeagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEERREdlee 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1604 ---DQEEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------E 1668
Cdd:PRK02224 524 liaERRETIEEKRERAEELRERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1669 EYEDKQKALREKRElesKLSTLSDQvnQRDFESEKRLRKDlkrtkalladaqimldhlknnapskreiaQLKNQLEESEF 1748
Cdd:PRK02224 603 DAEDEIERLREKRE---ALAELNDE--RRERLAEKRERKR-----------------------------ELEAEFDEARI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1749 TCAAAVKARKA-----MEVEMEDLHLQIDDIAKAKTALE---EQLSRLQREKNEIQNRLE 1800
Cdd:PRK02224 649 EEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVEnelEELEELRERREALENRVE 708
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1452-1676 |
8.24e-12 |
|
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: 69.41 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1452 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheETQREKLQ 1531
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 REKLQREKDM--LLAEAFSLKQQMEEKDL-DIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEE 1608
Cdd:COG4942 97 AELEAQKEELaeLLRALYRLGRQPPLALLlSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1609 LDEQAGSIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKA 1676
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAER 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1681-1944 |
8.81e-12 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 70.43 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1681 RELESKLSTLSDQVN--------QRDFESEKRlrkdlKRTKALLADAQIMLDHLKNNAPS-KREIAQLKNQLEEseftca 1751
Cdd:PHA02562 177 RELNQQIQTLDMKIDhiqqqiktYNKNIEEQR-----KKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN------ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1752 aavkarkaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdmaQ 1826
Cdd:PHA02562 246 --------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD----------K 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1827 MNDLQAQIEESNKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKL 1906
Cdd:PHA02562 308 LKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907082217 1907 TEERDQRaaaenreKEQNKRLQRQLRDTKEEMSELARK 1944
Cdd:PHA02562 371 QAEFVDN-------AEELAKLQDELDKIVKTKSELVKE 401
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1566-1972 |
1.06e-11 |
|
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: 70.54 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1566 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgsiqmleQAKLRLEMEMERMRQTHSKEMESRD 1645
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQsCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFEsekrlrkdLKRTKALLADAQIMLDH 1725
Cdd:pfam05557 73 EQAELNRL-KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1726 LKNNApskREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhLQIDDIAKAKTALEEQLS--------RLQREKNEIQN 1797
Cdd:pfam05557 144 LKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipelekelERLREHNKHLN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1798 RLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ----------ALQSQVEFLEQSmvDKSL 1867
Cdd:pfam05557 218 ENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQdtglnlrspeDLSRRIEQLQQR--EIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1868 VSRQ-----------------EAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERD-QRAAAENREKEQN-KRLQ 1928
Cdd:pfam05557 296 KEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELTmSNYS 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1907082217 1929 RQLRDTKEEMSELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1972
Cdd:pfam05557 376 PQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1312-1629 |
1.12e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.87 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1312 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTD-ERNTGESASQLLDAEtaERLRTEKE-MKELQTQYDAL-- 1387
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDaSRKIGEIEKEIEQLE--QEEEKLKErLEELEEDLSSLeq 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1388 KKQMEVMEMEVMEARL---------IRAAEinGEVDDDDAGGEWRlKYERAVREVDFTKKRLQ----------QELEDKM 1448
Cdd:TIGR02169 752 EIENVKSELKELEARIeeleedlhkLEEAL--NDLEARLSHSRIP-EIQAELSKLEEEVSRIEarlreieqklNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1449 EVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQRE 1528
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1529 KLQREKLQREKDMLLAEAFSLKQQMEE-------------KDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1595
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEiedpkgedeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL 988
|
330 340 350
....*....|....*....|....*....|....
gi 1907082217 1596 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEME 1629
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1302-1850 |
1.15e-11 |
|
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: 70.15 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1302 LSEEQIRNKDEEIQQLRSKLEKVEKERNElrlsSDRLETRISELTSELTDErnTGESASQLLDAETAERlRTEKEMKELQ 1381
Cdd:pfam05557 66 EAEEALREQAELNRLKKKYLEALNKKLNE----KESQLADAREVISCLKNE--LSELRRQIQRAELELQ-STNSELEELQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1382 TQYDALKKqmevmemevmearliRAAEINGEVDDDDAGGEWRLKYERAVREVDFtkkRLQQELEDKMEVEQQSRRQLerR 1461
Cdd:pfam05557 139 ERLDLLKA---------------KASEAEQLRQNLEKQQSSLAEAEQRIKELEF---EIQSQEQDSEIVKNSKSELA--R 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1462 LGDLQadsdesqRALQQLKKKCQRLTaELQDTKLHLEGQQvrnHELEKKQRRfdselsqahEETQREKLQreKLQREKDM 1541
Cdd:pfam05557 199 IPELE-------KELERLREHNKHLN-ENIENKLLLKEEV---EDLKRKLER---------EEKYREEAA--TLELEKEK 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1542 LLAEAFSLKQQMEEKDLDIA---GFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK-------DQEEELDE 1611
Cdd:pfam05557 257 LEQELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAqylkkieDLNKKLKR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1612 QAGSIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALRE 1679
Cdd:pfam05557 337 HKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLS-------VAEEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1680 KRELESKLSTLSDQVnqrdfesekrlrkDLKRTKALLADAqimldhlknnAPSKREIAQLKNQLEESEFTCAAAVKARKA 1759
Cdd:pfam05557 410 LGGYKQQAQTLEREL-------------QALRQQESLADP----------SYSKEEVDSLRRKLETLELERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1760 MEVEMED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRdma 1825
Cdd:pfam05557 467 LEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK--- 543
|
570 580
....*....|....*....|....*
gi 1907082217 1826 QMNDLQAQIEESNKEKQELQEKLQA 1850
Cdd:pfam05557 544 EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1312-1529 |
1.35e-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: 69.02 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1312 EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQm 1391
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1392 eVMEMEVMEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDFTK----KRLQQELEDKMEVEQQSRRQLE 1459
Cdd:COG4942 99 -LEAQKEELAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPARREQaeelRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1460 RRLGDLQadsdESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEETQREK 1529
Cdd:COG4942 178 ALLAELE----EERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PDZ_SHANK1_3-like |
cd06746 |
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ... |
223-307 |
1.46e-11 |
|
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.
Pssm-ID: 467228 [Multi-domain] Cd Length: 101 Bit Score: 63.00 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 223 LQRRPTGdFGFSLRRT---------TMLDRAPEGQAYRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIV 293
Cdd:cd06746 11 LQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASHEQVV 83
|
90
....*....|....
gi 1907082217 294 EMIRQSGDSVRLKV 307
Cdd:cd06746 84 NLIRQSGNTLVLKV 97
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1497-1883 |
1.50e-11 |
|
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: 69.54 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1497 LEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREkdmllaeafsLKQQMEEKDLDIAGFTQKVVSLEAELQD 1576
Cdd:pfam07888 36 LEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRE----------LESRVAELKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1577 ISsqeskdeASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScQ 1656
Cdd:pfam07888 106 LS-------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-Q 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1657 KKLKQMEVQLeeeyedkqkalrekRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREI 1736
Cdd:pfam07888 178 AKLQQTEEEL--------------RSLSKEFQELRNSLAQRD-TQVLQLQDTITTLTQKLTTAH---RKEAENEALLEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1737 AQLKNQLEESEFTCAA-------AVKARKAMEVEMEDLHLQIDD----IAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1805
Cdd:pfam07888 240 RSLQERLNASERKVEGlgeelssMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRARWAQERETLQQSAEADKDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1806 M----NELMKKHKAAVAQASR------DMAQMNDL-QAQIEESNKEKQELQEKLQALQSQVEFLeqsmvdksLVSRQE-- 1872
Cdd:pfam07888 320 IeklsAELQRLEERLQEERMEreklevELGREKDCnRVQLSESRRELQELKASLRVAQKEKEQL--------QAEKQEll 391
|
410
....*....|.
gi 1907082217 1873 AKIRELETRLE 1883
Cdd:pfam07888 392 EYIRQLEQRLE 402
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1301-1742 |
1.79e-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: 70.15 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1301 QLSEEQiRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1372
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1373 TEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1452
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEIT 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1453 QSRRQLERRLGDLQADSDESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNHelekkqrrfdSELSQAHEET----Q 1526
Cdd:pfam15921 521 KLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIENM----------TQLVGQHGRTagamQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1527 REKLQREKLQREKDMLLAEAFSLKqqmEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1606
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1607 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1655
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1656 QKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDHLKNNAPSKRE 1735
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
....*..
gi 1907082217 1736 IAQLKNQ 1742
Cdd:pfam15921 826 IIQRQEQ 832
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
220-309 |
2.23e-11 |
|
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.
Pssm-ID: 214570 [Multi-domain] Cd Length: 85 Bit Score: 62.01 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGdFGFSLRRttmlDRAPEGQAYrrVVHFAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:smart00228 4 LVELEKGGGG-LGFSLVG----GKDEGGGVV--VSSVVPGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLKKA 73
|
90
....*....|
gi 1907082217 300 GDSVRLKVQP 309
Cdd:smart00228 74 GGKVTLTVLR 83
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1286-1717 |
2.35e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.71 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1286 PWWKLFTTVRPLiQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDA 1365
Cdd:PRK03918 359 ERHELYEEAKAK-KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK---KAIEELKKA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1366 E----TAERLRTEKEMKELQTQYDA-LKKQMEVMEMEVMEARLIRAAEIngEVDDDDAGGEWRLKYERAVREVDFTKKRL 1440
Cdd:PRK03918 435 KgkcpVCGRELTEEHRKELLEEYTAeLKRIEKELKEIEEKERKLRKELR--ELEKVLKKESELIKLKELAEQLKELEEKL 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1441 QQELEDKMEVEQQSRRQLERRLGDLQADS---DESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSE 1517
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKEKLIKLKGEIkslKKELEKLEELKKKLAELEKKLDELEEELA-------ELLKELEELGFE 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1518 LSQAHEETQREklqREKLQREkdmlLAEAFSLKQQMEEKDldiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1597
Cdd:PRK03918 586 SVEELEERLKE---LEPFYNE----YLELKDAEKELEREE-------KELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LEAKVKDQEEEldeqagsiqMLEQAKLRLEMEMERMRqthskemeSRDEEVEEARQSCQKKLKqmevQLEEEYEDKQKAL 1677
Cdd:PRK03918 652 LEKKYSEEEYE---------ELREEYLELSRELAGLR--------AELEELEKRREEIKKTLE----KLKEELEEREKAK 710
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082217 1678 REKRELESKLSTLsdqvnqrdfeseKRLRKDLKRTKALLA 1717
Cdd:PRK03918 711 KELEKLEKALERV------------EELREKVKKYKALLK 738
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1643-1995 |
3.53e-11 |
|
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: 69.05 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1643 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIM 1722
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKNA--------LQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1723 LDHLKNNAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------------------- 1781
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1782 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE--------------LQE 1846
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1847 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQ----VKRLENLASRLKETMEKLTEERDQRAAAEnreke 1922
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1923 qnkrlqRQLRDTKEEMSELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDE 1995
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHE 344
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1516-1904 |
1.24e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 66.78 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1516 SELSQAHEETQREKLQREKLQRE--KDmLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---LEAE--LQDISSQE 1581
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1582 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1653
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1654 SCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEkRLR-------KDLKRTKALLADAQIM---- 1722
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEID-RVKqsytlneSELESVRQLEKQLESLekqy 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1723 LDHLKNNAPSKREIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLE-- 1800
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKRYLEks 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1801 ------EDQEDMNELMKKH-KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM----------- 1862
Cdd:PRK04778 438 nlpglpEDYLEMFFEVSDEiEALAEELEEKPINMEAVNRLLEEATEDVETLEEETEELVENATLTEQLIqyanryrsdne 517
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1863 -VDKSLVS--------RQEAKIRELETRLE-FEKTQVKRLENLASRLKETME 1904
Cdd:PRK04778 518 eVAEALNEaerlfreyDYKAALEIIATALEkVEPGVTKRIEDSYEKEKETIR 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1646-1871 |
1.35e-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: 65.94 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrLRKDLKRTKALLADAQIMLDH 1725
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1726 LKNN-APSKREIAQLKNQ------LEESEFtcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ-- 1796
Cdd:COG4942 102 QKEElAELLRALYRLGRQpplallLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEal 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1797 -NRLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1871
Cdd:COG4942 180 lAELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1299-1577 |
2.36e-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: 66.63 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE-----TAERLRT 1373
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSripeiQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1374 EKEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqELEDKMEVEQQ 1453
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1454 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQrEKLQRE 1533
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-EELSLE 954
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1534 KLQREKDMLLAEAFSLK-------QQMEEKDLDIAGFTQKVVSLEAELQDI 1577
Cdd:TIGR02169 955 DVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1765-1970 |
4.41e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 65.04 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1765 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdmaQMNDLQAQIEESNKEKQEL 1844
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1845 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFEKTQV-----------KRLENLASRLKETM 1903
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSARYtpnhpdvialrAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1904 EKLTEE-RDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQ 1970
Cdd:COG3206 312 QRILASlEAELEALQAREAS----LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1549-1992 |
4.48e-10 |
|
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: 65.38 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1549 LKQQMEEKDLDIAGFTqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ--EEELDEQAGSIQMLEQAKLRL 1626
Cdd:TIGR00618 158 LKAKSKEKKELLMNLF------PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLctPCMPDTYHERKQVLEKELKHL 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1627 EMEMERMRQTHSKEmeSRDEEVEEARQSCQKKLKQMEVQLEE------EYEDKQKALREKRELEsKLSTLSDQVNQRDFE 1700
Cdd:TIGR00618 232 REALQQTQQSHAYL--TQKREAQEEQLKKQQLLKQLRARIEElraqeaVLEETQERINRARKAA-PLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1701 SEkRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL--EESEFTCAAAVKA--RKAMEVEMEDLHlQIDDIAK 1776
Cdd:TIGR00618 309 AQ-RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhsQEIHIRDAHEVATsiREISCQQHTLTQ-HIHTLQQ 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1777 AKTALEEQ-------LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1849
Cdd:TIGR00618 387 QKTTLTQKlqslckeLDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1850 ALQSqvefLEQSMVDKSLVSRQEAKIRELE-TRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQnKRLQ 1928
Cdd:TIGR00618 467 SLKE----REQQLQTKEQIHLQETRKKAVVlARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY-AQLE 541
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1929 RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1992
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE 605
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1424-1988 |
4.55e-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: 65.45 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1424 LKYERAVREVDFTKKRLQQ---ELEDKME-VEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQdtklhLEG 1499
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKdnsELELKMEkVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERR-----LLN 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1500 QQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISS 1579
Cdd:TIGR00606 340 QEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQS 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1580 QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKL 1659
Cdd:TIGR00606 420 KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1660 KQMEVQLEEeyedkqkalrEKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMldhlKNNAPSKREIAQL 1739
Cdd:TIGR00606 500 KKEVKSLQN----------EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIR----KIKSRHSDELTSL 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 ------KNQLEEsefTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRL------EEDQEDMN 1807
Cdd:TIGR00606 566 lgyfpnKKQLED---WLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1808 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ-ALQSQVEFLEqsmvdksLVSRQEAKIRELETRLEFEK 1886
Cdd:TIGR00606 643 RLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQrVFQTEAELQE-------FISDLQSKLRLAPDKLKSTE 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 TQVKRLEnlasRLKETMEKLTEERDQRAAAENRE-KEQNKRLQRQLRDTKEEMSELARKEA--EASRKKHELEMDLESLE 1963
Cdd:TIGR00606 716 SELKKKE----KRRDEMLGLAPGRQSIIDLKEKEiPELRNKLQKVNRDIQRLKNDIEEQETllGTIMPEEESAKVCLTDV 791
|
570 580
....*....|....*....|....*
gi 1907082217 1964 AANQSLQADLKLAFKRIGDLQAAIE 1988
Cdd:TIGR00606 792 TIMERFQMELKDVERKIAQQAAKLQ 816
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1304-1846 |
6.69e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIS-------ELTSELTDERNTGESASQLL---DAETAERLRT 1373
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINdpvyknrNYINDYFKYKNDIENKKQILsniDAEINKYHAI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1374 EKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQELEDKMEVEQ 1452
Cdd:PRK01156 328 IKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSYLKSIESLKKKIEEYSKNIERMSA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1453 QSRRQLERRLGD---LQADSDESQRALQQLKKKCQRLTA----------ELQDTKLHLEGQQV----RNHELEKKQRR-- 1513
Cdd:PRK01156 392 FISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEMLNGQSVcpvcGTTLGEEKSNHii 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1514 --FDSELSQAHEETQREKLQREKLQREKDMLLaeafSLKQQMEEKDLD-IAGFTQKVVSLEAELQDissqeskDEASLAK 1590
Cdd:PRK01156 472 nhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKIESARADLED-------IKIKINE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1591 VKKQlrdleakvKDQEEELDEQAGSIQmLEQAKLRLEMEMERMRQTHSKEME---SRDEEVEEARQSCQKKLKQMEVQLE 1667
Cdd:PRK01156 541 LKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSRSNEIKKQLNDLESRLQEIEIGFP 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1668 EEYEDKQKALrekRELESKLSTLSDQVNQrdFESEKRLRKDLKRTkalladaqimLDHLKNNAPSKREIAQLKNQLeese 1747
Cdd:PRK01156 612 DDKSYIDKSI---REIENEANNLNNKYNE--IQENKILIEKLRGK----------IDNYKKQIAEIDSIIPDLKEI---- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1748 ftcaaAVKARKaMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMnELMKKHKAAVAQAS--RDMA 1825
Cdd:PRK01156 673 -----TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETL-ESMKKIKKAIGDLKrlREAF 745
|
570 580
....*....|....*....|....*..
gi 1907082217 1826 QMNDLQAQIEES------NKEKQELQE 1846
Cdd:PRK01156 746 DKSGVPAMIRKSasqamtSLTRKYLFE 772
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1432-1932 |
6.95e-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: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1432 EVDFTKKRLQQELEDKMEVEQQSRRQLerrlgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQ 1511
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR-----------IELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 RrfdsELSQAHEETQREKLQREKLQREKDMLLAEA----FSLKQQMEEKDLDIAGFTQKVVSLEAELQDIS--------- 1578
Cdd:pfam05557 72 R----EQAELNRLKKKYLEALNKKLNEKESQLADAreviSCLKNELSELRRQIQRAELELQSTNSELEELQerldllkak 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1579 -SQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRL----EMEME----RMRQTHSKEMESRDEEVE 1649
Cdd:pfam05557 148 aSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELaripELEKElerlREHNKHLNENIENKLLLK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1650 EARQSCQKKLKQME------VQLEEEYEDKQKAL---------------------REKRELESKLSTLSDQV-------- 1694
Cdd:pfam05557 228 EEVEDLKRKLEREEkyreeaATLELEKEKLEQELqswvklaqdtglnlrspedlsRRIEQLQQREIVLKEENssltssar 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1695 ----NQRDFESEKR--------LRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLE--ESEFTCAAAVKARKAM 1760
Cdd:pfam05557 308 qlekARRELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1761 EVEMEDLhlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDMAQMNDLQAQIEESNKE 1840
Cdd:pfam05557 382 IEEAEDM---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELE 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1841 KQELQEKLQALQSQVEFLE-QSMVDKS------LVSRQEAKIRELEtrlefeKTQVKRLENLASRLKETMEKLTEERDQR 1913
Cdd:pfam05557 457 RQRLREQKNELEMELERRClQGDYDPKktkvlhLSMNPAAEAYQQR------KNQLEKLQAEIERLKRLLKKLEDDLEQV 530
|
570
....*....|....*....
gi 1907082217 1914 AAAENREKEQNKRLQRQLR 1932
Cdd:pfam05557 531 LRLPETTSTMNFKEVLDLR 549
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
221-310 |
7.27e-10 |
|
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 7 of MUPP1 and PDZ domain 6 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ7 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467159 [Multi-domain] Cd Length: 96 Bit Score: 58.10 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 221 LELQRRPTGDFGFSL---RrtTMLDRAPEGQAYRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGQNVENKSRDEIVE 294
Cdd:cd06671 5 VELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEAVE 79
|
90
....*....|....*.
gi 1907082217 295 MIRQSGDSVRLKVQPI 310
Cdd:cd06671 80 AIRNAGNPVVFLVQSL 95
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1764-1990 |
7.69e-10 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 62.62 E-value: 7.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1764 MEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQE 1843
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1844 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFE-KTQVKRLEN---LASRLKETMEKLteerdQRAAAENR 1919
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRqQTEVLSPEEekeLVEKIKELEKEL-----EKAKKALE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1920 EKEQNKRLQRQLRDTKEEMSELARKEAEASRK--KHELEMDlESLEAANQsLQADLKLAFKRIGDLQAAIEDE 1990
Cdd:COG1340 158 KNEKLKELRAELKELRKEAEEIHKKIKELAEEaqELHEEMI-ELYKEADE-LRKEADELHKEIVEAQEKADEL 228
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1505-1863 |
9.30e-10 |
|
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: 63.72 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1505 HELEKKQRRFDSELSQ--AHEETQREKLQ--REKLQREKDMLLAEAFS-------LKQQMEEKDLDIAGFTQKVVS---L 1570
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1571 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGSIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1643
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1644 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ----------------------VNQRD 1698
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQnkelkeelervqqsytlnenelERVRG 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1699 FESE-KRLRKDLKRTKALLADAQI----MLDHLKnnapskreiaQLKNQLEEseftcaaavkarkaMEVEMEDLHLQIDD 1773
Cdd:pfam06160 334 LEKQlEELEKRYDEIVERLEEKEVayseLQEELE----------EILEQLEE--------------IEEEQEEFKESLQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1774 IAKAKTALEEQLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDMAQ----MNDLQAQIEESNKEKQEL 1844
Cdd:pfam06160 390 LRKDELEAREKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTL 469
|
410
....*....|....*....
gi 1907082217 1845 QEKLQALQSQVEFLEQSMV 1863
Cdd:pfam06160 470 YEKTEELIDNATLAEQLIQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1304-1767 |
1.09e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKD-EEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDE-----------RNTGESASQLLDAETAERL 1371
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1372 RTEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1424
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1425 ---------KYERAVRE----------VDFTKKRLQQELEDKMEVEQQS----------------RRQLERRLGDLQADS 1469
Cdd:COG4913 487 faltllvppEHYAAALRwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1470 desqraLQQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEETQREKLQR 1532
Cdd:COG4913 567 ------PEELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1533 EKLQRekdmlLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1612
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1613 AGSIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKALREKRE-LESKLSTLS 1691
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1692 DQVN------QRDFESEKRlrkDLKRTKALLADAQIMLDHLKNNA-PSKRE-IAQLKNQLEESEFT--CAAAVKARKAME 1761
Cdd:COG4913 787 EELEramrafNREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
....*.
gi 1907082217 1762 VEMEDL 1767
Cdd:COG4913 864 ERIDPL 869
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1428-1976 |
1.13e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 64.21 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1428 RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERR--LGDLQADSDES----QRALQQLKKKCQRLTA------ELQDTKL 1495
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELEARLesLSESVSEARERrmalRQQLEQLQARIQRLAArapawlAAQDALA 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1496 HLEGQQvrNHELEKKQRRfdSELSQAHEETQRE-KLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKV--VSLeA 1572
Cdd:PRK04863 614 RLREQS--GEEFEDSQDV--TEYMQQLLERERElTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAERFggVLL-S 688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1573 EL-QDISSQESKD-EASLAKVKKQL--RDLEAkVKDQEEELDEQAGSIQMLEQAKLRL--------EMEMERMRQTHSKE 1640
Cdd:PRK04863 689 EIyDDVSLEDAPYfSALYGPARHAIvvPDLSD-AAEQLAGLEDCPEDLYLIEGDPDSFddsvfsveELEKAVVVKIADRQ 767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1641 ME-SRDEEV----EEARQscqKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQR-------DFESE-KRLRK 1707
Cdd:PRK04863 768 WRySRFPEVplfgRAARE---KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeaDPEAElRQLNR 844
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1708 DLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESeftcaAAVKARKAMEVEMEDLHLQIDDIAKAK--------- 1778
Cdd:PRK04863 845 RRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPR-----LNLLADETLADRVEEIREQLDEAEEAKrfvqqhgna 919
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1779 -TALEEQLSRLQREKNEI---QNRLEEDQEDMNELMKKHKA-----------AVAQASRDMAQMNDLQAQIEESNKEKQE 1843
Cdd:PRK04863 920 lAQLEPIVSVLQSDPEQFeqlKQDYQQAQQTQRDAKQQAFAltevvqrrahfSYEDAAEMLAKNSDLNEKLRQRLEQAEQ 999
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1844 LQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFEKtqvkRLENLASRLKETME-KLTEERDQRAAAENRE 1920
Cdd:PRK04863 1000 ERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGVPADSGAEeRARARRDELHARLSAN 1072
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1921 KEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1976
Cdd:PRK04863 1073 RSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1304-1905 |
1.22e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.15 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKernELRLSSDRLEtRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTq 1383
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEK---SHSITLKEIE-RLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAES- 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1384 yDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYeravrevDFTKKRlqqELEDKMEVEQQSRRQLERRLG 1463
Cdd:PRK01156 264 -DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKN-------DIENKK---QILSNIDAEINKYHAIIKKLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1464 DLQADSDEsqraLQQLKKKCQRLTAELQDTKLHLEGQQ--VRNHELEKKQRRfdselsqahEETQREKLQREKLQREKDM 1541
Cdd:PRK01156 333 VLQKDYND----YIKKKSRYDDLNNQILELEGYEMDYNsyLKSIESLKKKIE---------EYSKNIERMSAFISEILKI 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1542 LLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEELDEQAG 1614
Cdd:PRK01156 400 QEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHYNEKKS 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1615 SiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLeEEYEDKQKALREKrelESKLSTL 1690
Cdd:PRK01156 480 R---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADL-EDIKIKINELKDK---HDKYEEI 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1691 SDQVNQRDFESekrlrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavKARKAMEVEMEDLHLQ 1770
Cdd:PRK01156 552 KNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1771 IDDIAKaktALEEQLSRLQREKNEIQNrLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ- 1849
Cdd:PRK01156 617 IDKSIR---EIENEANNLNNKYNEIQE-NKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDd 692
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1850 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLaSRLKETMEK 1905
Cdd:PRK01156 693 AKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDL-KRLREAFDK 747
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1734-1915 |
1.33e-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: 61.09 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1734 REIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1813
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1814 kaavaqasRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKtqvKRLE 1893
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170 180
....*....|....*....|..
gi 1907082217 1894 NLASRLKETMEKLTEERDQRAA 1915
Cdd:COG1579 149 EELAELEAELEELEAEREELAA 170
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1569-1968 |
1.42e-09 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 63.77 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1569 SLEAELQDISSQESKDEAS---LAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMermrqthsKEMESRD 1645
Cdd:PRK01156 177 MLRAEISNIDYLEEKLKSSnleLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVeearqscqkklKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkDLKRTKALLADAQIMLDH 1725
Cdd:PRK01156 249 DMK-----------NRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSN 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1726 LKNNAPSKREIAQLKNQLEE--SEFTcaaavkarkAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ 1803
Cdd:PRK01156 317 IDAEINKYHAIIKKLSVLQKdyNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1804 EDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM-----------------VDKS 1866
Cdd:PRK01156 388 RMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1867 L---------VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLTEERDQRAAAENRekeQNKRLQRQLRDTKEE 1937
Cdd:PRK01156 468 NhiinhynekKSRLEEKIREIE-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIK 537
|
410 420 430
....*....|....*....|....*....|..
gi 1907082217 1938 MSELARKEAEASRKKHELE-MDLESLEAANQS 1968
Cdd:PRK01156 538 INELKDKHDKYEEIKNRYKsLKLEDLDSKRTS 569
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1228-1644 |
1.46e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1228 LARLEEQRDEQTSRHLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIQVQLSEEQ 1306
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1307 IRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELT-SELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYD 1385
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1386 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEL 1444
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1521
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1522 HEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1599
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1600 -------AKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESR 1644
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1436-1855 |
1.93e-09 |
|
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: 63.00 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1436 TKKRLQQELEDKMEVEQQSRRQLerrlgdlqadSDESQR---ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQ 1511
Cdd:pfam15964 301 TIERLTKERDDLMSALVSVRSSL----------AEAQQRessAYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 RRFDSEL-SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1590
Cdd:pfam15964 370 ERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1591 VKKQLRDLEAKVKDQEEELdeqagsiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQscqkKLKQMEVQLEEEY 1670
Cdd:pfam15964 450 VCGEMRYQLNQTKMKKDEA-----------------EKEHREYRTKTGRQLEIKDQEIEKLGL----ELSESKQRLEQAQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1671 EDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQLEESEFTC 1750
Cdd:pfam15964 509 QDAARAREECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELT------QKMQQMEAQHDKTVNEQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1751 AAAVKARKAMEVEMED----LHLQIDDIAKAKTALEEQLSR----LQREKNEIQNRLEEDQED------MNELMK----- 1811
Cdd:pfam15964 583 YSLLTSQNTFIAKLKEecctLAKKLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQcvqhgrMHERMKqrlrq 662
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1907082217 1812 --KHKAAVAQasrdmaQMNDLQAQIEESNKEKQELQEKLQALQSQV 1855
Cdd:pfam15964 663 ldKHCQATAQ------QLVQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1440-1854 |
2.14e-09 |
|
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: 62.74 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1440 LQQELEDKMEVEQQSrrqLERRLGDLQADSDESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELS 1519
Cdd:pfam05667 216 LAAAQEWEEEWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSST 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQREKLQR-EKLQREKDMLLAEAFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDL 1598
Cdd:pfam05667 290 TDTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1599 EAKVKDQEEELDEQagsiqmlEQAKLRLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKAL- 1677
Cdd:pfam05667 362 ESSIKQVEEELEEL-------KEQNEELEKQYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLi 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1678 REKRELESKLSTlsdqvnqRDFESEKRLR--KDLK-RTKALLADAQimldhlknnapSKRE-IAQLKNQLEE-------S 1746
Cdd:pfam05667 433 EEYRALKEAKSN-------KEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1747 EFTcaaavkaRKAMEVeMEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRD 1823
Cdd:pfam05667 495 AYT-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKY 562
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907082217 1824 MAQMNDLQAQ----IEESNK---EKQELQEKLQALQSQ 1854
Cdd:pfam05667 563 LAALHENCEQliqtVEETGTimrEIRDLEEQIETESGK 600
|
|
| PDZ5_MAGI-1_3-like |
cd06735 |
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
222-309 |
3.45e-09 |
|
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467217 [Multi-domain] Cd Length: 84 Bit Score: 55.66 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 222 ELQRRPTGdFGFSLRrttmldrapEGQAYRR----VVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06735 5 ELERGPKG-FGFSIR---------GGREYNNmplyVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELI 71
|
90
....*....|...
gi 1907082217 297 RQSGDSVRLKVQP 309
Cdd:cd06735 72 RSGGSVVRLLLRR 84
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
4.03e-09 |
|
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of FRMPD1, FRMPD3, FRMPD4, and related domains. FRMPD1 (also known as FERM domain-containing protein 2, FRMD2), inhibits the malignant phenotype of lung cancer by activating the Hippo pathway via interaction with WWC3; the FRMPD1 PDZ domain binds WWC3. FRMPD3 is a target gene of the neuron-specific transcription factor NPAS4 that is involved in synaptic plasticity. FRMPD4 (also known as PDZ domain-containing protein 10, PDZD10, PDZK10, PSD-95-interacting regulator of spine morphogenesis, and Preso) regulates dendritic spine morphogenesis, and mGluR1/5 signaling; the FRMPD4 PDZ domain binds PAK-interacting exchange factor-beta (betaPix). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This FRMPD1,3,4-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467250 [Multi-domain] Cd Length: 75 Bit Score: 54.94 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRTTMLdrapegqayrrVVHFAEPGaGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQ 298
Cdd:cd06769 1 TVEIQRDAVLGFGFVAGSERPV-----------VVRSVTPG-GPSE---GkLLPGDQILKINNEPVEDLPRERVIDLIRE 65
|
....*....
gi 1907082217 299 SGDSVRLKV 307
Cdd:cd06769 66 CKDSIVLTV 74
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1311-1932 |
4.90e-09 |
|
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: 61.76 E-value: 4.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1311 DEEIQQLRSKLEKVEKERNELRLSSDRLETRIS--ELTSELTDE-----------RNTGESASQLLDAETAERLRTEKEM 1377
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRIEtqKQTLGARDEsikkllemlqsKGLPKKSGEEDWERTRRIAEAEMQL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYD-------ALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGgewrlKYERAVREVDFTKKRLQQELEDKMEV 1450
Cdd:pfam10174 195 GHLEVLLDqkekeniHLREELHRRNQLQPDPAKTKALQTVIEMKDTKIS-----SLERNIRDLEDEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1451 EQQSRRQLE----------RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRR---FDSE 1517
Cdd:pfam10174 270 REEEIKQMEvykshskfmkNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQRaaiLQTE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1518 ---LSQAHEETQR------EKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDissqesKDeasl 1588
Cdd:pfam10174 347 vdaLRLRLEEKESflnkktKQLQD--LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 akvkKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEE 1668
Cdd:pfam10174 415 ----KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQP 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1669 EYEDKQKALREKRELESKLST----LSDQVNQRDFESEKRlRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQL- 1743
Cdd:pfam10174 490 ELTEKESSLIDLKEHASSLASsglkKDSKLKSLEIAVEQK-KEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVa 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1744 ---EESEfTCAAAVKARKAM--EVEMEDlhlqiDDIAKAKTALEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAVA 1818
Cdd:pfam10174 569 rykEESG-KAQAEVERLLGIlrEVENEK-----NDKDKKIAELESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQLL 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1819 QASR---DMAQMNDLQAQIEES----NKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELETRLEF------- 1884
Cdd:pfam10174 639 EEARrreDNLADNSQQLQLEELmgalEKTRQELDATKARLSSTQQSLAEK--DGHLTNLRAERRKQLEEILEMkqealla 716
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1885 ---EK-TQVKRLENLASRLKETMEKLteerdqraAAENREKEqnkRLQRQLR 1932
Cdd:pfam10174 717 aisEKdANIALLELSSSKKKKTQEEV--------MALKREKD---RLVHQLK 757
|
|
| PDZ4_MAGI-1_3-like |
cd06734 |
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
270-309 |
5.53e-09 |
|
PDZ domain 4 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467216 [Multi-domain] Cd Length: 84 Bit Score: 54.93 E-value: 5.53e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082217 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1331-1860 |
5.73e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 61.89 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1331 LRLSSDR------LETRI-----SELTSELTD---ERNTG-ESASQLLDAETAERLRTEKEMKELQTQYDaLKKQMEVME 1395
Cdd:COG3096 187 LRSSSDRskfyrlIEASLyggisSAITRSLRDyllPENSGvRKAFQDMEAALRENRMTLEAIRVTQSDRD-LFKHLITEA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1396 MEVMEARLIRAAEingevddddaggEWRLKYERAV--REVDFTKKRLQQELEDKM-----EVEQQSRRQ--LERrlgDLQ 1466
Cdd:COG3096 266 TNYVAADYMRHAN------------ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAREsdLEQ---DYQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1467 ADSDESQRALQ--QLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDML-- 1542
Cdd:COG3096 331 AASDHLNLVQTalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqt 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1543 -----------LAEAfslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeskdeaslakvkkqLRDLEAKVKDQEEELDE 1611
Cdd:COG3096 411 raiqyqqavqaLEKA---RALCGLPDLTPENAEDYLAAFRAKEQQATEE--------------VLELEQKLSVADAARRQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1612 QAGSIQMLEqaklRLEMEMERmrqthSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLS 1691
Cdd:COG3096 474 FEKAYELVC----KIAGEVER-----SQAWQTARELLRRYRS--QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFC 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1692 dqvnqrdfeseKRLRKDLkrtkallaDAQIMLDHLKnnapskreiAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQI 1771
Cdd:COG3096 543 -----------QRIGQQL--------DAAEELEELL---------AELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1772 D---DIAKAKTALEEQLSRLQREKNEiqnrleedqedmnelmkkhkaAVAQASRDMAQMNDLQAQIEESNKEKQELQEKL 1848
Cdd:COG3096 595 KelaARAPAWLAAQDALERLREQSGE---------------------ALADSQEVTAAMQQLLEREREATVERDELAARK 653
|
570
....*....|..
gi 1907082217 1849 QALQSQVEFLEQ 1860
Cdd:COG3096 654 QALESQIERLSQ 665
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1421-1762 |
6.36e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1421 EWRLKYE-RAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdeSQRALQQLKKKCQRltaELQDTKLHLEG 1499
Cdd:pfam17380 255 EYTVRYNgQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM----------EQERLRQEKEEKAR---EVERRRKLEEA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1500 QQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMLLAEAFSLK-QQMEEKDLDIAGFTQKVVSLEAELQDI 1577
Cdd:pfam17380 322 EKARQAEMDRQAAIYAEQERMAMErERELERIRQEERKRELERIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAA 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1578 SSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQagsIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQ 1653
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1654 SCQKKLKQMEVQLEEEY----------EDKQKALREKR-------ELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALL 1716
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQrrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082217 1717 ADAQIMLDHLKNNAPSKREiAQLKNQLEESEftcaaavKARKAMEV 1762
Cdd:pfam17380 556 EQMRKATEERSRLEAMERE-REMMRQIVESE-------KARAEYEA 593
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1665-2039 |
6.60e-09 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 60.30 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1665 QLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQimldhlknnapskREIAQLKNQLE 1744
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1745 ESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAvaqasrdM 1824
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL-------E 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1825 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSlvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETME 1904
Cdd:COG4372 136 AQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS----EAEAEQALDELLKEANRNAEKEEELAEAEKLIES 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1905 KLTEERDQRAAAENREKEQNkRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1984
Cdd:COG4372 212 LPRELAEELLEAKDSLEAKL-GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEE 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1985 AAIEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPSKAPSDDGSL 2039
Cdd:COG4372 291 AALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1297-1700 |
7.40e-09 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.68 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1297 LIQVQLsEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgESASQLLDAETaerlRTEKE 1376
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1377 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---ELEDKMEVEQQ 1453
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1454 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETqreklqre 1533
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1534 klqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1613
Cdd:pfam07888 230 ----------AENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1614 GSIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKALRE-KRELESKLSTLs 1691
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL- 373
|
....*....
gi 1907082217 1692 dQVNQRDFE 1700
Cdd:pfam07888 374 -RVAQKEKE 381
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1737-2001 |
7.87e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 59.55 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1737 AQLKNQLEESEFTCAAAVKARKAM-EVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1815
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1816 AvaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTQVK----R 1891
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNVEmdaaR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1892 LENLASRLKETMEKLTEE-RDQRAAAENREKEQNKRLQRQ-------LRDTKEEMSELarkeaeaSRKKHELEMDLESLE 1963
Cdd:pfam00038 165 KLDLTSALAEIRAQYEEIaAKNREEAEEWYQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1964 AANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 2001
Cdd:pfam00038 238 KQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
9.65e-09 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 54.21 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRttMLDRAPEGQAYRRVVHFaepGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 1907082217 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1730-1925 |
1.33e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1730 APSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1809
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1810 ---MKKHKAAV-----------------------AQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV 1863
Cdd:COG3883 92 araLYRSGGSVsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1864 D-KSLVSRQEAKIRELETRlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNK 1925
Cdd:COG3883 172 ElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1680-1945 |
1.62e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 60.31 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1680 KRELESKLSTLSDQvnqRDFESEKrlrkdlkrtKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEseftcaAAVKARKA 1759
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAED---------KLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1760 MEvEMEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESN 1838
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1839 K---------------EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEfekTQVKRLENLAS-- 1897
Cdd:PRK11281 177 NllkggkvggkalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1898 RLKETMEKLTEERDQRAAAEN-------REKEQNKRLQRQLRDTKEEMSELARKE 1945
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1595-1945 |
2.28e-08 |
|
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: 58.39 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1595 LRDLEAKV------KDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEE-VEEARQSCQKKLKQMEVQLE 1667
Cdd:pfam13868 8 LRELNSKLlaakcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEErKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1668 EEYEDKQKALREKRELesklstLSDQVNQRDFESEKRLRKDLKRTKAlladaqimldhlknnapsKREIAQLKNQLEESe 1747
Cdd:pfam13868 88 KRQEEYEEKLQEREQM------DEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQAEW- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1748 ftcaaavKARKAMEVEMEDlhLQIDDIAKAKTALEEQLSRLQ----REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1823
Cdd:pfam13868 143 -------KELEKEEEREED--ERILEYLKEKAEREEEREAEReeieEEKEREIARLRAQQEKAQDEKAERDELRAKLYQE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 MAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV-----DKSLVSRQEAKIRELEtRLEFEKTQVKRLENLasR 1898
Cdd:pfam13868 214 EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeeaerEEEEFERMLRKQAEDE-EIEQEEAEKRRMKRL--E 290
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1907082217 1899 LKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1945
Cdd:pfam13868 291 HRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PDZ_SNX27-like |
cd23070 |
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ... |
231-307 |
2.62e-08 |
|
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SNX27, and related domains. SNX27 is involved in retrograde transport from endosome to plasma membrane. The PDZ domain of SNX27 links cargo identification to retromer-mediated transport. SNX27 binds to the retromer complex (vacuolar protein sorting 26(VPS26)-VPS29-VPS35), via its PDZ domain binding to VPS26. The SNX27 PDZ domain also binds to cargo including the G-protein-coupled receptors (GPCRs): beta2-adrenergic receptor (beta2AR), beta1AR, parathyroid hormone receptor (PTHR), alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs), NMDA receptors, 5-hydroxytryptamine 4a receptors, frizzled receptors, and somatostatin receptor subtype 5 (SSTR5). Additional binding partners of the SNX27 PDZ domain include G protein-gated inwardly rectifying potassium (Kir3) channels, angiotensin-converting enzyme 2 (ACE2), and PTEN (phosphatase and tensin homolog deleted on chromosome 10); PTEN binding to SNX27 prevents SNX27's association with the retromer complex. SNX27 has been reported to be a host factor needed for efficient entry of an engineered SARS-CoV-2 variant, the spike protein of which contains a deletion at the S1/S2 subunit cleavage site; the PDZ domain of SNX27 binds angiotensin-converting enzyme 2 (ACE2), and may be involved in recycling ACE2 to the plasma membrane, thereby promoting viral entry. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SNX27-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467283 [Multi-domain] Cd Length: 93 Bit Score: 53.57 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 231 FGFSLRRTTMLD---RAPEGQAYRRVVHFA---EPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23070 12 FGFNVRGQVSEGgqlRSINGELYAPLQHVSavlEGGAADKA---GVRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELT 88
|
...
gi 1907082217 305 LKV 307
Cdd:cd23070 89 LTV 91
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1733-1949 |
3.00e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 59.26 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEftcaAAVKARKAmEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1812
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1813 HKAAVAQASRDmAQMNDLQAQIEESNKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1885
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1886 KTQVKRLENLASRLKETMEKLTEERDQRAaaenrekeqnkRLQRQLRDTKEEMSELARKEAEAS 1949
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAELR-----------RLEREVEVARELYESLLQRLEEAR 378
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1303-1976 |
3.01e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.59 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1303 SEEQIRNKDEEIQQLRSKLEKVEKERNEL----RLSSDRL------------ETRISELTSELTDERNTGESASQLLDAE 1366
Cdd:PRK04863 298 SRRQLAAEQYRLVEMARELAELNEAESDLeqdyQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1367 TAER----LRTEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAvREVDF 1435
Cdd:PRK04863 378 QEENearaEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQA-KEQEA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1436 TKKRLQqeLEDKMEVEQQSRRQLERRLGDLQ--ADSDESQRALQQLKKKCQRL-TAELQDTKLhlegQQVRNHElekkqr 1512
Cdd:PRK04863 455 TEELLS--LEQKLSVAQAAHSQFEQAYQLVRkiAGEVSRSEAWDVARELLRRLrEQRHLAEQL----QQLRMRL------ 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1513 rfdSELSQAHEETQR-EKLQREKLQREKDMLLAEAFsLKQQMEEkdldiagftqkvvsLEAELQDISSQeskdeaslakv 1591
Cdd:PRK04863 523 ---SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES----------- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1592 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQMEVQlEEEYE 1671
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELTVE-RDELA 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 dkqkalREKRELESKLSTLSdqvnQRDFESEKRLRKDLKRTKA-LLAD--AQIMLDhlknNAP----------------- 1731
Cdd:PRK04863 652 ------ARKQALDEEIERLS----QPGGSEDPRLNALAERFGGvLLSEiyDDVSLE----DAPyfsalygparhaivvpd 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1732 ---SKREIAQLKNQLEE------------------SEFTCAAAVK-----------------ARKAMEVEMEDLHLQIDD 1773
Cdd:PRK04863 718 lsdAAEQLAGLEDCPEDlyliegdpdsfddsvfsvEELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREE 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1774 IAkaktaleEQLSRLQREKNEIQnRLeedQEDMNELMKKHkAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1853
Cdd:PRK04863 798 LA-------ERYATLSFDVQKLQ-RL---HQAFSRFIGSH-LAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QVEFLEQSMV-------------DKSLVSRQEAkIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnRE 1920
Cdd:PRK04863 866 QLEQAKEGLSalnrllprlnllaDETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLK-QD 943
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1921 KEQNKRLQRQLRDTKEEMSEL-ARKEAEASrkkHELEMDLESLEAANQSLQADLKLA 1976
Cdd:PRK04863 944 YQQAQQTQRDAKQQAFALTEVvQRRAHFSY---EDAAEMLAKNSDLNEKLRQRLEQA 997
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1470-1684 |
4.10e-08 |
|
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: 56.21 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1470 DESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKqrrfdselSQAHEETQREKlqreklQREKDMLLAE 1545
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRR--------IQTLEESLEQH------ERMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1546 AFSLKQQMEEKDL-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGSIQMLEQAK 1623
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1624 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKALREkRELE 1684
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1733-1964 |
4.33e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1812
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNE----LREELDE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1813 HKAAVAQASRDMAQMNDLQAQIEE----------SNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRL 1882
Cdd:COG1340 97 LRKELAELNKAGGSIDKLRKEIERlewrqqtevlSPEEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1883 EFEKTQVKRLENLASRLKETMEKLTEERDQ-RAAAE-------------NREKEQNKRLQRQLRDTKEEMSELARKEAEA 1948
Cdd:COG1340 177 EEIHKKIKELAEEAQELHEEMIELYKEADElRKEADelhkeiveaqekaDELHEEIIELQKELRELRKELKKLRKKQRAL 256
|
250
....*....|....*.
gi 1907082217 1949 SRKKHELEMDLESLEA 1964
Cdd:COG1340 257 KREKEKEELEEKAEEI 272
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1547-1931 |
4.37e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 58.69 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1547 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ-------EEELDEQAGSIQML 1619
Cdd:PRK04778 101 RKAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANrfsfgpaLDELEKQLENLEEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1620 -------------EQAK---LRLEMEMERMRQThskeMesrdEEVEEARQSCQKKLKQmevQLEEEYEDKQKALREKREL 1683
Cdd:PRK04778 181 fsqfveltesgdyVEAReilDQLEEELAALEQI----M----EEIPELLKELQTELPD---QLQELKAGYRELVEEGYHL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1684 ESKlstlsdqvnqrDFESE-KRLRKDLKRTKALLADAQimLDHLK-NNAPSKREIAQLKNQLEeseftcaAAVKARKAME 1761
Cdd:PRK04778 250 DHL-----------DIEKEiQDLKEQIDENLALLEELD--LDEAEeKNEEIQERIDQLYDILE-------REVKARKYVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1762 VEMEDLHLQIDDIAKAKTALEEQLSRLQ-----------------REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDM 1824
Cdd:PRK04778 310 KNSDTLPDFLEHAKEQNKELKEEIDRVKqsytlneselesvrqleKQLESLEKQYDEITERIAEQEIAYSELQEELEEIL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1825 AQMNDLQAQIEESN-------KEKQELQEKLQALQSQVE----FLEQS---------MVDKSLVSRQeakIRELETRLE- 1883
Cdd:PRK04778 390 KQLEEIEKEQEKLSemlqglrKDELEAREKLERYRNKLHeikrYLEKSnlpglpedyLEMFFEVSDE---IEALAEELEe 466
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1884 --FEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAE------NREKEQNKRLQRQL 1931
Cdd:PRK04778 467 kpINMEAVNRLLEEATEDVETLEEETEElVENATLTEqliqyaNRYRSDNEEVAEAL 523
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1510-1938 |
6.05e-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: 57.94 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1510 KQRRFDSELSQAheETQREKLQ----REKLQREKDMLLA-EAFSLKQQMEEKDLDIAgfTQKVVSLEAELQDIssQESKD 1584
Cdd:pfam06160 4 LRKKIYKEIDEL--EERKNELMnlpvQEELSKVKKLNLTgETQEKFEEWRKKWDDIV--TKSLPDIEELLFEA--EELND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1585 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsKEMESRdEEVEEAR---QSCQKKLKQ 1661
Cdd:pfam06160 78 KYRFKKAKKALDEIEELLDDIEEDIKQILEELDELLE-----------------SEEKNR-EEVEELKdkyRELRKTLLA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1662 MEVQLEEEYEDKQKALrekRELESKLSTLSDQVNQRDFESEK----RLRKDLKRTKALLADAQIMLDHLKNNAPskREIA 1737
Cdd:pfam06160 140 NRFSYGPAIDELEKQL---AEIEEEFSQFEELTESGDYLEARevleKLEEETDALEELMEDIPPLYEELKTELP--DQLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1738 QLKN---QLEESEFtcaaaVKARKAMEVEMEDLHlqiDDIAKAKTALEE-QLSRLQREKNEIQNRLEEDQEDM------- 1806
Cdd:pfam06160 215 ELKEgyrEMEEEGY-----ALEHLNVDKEIQQLE---EQLEENLALLENlELDEAEEALEEIEERIDQLYDLLekevdak 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1807 NELMKKHKAAVAQASRDMAQMNDLQAQIEESNK----------EKQELQEKLQALQSQVEFLEQSMVDKSLV-SRQEAKI 1875
Cdd:pfam06160 287 KYVEKNLPEIEDYLEHAEEQNKELKEELERVQQsytlneneleRVRGLEKQLEELEKRYDEIVERLEEKEVAySELQEEL 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1876 RELETRLE-FEKTQVKrlenlasrLKETMEKLTEErdqraaaENREKEQNKRLQRQLRDTKEEM 1938
Cdd:pfam06160 367 EEILEQLEeIEEEQEE--------FKESLQSLRKD-------ELEAREKLDEFKLELREIKRLV 415
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1674-1850 |
6.12e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1674 QKALREKRELESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQIMLDHLKNnapskrEIAQLKNQLEESEFTCAAA 1753
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1754 VKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQ 1831
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 1907082217 1832 AQIEESNKEKQELQEKLQA 1850
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
7.31e-08 |
|
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.
Pssm-ID: 467623 [Multi-domain] Cd Length: 88 Bit Score: 52.10 E-value: 7.31e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| PDZ_tamalin_CYTIP-like |
cd06713 |
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ... |
223-307 |
1.21e-07 |
|
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467197 [Multi-domain] Cd Length: 91 Bit Score: 51.47 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 223 LQRRPTGDFGF-------------SLRRTTMLDRapegqayrrvVHFAEPGagtkDLAlGLVPGDRLVEINGQNVENKSR 289
Cdd:cd06713 8 LEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVEGASH 72
|
90
....*....|....*...
gi 1907082217 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06713 73 QEIVELIRSSGNTLRLET 90
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1770-2005 |
1.25e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.95 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1770 QIDDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdmaqmnDLQAQIEESNKEKQELQEKL 1848
Cdd:PHA02562 167 EMDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1849 QALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeKTQVKRLENLASRLKE------TMEKLTEERDQRAAAENREKE 1922
Cdd:PHA02562 237 EELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKggvcptCTQQISEGPDRITKIKDKLKE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1923 QNKRLqRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAA---IEDEMES--DENE 1997
Cdd:PHA02562 311 LQHSL-EKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEfvdNAEELAKlqDELD 389
|
....*...
gi 1907082217 1998 DLINSEGD 2005
Cdd:PHA02562 390 KIVKTKSE 397
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1756-1952 |
1.33e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 55.69 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1756 ARKAMEVEMEDLHLQIDDIAKA-------KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQ-----ASRD 1823
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEieelkekRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKvkelkEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 M--AQMNDLQAQIEESNKEKQELQEK---LQALQSQVEFLEQSMVDKSLVSRQE----AKIRELETRLEfektQVKRLEN 1894
Cdd:COG1340 82 ElnEKLNELREELDELRKELAELNKAggsIDKLRKEIERLEWRQQTEVLSPEEEkelvEKIKELEKELE----KAKKALE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1895 LASRLKETMEKLTEERDQraAAENREKEQNKRLQRQlrDTKEEMSELaRKEAEASRKK 1952
Cdd:COG1340 158 KNEKLKELRAELKELRKE--AEEIHKKIKELAEEAQ--ELHEEMIEL-YKEADELRKE 210
|
|
| PDZ_SYNJ2BP-like |
cd06709 |
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ... |
220-308 |
1.40e-07 |
|
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNJ2BP, and related domains. SYNJ2BP (also known as mitochondrial outer membrane protein 25, OMP25) regulates endocytosis of activin type 2 receptor kinases through the Ral/RALBP1-dependent pathway and may be involved in suppression of activin-induced signal transduction. Binding partners of the SYNJ2BP PDZ domain include activin type II receptors (ActR-II), and SYNJ2. SYNJ2BP interacts with the PDZ binding motif of the Notch Delta-like ligand 1 (DLL1) and DLL4, promoting Delta-Notch signaling, and inhibiting sprouting angiogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNJ2BP-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467193 [Multi-domain] Cd Length: 86 Bit Score: 51.14 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGdFGFSLRRTTMLDRAPEGQA-YrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTDQPYIPNDSGiY--VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAVELFR 75
|
90
....*....|.
gi 1907082217 298 QSGDSVRLKVQ 308
Cdd:cd06709 76 NAGEDVKLKVQ 86
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1304-1801 |
1.55e-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: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNE-------LRLSSDRLETRISELTSELTderntgesasqlldaetaerlRTEKE 1376
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1377 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERAVREVDFTKKRLQQELEDK--- 1447
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEEKESFLNKKTKQLQDLTEEKstl 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1448 ----------MEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHL--------EGQQV-----RN 1504
Cdd:pfam10174 379 ageirdlkdmLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALttleealsEKERIierlkEQ 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1505 HELEKKQRRFDSELSQAHEETQREK---LQREKLQREKDM--LLAEAFSLKQQMEEKD-----LDIAGFTQK--VVSLEA 1572
Cdd:pfam10174 459 REREDRERLEELESLKKENKDLKEKvsaLQPELTEKESSLidLKEHASSLASSGLKKDsklksLEIAVEQKKeeCSKLEN 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1573 ELQDISSQESKDEASlAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAkLRlEMEMERmrqtHSKEMESRDEEVEEAR 1652
Cdd:pfam10174 539 QLKKAHNAEEAVRTN-PEINDRIRLLEQEVARYKEESGKAQAEVERLLGI-LR-EVENEK----NDKDKKIAELESLTLR 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1653 QSCQKKLKQMEVQLEEEyEDKQKALREKRELESKLSTLSDQVNQRDFE----SEKRLRKDLKRTKALLADAQIMLD---- 1724
Cdd:pfam10174 612 QMKEQNKKVANIKHGQQ-EMKKKGAQLLEEARRREDNLADNSQQLQLEelmgALEKTRQELDATKARLSSTQQSLAekdg 690
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1725 HLKNNAPSKREiaQLKNQLEESEFTCAAAVKARKAmevemeDLHLQIDDIAKAKTALEEQLSrLQREKNEIQNRLEE 1801
Cdd:pfam10174 691 HLTNLRAERRK--QLEEILEMKQEALLAAISEKDA------NIALLELSSSKKKKTQEEVMA-LKREKDRLVHQLKQ 758
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1572-1755 |
2.08e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 56.18 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1572 AELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMER------MRQTH------SK 1639
Cdd:PHA02562 216 ARKQNKYDELVEEAKTI---KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqkvikMYEKGgvcptcTQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1640 EMESRDEEVEEARQS---CQKKLKQMEVQLEEEYE---DKQKALREKRELESKLSTLsDQVNQRDFESEKRLRKDLKRTK 1713
Cdd:PHA02562 293 QISEGPDRITKIKDKlkeLQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTN-KQSLITLVDKAKKVKAAIEELQ 371
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907082217 1714 ALLADaqimldhlknnapSKREIAQLKNQLEESEFTCAAAVK 1755
Cdd:PHA02562 372 AEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1299-1992 |
2.10e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 56.76 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNkdeEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESasqllDAETAERLRTEKEMK 1378
Cdd:PTZ00440 788 TILNKENKISN---DINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT-----EDENLNLKELEKEFN 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1379 ELQTQYDALKKQMEvmemevmearliraaEINGEVDdddaggewrlkyerAVREVDFTKKRL---QQELEDKMEVEQQSR 1455
Cdd:PTZ00440 860 ENNQIVDNIIKDIE---------------NMNKNIN--------------IIKTLNIAINRSnsnKQLVEHLLNNKIDLK 910
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1456 RQLERRLGDLQADS----DESQRALQQLKKKCQRLTAELQDTK---LHLEGQQVRNHeLEKKQRRFDSELSQAHEETQRE 1528
Cdd:PTZ00440 911 NKLEQHMKIINTDNiiqkNEKLNLLNNLNKEKEKIEKQLSDTKinnLKMQIEKTLEY-YDKSKENINGNDGTHLEKLDKE 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1529 KLQREKLQREKDMLLAEAFSLKQQM-------------------EEKDLDIAGFTQKVVSLEAELQD-ISSQESKDEASL 1588
Cdd:PTZ00440 990 KDEWEHFKSEIDKLNVNYNILNKKIddlikkqhddiielidkliKEKGKEIEEKVDQYISLLEKMKTkLSSFHFNIDIKK 1069
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 ---AKVKKQLRDLEAKVKDQEEELDEQAGSIqmlEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLKQMEVQ 1665
Cdd:PTZ00440 1070 yknPKIKEEIKLLEEKVEALLKKIDENKNKL---IEIKNKSHEHVVNAD----KEKNKQTEHYNKKKKSLEKIYKQMEKT 1142
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1666 LEE--EYEDKQKALRE--KRELESKLSTLSDQVNQRDFESEKR--LRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQL 1739
Cdd:PTZ00440 1143 LKEleNMNLEDITLNEvnEIEIEYERILIDHIVEQINNEAKKSktIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAY 1222
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 KNQLEESEFTCAAAVKARKAMEVEMEDlHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdQEDMNELMK--KHKAAV 1817
Cdd:PTZ00440 1223 YDKATASYENIEELTTEAKGLKGEANR-STNVDELKEIKLQVFSYLQQVIKENNKMENALHE-IKNMYEFLIsiDSEKIL 1300
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1818 AQASRDMAQM----NDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKSLvsrqEAKIRELETRLEFEKTQVKRLE 1893
Cdd:PTZ00440 1301 KEILNSTKKAeefsNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQI----DDEIKKIEQIKEEISNKRKEIN 1376
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1894 NLASRLKETMEKLTEE-------RDQRAAAENREKEQNKRLQR--------QLRDTKEEMSELARKEAEASRKK---HEL 1955
Cdd:PTZ00440 1377 KYLSNIKSNKEKCDLHvrnasrgKDKIDFLNKHEAIEPSNSKEvniikitdNINKCKQYSNEAMETENKADENNdsiIKY 1456
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907082217 1956 EMDLESLeaANQSLQADLKLAFKRIGDLQAAIEDEME 1992
Cdd:PTZ00440 1457 EKEITNI--LNNSSILGKKTKLEKKKKEATNIMDDIN 1491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1842-2027 |
2.26e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1842 QELQEKLQALQSQVEFLeqsmvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREK 1921
Cdd:COG1196 216 RELKEELKELEAELLLL---------------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1922 EQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLIN 2001
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180
....*....|....*....|....*.
gi 1907082217 2002 SEGDSDVDSELEDRVDGVKSWLSKNK 2027
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAE 386
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1585-1947 |
2.53e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.50 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1585 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1660
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1661 QMEVQLEEEYEDKQKALREKRELESKLSTLSDQVnqrdfesekrlrkdlKRTKALLADAQIMLDHLKnnapsKREIA--Q 1738
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1739 LKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQreknEIQNRLEEdqedmneLMKKHKAAVA 1818
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ----AAHSQFEQ-------AYQLVRKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1819 QASRDMAQmNDLQAQIEESNKEKQELQeKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASR 1898
Cdd:PRK04863 488 EVSRSEAW-DVARELLRRLREQRHLAE-QLQQLRMRLSELEQ---RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE 562
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907082217 1899 LKETMEKLTEErdQRAAAENREkeqnkRLQRQLRDTKEEMSELARKEAE 1947
Cdd:PRK04863 563 LEARLESLSES--VSEARERRM-----ALRQQLEQLQARIQRLAARAPA 604
|
|
| PDZ2_L-delphilin-like |
cd06744 |
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
224-308 |
3.22e-07 |
|
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467226 [Multi-domain] Cd Length: 75 Bit Score: 49.58 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 224 QRRPTGDFGFSLRrttmlDRAPegqAYRRVVhfaEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSV 303
Cdd:cd06744 4 VYRGNGSFGFTLR-----GHAP---VYIESV---DPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGSMP 70
|
....*
gi 1907082217 304 RLKVQ 308
Cdd:cd06744 71 TLVVE 75
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1443-1818 |
4.17e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1443 ELEDKMEVEQQSRRQLERRLGDLQADSDESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSEL 1518
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1519 SQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1598
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1599 EAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEearqscqKKLKQMEVQLEEEYEDKQKALR 1678
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE-------KLIESLPRELAEELLEAKDSLE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1679 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARK 1758
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALS 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1759 AMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1818
Cdd:COG4372 309 LIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1656-1997 |
5.11e-07 |
|
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: 54.96 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1656 QKKLKQMEVQ-LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLR--KDLKRTKALLadaQIMLDHLKNNAPS 1732
Cdd:COG5185 165 FGKLTQELNQnLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGseSTLLEKAKEI---INIEEALKGFQDP 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEFtcaaAVKARKamEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE-----DQEDMN 1807
Cdd:COG5185 242 ESELEDLAQTSDKLEK----LVEQNT--DLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSidikkATESLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1808 ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQEAKIRELETRLEFEKT 1887
Cdd:COG5185 316 EQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKE 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1888 ----QVKRLENLASRLKETMEKLTEERDQraaaenrekeQNKRLQRQLRDTKEEMSELARK--EAEASRKKHELEMDLES 1961
Cdd:COG5185 392 sldeIPQNQRGYAQEILATLEDTLKAADR----------QIEELQRQIEQATSSNEEVSKLlnELISELNKVMREADEES 461
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1907082217 1962 LE-------AANQSLQADLKLAFKRIGDLQAAIEDEMESDENE 1997
Cdd:COG5185 462 QSrleeaydEINRSVRSKKEDLNEELTQIESRVSTLKATLEKL 504
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
5.25e-07 |
|
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467174 [Multi-domain] Cd Length: 99 Bit Score: 50.04 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLR----RTTMLDRAPegqayrrVVHFAEPGAGTKDLALgLVPGDRLVEINGQNVENKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 1907082217 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1624-1974 |
5.25e-07 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 55.25 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1624 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKALrekrELESKLSTLSDqvnqrdfESEK 1703
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLRE-------EFSK 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1704 RLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEeseftcaaavkarkamevemedlhlQIDDIAKAKTALEE 1783
Cdd:PLN03229 498 ANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1784 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDMAQMNDLQAQIEESNKEKQ-ELQEKLQALQSQVEFL 1858
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1859 EQsmvdKSLVSRQEAKIRELETRLEFEKTQV-KRLENL--ASRLKETMEKLTEERDQRAAAEN-REKEQNKRLQRQLRDT 1934
Cdd:PLN03229 632 TK----KNKDTAEQTPPPNLQEKIESLNEEInKKIERVirSSDLKSKIELLKLEVAKASKTPDvTEKEKIEALEQQIKQK 707
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1907082217 1935 -KEEMSELARKEaeasrKKHELEMDLESLEAANQSLQADLK 1974
Cdd:PLN03229 708 iAEALNSSELKE-----KFEELEAELAAARETAAESNGSLK 743
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1641-1854 |
6.24e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1641 MESRDEEVEEARQSCQKKLKQMEVQLEEeyedKQKALREKRElESKLSTLSDQVNQRDfESEKRLRKDLKRTKALLADAQ 1720
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQ-KNGLVDLSEEAKLLL-QQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1721 IMLDHLKNNAPSKRE----------IAQLKNQLEESEFTCAAAVK-------ARKAMEVEMEDLHLQIDD-IAKAKTALE 1782
Cdd:COG3206 240 ARLAALRAQLGSGPDalpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1783 EQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1854
Cdd:COG3206 320 AELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
6.41e-07 |
|
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of human PTPN13, and related domains. PTPN13, also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1), negatively regulates FAS-mediated apoptosis and NGFR-mediated pro-apoptotic signaling, and may also regulate phosphoinositide 3-kinase (PI3K) signaling. It contains 5 PDZ domains; interaction partners of its second PDZ domain (PDZ2) include the Fas receptor (TNFRSF6) and thyroid receptor-interacting protein 6 (TRIP6). The second PDZ (PDZ2) domain, but not PDZ1 or PDZ3, of FRMPD2 binds to GluN2A and GluN2B, two subunits of N-methyl-d-aspartic acid (NMDA) receptors. Other binding partners of the FRMPDZ2 PDZ2 domain include NOD2, and catenin family members, delta catenin (CTNND2), armadillo repeat gene deleted in velo-cardio-facial syndrome (ARVCF) and p0071 (also known as plakophilin 4; PKP4). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467254 [Multi-domain] Cd Length: 87 Bit Score: 49.13 E-value: 6.41e-07
10 20 30
....*....|....*....|....*....|....*.
gi 1907082217 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1299-1992 |
6.55e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 55.34 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNEL------------RLSSDRLETRISELTSELTDERNtgESASQLLDAE 1366
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqALEKARALCGLPDLTPENAEDYL--AAFRAKEQQA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1367 TAERLRTEKEM---KELQTQYDAlkkqmevmemevmEARLIRAaeINGEVDDDDAggewrlkYERAvREVdftkkrLQQE 1443
Cdd:COG3096 454 TEEVLELEQKLsvaDAARRQFEK-------------AYELVCK--IAGEVERSQA-------WQTA-REL------LRRY 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1444 LEDKMEVEQQSrrQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhlegqqvrNHELEKKQRRFDSELSQAHE 1523
Cdd:COG3096 505 RSQQALAQRLQ--QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA-----------AEELEELLAELEAQLEELEE 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1524 ETQREKLQREKLQREKDMLLAEAFSLKQQmeekdldiAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1603
Cdd:COG3096 572 QAAEAVEQRSELRQQLEQLRARIKELAAR--------APAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREAT 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1604 DQEEEldeqagsiqmLEQAKLRLEMEMERMRQTHSkemesrdeeVEEARqscqkkLKQME-----VQLEEEYEDkqKALR 1678
Cdd:COG3096 644 VERDE----------LAARKQALESQIERLSQPGG---------AEDPR------LLALAerlggVLLSEIYDD--VTLE 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1679 EKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKRE-----IAQLKN-QLEESEFTcAA 1752
Cdd:COG3096 697 DAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLYLIEGDPDSFDDSVFDAEEledavVVKLSDrQWRYSRFP-EV 775
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1753 AVKARKAMEVEMEDLHLQIDDIAK--AKTAL----------------------------EEQLSRLQREKNEIQNRLEED 1802
Cdd:COG3096 776 PLFGRAAREKRLEELRAERDELAEqyAKASFdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQH 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1803 QEDmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL 1882
Cdd:COG3096 856 RAQ----EQQLRQQLDQLKEQLQLLNKLLPQANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLV 926
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1883 ----------EFEKTQVKRLENLASRLKETMEKLTEERDQRAA----------AENRekEQNKRLQRQLRDTKEEMSElA 1942
Cdd:COG3096 927 avlqsdpeqfEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedavgllGENS--DLNEKLRARLEQAEEARRE-A 1003
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1943 RKEAEASRKKHE----LEMDLES-LEAANQSLQAdlklAFKRIGDLQAAIEDEME 1992
Cdd:COG3096 1004 REQLRQAQAQYSqynqVLASLKSsRDAKQQTLQE----LEQELEELGVQADAEAE 1054
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1452-1785 |
7.30e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.14 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1452 QQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQ 1531
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 REKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR-----DLEAKVKDQE 1606
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1607 EELDEQAGSIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELE 1684
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1685 SKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1764
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVG 349
|
330 340
....*....|....*....|.
gi 1907082217 1765 EDLHLQIDDIAKAKTALEEQL 1785
Cdd:COG4372 350 LLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1816-1990 |
8.04e-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: 52.62 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1816 AVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKTQVKRLEN 1894
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAaKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1895 LASRLK-----ETMEK-LTEERDQRAAAENREKEQNKRLqrqlrDTKEEmsELARKEAEASRKKHELEMDLESLEAANQS 1968
Cdd:COG1579 81 QLGNVRnnkeyEALQKeIESLKRRISDLEDEILELMERI-----EELEE--ELAELEAELAELEAELEEKKAELDEELAE 153
|
170 180
....*....|....*....|..
gi 1907082217 1969 LQADLKLAFKRIGDLQAAIEDE 1990
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPE 175
|
|
| PDZ2_DLG5-like |
cd06765 |
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
270-308 |
1.04e-06 |
|
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PSZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467246 [Multi-domain] Cd Length: 77 Bit Score: 48.50 E-value: 1.04e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1907082217 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1517-1707 |
1.14e-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: 52.23 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1596
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1597 DLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEMERMRqthskemesrdEEVEEArqscQKKLKQMEVQLEE---EYEDK 1673
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIEELE-----------EELAEL----EAELAELEAELEEkkaELDEE 150
|
170 180 190
....*....|....*....|....*....|....*
gi 1907082217 1674 QKALREKRE-LESKLSTLSDQVNQRDFESEKRLRK 1707
Cdd:COG1579 151 LAELEAELEeLEAEREELAAKIPPELLALYERIRK 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1305-1730 |
1.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESAsqlldaeTAERLRTEKEMKELQTQY 1384
Cdd:PRK02224 349 EDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-------PVDLGNAEDFLEELREER 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1385 DALKKQMEVMEMEVMEAR-LIRAAEingevddddaggewRLKYERAVREVDftkkrlqQELEDKMEVEQQSRRqlERRLG 1463
Cdd:PRK02224 422 DELREREAELEATLRTAReRVEEAE--------------ALLEAGKCPECG-------QPVEGSPHVETIEED--RERVE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1464 DLQADSDESQRALQQLKKKCQRLTaELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLL 1543
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE-------RLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1544 AEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdeaSLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAK 1623
Cdd:PRK02224 551 AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLAAIADAEDEIERLREKREALAELNDERR 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1624 LRLEMEMERMRQTHSKEMESRdeeVEEARQScqkklKQMEVQLEEEYEDKQKALREKR-ELESKLSTLsdqvnQRDFESE 1702
Cdd:PRK02224 627 ERLAEKRERKRELEAEFDEAR---IEEARED-----KERAEEYLEQVEEKLDELREERdDLQAEIGAV-----ENELEEL 693
|
410 420
....*....|....*....|....*...
gi 1907082217 1703 KRLRKDLKRtkalLADAQIMLDHLKNNA 1730
Cdd:PRK02224 694 EELRERREA----LENRVEALEALYDEA 717
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1456-1612 |
1.62e-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: 51.85 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1456 RQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLhlegqQVRNHELEKKQrrfdselSQAHEETQREKLQREKL 1535
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-----EIKRLELEIEE-------VEARIKKYEEQLGNVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1536 QREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1612
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1445-1867 |
1.75e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1521
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1522 HEETQREKLQREKLQREKDML--LAEAFSLkqqmeekdLDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1599
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1600 akvkdqeEELDEQAGSIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1671
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKALREKRELESKLSTLSDQVNQ-RDfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKREI-AQLKNQLEesEFT 1749
Cdd:PRK04863 975 DAAEMLAKNSDLNEKLRQRLEQAEQeRT-----RAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1750 CAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDMAQM 1827
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1907082217 1828 NDLqaqieesnkEKQELQEKLQALQSQVeflEQSMVDKSL 1867
Cdd:PRK04863 1128 NGV---------ERRLHRRELAYLSADE---LRSMSDKAL 1155
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1700-1999 |
1.76e-06 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 52.51 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1700 ESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMevemedlhlqiddiAKAKT 1779
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1780 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQS 1853
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QVEFLEQSMVDkslvsrqeakireletrlefEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD 1933
Cdd:pfam15905 206 KLVSTEKEKIE--------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1934 TKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1999
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1311-1612 |
2.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1311 DEEIQQLRSKLEKVEKERNELRLSSDRLEtrisELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1390
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1391 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDKMeveqqsrRQLERRLGDLQADSD 1470
Cdd:COG4913 736 LEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAM-------RAFNREWPAETADLD 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1471 ESQRALQQLKKKCQRLTAElqdtklHLEGQQVRNHELEKKQ-----RRFDSELSQAHEETqreklqREKLQREKDMLLAE 1545
Cdd:COG4913 809 ADLESLPEYLALLDRLEED------GLPEYEERFKELLNENsiefvADLLSKLRRAIREI------KERIDPLNDSLKRI 876
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1546 AFS----LKQQMEE-KDLDIAGFTQkvvsleaELQDISSQESKDEASLAKVK-KQLRDLEAKVKDQEEELDEQ 1612
Cdd:COG4913 877 PFGpgryLRLEARPrPDPEVREFRQ-------ELRAVTSGASLFDEELSEARfAALKRLIERLRSEEEESDRR 942
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1485-1850 |
2.68e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1485 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFT 1564
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1565 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMErMRQTHSKEMESR 1644
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1645 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLD 1724
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1725 HLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1804
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1805 DM----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQA 1850
Cdd:COG4372 316 ALlaalLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1526-1716 |
3.30e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1526 QREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK--VVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK 1603
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1604 DQEEELDE---------QAGSIQMLEQAKLRLEMEMERMRQTHSKE---MESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1671
Cdd:COG3206 244 ALRAQLGSgpdalpellQSPVIQQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQEAQRILASLEAELE 323
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082217 1672 DKQKALREKRELESKLSTLSDQVNQRDFESEkRLRKDLKRTKALL 1716
Cdd:COG3206 324 ALQAREASLQAQLAQLEARLAELPELEAELR-RLEREVEVARELY 367
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1365-1613 |
3.31e-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: 52.07 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1365 AETAERLRTEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEL 1444
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1524
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1525 TQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1604
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 1907082217 1605 QEEELDEQA 1613
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1304-1973 |
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: 53.03 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1304 EEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQTQ 1383
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1384 YDALKKQMEVMEMEVmeARLIRAAEINGE-VDDDDAGGEWRLKYERAVREVDFTKKRLQQEledKMEVEQQSRRQLerrl 1462
Cdd:COG3096 594 IKELAARAPAWLAAQ--DALERLREQSGEaLADSQEVTAAMQQLLEREREATVERDELAAR---KQALESQIERLS---- 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1463 gdlQADSDESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ-------------- 1511
Cdd:COG3096 665 ---QPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcpedlyli 737
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 ----RRFDSELSQAHEETQREKLQREKLQ----------------REK--DMLLAEAFSLKQQMEEKDLDIagftQKVVS 1569
Cdd:COG3096 738 egdpDSFDDSVFDAEELEDAVVVKLSDRQwrysrfpevplfgraaREKrlEELRAERDELAEQYAKASFDV----QKLQR 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1570 LEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKEMES 1643
Cdd:COG3096 814 LHQAFSQFVGGhlavafAPDPEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKLLPQANLLADET 890
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1644 RDEEVEEARqscqkklkqmevqleEEYEDKQKALREKRELESKLSTLSDQVN--QRDFESEKRLRKDLKRTKALLADAQI 1721
Cdd:COG3096 891 LADRLEELR---------------EELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDPEQFEQLQADYLQAKEQQRRLKQ 955
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1722 MLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAKaktaleeqlsrlqrekneiqnRLEE 1801
Cdd:COG3096 956 QIFALSE-------------------------VVQRRP--------HFSYEDAVG---------------------LLGE 981
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1802 DQeDMNELMKkHKAAVAQASRDMA--QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA 1873
Cdd:COG3096 982 NS-DLNEKLR-ARLEQAEEARREAreQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELeelgvqADAEAEERARI 1059
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1874 KIRELETRL--------EFEKTQVKR---LENLASRLKETMEKLTEERDQRAAAenreKEQNKRLQRQLRDTKEE----M 1938
Cdd:COG3096 1060 RRDELHEELsqnrsrrsQLEKQLTRCeaeMDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVErrlhR 1135
|
730 740 750
....*....|....*....|....*....|....*
gi 1907082217 1939 SELARKEAEASRkkhelEMDLESLEAANQSlQADL 1973
Cdd:COG3096 1136 RELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1551-1850 |
3.78e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1551 QQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAGSIQMLEQAKLRLEMEM 1630
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK----ELREEAQELREKRDELNEKVKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1631 ERMRQTHSKEMESRDEEVEEarqscQKKLKQMEVQLEEEYEDKQKALrekRELESKLstlsdQVNQRDFESEKRLRKDLK 1710
Cdd:COG1340 77 KEERDELNEKLNELREELDE-----LRKELAELNKAGGSIDKLRKEI---ERLEWRQ-----QTEVLSPEEEKELVEKIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1711 RTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQR 1790
Cdd:COG1340 144 ELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1791 EKNEIQNRLEEDQEDMNELMKKHKAAvaqasRDMAQMNDLQAQIEESNKEKQELQEKLQA 1850
Cdd:COG1340 224 KADELHEEIIELQKELRELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1646-1954 |
3.79e-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: 52.27 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRtkallA 1717
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKS-----I 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1718 DAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaAAVKARKA-MEVEMEDLHLQIDDIAKAKTAL--EEQLSRLQREKNE 1794
Cdd:COG5185 306 DIKKATESLEEQLAAAEAEQELEESKRETE----TGIQNLTAeIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1795 IQNRLE----EDQEDMNELMKKHKAAVAQASRDMA----QMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVDKS 1866
Cdd:COG5185 382 FKDTIEstkeSLDEIPQNQRGYAQEILATLEDTLKaadrQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEES 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1867 LVSRQEAK---IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELAR 1943
Cdd:COG5185 462 QSRLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
330
....*....|.
gi 1907082217 1944 KEAEASRKKHE 1954
Cdd:COG5185 542 ENLIPASELIQ 552
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1582-1697 |
4.01e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1582 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1661
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907082217 1662 MEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQR 1697
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEK 618
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1455-1967 |
4.16e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1455 RRQLERRLGDLQADSDESQRALQ-------QLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1520
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEaaeaakaQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1521 ---AHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEkdldiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1596
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1597 DLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKA 1676
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1677 LREKREL----ESKLSTLSDQvNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIA-QLKNQLEEsEFTCA 1751
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1752 AAVKARKAMEvemedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDMAQMNDL- 1830
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLa 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1831 QAQIEESNKEKQElQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELETRLEFEKT------------QVKRLENLASR 1898
Cdd:pfam05701 401 QAAREELRKAKEE-AEQAKAAASTVE------------SRLEAVLKEIEAAKASEKLalaaikalqeseSSAESTNQEDS 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1899 LKETMEKLTEERDQRAAAENREKEQNKRLQR---QLRDTKEEMSELARKEAEASRkkhELEMDLESLEAANQ 1967
Cdd:pfam05701 468 PRGVTLSLEEYYELSKRAHEAEELANKRVAEavsQIEEAKESELRSLEKLEEVNR---EMEERKEALKIALE 536
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1590-1745 |
4.36e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1590 KVKKQLRDLEAKVKDQEEELDEQAGSIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1669
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1670 YEDKQKALREKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLAD--AQIMLDHLKNNApsKREIAQLKNQLE 1744
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 1907082217 1745 E 1745
Cdd:PRK12704 180 E 180
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
586-872 |
4.45e-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: 52.44 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 586 LLEAFGNSPTIMNGSATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 654
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 655 A-----TLRTELHLNHL----------AENNVFGIVplSKPEEKQKAAQQFSKLQAAMKVLAISPEEQKTCWLILASIYH 719
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 720 LGAAgatkePLEEQDEAAEAGRKQFARHEWAQKAAYLLGC-SLEELSSAIFKhqlKGGTLQRSTSFRQGPEESGLGEGTK 798
Cdd:cd14894 413 LGNI-----ELDYREVSGKLVMSSTGALNAPQKVVELLELgSVEKLERMLMT---KSVSLQSTSETFEVTLEKGQVNHVR 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 799 lsaleclEGMASGLYSELFTLLISLVNRALKSS-------QHSLCS----------MMIVDTPGFQNpewggsARGASFE 861
Cdd:cd14894 485 -------DTLARLLYQLAFNYVVFVMNEATKMSalstdgnKHQMDSnasapeavslLKIVDVFGFED------LTHNSLD 551
|
330
....*....|.
gi 1907082217 862 ELCHNYAQDRL 872
Cdd:cd14894 552 QLCINYLSEKL 562
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1646-1964 |
4.75e-06 |
|
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: 51.99 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1646 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDF----------ESEKRLRKDLKRTKAL 1715
Cdd:pfam15070 18 ENLKEEGAVWQQKMQQLSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAeeeqppagpsEEEQRLQEEAEQLQKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1716 LADAQIML-DHLKNNAPSKREIAQLKNQLEESEFTC---AAAVKARKAMeveMEDLHLQIDDIAKAKT---ALEEQLSRL 1788
Cdd:pfam15070 98 LEALAGQLqAQVQDNEQLSRLNQEQEQRLLELERAAerwGEQAEDRKQI---LEDMQSDRATISRALSqnrELKEQLAEL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1789 Q-------REKNEIQNRLEEDQEDMNELMKKhkaavaqasrdMAQMN----DLQAQIEESNKEKQELQEK----LQALQS 1853
Cdd:pfam15070 175 QngfvkltNENMELTSALQSEQHVKKELAKK-----------LGQLQeelgELKETLELKSQEAQSLQEQrdqyLAHLQQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVK-RLENLASRLKETMEKLTeerdqrAAAenrekEQNKRLQRQLR 1932
Cdd:pfam15070 244 YVAAYQQLASEKEELHKQYLLQTQLMDRLQHEEVQGKvAAEMARQELQETQERLE------ALT-----QQNQQLQAQLS 312
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907082217 1933 DTKEEMS----ELARKEAEASRKKHELEMDLESLEA 1964
Cdd:pfam15070 313 LLANPGEgdglESEEEEEEAPRPSLSIPEDFESREA 348
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1303-1919 |
4.77e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1303 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT 1382
Cdd:PRK04863 514 QLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1383 QYDALKKQMEVMEMEVmeARLIRAAEINGEVDDDDAGGEwrlkyeravrevDFTKKRLQQELEDKMEVEQ--QSRRQLER 1460
Cdd:PRK04863 594 RIQRLAARAPAWLAAQ--DALARLREQSGEEFEDSQDVT------------EYMQQLLERERELTVERDElaARKQALDE 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1461 RLGDLQADSDESQRALQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ------------ 1511
Cdd:PRK04863 660 EIERLSQPGGSEDPRLNAL---AERFGGVLlseiyDDVSLEdapyfsaLYGPArhaivVPDLSDAAEQlagledcpedly 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 ------RRFDSELSQAhEETQREKLQRE-----------------KLQREK--DMLLAEAFSLKQQMEEKDLDIagftQK 1566
Cdd:PRK04863 737 liegdpDSFDDSVFSV-EELEKAVVVKIadrqwrysrfpevplfgRAAREKriEQLRAEREELAERYATLSFDV----QK 811
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1567 VVSLEAELQDISSQ------ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAgsiQMLEQAKLRLEMEMERMRQTHSKE 1640
Cdd:PRK04863 812 LQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELERALADHESQEQQQR---SQLEQAKEGLSALNRLLPRLNLLA 888
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1641 MESRDEEVEEARQscqkklkqmevQLEEEYEDK------QKALrekRELESKLSTLsdQVNQRDFEsekRLRKDLKRTKA 1714
Cdd:PRK04863 889 DETLADRVEEIRE-----------QLDEAEEAKrfvqqhGNAL---AQLEPIVSVL--QSDPEQFE---QLKQDYQQAQQ 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1715 LLADAQIMLDHLKNnapskreiaqlknqleeseftcaaaVKARKAmevemedlHLQIDDIAK---AKTALEEQLSRlqre 1791
Cdd:PRK04863 950 TQRDAKQQAFALTE-------------------------VVQRRA--------HFSYEDAAEmlaKNSDLNEKLRQ---- 992
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1792 kneiqnRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEF--LEQSMVDKS--- 1866
Cdd:PRK04863 993 ------RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgaEERARARRDelh 1066
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1867 -LVSRQEAKIRELETRLEFEKTqvkRLENLASRLKETMEKLTEERDQRAAAENR 1919
Cdd:PRK04863 1067 aRLSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAKAG 1117
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1585-1945 |
4.78e-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: 52.26 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1585 EASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscQKKLK 1660
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL----TERLE 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1661 QMEVQLEEEYEDKQKAlREKRElesklstlsdqvnqrdfesekRLRKDLKRTKALLADAQIMLDHLKNNAPSKReiaQLK 1740
Cdd:COG3096 365 EQEEVVEEAAEQLAEA-EARLE---------------------AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1741 NQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAV-AQ 1819
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVeRS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1820 ASRDMAQmndlqaQIEESNKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELEtrlEFEKTQVKRLENlASRL 1899
Cdd:COG3096 492 QAWQTAR------ELLRRYRSQQALAQRLQQLRAQLAELEQ------RLRQQQNAERLLE---EFCQRIGQQLDA-AEEL 555
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1907082217 1900 KETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKE 1945
Cdd:COG3096 556 EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| PDZ_Par6-like |
cd06718 |
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ... |
222-297 |
5.77e-06 |
|
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F (RhoGAP100F), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Par6 (also known as PAR6 or Par-6), RhoGAP100F, and related domains. Par6 is part of a conserved machinery that directs metazoan cell polarity, a process necessary for the function of diverse cell types. Par6 forms a cell polarity-regulatory complex with atypical protein kinase C (aPKC) and Par3. Par6 can also directly associate with PALS1 (proteins associated with Lin7, also known as Stardust) providing a link between the Par3/aPKC/Par6 complex and the PALS1-PATJ (protein-associated TJ) complex. Binding partners of the Par6-PDZ domain include Par3, PALS1/Stardust; leucine-rich repeat-containing protein netrin-G ligand-2 (NGL-2), human crumbs (CRB3) involve in the morphogenesis of the tight junctions in mammalian epithelial cells, and PAR-6 co-operates with the Par6 semi-CRIB domain to bind CDC42. CDC42 regulates the Par6 PDZ domain through an allosteric CRIB-PDZ transition. Drosophila RhoGAP100F, also known as synapse defective protein 1 homolog (syd-1 homolog), is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound form. The RhoGAP100F-PDZ domain binds the neurexin C terminus to control synapse formation at the Drosophila neuromuscular junction. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par6-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467202 [Multi-domain] Cd Length: 84 Bit Score: 46.41 E-value: 5.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 222 ELQRRPTGDFGFSLRRTTMLDRAPeGQAYRRVVhfaePGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIR 297
Cdd:cd06718 4 ELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1305-1972 |
6.04e-06 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 52.14 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1305 EQIRNKDEEIQQLRSKLEKVEKER------NELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAeRLRTEKEMK 1378
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1379 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQELEDKMEVEQQSRRQ 1457
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1458 LERRLGDLQADSDesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EET 1525
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1526 QREKLQREKLQREKDML------LAEAFSLKQQMEEKDLDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1597
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LEAKVKDQEEELDEQAGSIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1671
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKA---LREKRELESKLSTLSDQVNQRDFES-EKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEES- 1746
Cdd:PTZ00440 1553 IKDEIetiLNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1747 --------EFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1811
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1812 KhkaavaqASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFEKTQVKR 1891
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1892 LENLASRLKETMEKLTEErDQRAAAENREKEQNKRLQRQLRDT-KEE-------------------MSELARKE--AEAS 1949
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDE-NNLSDSLNQAEDKNKEVANLTHYTnKNEaknllghvvksanfigikiMTGLQPTEltPDAS 1863
|
730 740 750
....*....|....*....|....*....|
gi 1907082217 1950 RKK-------HELEMDLESLEAANQSLQAD 1972
Cdd:PTZ00440 1864 LETapeltfeSENNSDLELDHLSSNKNELD 1893
|
|
| PDZ4_PTPN13-like |
cd06696 |
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
220-307 |
6.06e-06 |
|
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)] and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467182 [Multi-domain] Cd Length: 85 Bit Score: 46.53 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRTTMldraPEGQAYRRVVHfaEPgagtkdlALG---LVPGDRLVEINGQNVENKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 1907082217 297 RQSGDSVRLKV 307
Cdd:cd06696 72 RAAPKEVTLVL 82
|
|
| PDZ3_Dlg1-2-4-like |
cd06795 |
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
237-312 |
6.45e-06 |
|
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila Dlg1, human Dlg1, 2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197; SAP-97), Dlg2 (also known as channel-associated protein of synapse-110; postsynaptic density protein 93, PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95; synapse-associated protein 90, SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling, regulating surface expression of NMDA receptors in dorsal horn neurons of the spinal cord; it interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. The Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development; postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467257 [Multi-domain] Cd Length: 91 Bit Score: 46.58 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 237 RTTMLDRAPEGQAYRRV---------VHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06795 3 RKIVLHKGSTGLGFNIVggedgegifISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKNAGQTVTIIA 81
|
....*
gi 1907082217 308 QPIPE 312
Cdd:cd06795 82 QYKPE 86
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1739-1973 |
6.53e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 6.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1739 LKNQLEESEFTCAAAVKARKAMEVEMEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1818
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1819 QASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSR--QEAKIRELETRLEFEKTQVK 1890
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELermkerAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1891 RL--------------ENLASRLKETMEKLTeerdQRAAAENREKEQNKRLQRQLRDTKEEmselarkeAEASRKKHE-L 1955
Cdd:pfam07888 189 SLskefqelrnslaqrDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQER--------LNASERKVEgL 256
|
250
....*....|....*...
gi 1907082217 1956 EMDLESLEAANQSLQADL 1973
Cdd:pfam07888 257 GEELSSMAAQRDRTQAEL 274
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
6.92e-06 |
|
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1-7 (also known as MAGUK p55 subfamily members 1-7), and related domains. MPPs comprise a subfamily of a larger group of multidomain proteins, namely, membrane-associated guanylate kinases (MAGUKs). MPPs form diverse protein complexes at the cell membranes, which are involved in a wide range of cellular processes, including establishing proper cell structure, polarity and cell adhesion. MPPs have only one PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467208 [Multi-domain] Cd Length: 80 Bit Score: 46.10 E-value: 6.92e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1907082217 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
7.31e-06 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ domain-containing protein 2 (FRMPD2), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], FRMPD2 (also known as PDZ domain-containing protein 4; PDZ domain-containing protein 5C), and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. FRMPD2 is localized in the basolateral membranes of polarized epithelial cells and is associated with tight junction formation and immune response; it contains 3 PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467180 [Multi-domain] Cd Length: 92 Bit Score: 46.62 E-value: 7.31e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907082217 258 EPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRL 305
Cdd:cd06694 38 IPG-GPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1520-1746 |
7.50e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1599
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1600 AKVKDQEEELDEQAGSIQMLEQAKLRLEM---------------EMERMRQTHSKEMesrdEEVEEARQSCQKKLKQMEV 1664
Cdd:COG3883 79 AEIEERREELGERARALYRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLL----EELKADKAELEAKKAELEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1665 QLEEEYEDKQKALREKRELESKLSTLSDQVNQrdfesekrLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLE 1744
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQ--------LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
..
gi 1907082217 1745 ES 1746
Cdd:COG3883 227 AA 228
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1441-1940 |
7.59e-06 |
|
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: 51.45 E-value: 7.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1441 QQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSELSQ 1520
Cdd:pfam15964 219 RLELEKLKLLYEAKTEVLESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAVLAQ 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1521 AHEETQREKLQRekLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QLRDL 1598
Cdd:pfam15964 293 THTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQCEQL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1599 EAKVKDQEEELDEQAGSiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqKALR 1678
Cdd:pfam15964 362 KSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------KVTR 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1679 EKRELESKLSTLSDQVNQRDFESEK---RLRKDLKRTKALLADAQimLDHLKNNAPSKR-------EIAQLKNQLEESef 1748
Cdd:pfam15964 425 EKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAE--KEHREYRTKTGRqleikdqEIEKLGLELSES-- 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1749 tcaaavkaRKAMEVEMEDLHLQIDDIAKaktaLEEQLSRLQREKNeiqnrleedqedmneLMKKHKAAVAQASRDMAQMN 1828
Cdd:pfam15964 501 --------KQRLEQAQQDAARAREECLK----LTELLGESEHQLH---------------LTRLEKESIQQSFSNEAKAQ 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1829 DLQAQIEEsnkekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTE 1908
Cdd:pfam15964 554 ALQAQQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQ 612
|
490 500 510
....*....|....*....|....*....|..
gi 1907082217 1909 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSE 1940
Cdd:pfam15964 613 KSRSEVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1298-1617 |
7.90e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1377
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYDALKKQMevmemevmearliraaeingevddddaggewrlkyeravrevdftkKRLQQELEDKmeveQQSRRQ 1457
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1458 LERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQR 1537
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1538 EKDMLLAEAfslKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQ 1617
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1309-1634 |
8.85e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 50.30 E-value: 8.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1309 NKDEEIQQLRSKL----EKVEkernELRLSSDRLETRISELTSELTDERN--------TGESASQLLDAETAERLRTEKE 1376
Cdd:pfam00038 1 NEKEQLQELNDRLasyiDKVR----FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1377 MKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQELedkmeveq 1452
Cdd:pfam00038 77 LDNLRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEEV-------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1453 qsrRQLERRLGDlqadsdeSQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQAhEETQREKLQ 1531
Cdd:pfam00038 145 ---RELQAQVSD-------TQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQA-AARNGDALR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 REKlqrekdmllAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1611
Cdd:pfam00038 214 SAK---------EEITELRRTIQSLEIELQSLKKQKASLERQLAET---EERYELQLADYQELISELEAELQETRQEMAR 281
|
330 340
....*....|....*....|...
gi 1907082217 1612 QAGSIQMLEQAKLRLEMEMERMR 1634
Cdd:pfam00038 282 QLREYQELLNVKLALDIEIATYR 304
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
220-307 |
8.94e-06 |
|
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467185 [Multi-domain] Cd Length: 98 Bit Score: 46.45 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLR------RTTMLDRAPEGQAYRRVVHfaePGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEI 292
Cdd:cd06701 6 ELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGATHQEA 79
|
90
....*....|....*
gi 1907082217 293 VEMIRQSGDSVRLKV 307
Cdd:cd06701 80 VRILRSVGDTLTLLV 94
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1445-1998 |
9.43e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.34 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLE----RRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1511
Cdd:PRK10246 231 EEKQLLTAQQQQQQSlnwlTRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHweriqeqsaALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDlDIAGFTQKVVSLEAELqdisSQESKDEASLAKV 1591
Cdd:PRK10246 311 QQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHD-RFRQWNNELAGWRAQF----SQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1592 KKQLRDLEAKVKDQEE-----ELDEQAGSI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQME 1663
Cdd:PRK10246 386 QQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQRN 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1664 VQLEEeyedKQKALREKRELESKLSTLSDQvnqrdfesEKRLrKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKnqL 1743
Cdd:PRK10246 461 AALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALE--P 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1744 EESEFTCAAAVKARKAMEVEMEDLHLQIDdiakaktALEEQLsrlQREKNEIQNRLEEDQEdmneLMKKHKAAVAQASRD 1823
Cdd:PRK10246 526 GVNQSRLDALEKEVKKLGEEGAALRGQLD-------ALTKQL---QRDESEAQSLRQEEQA----LTQQWQAVCASLNIT 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 MAQMNDLQAQIEESNKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVK-RLENLASRLK 1900
Cdd:PRK10246 592 LQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYALTLP 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1901 ETMEKLT--EERDQRAAAENREKEQNKRLQRQ------LRDTKEEMSELARKEAEAS----RKKHElemDLESLEAANQS 1968
Cdd:PRK10246 659 QEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHSQLQT 735
|
570 580 590
....*....|....*....|....*....|
gi 1907082217 1969 LQADLKLAFKRIGDLQAAIEDEMESDENED 1998
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1510-1917 |
1.11e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 51.06 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1510 KQRRFDSElsqaheETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLD-IAGFTQKVVSLEAELQDISSQesKDEASL 1588
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLRdleaKVKDQEEELDEQAGS-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1667
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1668 EEYEDKQKALREKRELEsklsTLSDQVNQRDFESEKRLRKDLKRTKALLADaqimLDHLK-NNAPSKREIAQLKNQL--- 1743
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLSKE----LDVLKeENMLLKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1744 EESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEIqnrLEEDQEDMNELMKKHKAAVAQASRD 1823
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKF-------IVAQEDVSKLSPLQYDC---WWEKVENLQDLLDRATNQVEKAALV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 MAQMNDLQAQI---EESNKEKQELQEKLQalqsQVEFLEQSMvdKSLVSRQEAKIRELETrlefektQVKRLENLASRLK 1900
Cdd:PLN02939 323 LDQNQDLRDKVdklEASLKEANVSKFSSY----KVELLQQKL--KLLEERLQASDHEIHS-------YIQLYQESIKEFQ 389
|
410
....*....|....*..
gi 1907082217 1901 ETMEKLTEERDQRAAAE 1917
Cdd:PLN02939 390 DTLSKLKEESKKRSLEH 406
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1470-1847 |
1.11e-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: 50.19 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1470 DESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-ETQREKLQREKLQREKDMllaeafs 1548
Cdd:pfam15905 24 EKSQRFRKQKAAESQPNLNNSKDASTPATARKVKSLELKKKSQKNLKESKDQKElEKEIRALVQERGEQDKRL------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1549 lkQQMEEKdldiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDLeAKVKDqeeeldeqagsiqmLEQAKLRLEM 1628
Cdd:pfam15905 97 --QALEEE----------LEKVEAKLNAAVREKTSLSASVASLEKQLLEL-TRVNE--------------LLKAKFSEDG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1629 EMERMRQTHSKEMESRDEeVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRkd 1708
Cdd:pfam15905 150 TQKKMSSLSMELMKLRNK-LEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1709 lkrtkalladaqimldhlknnapskrEIAQLKNQLEESEftcaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRL 1788
Cdd:pfam15905 227 --------------------------YITELSCVSEQVE-------KYKLDIAQLEELLKEKNDEIESLKQSLEEKEQEL 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1789 QREKNEIQNRLEEDQEDMNELMKKHKAavaQASRDMAQMNDLQAQIEESNKEKQELQEK 1847
Cdd:pfam15905 274 SKQIKDLNEKCKLLESEKEELLREYEE---KEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1427-1684 |
1.20e-05 |
|
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: 49.92 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1427 ERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRlgdlqadsdESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHE 1506
Cdd:pfam13868 51 EERERALEEEEEKEEERKEERKRYRQELEEQIEER---------EQKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1507 LEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKdldiagftqkvvsLEAELQDIssqeskdEA 1586
Cdd:pfam13868 121 KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEE-------------REAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1587 SLAKVKKQLRDLEAKVKDQEEELDEQagsiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQM 1662
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRL 252
|
250 260
....*....|....*....|..
gi 1907082217 1663 EVQLEEEYEDKQKALREKRELE 1684
Cdd:pfam13868 253 AEEAEREEEEFERMLRKQAEDE 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1538-1860 |
1.59e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1538 EKDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1597
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1661
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1662 MEVQLEEeYEDKQKALREK-RELESKLSTLSDQVNQRD------------------FESEKRLRKDLKRTKALLADAQIM 1722
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqayqlvrkiagevsrseaWDVARELLRRLREQRHLAEQLQQL 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1723 LDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE- 1801
Cdd:PRK04863 519 RMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRl 598
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1802 ---------DQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1860
Cdd:PRK04863 599 aarapawlaAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQ 666
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1291-1666 |
1.79e-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: 50.29 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1291 FTTVRPLIQV-QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRlssdrletriSELTSELTDERNTGESASQLLDAETAE 1369
Cdd:pfam15964 349 FEKTKALIQCeQLKSELERQKERLEKELASQQEKRAQEKEALR----------KEMKKEREELGATMLALSQNVAQLEAQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1370 RLRTEKEMKELQTQYDALKKQMEVMemevmearliraaeingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQ 1442
Cdd:pfam15964 419 VEKVTREKNSLVSQLEEAQKQLASQ-----------------EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGR 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1443 ELEDKmeveQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-S 1519
Cdd:pfam15964 482 QLEIK----DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQREK----------LQREKLQREKDMLLAEAFSLkqqmeekdldIAGFTQKVVSLEAELQDISSQESKDEASLA 1589
Cdd:pfam15964 553 QALQAQQREQeltqkmqqmeAQHDKTVNEQYSLLTSQNTF----------IAKLKEECCTLAKKLEEITQKSRSEVEQLS 622
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1590 KVKKQLRDLEAKVKDQEEELDEQAgsIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQME 1663
Cdd:pfam15964 623 QEKEYLQDRLEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLR 699
|
...
gi 1907082217 1664 VQL 1666
Cdd:pfam15964 700 SQV 702
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1464-1959 |
1.88e-05 |
|
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: 50.07 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1464 DLQADSDESQralqQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEETQREKLQR 1532
Cdd:pfam05622 1 DLSEAQEEKD----ELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1533 EKLQREKDmllAEAFSLKQQMEEKD-LDIAGFTQKVVSLEAElqdisSQESKDE-----ASLAKVKKqlrdLEAKV---K 1603
Cdd:pfam05622 74 ENFRLETA---RDDYRIKCEELEKEvLELQHRNEELTSLAEE-----AQALKDEmdilrESSDKVKK----LEATVetyK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1604 DQEEELDEQAGSIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKALREKRE 1682
Cdd:pfam05622 142 KKLEDLGDLRRQVKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1683 LESKLSTLsdqvnQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS--------------------KREIAQLknQ 1742
Cdd:pfam05622 216 LEEKLEAL-----QKEKERLIIERDTLRETNEELRCAQLQQAELSQADALlspssdpgdnlaaeimpaeiREKLIRL--Q 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1743 LEESEFTCaaavKARKAMEVEMEDLHLQIDDIAKAKTALEEQLsRLQREK-NEIQNRLEEDQEDMNELMKKHKAAVAqas 1821
Cdd:pfam05622 289 HENKMLRL----GQEGSYRERLTELQQLLEDANRRKNELETQN-RLANQRiLELQQQVEELQKALQEQGSKAEDSSL--- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1822 rdmaqmndLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvdkSLVSRQEAKIRELETRLefektQVKRLENLA--SRL 1899
Cdd:pfam05622 361 --------LKQKLEEHLEKLHEAQSELQKKKEQIEELEP-----KQDSNLAQKIDELQEAL-----RKKDEDMKAmeERY 422
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1900 KETMEKLTEE-RDQRAAAENREKEQNKRLQRQLRDtKEEMSELARKEAEASRKKHELEMDL 1959
Cdd:pfam05622 423 KKYVEKAKSViKTLDPKQNPASPPEIQALKNQLLE-KDKKIEHLERDFEKSKLQREQEEKL 482
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1703-1989 |
1.91e-05 |
|
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: 49.53 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1703 KRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----MEDLHLQIDDIAKA 1777
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQIEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1778 KtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQE-KLQALQSQVE 1856
Cdd:pfam13868 89 R---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1857 FLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKR-----LQRQL 1931
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQelqqaREEQI 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1932 RDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRigDLQAAIED 1989
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRR--ELEKQIEE 301
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1644-1985 |
1.94e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1644 RDEEVEEArQSCQKKLKQMEVQLEEEyedkQKALREkreLESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIML 1723
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAE----QYRLVE---MARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1724 DHLKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1799
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1800 EEDQEdMNELMKkhkAAVAQASRDMAQmndLQAQIEESNKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1873
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1874 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaAENREKEQNKRLQRQLRDtkEEMSELARKEAEASRK 1951
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD--EDELEQLQEELEARLE 568
|
330 340 350
....*....|....*....|....*....|....
gi 1907082217 1952 khELEMDLESLEAANQSLQADLKLAFKRIGDLQA 1985
Cdd:PRK04863 569 --SLSESVSEARERRMALRQQLEQLQARIQRLAA 600
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1563-1630 |
1.95e-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: 47.23 E-value: 1.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1563 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML--EQAKLRLEMEM 1630
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1796-1989 |
2.00e-05 |
|
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: 48.45 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1796 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1875
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1876 RELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQR------QLRDTKEEMSELARKEAEAS 1949
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQirnrlnGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082217 1950 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1989
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1656-1971 |
2.11e-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: 49.76 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1656 QKKLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRLRKDLKRTKALLADAQIMLDHLKNNAPS 1732
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEFTCAAAVKARKAME--VEMEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1808
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1809 lmkKHKAAVAQASRDMAQmndLQAQIEEsnKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFEK 1886
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 TQVKRLENLASRLKETMEKLTEERDQRaaAENREKEQNKRLQRQ-LRDTKEEMSE----LARKEAEASRKKHELEMDLES 1961
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEH--LKDVLVEQEIELQREfLQDIKEKVEEeragRLLKLNELLANLKGLEKATSS 431
|
330
....*....|.
gi 1907082217 1962 -LEAANQSLQA 1971
Cdd:pfam09731 432 hSEVEDENRKA 442
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1781-2028 |
2.61e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1781 LEEQLSRLQREKNeiQNRLEEDQEdMNELMKKHKAAVAQASRDMAQMNDLQAQIeeSNKEKQElQEKLQALQSQVEfleq 1860
Cdd:pfam05557 7 SKARLSQLQNEKK--QMELEHKRA-RIELEKKASALKRQLDRESDRNQELQKRI--RLLEKRE-AEAEEALREQAE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1861 smvdkslVSRQEAKIRELETRLEFEKTQvkrLENLASRLKETMEKLTEERDQRAaaeNREKEQNKRLQRQLRDTKEEMSE 1940
Cdd:pfam05557 77 -------LNRLKKKYLEALNKKLNEKES---QLADAREVISCLKNELSELRRQI---QRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1941 LARKEAEASRKKHELEMDLESLEAANQ---------SLQADLKLAFKRIGDLQAAIEdEMES------DENEDLINSEGD 2005
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiQSQEQDSEIVKNSKSELARIP-ELEKelerlrEHNKHLNENIEN 222
|
250 260
....*....|....*....|...
gi 1907082217 2006 SDVdseLEDRVDGVKSWLSKNKG 2028
Cdd:pfam05557 223 KLL---LKEEVEDLKRKLEREEK 242
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
2.64e-05 |
|
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440556 [Multi-domain] Cd Length: 341 Bit Score: 48.71 E-value: 2.64e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1776-2118 |
2.87e-05 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 49.66 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1776 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDMAQMNDLQAQIEESNKEKQELQEKLqaLQS 1853
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFEKTQVKR--LENLAsRLKETMEKlTEERDQRAAAENREKEQNKRL-QRQ 1930
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEE-QEEVEEKEIAKEQRLKSKTKGkASK 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1931 LRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDS 2010
Cdd:PTZ00108 1169 LRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKN 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 2011 ELEDRVDGVKSWLSKNKGPSKAPSDDGSLKSSRTALNSLPKEGKGPEERPSSVLSSlsyrkrltlkDSIGGTGDQDSLLT 2090
Cdd:PTZ00108 1249 NSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSS----------PTKKKVKKRLEGSL 1318
|
330 340
....*....|....*....|....*...
gi 1907082217 2091 TLSERATSPERPPRKARGGPREEPDQAQ 2118
Cdd:PTZ00108 1319 AALKKKKKSEKKTARKKKSKTRVKQASA 1346
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1445-1654 |
2.88e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1524
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1525 TQREKLQREKLqrekDMLL-AEAFS--------LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1595
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1596 RDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1654
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1301-1672 |
3.11e-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: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1301 QLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETrisELTSELTDERNTGESASQlldaETAERLRTEKEMKEL 1380
Cdd:COG5185 235 LKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENA---ESSKRLNENANNLIKQFE----NTKEKIAEYTKSIDI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1381 QTQYDALKKQmevmemevmearlIRAAEINGEvddddaggewrlkYERAVREVDFTKKRLQQELEdkmeveqQSRRQLER 1460
Cdd:COG5185 308 KKATESLEEQ-------------LAAAEAEQE-------------LEESKRETETGIQNLTAEIE-------QGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1461 RLGDLQADSDESQRALQQlkkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKL-QREKLQREK 1539
Cdd:COG5185 355 NLEAIKEEIENIVGEVEL-----SKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADrQIEELQRQI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1540 DmllaeafSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESKDEASLAK--VKKQLRDLEAKVKDQEEELDEQAGSiq 1617
Cdd:COG5185 430 E-------QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINrsVRSKKEDLNEELTQIESRVSTLKAT-- 500
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1618 mLEQAKLRLEMEMERMRQTHSKEMESRDEEvEEARQSCQKKLKQMEVQLEEEYED 1672
Cdd:COG5185 501 -LEKLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLIPASELIQA 553
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1700-1973 |
3.42e-05 |
|
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: 48.43 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1700 ESEKRLRKDLKRTKALLADAQimlDHLKNNAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEMEDLHLQIDdiaKAK 1778
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1779 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFL 1858
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1859 EQSMVDKSLVSRQEAKiRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLqRQLRDTKEEM 1938
Cdd:pfam09311 167 EEKLKAEILFLKEQIQ-AEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQLENGLTEKI-RQLEDLQTTK 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1907082217 1939 SELARKEAEASRKKHELEMDLESLEAANQSLQADL 1973
Cdd:pfam09311 245 GSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1609-1961 |
3.42e-05 |
|
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: 48.29 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1609 LDEQAGSIQMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKREleskls 1688
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYK-LRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQALKKEKE------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1689 TLSDQVNQRdfesEKRLRKDLKRTkalladaqimLDHLKnnapskREIAQLKNQLEeseftcaaavkarKAMEVEMEDLH 1768
Cdd:pfam09755 96 TLAMNYEQE----EEFLTNDLSRK----------LTQLR------QEKVELEQTLE-------------QEQEYQVNKLM 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1769 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM-NELMKKhkaavaqasrdmaqMNDLQAqieesnkEKQELQEK 1847
Cdd:pfam09755 143 RKIEKLEAETLNKQTNLEQLRREKVELENTLEQEQEALvNRLWKR--------------MDKLEA-------EKRLLQEK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1848 LQALQSQVEFLEQSMVDKSLVSRQEAKIRELetrlefeKTQVKRLENlasRLKETMEKLTEERDQRAAAENREKEQNKRL 1927
Cdd:pfam09755 202 LDQPVSAPPSPRDSTSEGDTAQNLTAHIQYL-------RKEVERLRR---QLATAQQEHTEKMAQYAQEERHIREENLRL 271
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907082217 1928 QRQLRDTKEEMSELARK--EAEASrkkheLEMDLES 1961
Cdd:pfam09755 272 QRKLQLEMERREALCRHlsESESS-----LEMDEER 302
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1602-1936 |
3.53e-05 |
|
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: 48.52 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1602 VKDQEEELDEQAGSIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1665
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1666 LEEEYEDKQKALREkRELESKLSTLSDQvnqrdfeSEKRLRKDLKRTKALLADAQIMldhlknnapskreIAQLKNQLEE 1745
Cdd:pfam15742 81 LTAEWKHCQQKIRE-LELEVLKQAQSIK-------SQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLEH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1746 SEFTCAAAVKA--RKAMEVEMEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA 1820
Cdd:pfam15742 140 AHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1821 SRDMAQMNDLQAQI---EESNKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRLEFE 1885
Cdd:pfam15742 217 QQQEAQLKQLENEKrksDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRLVHE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1886 KTQ----VKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKE 1936
Cdd:pfam15742 297 VEQrderIKQLENEIGILQQQSEKEKAFQKQVTAQNEILLLEKRKLLEQLTEQEE 351
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
3.86e-05 |
|
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of Par3 (or PAR3 or Par-3, also known as Atypical PKC isotype-specific-interacting protein, ASIP, Drosophila Bazooka) and related domains. Par3 is a scaffold protein involved in organizing cell polarity across animals. Par3 binds numerous molecules both for its recruitment to one pole of the cell and for downstream contributions to polarized cell function. It regulates cell polarity by targeting the Par complex proteins Par6 and atypical protein kinase C (aPKC) to specific cortical sites. Physical interactions between Par3 and the Par complex include Par3 PDZ domain 1 binding to the Par6 PDZ domain, Par3 PDZ domain 1 and PDZ domain 3 binding the Par6's PDZ-binding motif, and an interaction with an undefined region of aPKC that requires both Par3 PDZ2 and PDZ3. The PDZ domains of Par3 have also been implicated as potential phosphoinositide signaling integrators, since its second PDZ domain binds to phosphoinositides, and the third PDZ interacts with phosphoinositide phosphatase PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Par3 family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467271 [Multi-domain] Cd Length: 93 Bit Score: 44.55 E-value: 3.86e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 260 GAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1630-1976 |
3.93e-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: 48.98 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1630 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQ----LEEEYEDKQKALREKRELESKLSTLSDQVNQRDFE----- 1700
Cdd:pfam07111 21 LERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEgsqaLSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRleaqa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1701 --------SEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEMEDLHLQID 1772
Cdd:pfam07111 101 meldalavAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSKAEGLEKSLN 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1773 DIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQ 1849
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1850 ALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEerdQRAAAENREKEQNKR 1926
Cdd:pfam07111 260 DLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQDLEHRDSVKQ 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1927 LQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1976
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
4.07e-05 |
|
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
Pssm-ID: 436067 [Multi-domain] Cd Length: 54 Bit Score: 42.90 E-value: 4.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907082217 269 GLVPGDRLVEINGQNVENKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1445-1849 |
4.43e-05 |
|
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: 48.86 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1445 EDKMEVEQQSRRQLERRLGDLQADSDESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1516
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEETQREKLQREKLQREKDMLLAEA-FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1595
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1596 RDLEAKVKDQEEELDEQAGSIQMLEQAKlrlememermrqTHSKEMEsrdeevEEARQSCQKKLKQ-MEVQLEEEYEDKQ 1674
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------TDREKAE------EEAKRRADAKLKEaVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1675 KAlREKRELESKLSTlsdqvnqrdfesekrlrKDLKRTKALLADAQIMLDHLKNnaPSKREiaqlKNQLEESEFTCAAAV 1754
Cdd:NF033838 262 KR-RAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPS--PSLKP----EKKVAEAEKKVEEAK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1755 KARKAMEVE---------MEDLHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASRdM 1824
Cdd:NF033838 318 KKAKDQKEEdrrnyptntYKTLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR-L 388
|
410 420
....*....|....*....|....*
gi 1907082217 1825 AQMNDLQAQIEESNKEKQELQEKLQ 1849
Cdd:NF033838 389 EKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1298-1608 |
4.44e-05 |
|
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: 48.95 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1298 IQVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEM 1377
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQELEDK---MEVEQQS 1454
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1455 RRQLERRlgdlqadSDESQRALQQLKKKCQRLTAELQDTKLHLeGQQVRNHELEKKQRRFDSElsQAHEETQREKLQRE- 1533
Cdd:pfam05483 617 NKALKKK-------GSAENKQLNAYEIKVNKLELELASAKQKF-EEIIDNYQKEIEDKKISEE--KLLEEVEKAKAIADe 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1534 --KLQREKDML----LAEAFSLKQQ--------MEEKDLDIAGFTQK-------VVSLEAELQDIssqeskdEASLAKVK 1592
Cdd:pfam05483 687 avKLQKEIDKRcqhkIAEMVALMEKhkhqydkiIEERDSELGLYKNKeqeqssaKAALEIELSNI-------KAELLSLK 759
|
330
....*....|....*....
gi 1907082217 1593 KQL---RDLEAKVKDQEEE 1608
Cdd:pfam05483 760 KQLeieKEEKEKLKMEAKE 778
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1555-1714 |
4.63e-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: 47.23 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1555 EKDLDIAGFTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEmemERMR 1634
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAEL-------EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE---EQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1635 QTHS-KEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKALRE-KRELESKLSTLSDQVNQRDfESEKRLRKDLKRT 1712
Cdd:COG1579 84 NVRNnKEYEALQKEIESLKRR-ISDLEDEILELMERIEELEEELAElEAELAELEAELEEKKAELD-EELAELEAELEEL 161
|
..
gi 1907082217 1713 KA 1714
Cdd:COG1579 162 EA 163
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1783-2004 |
5.45e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.81 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1783 EQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSM 1862
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1863 VDKSLVSRQEAKIRELETRLEFEK------------TQV-KRLENLASRLKETMEKLTEERDQRAA--AENREKEQNKRL 1927
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERINRARkaaplaahikavTQIeQQAQRIHTELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1928 QRQLRDTKEEMSELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL-----QAAIEDEMESDENEDL 1999
Cdd:TIGR00618 347 LQTLHSQEIHIRDAHEVATsirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILqreqaTIDTRTSAFRDLQGQL 426
|
....*
gi 1907082217 2000 INSEG 2004
Cdd:TIGR00618 427 AHAKK 431
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1735-1964 |
6.50e-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: 47.75 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1735 EIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1814
Cdd:pfam19220 91 RLAKLEAALREAEAAKEELRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1815 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFEKT-QVKRL 1892
Cdd:pfam19220 171 LLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeQAERERAEAQLEEAVEAHRAERAsLRMKL 250
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1893 ENLASRLKETMEKLTEERDqraaaenrekeqnkrlqrQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1964
Cdd:pfam19220 251 EALTARAAATEQLLAEARN------------------QLRDRDEAIRAAERRLKEASIERDTLERRLAGLEA 304
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1789-1968 |
6.91e-05 |
|
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: 48.02 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1789 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVE----FLEQSMVD 1864
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAqeraRQQQEEFR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1865 KSLVSRQEAKIRELETRLEFEKTQVKRLE-NLASRLKETMEKLTEERDQraaaenrekeqnkrLQRQlrdtKEEMSELAR 1943
Cdd:pfam15709 430 RKLQELQRKKQQEEAERAEAEKQRQKELEmQLAEEQKRLMEMAEEERLE--------------YQRQ----KQEAEEKAR 491
|
170 180
....*....|....*....|....*
gi 1907082217 1944 KEAEASRKKHELEMDLESLEAANQS 1968
Cdd:pfam15709 492 LEAEERRQKEEEAARLALEEAMKQA 516
|
|
| PDZ_syntrophin-like |
cd06801 |
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
270-308 |
7.06e-05 |
|
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of syntrophins (including alpha-1-syntrophin, beta-1-syntrophin, beta-2-syntrophin, gamma-1-syntrophin, and gamma-2-syntrophin), and related domains. Syntrophins play a role in recruiting various signaling molecules into signaling complexes and help provide appropriate spatiotemporal regulation of signaling pathways. They function in cytoskeletal organization and maintenance; as components of the dystrophin-glycoprotein complex (DGC), they help maintain structural integrity of skeletal muscle fibers. They link voltage-gated sodium channels to the actin cytoskeleton and the extracellular matrix, and control the localization and activity of the actin reorganizing proteins such as PI3K, PI(3,4)P2 and TAPP1. Through association with various cytoskeletal proteins within the cells, they are involved in processes such as regulation of focal adhesions, myogenesis, calcium homeostasis, and cell migration. They also have roles in synapse formation and in the organization of utrophin, acetylcholine receptor, and acetylcholinesterase at the neuromuscular synapse. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This syntrophin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467262 [Multi-domain] Cd Length: 83 Bit Score: 43.33 E-value: 7.06e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1907082217 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| PDZ2_MAGI-1_3-like |
cd06732 |
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
269-308 |
7.33e-05 |
|
PDZ domain 2 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467214 [Multi-domain] Cd Length: 82 Bit Score: 43.31 E-value: 7.33e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS--GDSVRLKVQ 308
Cdd:cd06732 39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKECpkGSEVTLLVQ 80
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1437-1635 |
8.98e-05 |
|
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: 47.06 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1437 KKRLQQELEDKMEVEQ-QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfd 1515
Cdd:pfam09787 23 KEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1516 SELSQAHEETQREKLQREKLQrekdmllAEAFSLKQQM----EEKDLDIAGFTQKVVSLEAELQDISSQ-ESKDEASLAK 1590
Cdd:pfam09787 93 EQLQELEEQLATERSARREAE-------AELERLQEELryleEELRRSKATLQSRIKDREAEIEKLRNQlTSKSQSSSSQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1907082217 1591 vkkqlRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ 1635
Cdd:pfam09787 166 -----SELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERMEQ 205
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1299-1668 |
1.05e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 47.52 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRIseltseLTDERNTGESASQLldaetaerlrtEKEMK 1378
Cdd:PRK04778 113 LLDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1379 ELQTQYDalkkqmevmemevmearliRAAEINGEVDdddaggewrlkYERAVREVDFTKKRLQQeLEDKME------VEQ 1452
Cdd:PRK04778 176 NLEEEFS-------------------QFVELTESGD-----------YVEAREILDQLEEELAA-LEQIMEeipellKEL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1453 QSR------------RQLER---RLGDLQADSDesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK------- 1510
Cdd:PRK04778 225 QTElpdqlqelkagyRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydi 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1511 -QRRFDSElSQAHEETQREKLQREKLQREKDMLLAEAFSLKQ--QMEEKDLDIA-GFTQKVVSLEAELQDISSQESKDEA 1586
Cdd:PRK04778 298 lEREVKAR-KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEI 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1587 SLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKK 1658
Cdd:PRK04778 377 AYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDE 456
|
410
....*....|
gi 1907082217 1659 LKQMEVQLEE 1668
Cdd:PRK04778 457 IEALAEELEE 466
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1470-1613 |
1.12e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1470 DESQRALQQLKKKCQrLTA--ELQDTKLHLEGQ-QVRNHELEKKQRRFdselsQAHEETQREKLqrEKLQREKDMLLAEA 1546
Cdd:PRK12704 45 EEAKKEAEAIKKEAL-LEAkeEIHKLRNEFEKElRERRNELQKLEKRL-----LQKEENLDRKL--ELLEKREEELEKKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1547 FSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQeSKDEAS---LAKVKKQLR-DLEAKVKDQEEELDEQA 1613
Cdd:PRK12704 117 KELEQKQQELEKKEEELEELIEEQLQELERISGL-TAEEAKeilLEKVEEEARhEAAVLIKEIEEEAKEEA 186
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
1.14e-04 |
|
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467248 [Multi-domain] Cd Length: 82 Bit Score: 42.70 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1868-1985 |
1.16e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1868 VSRQEAKIRELEtrlefekTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRDTKEEMSELARKEAE 1947
Cdd:COG2433 408 LTEEEEEIRRLE-------EQVERLEAEVEELEAELEEK--------------DERIERLERELSEARSEERREIRKDRE 466
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907082217 1948 ASRKKHE---LEMDLESLEAANQSLQADLKLaFKRIGDLQA 1985
Cdd:COG2433 467 ISRLDREierLERELEEERERIEELKRKLER-LKELWKLEH 506
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1311-1490 |
1.16e-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: 46.07 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1311 DEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAETAERLRTEKEMKELQT--QYDALK 1388
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1389 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLGDLQAD 1468
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 1907082217 1469 SDESQRALQQLKKKCQRLTAEL 1490
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
1.17e-04 |
|
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP3, MPP4, and MPP7, and related domains. MPP3 (also known as MAGUK p55 subfamily member 3, erythrocyte membrane protein p55, or EMP55), MPP4 (also known as MAGUK p55 subfamily member 4 or Discs large homolog 6), and MPP7 (also known as MAGUK p55 subfamily member 7) are membrane-associated guanylate kinase (MAGUK)-like proteins. MPP3 is part of a cell adhesion protein complex including tumor suppressor CADM1 and actin-binding protein 4.1B. Participation in the Crumbs cell polarity complex has also been demonstrated for MPP7 in epithelial cells, and for MPP3 and MPP4 in the retina. MPP4 is needed for proper localization of plasma membrane calcium ATPases and maintenance of calcium homeostasis at the rod photoreceptor synaptic terminals. Binding partners of the MPP3 PDZ domain include nectin-3, serotonin 5-hydroxytryptamine, 5-HT(2C) receptor, and a cell adhesion protein, TSLC1 (tumor suppressor in lung cancer 1); fragments of MPP4 having the PDZ domain bind CRB (PDZ-SH3-GUK) and GABA transporter GAT1 (PDZ-SH3). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467260 [Multi-domain] Cd Length: 81 Bit Score: 42.62 E-value: 1.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907082217 269 GLV-PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1873-1998 |
1.29e-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: 43.93 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1873 AKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEnrekEQNKRLQRQLRDTKEEMSELARKEAEASRKK 1952
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082217 1953 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1998
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1779-1964 |
1.31e-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: 46.67 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1779 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQ 1854
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1855 VEFLEQSMVdKSLVSRQEaKIRELETRLEFEKTQVK--------------RLENLASRL--KETM-EKLTEERDQRAAAE 1917
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLTsksqssssqselenRLHQLTETLiqKQTMlEALSTEKNSLVLQL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1907082217 1918 NREKEQNKRLQ-RQLRDTKEEMSELARKEAEASRKKHELEMDLESLEA 1964
Cdd:pfam09787 201 ERMEQQIKELQgEGSNGTSINMEGISDGEGTRLRNVPGLFSESDSDRA 248
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1733-1943 |
1.42e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 47.00 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1733 KREIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1812
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1813 HKAAVAQASRDMAQ-------------------MNDLQAQIEESNKEKQELQEKlQALQSQVEFLEQSMVDKSLVSRQEA 1873
Cdd:PRK11637 139 HTGLQLILSGEESQrgerilayfgylnqarqetIAELKQTREELAAQKAELEEK-QSQQKTLLYEQQAQQQKLEQARNER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1874 K--IRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRD-------TKEEMSELAR 1943
Cdd:PRK11637 218 KktLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAEREAREAARVRDKQKQAKRkgstykpTESERSLMSR 296
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
225-307 |
1.55e-04 |
|
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467196 [Multi-domain] Cd Length: 78 Bit Score: 42.19 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 225 RRPTGDFGFSLRrttmlDRAPegqayrrV-VHFAEPGaGTKDLAlGLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DS 302
Cdd:cd06712 7 TKEEGGFGFTLR-----GDSP-------VqVASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGeEG 72
|
....*
gi 1907082217 303 VRLKV 307
Cdd:cd06712 73 LELQV 77
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1560-1804 |
1.71e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1560 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQaklrlememermrqthsk 1639
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1640 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESK-LSTLSDQVNQRDF--ESEKRLRKDLKRTKALL 1716
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDFLDRLSALSKiaDADADLLEELKADKAEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1717 ADAQIMLDHLKNnapskrEIAQLKNQLEEseftcaaavkARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ 1796
Cdd:COG3883 146 EAKKAELEAKLA------ELEALKAELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
....*...
gi 1907082217 1797 NRLEEDQE 1804
Cdd:COG3883 210 AAAAAAAA 217
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
1.74e-04 |
|
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467264 [Multi-domain] Cd Length: 78 Bit Score: 41.91 E-value: 1.74e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1752-1943 |
1.81e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.20 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1752 AAVKARKAMEVEMEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDMA------ 1825
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1826 ------QMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFEKTQVKRLENLAS-R 1898
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGiD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1899 LKETMEKLT--EERDQRAAAEN---REKEQNKRLQRQLRDTKEEMS---ELAR 1943
Cdd:COG1842 160 SDDATSALErmEEKIEEMEARAeaaAELAAGDSLDDELAELEADSEvedELAA 212
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1695-1966 |
1.84e-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: 45.37 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1695 NQRDFESEKRLRKDLKRTKALLADAQImldhlknnapSKREIAQLKNQLEEseftcaAAVKARKAMEvemEDLHLQIDDI 1774
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDA----------SKQRAAAYQKALDD------APAELRELRQ---ELAALQAKAE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1775 AKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNELMKkhkaavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQS 1853
Cdd:pfam12795 69 AAPKEILASLsLEELEQRLLQTSAQLQELQNQLAQLNS--------------QLIELQTRPERAQQQLSEARQRLQQIRN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QvefLEQSMVDKSLVSrqEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRaaaenreKEQNKRLQRQLRD 1933
Cdd:pfam12795 135 R---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKARRDLL-------TLRIQRLEQQLQA 202
|
250 260 270
....*....|....*....|....*....|...
gi 1907082217 1934 TKEEMSELARKEAEASRKkhELEMDLESLEAAN 1966
Cdd:pfam12795 203 LQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| PDZ1_L-delphilin-like |
cd06743 |
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
269-299 |
2.25e-04 |
|
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467225 [Multi-domain] Cd Length: 76 Bit Score: 41.88 E-value: 2.25e-04
10 20 30
....*....|....*....|....*....|.
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1500-1974 |
2.28e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 46.74 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1500 QQVRNHELEKKQRRFDSE--LSQAHEETQR----EKLQREKLQREkdmLLAEAFSLKQQMEEK------------DLDIA 1561
Cdd:NF041483 76 QLLRNAQIQADQLRADAEreLRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQLDQElaerrqtveshvNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1562 GFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEM-------- 1630
Cdd:NF041483 153 WAEQLRARTESQarrLLDESRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARKDAERLLnaastqaq 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1631 ------ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNqrdfesEKR 1704
Cdd:NF041483 233 eatdhaEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAESAN------EQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1705 LRKdlkrtkalladaqimldhlknnapSKREIAQLKNQ-LEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEE 1783
Cdd:NF041483 307 TRT------------------------AKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1784 --QLSRLQREKNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQ--------ELQEKL 1848
Cdd:NF041483 363 aaQLAKAARTAEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1849 QALQSQVEFLEQSMVDKSLVSRQEAKireletrlefeKTQVKRLENLASRLKETMEKLTEERDQ--RAAAENREKEQNKR 1926
Cdd:NF041483 443 RRLRGEAEQLRAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEA 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1927 LQR--QLRDTKEEMSELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1974
Cdd:NF041483 512 IERatTLRRQAEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1310-1615 |
2.44e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 46.49 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1310 KDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERNTGESASQLLDAE---TAERLRTEKEMKELQTQYDA 1386
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEaeqELEESKRETETGIQNLTAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1387 LKKQMEVMEmevmearliRAAEINGEVDDDDAGGEWRLKYER---AVREVDFTKKRLQQELEDKMEVEQQSRRQLERRLG 1463
Cdd:COG5185 346 EQGQESLTE---------NLEAIKEEIENIVGEVELSKSSEEldsFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1464 DLQADSDESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDSELSQAHEETQREKLQR-----EKLQRE 1538
Cdd:COG5185 417 AADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADEESQSRLEEAYDEINRSvrskkEDLNEE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1539 KDMLLAEAFSLKQQMEEKDLDIAGFTQKVVSLE---AELQDISSQESKDEASLAKVKKQlRDLEAKvKDQEEELDEQAGS 1615
Cdd:COG5185 487 LTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHILALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1528-1679 |
2.52e-04 |
|
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: 44.51 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1528 EKLQREKLQREKDMLLAEAFSLKQQMEEKdldIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1607
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1608 ELDeqagsiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKALRE 1679
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1592-1772 |
2.55e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1592 KKQLRDLEAKVKDQEEELDEQAgsiqMLEQAKLRLEMEMERMRqtHSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYE 1671
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEE----KLEAALLEAKELLLRER--NQQRQEARREREELQRE--EERLVQKEEQLDARAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKALREKRELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEEsEFTCA 1751
Cdd:PRK12705 99 KLDNLENQLEEREKALSARELELEEL----EKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE-EADLE 173
|
170 180
....*....|....*....|.
gi 1907082217 1752 AAVKARKAMEVEMEDLHLQID 1772
Cdd:PRK12705 174 AERKAQNILAQAMQRIASETA 194
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1299-1520 |
2.62e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.44 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1299 QVQLSEEQIRNKDEEIQQLRSKLEKVEKERNElRLSSDRLETRISELTSELTDERNT-GESASQLLDAETAERlRTEKEM 1377
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQPE-RAQAAL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1378 KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQQELEDKMEVEQQsrrQ 1457
Cdd:PRK11281 166 YANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNA----QNDLQRKSLEGNTQLQDLLQKQRDYLTARIQ---R 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1458 LERRLGDLQADSdeSQRALQQLKKKCQRltAELQDtklhlEGQQVRNHELEKKQRRFDSELSQ 1520
Cdd:PRK11281 239 LEHQLQLLQEAI--NSKRLTLSEKTVQE--AQSQD-----EAARIQANPLVAQELEINLQLSQ 292
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1740-1914 |
2.95e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 KNQLEESEFTCAAAVK-ARKAMEVEMEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1817
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1818 AQASRDMAQMNDLQAQIEESNKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFEKtqvkrlen 1894
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180
....*....|....*....|
gi 1907082217 1895 lASRLKETMEKLTEERDQRA 1914
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADKKA 190
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1680-1854 |
3.02e-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: 45.39 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1680 KRELESKLSTLSdqvnqrdfESEKRLRKDLKRTKALLADAQIMLDHLKnnapskREIAQLKNQleeseftcaaavkarka 1759
Cdd:smart00787 146 KEGLDENLEGLK--------EDYKLLMKELELLNSIKPKLRDRKDALE------EELRQLKQL----------------- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1760 mEVEMEDLHLQIDDIAKAKtaleeqLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEE--- 1836
Cdd:smart00787 195 -EDELEDCDPTELDRAKEK------LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrg 267
|
170
....*....|....*....
gi 1907082217 1837 -SNKEKQELQEKLQALQSQ 1854
Cdd:smart00787 268 fTFKEIEKLKEQLKLLQSL 286
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1781-1970 |
3.13e-04 |
|
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: 45.82 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1781 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkKHKAAVAQASRDM------AQMNDLQAQIEESNKEKQELQEKLQAlqsQ 1854
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAEL--KNQAAVPPAEEEQppagpsEEEQRLQEEAEQLQKELEALAGQLQA---Q 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1855 VEFLEQSmvdKSLVSRQEAKIRELETRLEFEKTQVKRLEnlasRLKETME--KLTeerDQRAAAENRE-KEQNKRLQRQ- 1930
Cdd:pfam15070 109 VQDNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGf 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1931 LRDTKEEM-------------SELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1970
Cdd:pfam15070 179 VKLTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
3.19e-04 |
|
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467157 [Multi-domain] Cd Length: 98 Bit Score: 41.83 E-value: 3.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| PDZ_MPP1-like |
cd10830 |
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 ... |
273-309 |
3.31e-04 |
|
PDZ domain of membrane palmitoylated protein1 (MPP1), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MPP1, and related domains. MPP1 (also known as MAGUK p55 subfamily member 1, erythrocyte membrane protein p55, EMP55) is a membrane-associated guanylate kinase (MAGUK)-like protein which forms a complex with protein 4.1 and glycophorin C (GPC) at the cytoplasmic face of the plasma membrane; this complex is essential for cytoskeleton-membrane linkage in erythrocytes and many non-erythroid cells, and participates in the determination of membrane stability and cell shape. MPP1, by interacting with various scaffold proteins and cytoskeletal proteins in the postsynaptic density, also plays an important role in organizing synaptic and non-synaptic structures. MPP1 is also a component of the Crumbs protein complex in the mammalian retina and may link the Usher protein network and the Crumbs protein complex. The MPP1 PDZ domain binding partners include GPC, ABCC4, and CADM1/Necl-2/SynCAM1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467266 [Multi-domain] Cd Length: 81 Bit Score: 41.39 E-value: 3.31e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1907082217 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10830 45 GDEILEINGKSVTNHSVDQLQKMLKETKGMVSLKVIP 81
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1825-2000 |
3.49e-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: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1825 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETrlEFEKTQvKRLENLASRLKEtME 1904
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAE------VAALNRRIQLLEE--ELERTE-ERLAEALEKLEE-AE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1905 KLTEERDQ-RAAAENREKEQNKR---LQRQLRDTKEEMSELARKEAEASRKKHELEMDLE-------SLEAANQSLQADL 1973
Cdd:pfam00261 71 KAADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEEL 150
|
170 180
....*....|....*....|....*...
gi 1907082217 1974 KLAFKRIGDLQAAIEDEMES-DENEDLI 2000
Cdd:pfam00261 151 KVVGNNLKSLEASEEKASEReDKYEEQI 178
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1363-1629 |
3.72e-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: 45.84 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1363 LDAETAERLRTEKEMKELQTQYDALKKQMEVMEMEVMEARliraaEINGEV-----------DDDDAGGEWRLKYERAVR 1431
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLR-----ETNEELrcaqlqqaelsQADALLSPSSDPGDNLAA 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1432 EV---DFTKKRLQQELEDKMEVEQQSrRQLERRLGDLQADSDESQRALQ----QLKKKCQR---LTAELQDTKLHLEGQQ 1501
Cdd:pfam05622 274 EImpaEIREKLIRLQHENKMLRLGQE-GSYRERLTELQQLLEDANRRKNeletQNRLANQRileLQQQVEELQKALQEQG 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1502 VRNHELEKKQRRFDS---ELSQAHEETQREKLQREKLQREKDMLLAE-AFSLKQQMEEKDLDIAGFTQK----------- 1566
Cdd:pfam05622 353 SKAEDSSLLKQKLEEhleKLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksv 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1567 VVSLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagsiqmLEQAKLRLEME 1629
Cdd:pfam05622 433 IKTLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1776-1940 |
3.94e-04 |
|
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: 42.67 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1776 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQV 1855
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1856 EFLEQSmvdkslvsrqeakireletrLEFEKTQVKRLENLASRLKETMEKLTEERDQraaaenrEKEQNKRLQRQLRDTK 1935
Cdd:pfam10473 83 ENLTKE--------------------LQKKQERVSELESLNSSLENLLEEKEQEKVQ-------MKEESKTAVEMLQTQL 135
|
....*
gi 1907082217 1936 EEMSE 1940
Cdd:pfam10473 136 KELNE 140
|
|
| PDZ4_DLG5-like |
cd06766 |
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
237-308 |
3.98e-04 |
|
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 4 of Drosophila and mammalian Dlg5, and related domains. Dlg5 is a scaffold protein with multiple conserved functions that are independent of each other in regulating growth, cell polarity, and cell adhesion. It has a coiled-coil domain, 4 PDZ domains and a MAGUK domain (an SH3 domain next to a non-catalytically active guanylate kinase domain). Deregulation of Dlg5 has been implicated in the malignancy of several cancer types. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg5-like family PDZ4 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467247 [Multi-domain] Cd Length: 81 Bit Score: 41.22 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 237 RTTMLDRAPE--------GQAYRRVVHFAEPGAGTKDLAlGLVPGDRLVEINGQNVENKSRDEI-VEMIRQSgDSVRLKV 307
Cdd:cd06766 3 RLVFLKKSQVelgiqlcgGNLHGIFVEDVEDDSPAKGPD-GLVPGDLILEYNSVDMRNKTAEEAyLEMLKPA-ETVTLKV 80
|
.
gi 1907082217 308 Q 308
Cdd:cd06766 81 Q 81
|
|
| secA |
PRK12903 |
preprotein translocase subunit SecA; Reviewed |
1822-1998 |
4.01e-04 |
|
preprotein translocase subunit SecA; Reviewed
Pssm-ID: 237258 [Multi-domain] Cd Length: 925 Bit Score: 45.82 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1822 RDMAQMNDLQAQIEESNKEKQELQEKLqALQSQVEFLEQSMVDKSLvsrqeaKIRELETRLEFEKTQVKRLENLASRL-K 1900
Cdd:PRK12903 741 VQYSQKNPYQVYTEEGTKKFNILLQEI-AYDVIVSLFNNPNAEKIL------IITEILSDGINNSDINDRPQELIDQIiE 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1901 ETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFK-R 1979
Cdd:PRK12903 814 SEEERLKALRIQREEMLMRPEELELINEEQKNLKQEIKLELSEIQEAEEEIQNINENKNEFVEFKNDPKKLNKLIIAKdV 893
|
170
....*....|....*....
gi 1907082217 1980 IGDLQAAIEDEMESDENED 1998
Cdd:PRK12903 894 LIKLVISSDEIKQDEKTTK 912
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
4.18e-04 |
|
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of PDZ-LIM family proteins including PDLIM1-7, and related domains. PDZ-LIM family proteins (also known as Zasp PDZ domain proteins) are involved in the rearrangement of the actin cytoskeleton; they mediate association with the cytoskeleton through alpha-actinin as well as with other proteins involved in signal transduction pathways. Members of this family include PDLIM1 (also known as C-terminal LIM domain protein 1, elfin, LIM domain protein CLP-36), PDLIM2 (also known as PDZ-LIM protein mystique), PDLIM3 (also known as actinin-associated LIM protein, alpha-actinin-2-associated LIM protein, ALP), PDLIM4 (also known as LIM protein RIL, Reversion-induced LIM protein), PDLIM5 (also known as enigma homolog, ENH, enigma-like PDZ and LIM domains protein), PDLIM6 (also known as LIM domain-binding protein 3, ZASP, Cypher, Oracle), and PDLIM7 (also known as PDZ and LIM domain protein 7, LIM mineralization protein, LMP; protein enigma). PDLIM1 has been shown to negatively regulate NF-kappaB-mediated signaling in the cytoplasm. PDLIM7 negatively regulates p53 through binding murine double minute 2 (MDM2). The PDZ domains of PDZ-LIM family proteins PDLIM1, 2, 3, 5, 6, 7 have been shown to bind actin. Other PDZ-LIM family PDZ domain binding partners include thyroid receptor interacting protein-6 (PDLIM4-PDZ), the LIM domain of PDLIM4 (PDLIM4-PDZ), tropomyosin (PDLIM7-PDZ), myotilin and calsarcin 1 (PDLIM6-PDZ), and proteins from the myotilin and FATZ (calsarcin/myozenin) families (PDLIM1, 3, 4, 6 PDZ domains). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PDLIM-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467235 [Multi-domain] Cd Length: 79 Bit Score: 40.98 E-value: 4.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| PDZ2_Dlg1-2-4-like |
cd06724 |
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
258-308 |
4.22e-04 |
|
PDZ domain 2 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Dlg1, human Dlg1,2, and 4 and related domains. Dlg1 (also known as synapse-associated protein Dlg197 or SAP-97), Dlg2 (also known as channel-associated protein of synapse-110, postsynaptic density protein 93, or PSD-93), Dlg4 (also known as postsynaptic density protein 95, PSD-95, synapse-associated protein 90, or SAP-90) each have 3 PDZ domains and belong to the membrane-associated guanylate kinase family. Dlg1 regulates antigen receptor signaling and cell polarity in lymphocytes, B-cell proliferation and antibody production, and TGFalpha bioavailability; its PDZ3 domain binds pro-TGFalpha, and its PDZ2 domain binds the TACE metalloprotease responsible for cleaving pro-TGFalpha to a soluble form. Dlg2 is involved in N-methyl-D-aspartate (NMDA) receptor signaling. It regulates surface expression of NMDA receptors in dorsal horn neurons of the spinal cord, and it also interacts with NMDA receptor subunits and with Shaker-type K+ channel subunits to cluster into a channel complex. Dlg4 PDZ1 domain binds NMDA receptors, and its PDZ2 domain binds neuronal nitric oxide synthase (nNOS), forming a complex in neurons. The Drosophila Scribble complex (Scribble, Dlg, and lethal giant larvae) plays a role in apico-basal cell polarity, and in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Postsynaptic targeting of Drosophila DLG requires interactions mediated by the first two PDZ domains. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Dlg-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467207 [Multi-domain] Cd Length: 85 Bit Score: 41.10 E-value: 4.22e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 258 EPGAGTKDLALGLvpGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1631-1956 |
4.51e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1631 ERMRQTHSKEMESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKalrekrelesklstLSDQVNQRDFESEKRLRKDL 1709
Cdd:pfam02029 18 ERRRQKEEEEPSGQvTESVEPNEHNSYEEDSELKPSGQGGLDEEEA--------------FLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1710 KRTKALLadaqimldhlKNNAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEMEdlhlqiddiakaktalEEQLSRlq 1789
Cdd:pfam02029 84 ERQKEFD----------PTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYK----------------EEETEI-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1790 REKNEIQNRLEEDQEDMNELMKKHKAAVAQASR-DMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS------M 1862
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEvPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngeeE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1863 VDKSLVS--RQEAKIRELETRLEFEKTQV---KRLENLASRLKET----MEKLtEERDQRAAAE----NREKEQNKRL-- 1927
Cdd:pfam02029 216 VTKLKVTtkRRQGGLSQSQEREEEAEVFLeaeQKLEELRRRRQEKeseeFEKL-RQKQQEAELEleelKKKREERRKLle 294
|
330 340
....*....|....*....|....*....
gi 1907082217 1928 QRQLRDTKEEMSELARKEAEASRKKHELE 1956
Cdd:pfam02029 295 EEEQRRKQEEAERKLREEEEKRRMKEEIE 323
|
|
| DUF1633 |
pfam07794 |
Protein of unknown function (DUF1633); This family contains sequences derived from a group of ... |
1592-1788 |
5.36e-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: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1592 KKQLRDLEAKVK-DQEEELDEQAgsiQMLEQAKLRLEMEMermrqTHSKEMESRDEEveearqscqkKLKQMEVQLEEEY 1670
Cdd:pfam07794 457 ERAIREEDPHLGaDQDREVRFGA---EGIVPGIERLKIEL-----STSKDLEKGYAE----------KIGFMEMEFGGLE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1671 EDKQKALREKRELESKLSTLSDQVnqRDFESEKR-LRKDLKRTKALLADAQI-MLDHLKNNAPSKREIAQLKNQLEESEF 1748
Cdd:pfam07794 519 ADKQMARNQIHRLEEKKDELSKKV--LDLTSIAQgAKKAVHDAKVELAAAYLkLLAGIKDKWVAKKEFTVLEGQAAEVES 596
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907082217 1749 TCA---AAVKARKAMEVEMEDLHLQIDDIaKAKTALEE----QLSRL 1788
Cdd:pfam07794 597 NLAlidQITKAAIDLTLEKPRFQAEIDDL-EARCKLKEvsdfTLSKL 642
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1835-1953 |
5.51e-04 |
|
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: 41.83 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1835 EESNKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKL------TE 1908
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1907082217 1909 ERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKH 1953
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1476-1693 |
5.67e-04 |
|
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: 45.51 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1476 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEetqreklqrEKLQREKDMLLaeafSLKQQME 1554
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1555 EKDLDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGSIQMLEQAKLRLEMEM 1630
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1631 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKALREKRELESKLSTLSDQ 1693
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
6.23e-04 |
|
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of PTPN13 [also known as Fas-associated protein-tyrosine phosphatase 1 (FAP-1), protein-tyrosine phosphatase 1E (PTP-E1), and protein-tyrosine phosphatase (PTPL1)], and related domains. PTPN13 regulates negative apoptotic signaling and mediates phosphoinositide 3-kinase (PI3K) signaling. PTPN13 has five PDZ domains. Proteins known to interact with PTPN13 PDZ domains include: PLEKHA1 and PLEKHA2 via PTPN13-PDZ domain 1, Fas receptor and thyroid receptor-interacting protein 6 via PTPN13-PDZ domain 2, nerve growth factor receptor and protein kinase N2 via PTPN13-PDZ domain 3, PDZ and LIM domain 4 (PDLIM4) via PTPN13-PDZ domains 2 and 4, and brain calpain-2 via PTPN13-PDZ domains 3, 4 and 5. Calpain-2-mediated PTPN13 fragments may be involved in abnormal tau aggregation and increased risk for Alzheimer's disease. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13 family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467285 [Multi-domain] Cd Length: 92 Bit Score: 40.94 E-value: 6.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| PDZ2_MUPP1-like |
cd06667 |
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
259-307 |
6.30e-04 |
|
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467155 [Multi-domain] Cd Length: 80 Bit Score: 40.73 E-value: 6.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1907082217 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06667 31 PG-GVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1312-1806 |
6.53e-04 |
|
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: 45.05 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1312 EEIQQLRSKLEKVEKERnelrlssDRLETRISELTSELTDERNTGESASQLLDAETA----ERLRTEKEMKELQTQYDAL 1387
Cdd:pfam15070 29 QKMQQLSEQVRTLREEK-------ERSVSQVQELETSLAELKNQAAVPPAEEEQPPAgpseEEQRLQEEAEQLQKELEAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1388 kkqmevmemevmearlirAAEINGEVDDDDagGEWRLKYERAVREVDftkkrLQQELEDKMEVEQQSRRQLErrlgDLQA 1467
Cdd:pfam15070 102 ------------------AGQLQAQVQDNE--QLSRLNQEQEQRLLE-----LERAAERWGEQAEDRKQILE----DMQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1468 DSDESQRALQQLKKKCQRLtAELQD-------------TKLHLEgQQVRNhELEKKQRRFDSELSQAHEETQREKLQREK 1534
Cdd:pfam15070 153 DRATISRALSQNRELKEQL-AELQNgfvkltnenmeltSALQSE-QHVKK-ELAKKLGQLQEELGELKETLELKSQEAQS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1535 LQREKDMLLAE----AFSLKQQMEEKDLdiagfTQKVVSLEAELQD-ISSQESKDEASLAKVKKQLRD----LEAKVKDQ 1605
Cdd:pfam15070 230 LQEQRDQYLAHlqqyVAAYQQLASEKEE-----LHKQYLLQTQLMDrLQHEEVQGKVAAEMARQELQEtqerLEALTQQN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1606 EEEldeQAGSIQMLEQAK---LRLEMEMERMRQTH---SKEMESRDEEVE---EARQSCQKKLKQMEVQLEEEYedkqka 1676
Cdd:pfam15070 305 QQL---QAQLSLLANPGEgdgLESEEEEEEAPRPSlsiPEDFESREAMVAffnSALAQAEEERAELRRQLKEQK------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1677 lREKRELESKLSTLSDQvnQRDFESEKRLRKD---LKRTKALladaQIMLDHLKNNAPS-KREIAQLKNQLEESEFTCAa 1752
Cdd:pfam15070 376 -RRCRRLAQQAAPAQEE--PEHEAHAPGTGGDsvpVEVHQAL----QVAMEKLQSRFTElMQEKADLKERVEELEHRCI- 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1753 avkarkamevemeDLHLQIDDIAKAKTALEEQ---LSRLQREKNEIQNRLEEDQEDM 1806
Cdd:pfam15070 448 -------------QLSGETDTIGEYIALYQSQraiLKQRHREKEEYISRLAQDKEEM 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1455-1672 |
6.87e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1455 RRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEETQREK 1529
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1530 LQREKLQREKDMLLAEAFSLKQqmeekDLDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1605
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1606 ----EEELDEQAGSIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1672
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1453-1696 |
7.48e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 44.68 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1453 QSRRQLERRLGDLQADSDESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheetqrEKLq 1531
Cdd:COG0497 165 RAWRALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1532 REKLQREKDML----------LAEAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK- 1593
Cdd:COG0497 225 REALQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1594 --QLRDLEAKVKDQEEELdeqagsIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYE 1671
Cdd:COG0497 305 laLLRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELL 358
|
250 260
....*....|....*....|....*
gi 1907082217 1672 DKQKALREKRELESKlsTLSDQVNQ 1696
Cdd:COG0497 359 EAAEKLSAARKKAAK--KLEKAVTA 381
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1440-1601 |
8.56e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.97 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1440 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1516
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1517 ELSQAHEEtqreKLQR-EKLQREKDMLLAE----AFSLKQQMEEKDLDIAgftQKVVSL-------EAELQDISSQESKD 1584
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERDELYDKfeaaIQDVQQKTGLKNLLLE---KKLQALgetlekkEAQLNEVLAAANLD 175
|
170
....*....|....*...
gi 1907082217 1585 EASLAKVKKQLRD-LEAK 1601
Cdd:pfam13851 176 PDALQAVTEKLEDvLESK 193
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1311-1491 |
8.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1311 DEEIQQLRSKLEKVEKERNELRLSSDrletriseltseLTDERNTGESASQLLDAETAERLRTEKEMKELQTQYDALKKQ 1390
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1391 MEVMEMEVMEAR--------LIRAAEINGEVDdddaggEWRLKY-------ERAVREVDFTKKRLQQELEDKMEVEQQSR 1455
Cdd:COG3206 249 LGSGPDALPELLqspviqqlRAQLAELEAELA------ELSARYtpnhpdvIALRAQIAALRAQLQQEAQRILASLEAEL 322
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907082217 1456 RQLERRLGDLQADSDESQRALQQLKKKCQRLtAELQ 1491
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAEL-RRLE 357
|
|
| PDZ5_DrPTPN13-like |
cd23060 |
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ... |
220-307 |
9.08e-04 |
|
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of Danio rerio Ptpn13, and related domains. Protein-tyrosine phosphatases (PTPs) dephosphorylate phosphotyrosyl residues in proteins that are phosphorylated by protein tyrosine kinases (PTKs). Danio rerio Ptpn13 is a classical non-receptor-like PTP. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This PTPN13-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467273 [Multi-domain] Cd Length: 80 Bit Score: 40.03 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRRttmldrAPEGQAYRrvVHFAEPGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQS 299
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSGIF--VKSISPG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKA 71
|
....*...
gi 1907082217 300 GDSVRLKV 307
Cdd:cd23060 72 KGTVQLTV 79
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1594-1908 |
9.66e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 9.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1594 QLRDLeaKVKDQEEELDEQAGSIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1671
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1672 DKQKALR----EKRELESKLSTLSdqvNQRDFESEKRLRKDLKRTKALLADAQimldhlKNNAPSKREIAQLKNQLEESE 1747
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1748 F----TCAAAVKARKAMEV--EMEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1821
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1822 rdmaqmNDLQAQIEESNKEKQELQEKLQALQS----QVE-FLEQSMVD--KSLVSRQEAK---IRELETRLEFEKTQVKr 1891
Cdd:PRK05771 247 ------EELLALYEYLEIELERAEALSKFLKTdktfAIEgWVPEDRVKklKELIDKATGGsayVEFVEPDEEEEEVPTK- 319
|
330
....*....|....*..
gi 1907082217 1892 LENlaSRLKETMEKLTE 1908
Cdd:PRK05771 320 LKN--PKFIKPFESLTE 334
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1303-1389 |
9.79e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1303 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDERntgesasqlldAETAERLRTEKEMKELQT 1382
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKDREISRLDR 472
|
....*..
gi 1907082217 1383 QYDALKK 1389
Cdd:COG2433 473 EIERLER 479
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1440-1577 |
9.97e-04 |
|
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: 43.82 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1440 LQQELEDKmEVEQQSRRQLERRLgdlqadsDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDSELS 1519
Cdd:pfam02841 178 LQEFLQSK-EAVEEAILQTDQAL-------TAKEKAIEAERAKAEAAEAEQELLREKQKEEEQM---MEAQERSYQEHVK 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1520 QAHEETQREklqREKLQREKDMLLAeafslKQQMEEKDLDIAGFTQKVVSLEAELQDI 1577
Cdd:pfam02841 247 QLIEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| PDZ_RGS12-like |
cd06710 |
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ... |
222-308 |
1.04e-03 |
|
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of RGS12, and related domains. RGS12 downregulates GPCR signal transduction by increasing the GTPase activity of G-protein alpha subunits, thereby driving G-proteins into their inactive GDP-bound form. The RGS12 PDZ domain can bind selectively to C-terminal (A/S)-T-X-(L/V) motifs as found within both the CXCR2 IL-8 receptor, and the alternative 3' exon form of RGS12. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This RGS12-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467194 [Multi-domain] Cd Length: 76 Bit Score: 39.92 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 222 ELQRRPTGdFGFSLRrttmldrapeGQAYRRVVHFaepGAGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGD 301
Cdd:cd06710 4 EIARGRAG-YGFTIS----------GQAPCVLSCV---VRGSPADVAGLKAGDQILAVNGINVSKASHEDVVKLIGKCTG 69
|
....*..
gi 1907082217 302 SVRLKVQ 308
Cdd:cd06710 70 VLRLVIA 76
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1764-1855 |
1.05e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.90 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1764 MEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRDMAQMNDLQA 1832
Cdd:PRK05431 1 MLDIKLIRENPEAVKEALAkrgfpldvDELLELDEERRELQTELEELQAERNALskeIGQAKRKGEDAEALIAEVKELKE 80
|
90 100
....*....|....*....|...
gi 1907082217 1833 QIEESNKEKQELQEKLQALQSQV 1855
Cdd:PRK05431 81 EIKALEAELDELEAELEELLLRI 103
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1708-1964 |
1.07e-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: 44.51 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1708 DLKRTKALladaqIMLDHLKNNAPSKREiaQLKNQLE-ESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLS 1786
Cdd:pfam15964 348 NFEKTKAL-----IQCEQLKSELERQKE--RLEKELAsQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1787 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDMA-QMNDLQAQIEESNKEKQELQEKlqaLQSQVEFLEQsmvdk 1865
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1866 slvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDqraaaenrEKEQNKRLQRQLRDTKEE-MSELARK 1944
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 1907082217 1945 EA-EASRKKHELEMDLESLEA 1964
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1893-2002 |
1.14e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1893 ENLASRLKETMEKLTEERDQRAaaenREKEQNKRLQRQLRDTKEEMSELArKEAEAsrKKHELEMDLESLEAANQSLQAD 1972
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQA----REKAQSQALAEAQQQELVALEGLA-AELEE--KQQELEAQLEQLQEKAAETSQE 213
|
90 100 110
....*....|....*....|....*....|
gi 1907082217 1973 LKLAFKRIGDlQAAIEDEMESDENEDLINS 2002
Cdd:PRK11448 214 RKQKRKEITD-QAAKRLELSEEETRILIDQ 242
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1592-1679 |
1.24e-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: 41.41 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1592 KKQLRDLEAKVKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1671
Cdd:pfam03938 18 KAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQELQKKQQELLQPIQ 97
|
....*....
gi 1907082217 1672 DK-QKALRE 1679
Cdd:pfam03938 98 DKiNKAIKE 106
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
1.26e-03 |
|
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];
Pssm-ID: 440513 [Multi-domain] Cd Length: 349 Bit Score: 43.54 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907082217 269 GLVPGDRLVEINGQNVEnkSRDEIVEMIRQS-GDSVRLKVQ 308
Cdd:COG0750 145 GLQPGDRIVAINGQPVT--SWDDLVDIIRASpGKPLTLTVE 183
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1811-1958 |
1.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1811 KKHKAAVAQASRDMAQMndlqaqIEESNKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFEKTQV 1889
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1890 KRLENLASRLKETMEKLTEERDQR--------AAAENREKEQNKRLQRQLRDTKEE-----MSELARK-EAEASRKKHEL 1955
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKqqelekkeEELEELIEEQLQELERISGLTAEEakeilLEKVEEEaRHEAAVLIKEI 178
|
...
gi 1907082217 1956 EMD 1958
Cdd:PRK12704 179 EEE 181
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1888-2013 |
1.44e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1888 QVKRLENLASRLKETMEKLTEERDQRAAAENREKEqnkrLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQ 1967
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKA----LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907082217 1968 SLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 2013
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ 139
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
1.74e-03 |
|
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family domain PDZ5 is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467170 [Multi-domain] Cd Length: 85 Bit Score: 39.64 E-value: 1.74e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907082217 270 LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1871-1979 |
1.80e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.69 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1871 QEAKIRELETRLEFEKTQVKRLENLASRLKETMEklteERDQRAAaenREKEQNKRLQRQLRDTKEEMSELARKEAEASR 1950
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 1907082217 1951 KKHELE---MDLESLEAANQSLQADLKLAFKR 1979
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1629-1802 |
1.88e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1629 EMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKALREKRELESKLSTLSDQV-NQRDFES-EKRLr 1706
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVrNNKEYEAlQKEI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1707 KDLKRTKALLADaqimldhlknnapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAktaLEEQLS 1786
Cdd:COG1579 99 ESLKRRISDLED----------------EILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAE---LEAELE 159
|
170
....*....|....*.
gi 1907082217 1787 RLQREKNEIQNRLEED 1802
Cdd:COG1579 160 ELEAEREELAAKIPPE 175
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1303-1521 |
1.89e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1303 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELTDerntgesasqlldaetaerlrTEKEMKELQT 1382
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1383 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQELEDKMEVEQQ 1453
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1454 SRRQLERRLGDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1521
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
1825-1909 |
1.90e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 39.90 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1825 AQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQS--------MVDKSLVSR-QEAKIRELETRLEFEKTQVKRLENL 1895
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELELLdedtkvykLIGDVLVKQdKEEVKEQLEERKETLEKEIKTLEKQ 81
|
90
....*....|....
gi 1907082217 1896 ASRLKETMEKLTEE 1909
Cdd:pfam01920 82 LEKLEKELEELKEE 95
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1580-1944 |
1.92e-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: 43.51 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1580 QESKD-EASLAKVKKQLRDLEAKVKDQEEELdeqagsiqmlEQAKLRLEMEMERMRQTHSKEMESR-DEEVEEARQSCQK 1657
Cdd:pfam13166 89 EESIEiQEKIAKLKKEIKDHEEKLDAAEANL----------QKLDKEKEKLEADFLDECWKKIKRKkNSALSEALNGFKY 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1658 KLKQMEVQLEE--EYEDKQKALREKRELESKLSTLSDQ---------VNQRDFESEKRLRKDLKRTKALLADAQIMLDHL 1726
Cdd:pfam13166 159 EANFKSRLLREieKDNFNAGVLLSDEDRKAALATVFSDnkpeiapltFNVIDFDALEKAEILIQKVIGKSSAIEELIKNP 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1727 KNNAPSKREIAQLKNQLEESEFtC--------AAAVKAR--KAMEVEMEDLHLQIDDIAKAKTALEEQL----------S 1786
Cdd:pfam13166 239 DLADWVEQGLELHKAHLDTCPF-CgqplpaerKAALEAHfdDEFTEFQNRLQKLIEKVESAISSLLAQLpavsdlasllS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1787 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR---------DMAQMNDLQAQIEES----NKEKQELQEKLQALQS 1853
Cdd:pfam13166 318 AFELDVEDIESEAEVLNSQLDGLRRALEAKRKDPFKsieldsvdaKIESINDLVASINELiakhNEITDNFEEEKNKAKK 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1854 QVEfleqsmvdKSLVSRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLteerdqraaaenreKEQNKRLQRQLRD 1933
Cdd:pfam13166 398 KLR--------LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKL--------------REEIKELEAQLRD 455
|
410
....*....|....
gi 1907082217 1934 TK---EEMSELARK 1944
Cdd:pfam13166 456 HKpgaDEINKLLKA 469
|
|
| PDZ3_MUPP1-like |
cd06791 |
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
272-307 |
1.93e-03 |
|
PDZ domain 3 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MUPP1 and PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467253 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 1.93e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1907082217 272 PGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06791 52 VNDQIIAVDGVNLQGFTNQEAVEVLRNTGQVVHLTL 87
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1764-1931 |
1.94e-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: 42.42 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1764 MEDLHLQIDDIAKAKTALEEQ----LSRL----QRE----------KNEIQN----------RLEEDQEDMNELMKKHKA 1815
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQsqnlLSKLeiaqQKEskflenlaslKHENDNlssmlnrkerRLKDLEDQLSELKNSYEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1816 AVaqasrdmAQMNDLQAQIEESNKEKQELQEKLQALQSQVEfleqSMVDKSLVSRQ--EAKIRELETRLE-FEKTQVKRL 1892
Cdd:pfam17078 85 LT-------ESNKQLKKRLENSSASETTLEAELERLQIQYD----ALVDSQNEYKDhyQQEINTLQESLEdLKLENEKQL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907082217 1893 ENLASRL----KETMEKLTEERDQRAAAENREKEQNKRLQRQL 1931
Cdd:pfam17078 154 ENYQQRIssndKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1800-1950 |
1.98e-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: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1800 EEDQEDMNELMKKHKAAVAQASRDMAQ-MNDLQAQIEESNKEKQELQEKLQalqsqvefleqsmvdkslvsRQEAKIREL 1878
Cdd:COG2433 387 EKELPEEEPEAEREKEHEERELTEEEEeIRRLEEQVERLEAEVEELEAELE--------------------EKDERIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907082217 1879 ETRLEFEKTQVKRlenlasrlketmekltEERDQRaAAENREKEqNKRLQRQLRDTKEEMSELARKEAEASR 1950
Cdd:COG2433 447 ERELSEARSEERR----------------EIRKDR-EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1734-1963 |
2.02e-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: 42.32 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1734 REIAQLKNQLEESEFTCAAAVKARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1813
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1814 KAAVAQASRDMAQMNDLQAQI-------EESNKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEK 1886
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907082217 1887 TQVKRLEnlasrlketmekLTEErdqrAAAENREKEQNkrlqrQLRDTKEEMSELARKEAEASRKKHELEMDLESLE 1963
Cdd:pfam00261 155 NNLKSLE------------ASEE----KASEREDKYEE-----QIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLE 210
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1814-1956 |
2.06e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1814 KAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFEKTqvKRLE 1893
Cdd:TIGR02794 39 QAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA---------EQARQKELEQRAAAEKA--AKQA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1894 NLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELE 1956
Cdd:TIGR02794 108 EQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEE 170
|
|
| PDZ2_GRIP1-2-like |
cd06681 |
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
2.13e-03 |
|
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) binding proteins GRIP1 (ABP/GRIP2) and GRIP2, and related domains. GRIP1 and GRIP2 each have 7 PDZ domains. The interaction of GRIP1 and GRIP2 with GluA2/3 (AMPAR subunit) regulates AMPAR trafficking and synaptic targeting. GRIP1 has an essential role in regulating AMPAR trafficking during synaptic plasticity and learning and memory. GRIP1 and GRIP2 interact with a variety of other proteins associated with protein trafficking and internalization, for example GRIP1 also interacts with KIF5 (also known as kinesin 1), EphB receptors, scaffold protein liprin-alpha, and the rasGEF GRASP-1. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This GRIP family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467169 [Multi-domain] Cd Length: 89 Bit Score: 39.52 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPtGDFGFSLR----RTTMLDRA-------PEGQAYRRvvhfaepgaGTkdlalgLVPGDRLVEINGQNVENKS 288
Cdd:cd06681 4 EVTLEKEG-NSFGFVIRggahEDRNKSRPltvthvrPGGPADRE---------GT------IKPGDRLLSVDGISLHGAT 67
|
90 100
....*....|....*....|
gi 1907082217 289 RDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 68 HAEAMSILKQCGQEATLLIE 87
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1569-1870 |
2.14e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1569 SLEAeLQDISSQESKDEASLAKVKKQLRDLeAKVKDQEEELDEqagsiqmLEQaklRLEMEMERMRQThSKEMES-RDEE 1647
Cdd:PRK11281 44 QLDA-LNKQKLLEAEDKLVQQDLEQTLALL-DKIDRQKEETEQ-------LKQ---QLAQAPAKLRQA-QAELEAlKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1648 VEEARQSCQK-KLKQMEVQLEE---EYEDKQKALREKRELESKLSTLSDQVNQRDFESEKRL---RKDLKRT----KALL 1716
Cdd:PRK11281 111 DEETRETLSTlSLRQLESRLAQtldQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLqqiRNLLKGGkvggKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1717 ADAQIMLdhlknNApskrEIAQLKNQLEESEFTCAAAVKarkameveMEDLHLQIDDIAKAKTA-LEEQLSRLQREKNei 1795
Cdd:PRK11281 191 PSQRVLL-----QA----EQALLNAQNDLQRKSLEGNTQ--------LQDLLQKQRDYLTARIQrLEHQLQLLQEAIN-- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1796 QNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQI--------EESNK-EKQELQEKLQ---ALQSQVEFLEQSMV 1863
Cdd:PRK11281 252 SKRLTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISV 331
|
....*....
gi 1907082217 1864 DK-SLV-SR 1870
Cdd:PRK11281 332 LKgSLLlSR 340
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1440-1679 |
2.31e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 41.66 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1440 LQQELEDKMEVEQQSRRQLERRLGDLQADSDESQraLQQLKKKCQRLTAELQdtklhleGQQVRNHELEKKQRRFDSELS 1519
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLES--VEALLKKHEALEAELA-------AHEERVEALNELGEQLIEEGH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1520 QAHEETQReklQREKLQREKDMLLAEAFSLKQQMEEKdLDIAGFTQKVVSLEAELQDISSQESKDE--ASLAKVKKQLRD 1597
Cdd:cd00176 72 PDAEEIQE---RLEELNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDlgKDLESVEELLKK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1598 LeakvKDQEEELDEQAGSIQMLEQAKLRLEmemermrqthskemESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKAL 1677
Cdd:cd00176 148 H----KELEEELEAHEPRLKSLNELAEELL--------------EEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
|
..
gi 1907082217 1678 RE 1679
Cdd:cd00176 210 EE 211
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1755-1860 |
2.32e-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: 40.24 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1755 KARKAMEVEM------EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMN 1828
Cdd:pfam13863 4 KKREMFLVQLaldakrEEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIK 83
|
90 100 110
....*....|....*....|....*....|..
gi 1907082217 1829 DLQAQIEESNKEKQELQEKLQALQSQVEFLEQ 1860
Cdd:pfam13863 84 KLTAQIEELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PDZ1_harmonin |
cd06737 |
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
220-310 |
2.33e-03 |
|
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of harmonin isoforms a, b, and c, and related domains. Harmonin (also known as Usher Type 1C, PDZ-73 and AIE-75) is a key organizer of the Usher (USH) protein interactome. USH syndrome is the leading cause of hereditary sensory deaf-blindness in humans; three clinically distinct types of USH have been identified, type 1 to 3. The gene encoding harmonin (USH1C) is the causative gene for the USH type 1C phenotype. There are at least 10 alternatively spliced isoforms of harmonin, which are divided into three subclasses (a, b, and c). All isoforms contain the first two PDZ domains and the first coiled-coil domain. The a and b isoforms all have a third PDZ domain. The different PDZ domains are responsible for interactions with all known Usher syndrome type 1 proteins, and most Usher syndrome type 2 proteins. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This harmonin family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467219 [Multi-domain] Cd Length: 85 Bit Score: 39.16 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 220 ELELQRRPTGDFGFSLRR---------TTMLDraPEGQAYRRvvhfaepgagtkdlalGLVPGDRLVEINGQNVENKSRD 290
Cdd:cd06737 4 LVRLDRRGPESLGFSVRGglehgcglfVSHVS--PGSQADNK----------------GLRVGDEIVRINGYSISQCTHE 65
|
90 100
....*....|....*....|
gi 1907082217 291 EIVEMIRQSgDSVRLKVQPI 310
Cdd:cd06737 66 EVINLIKTK-KTVSLKVRHV 84
|
|
| DUF4795 |
pfam16043 |
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. ... |
1793-1918 |
2.37e-03 |
|
Domain of unknown function (DUF4795); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 285 and 978 amino acids in length.
Pssm-ID: 464990 [Multi-domain] Cd Length: 181 Bit Score: 41.52 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1793 NEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEK-------QELQEK--LQALQSQVEF------ 1857
Cdd:pfam16043 10 DQLQALILDLQEELEKLSETTSELSERLQQRQKHLEALYQQIEKLEKVKadkevveEELDEKadKEALASKVSRdqfdet 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1858 ---LEQSMVDK-SLVSRQEAKIR---ELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAEN 1918
Cdd:pfam16043 90 leeLNQMLQELlDKLEGQEDAWKkalETLSEELDTKLDRLELDPLKELLERRIKALQKLLQEGSEELD 157
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1816-1949 |
2.68e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1816 AVAQASRDMAQMNDLQAQIEESNKEKQ-ELQEKL--QALQSQVEFLEQsmvdkslVSRQEAKIRELEtrlefektqvKRL 1892
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLlEAEDKLvqQDLEQTLALLDK-------IDRQKEETEQLK----------QQL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1893 ENLASRLKETMEKLT--EERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEAS 1949
Cdd:PRK11281 90 AQAPAKLRQAQAELEalKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1731-1931 |
2.80e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.36 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1731 PSKREIaqlKNQLEeseftcaaAVKARKAMEVE-------MEDLHLQIDDIAKAK---TALEEQLSRLQREKNEIQNRLE 1800
Cdd:PRK11281 36 PTEADV---QAQLD--------ALNKQKLLEAEdklvqqdLEQTLALLDKIDRQKeetEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1801 EdqedmnelMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQvefleqsmvdksLVSRQEAKIReLET 1880
Cdd:PRK11281 105 A--------LKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQ------------LVSLQTQPER-AQA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1881 RLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1931
Cdd:PRK11281 164 ALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKS 214
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1740-1964 |
2.99e-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: 42.90 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1740 KNQLEESEFTCAAAVKARKAMEVEMEDLHLQ--IDDIAKAKTALEEQLS---RLQREKNEIQNRLEEDQEdmnelmkkhk 1814
Cdd:pfam15066 329 KQQMQIQDLQCSNLYLEKKVKELQMKITKQQvfVDIINKLKENVEELIEdkyNVILEKNDINKTLQNLQE---------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1815 aavaqasrdmaQMNDLQAQIEESNKEKQELQEKLQALQ-SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFEKTQVKRLE 1893
Cdd:pfam15066 399 -----------ILANTQKHLQESRKEKETLQLELKKIKvNYVHLQERYITEMQQKNKSVSQCLEMDKTLSKKEEEVERLQ 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 1894 nlasRLKETMEKLTEerdqrAAAENREKEQNKRLQRQLRDTKeemsELARKEAEASRKKHELEMDLESLEA 1964
Cdd:pfam15066 468 ----QLKGELEKATT-----SALDLLKREKETREQEFLSLQE----EFQKHEKENLEERQKLKSRLEKLVA 525
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1463-1607 |
3.00e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1463 GDLQADSDESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEETQREKLQREKLQREKDML 1542
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1543 LAEAFSLKQQMEEKDLDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1607
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1540-2027 |
3.22e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1540 DMLLAEAFSLKQQMEEKDLDIagfTQKVVSLEAELQDISSQESKDEASL-----------AKVKKQLRDLEAKVKDQEEE 1608
Cdd:PTZ00440 601 EELINEALFNKEKFINEKNDL---QEKVKYILNKFYKGDLQELLDELSHflddhkylyheAKSKEDLQTLLNTSKNEYEK 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1609 LDEQAGSI--QMLEQAKLRLEmemermrqtHSKEMESR--DEEVEEARQSCQKKLKQMEvqleEEYEDKQKALREKRELE 1684
Cdd:PTZ00440 678 LEFMKSDNidNIIKNLKKELQ---------NLLSLKENiiKKQLNNIEQDISNSLNQYT----IKYNDLKSSIEEYKEEE 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1685 SKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEM 1764
Cdd:PTZ00440 745 EKLEVYKHQIINR----KNEFILHLYENDKDLPDGKNTYEEFLQY---KDTILNKENKISNDINILKENKKNNQDLLNSY 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1765 EDLHLQIDDIAKAKTALEEQLsrLQREKNEIQN-RLEEDQEDMNELMKKhkaavaqasrdmaqMNDLQAQIEESNKekqe 1843
Cdd:PTZ00440 818 NILIQKLEAHTEKNDEELKQL--LQKFPTEDENlNLKELEKEFNENNQI--------------VDNIIKDIENMNK---- 877
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1844 lqeKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEfektqvkrlenlaSRLKETMEKLTEERDQRAAAENREKEQ 1923
Cdd:PTZ00440 878 ---NINIIKTLNIAINRSNSNKQLVEHLLNNKIDLKNKLE-------------QHMKIINTDNIIQKNEKLNLLNNLNKE 941
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1924 NKRLQRQLRDTKeeMSELaRKEAEASRKKHE---------LEMDLESLEAANQSLQaDLKLAFKRIGD----LQAAIEDE 1990
Cdd:PTZ00440 942 KEKIEKQLSDTK--INNL-KMQIEKTLEYYDkskeningnDGTHLEKLDKEKDEWE-HFKSEIDKLNVnyniLNKKIDDL 1017
|
490 500 510
....*....|....*....|....*....|....*...
gi 1907082217 1991 MESDENEDLINSEGD-SDVDSELEDRVDGVKSWLSKNK 2027
Cdd:PTZ00440 1018 IKKQHDDIIELIDKLiKEKGKEIEEKVDQYISLLEKMK 1055
|
|
| PDZ1_Scribble-like |
cd06704 |
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
226-308 |
3.40e-03 |
|
PDZ domain 1 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 1 of Drosophila Scribble (also known as LAP4), human Scribble homolog (also known as hScrib, LAP4, CriB1, ScrB1 and Vartul), and related domains. They belong to the LAP family, which describes proteins that contain either one or four PDZ domains and 16 LRRs (leucine-rich repeats) and function in controlling cell shape, size and subcellular protein localization. In Drosophila, the Scribble complex, comprising Scribble, discs large, and lethal giant larvae, plays a role in apico-basal cell polarity, in other forms of polarity, including regulation of the actin cytoskeleton, cell signaling and vesicular trafficking, and in tumor development. Mammalian Scribble is important in many aspects of cancer development. Scribble and its homologs can be downregulated or overexpressed in cancer; they have a role in cancer beyond their function in loss of cell polarity. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Scribble-like family PDZ1 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467188 [Multi-domain] Cd Length: 87 Bit Score: 38.80 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 226 RPTGDFGFSL---RRTTMLDRAPEGQAYRRVvhfAEPGAGTKDlalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDS 302
Cdd:cd06704 7 RQTGGLGISIaggKGSTPYKGDDEGIFISRV---TEGGPAAKA---GVRVGDKLLEVNGVDLVDADHHEAVEALKNSGNT 80
|
....*.
gi 1907082217 303 VRLKVQ 308
Cdd:cd06704 81 VTMVVL 86
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1784-1973 |
3.50e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.37 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1784 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdmaQMNDLQAQIEESNKEKQELQEKLQALQSQvefleQ 1860
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1861 SMVDKSLVSRQEAKIRE-----LETRLEFEKTQVK-RLENLASRL----KETMEKLTEERDQrAAAENREKEQNKRLQRQ 1930
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1907082217 1931 -LRDTKEEMSELarKEAEASRKKhelemDLESLEAANQSLQADL 1973
Cdd:PRK11637 199 lLYEQQAQQQKL--EQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| PDZ_Lin-7-like |
cd06796 |
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
259-311 |
4.44e-03 |
|
PDZ domain of protein Lin-7 and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Lin-7 (also known as LIN-7 or LIN7), and related domains. Lin-7 targets and organize protein complexes to epithelial and synaptic plasma membranes. There are three mammalian Lin-7 homologs: Lin-7A (protein lin-7 homolog A, also known as mammalian lin-seven protein 1 (MALS-1), vertebrate lin-7 homolog 1 (Veli-1), tax interaction protein 33); Lin-7B (also known as MALS-2, Veli-2); and Lin-7C (also known as MALS-3, Veli-3). Lin-7 is involved in localization of the Let-23 growth factor receptor to the basolateral membrane of epithelial cells, in tight junction localization of insulin receptor substrate p53 (IRSp53), in retaining gamma-aminobutyric (GABA) transporter (BGT-1) at the basolateral surface of epithelial cells, and in regulating recruitment of neurotransmitter receptors to the postsynaptic density (PSD). The Lin7 PDZ domain binds Let-23, BGT and beta-catenin, and NMDA (N-methyl-D-aspartate) receptor NR2B. Lin-7 also binds to the PDZ binding motif located in the C-terminal tail of Rhotekin, an effector protein for small GTPase Rho. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Lin-7-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467258 [Multi-domain] Cd Length: 86 Bit Score: 38.57 E-value: 4.44e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 259 PGaGTKDLALGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQPIP 311
Cdd:cd06796 35 PG-GVADRHGGLKRGDQLLSVNGVSVEGEHHEKAVELLKAAQGSVKLVVRYTP 86
|
|
| PDZ_CASK-like |
cd10831 |
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related ... |
273-309 |
4.72e-03 |
|
PDZ domain of peripheral plasma membrane protein CASK, Caenorhabditis Lin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CASK, Caenorhabditis elegans Lin-2, and related domains. CASK and Lin-2 are membrane-associated guanylate kinase (MAGUK)-like proteins. CASK (also known as Calcium/calmodulin-dependent protein kinase, CAKI, and Camguk) has a role in synaptic transmembrane protein anchoring and ion channel trafficking. CASK may regulate transmembrane proteins that bind calcium, calmodulin, or nucleotides; it regulates the Drosophila ether a go-go (eag) potassium channel, and also regulates autophosphorylation of CaMKII. CASK binding partners include the transcription factor TBR1, and cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. Lin-2, as a component of the CLin-10-Lin-2-Lin-7 complex, plays a role in controlling the basolateral localization of the EGF receptor Let-23; this complex also associates with the neuron-specific motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor 2B along microtubules. CASK may also function in targeting or scaffolding of the protein parkin which is selectively truncated by a Parkinson's disease-causing mutation; the C-terminus of parkin functions as a class II PDZ-binding motif that binds CASK. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MPP6-MPP2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467267 [Multi-domain] Cd Length: 81 Bit Score: 38.23 E-value: 4.72e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1907082217 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd10831 45 GDEIREINGISVANQTVEQLQKMLREARGSITFKIVP 81
|
|
| PDZ_MAST1 |
cd23073 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ... |
225-314 |
4.74e-03 |
|
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinase MAST1, and related domains. MAST1 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. MAST1 functions as a scaffold protein to link the dystrophin/utrophin network with microfilaments via syntrophin, and it has been identified as a main driver of cisplatin resistance in human cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST1 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F
Pssm-ID: 467286 [Multi-domain] Cd Length: 95 Bit Score: 38.47 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 225 RRPTGDFGFSLRRTTMLDRAPEGQAYRRVVHFAEPGAGTKDLalGLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVR 304
Cdd:cd23073 8 QRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEA--GLCAGDLITHVNGEPVHGMVHPEVVELILKSGNKVA 85
|
90
....*....|
gi 1907082217 305 LKVQPIPELS 314
Cdd:cd23073 86 VTTTPFENTS 95
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1564-1661 |
4.77e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.49 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1564 TQKVVSLEAELQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSiqMLEQAKLRLEMEMERMRQTHSKEMES 1643
Cdd:smart00935 6 VQKILQESPAGKAAQKQ---LEKEFKKRQAELEKLEKELQKLKEKLQKDAAT--LSEAAREKKEKELQKKVQEFQRKQQK 80
|
90
....*....|....*...
gi 1907082217 1644 RDEEVEEARQSCQKKLKQ 1661
Cdd:smart00935 81 LQQDLQKRQQEELQKILD 98
|
|
| mS26_Tt |
cd23695 |
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is ... |
1421-1743 |
4.92e-03 |
|
Tetrahymena thermophila ribosomal protein mS26 and similar proteins; Ribosomal protein mS26 is a component of small subunit (SSU) in Tetrahymena thermophila mitochondrial ribosome (mitoribosome). The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit; the large mitoribosomal subunit (LSU) lacks 5S rRNA.
Pssm-ID: 467909 [Multi-domain] Cd Length: 496 Bit Score: 42.12 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1421 EWRLK--YERAVREVDFTKKRLQQELEDKMEveqqsrrQLERRLGDLQADSDESqraLQQLKKKCQRLTAELQDtklhle 1498
Cdd:cd23695 193 LFKLLkeYQDAKAIIIEDFRESSEEGAEKLE-------KLEKAFATLLKNYKEE---LEEPEKQLEFMQKRLLD------ 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1499 gqqvrnheLEKKQRRFDSELSQAH--EETQREKLQREKLQREKdmllaeaFSLKQQMEEKDLDIAGFTQKVVSLEAELQD 1576
Cdd:cd23695 257 --------LYNLLRLWGQYITIVKmpDSVVRDIMNKTQARPEV-------AKLNSKQELEDAKNRKRDTEENEFDDDYES 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1577 ISSQESKDEaslakvkkqlrdleakvkdqEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQ 1656
Cdd:cd23695 322 ADEGETSDE--------------------EDEIEEENFQLQKEKKKEEELNAEFNIAKNSLYKFSPQNDKNVVDDRDFYS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1657 KklKQMEVQLEEE------------YEDKQKALREKRELESkLSTLSDQVNQRDFESEKRLRKDLKrtkalladAQIMLD 1724
Cdd:cd23695 382 G--VDLENVFPRAllnnlndftgldFQNVKEILNNEEKLKI-IQGEDDQNDQEDFNNPRKFQTSLI--------VQTYKQ 450
|
330 340
....*....|....*....|.
gi 1907082217 1725 HLKN--NAPSKREIAQLKNQL 1743
Cdd:cd23695 451 KINNldAESLTRATQEKKNDI 471
|
|
| LXG |
pfam04740 |
LXG domain of WXG superfamily; This domain is present is the N-terminal region of a group of ... |
1792-1887 |
5.09e-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: 40.69 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1792 KNEIQNRLEEDQEDMNELMKKHKAAVAQASR----DMAQMNDLQAQIEESNKEKQELQEKLQAL-QSQVEFLEQSmvdKS 1866
Cdd:pfam04740 101 EHELENGLKKAKEKTEELTDEINSILASVSDivslPKLSDSEVQDSLQKAKKKVKDTIEKLYDFdQEQTSELSEL---EA 177
|
90 100
....*....|....*....|.
gi 1907082217 1867 LVSRQEAKIRELETRLEFEKT 1887
Cdd:pfam04740 178 DLQALKTYVSELEEMTSNGKI 198
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1312-1609 |
5.43e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1312 EEIQQLRSKLEKVEKERNELRlssdrletrisELTSELTDERNtgESASQLldAETAERLRTEKEMK-ELQTQYDALKKQ 1390
Cdd:COG1340 15 EKIEELREEIEELKEKRDELN-----------EELKELAEKRD--ELNAQV--KELREEAQELREKRdELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1391 mevmemevmeaRLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQeLEDKMEVEQQSR---RQLERRLGDLQA 1467
Cdd:COG1340 80 -----------RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER-LEWRQQTEVLSPeeeKELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1468 DSDESQRALQQlKKKCQRLTAELQdtklhlegqqvrnhELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAF 1547
Cdd:COG1340 148 ELEKAKKALEK-NEKLKELRAELK--------------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEAD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1548 SLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQES--KDEASLAKVKKQLRDLEAKVKDQEEEL 1609
Cdd:COG1340 213 ELHKEIVEAQEKADELHEEIIELQKELRELRKELKklRKKQRALKREKEKEELEEKAEEIFEKL 276
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1808-1983 |
5.50e-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: 40.66 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1808 ELMKKHKAAVAQA------------------SRDMAQMNDLQAQIE----ESNKEKQELQEKLQALQSQVEfleqsmvdk 1865
Cdd:pfam13851 1 ELMKNHEKAFNEIknyynditrnnlelikslKEEIAELKKKEERNEklmsEIQQENKRLTEPLQKAQEEVE--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1866 slvsrqeakirELETRLEFEKTQVKRLENLASRLKET-----------------MEKLTEERDQ------RAAAENREKE 1922
Cdd:pfam13851 72 -----------ELRKQLENYEKDKQSLKNLKARLKVLekelkdlkwehevleqrFEKVERERDElydkfeAAIQDVQQKT 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1923 QNKR--LQRQLrdtkEEMSE-LARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL 1983
Cdd:pfam13851 141 GLKNllLEKKL----QALGEtLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1358-1617 |
5.54e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1358 SASQLLDAETAERLRTEKEmkeLQTQYDALKKQMEVmemevmearliraaeingEVDDddaggewrlkyeravrevdftk 1437
Cdd:PRK11281 22 LSSAFARAASNGDLPTEAD---VQAQLDALNKQKLL------------------EAED---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1438 KRLQQELE------DKMEVEQQSRRQLERRLGDLQADSDESQRALQQLKKKcqrltaELQDTKLHLEGQQVRnhELEKKQ 1511
Cdd:PRK11281 59 KLVQQDLEqtlallDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDD------NDEETRETLSTLSLR--QLESRL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1512 RRFDSELSQAHEE------------TQREKLQRE---KLQR---------------------EKDMLLAEAFSLKQQMEE 1555
Cdd:PRK11281 131 AQTLDQLQNAQNDlaeynsqlvslqTQPERAQAAlyaNSQRlqqirnllkggkvggkalrpsQRVLLQAEQALLNAQNDL 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907082217 1556 KDLDIAGFTQkvvsleaeLQDIsSQESKDEASL--AKVKKQLRDLE----AKVKDQEEELDEQAGSIQ 1617
Cdd:PRK11281 211 QRKSLEGNTQ--------LQDL-LQKQRDYLTAriQRLEHQLQLLQeainSKRLTLSEKTVQEAQSQD 269
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1762-1856 |
5.64e-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: 39.48 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1762 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQM-NDLQAQIEESNKE 1840
Cdd:pfam03938 5 VDMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKeQELQQLQQKAQQE 84
|
90
....*....|....*..
gi 1907082217 1841 -KQELQEKLQALQSQVE 1856
Cdd:pfam03938 85 lQKKQQELLQPIQDKIN 101
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1824-1976 |
6.04e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.43 E-value: 6.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1824 MAQMNDLQAQIEESNKEkqeLQEKLQALQSQVEFLEQSMVdkslvsRQEAKIRELETRLEFEKTQVKRLENLAsrlKETM 1903
Cdd:pfam04012 10 RANIHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALA------QTIARQKQLERRLEQQTEQAKKLEEKA---QAAL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907082217 1904 EKLTEERDQRAAaenrekEQNKRLQRQLRDTKEEMSELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1976
Cdd:pfam04012 78 TKGNEELAREAL------AEKKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAA 144
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1758-1944 |
6.19e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 41.60 E-value: 6.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1758 KAMEVEMEDLHLQIDDIAKAktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLqaQIEES 1837
Cdd:pfam04108 20 RSLLEELVVLLAKIAFLRRG---LSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNT--PVEPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1838 NKEKQELQEKLqalqsqvefleQSMVDKSLVSRQEAKIRELETRLefeKTQVKRLENLASRLKETMEKLTEERDQRAAAe 1917
Cdd:pfam04108 95 LPPGEEKQKTL-----------LDFIDEDSVEILRDALKELIDEL---QAAQESLDSDLKRFDDDLRDLQKELESLSSP- 159
|
170 180
....*....|....*....|....*..
gi 1907082217 1918 NREKEQNKRLQRQLRDTKEEMSELARK 1944
Cdd:pfam04108 160 SESISLIPTLLKELESLEEEMASLLES 186
|
|
| PDZ3_MAGI-1_3-like |
cd06733 |
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ... |
223-300 |
6.47e-03 |
|
PDZ domain 3 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 3 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ3 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as beta-strands A, -B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467215 [Multi-domain] Cd Length: 85 Bit Score: 37.98 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 223 LQRRPTGdFGFSLrrttmLDRAPEG-QAYrrVVHFAEPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSG 300
Cdd:cd06733 6 LRRQETG-FGFRI-----LGGTEEGsQVS--IGAIVPGGAADLD---GrLRTGDELLSVDGVNVVGASHHKVVDLMGNAA 74
|
|
| Nuf2_DHR10-like |
pfam18595 |
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ... |
1864-1964 |
6.94e-03 |
|
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.
Pssm-ID: 465814 [Multi-domain] Cd Length: 117 Bit Score: 38.72 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1864 DKSLVSRQEAKIRELETRLE----FEK------TQVKRLENLASRLKETMEKLTEERDQRAAAENREKE---QNKRLQRQ 1930
Cdd:pfam18595 7 EKEELAELERKARELQAKIDalqvVEKdlrsciKLLEEIEAELAKLEEAKKKLKELRDALEEKEIELRElerREERLQRQ 86
|
90 100 110
....*....|....*....|....*....|....
gi 1907082217 1931 LRDTKEemsELARKEAEASRKKHELEMDLESLEA 1964
Cdd:pfam18595 87 LENAQE---KLERLREQAEEKREAAQARLEELRE 117
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
7.14e-03 |
|
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, APBA3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of APBA1, APBA2, APBA3, and related domains. The APBA/X11/Mint protein family includes three members: neuron specific APBA1 (also known as X11alpha and Mint1) and APBA2 (also known as X11beta and Mint2), and the ubiquitously expressed APBA3 (also known as X12gamma and Mint3). They are involved in regulating neuronal signaling, trafficking, and plasticity. They contain two PDZ domains (PDZ1 and PDZ2) which bind a variety of proteins: Arf GTPases (APBA1 and APBA2 PDZ2) and neurexin (APBA1 and APBA2 PDZ1 and 2) which are involved in vesicle docking and exocytosis; alpha1B subunit of N-type Ca2+ channel (APBA1 PDZ1) that is involved in ion channels; KIF17 (APBA1 PDZ1) that is involved in transport and traffic; and Alzheimer's disease related proteins, APP (APBA3 PDZ2), CCS (APBA1 PDZ2), NF-kappa-B/p65 (APBA2 PDZ2), presenilin-1 (APBA1 and APBA2 PDZ1 and PDZ2). PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This APBA1,3-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467255 [Multi-domain] Cd Length: 78 Bit Score: 37.38 E-value: 7.14e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1907082217 273 GDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| COG5644 |
COG5644 |
U3 small nucleolar RNA-associated protein 14 [Function unknown]; |
1476-1958 |
7.16e-03 |
|
U3 small nucleolar RNA-associated protein 14 [Function unknown];
Pssm-ID: 227931 [Multi-domain] Cd Length: 869 Bit Score: 41.61 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1476 LQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQ---RRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFS 1548
Cdd:COG5644 1 LPQPQGKHQRKGKKQLENKILHSYEEESagfdSEELEDNDeqgYSFGVNSEDDEEIDSDEAFDEEDEKRFADWSFNASKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1549 LKQQMEEKDLDiagfTQKVVSLEAELQDISSQESKDEASLAKV-KKQLRDLEaKVKDQEEELDEQAGSIQMLEQAKLRLE 1627
Cdd:COG5644 81 GKSNKDHKNLN----NTKEISLNDSDDSVNSDKLENEGSVSSIdENELVDLD-TLLDNDQPEKNESGNNDHATDKENLLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1628 MEMERMRQTHSKEMESRDEEVEEarqscqkklkqmevqlEEEYEDKQKALREKRELESKLSTLSDQVNQR------DFES 1701
Cdd:COG5644 156 SDASSSNDSESEESDSESEIESS----------------DSDHDDENSDSKLDNLRNYIVSLKKDEADAEsvlssdDNDS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1702 EKRLRKDLKRT-KALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEFTCAAAVKarkamevemedlhlQIDDIAKAKTA 1780
Cdd:COG5644 220 IEEIKYDPHETnKESGSSETIDITDLLDSIPMEQLKVSLKPLVSESSKLDAPLAK--------------SIQDRLERQAA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1781 LEEQLSRLQREKNEIQNRLEEDQE--DMNELMKKHKAAVAQASRDMAQmNDLQAQIEE-------SNKEKQELQEKLQAL 1851
Cdd:COG5644 286 YEQTKNDLEKWKPIVADNRKSDQLifPMNETARPVPSNNGLASSFEPR-TESERKMHQalldaglENESALKKQEELALN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1852 QSQVEFLEQSMVD----KSLVSRQEAKIRELETRLEFEKTQVKRLENLASR-LKETMEKLTEERDQRAAAENREKEQNKR 1926
Cdd:COG5644 365 KLSVEEVAERTRQlrfmRELMFREERKAKRVAKIKSKTYRKIRKNRKEKEMaLIPKSEDLENEKSEEARALERMTQRHKN 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1907082217 1927 LQRQLRD----------TKEEMSELARKEAEASRKKHELEMD 1958
Cdd:COG5644 445 TSSWTRKmlerashgegTREAVNEQIRKGDELMQRIHGKEIM 486
|
|
| TMF_TATA_bd |
pfam12325 |
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ... |
1887-1962 |
7.19e-03 |
|
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.
Pssm-ID: 432481 [Multi-domain] Cd Length: 115 Bit Score: 38.68 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1887 TQVKRLENLASRLKETMEKLTEERDQrAAAE----NREKEQNKRLQRQLRDTKEEMSELARKEA-------EASRKKHEL 1955
Cdd:pfam12325 19 STIRRLEGELASLKEELARLEAQRDE-ARQEivklMKENEELKELKKELEELEKELKELEQRYEttlellgEKSEEVEEL 97
|
....*..
gi 1907082217 1956 EMDLESL 1962
Cdd:pfam12325 98 KADVEDL 104
|
|
| SynN |
cd00179 |
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the ... |
1785-1940 |
7.30e-03 |
|
Syntaxin N-terminus domain; syntaxins are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane; they are a family of receptors for intracellular transport vesicles; each target membrane may be identified by a specific member of the syntaxin family; syntaxins contain a moderately well conserved amino-terminal domain, called Habc, whose structure is an antiparallel three-helix bundle; a linker of about 30 amino acids connects this to the carboxy-terminal region, designated H3 (t_SNARE), of the syntaxin cytoplasmic domain; the highly conserved H3 region forms a single, long alpha-helix when it is part of the core SNARE complex and anchors the protein on the cytoplasmic surface of cellular membranes; H3 is not included in defining this domain
Pssm-ID: 238105 [Multi-domain] Cd Length: 151 Bit Score: 39.19 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1785 LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQsmvd 1864
Cdd:cd00179 1 LEEFFEEVEEIRGNIDKISEDVEELQKLHSQLLTAPDADPELKQELESLVQEIKKLAKEIKGKLKELEESNEQNEA---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1865 ksLVSRQEAKIReletrlefeKTQVkrlENLASRLKETMEKLTEERdQRAAAENREkeqnkRLQRQLRDTKEEMSE 1940
Cdd:cd00179 77 --LNGSSVDRIR---------KTQH---SGLSKKFVEVMTEFNKAQ-RKYRERYKE-----RIQRQLEITGGEATD 132
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1439-1630 |
7.37e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1439 RLQQELEDKMEVEQQSRRQLE-RRLGDLQADSDESQRAlqQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRR---F 1514
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEqRRLQQEQLERAEKMRE--ELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLqlqA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1515 DSELSQAHEETQREKLQreKLQREKDMLLAE-AFSLKQQMEEKDLDIAGfTQKVVSLEAELQDISSQESKDEAslakvkK 1593
Cdd:pfam15709 417 AQERARQQQEEFRRKLQ--ELQRKKQQEEAErAEAEKQRQKELEMQLAE-EQKRLMEMAEEERLEYQRQKQEA------E 487
|
170 180 190
....*....|....*....|....*....|....*..
gi 1907082217 1594 QLRDLEAKVKDQEEEldeqagsiqmlEQAKLRLEMEM 1630
Cdd:pfam15709 488 EKARLEAEERRQKEE-----------EAARLALEEAM 513
|
|
| PDZ_ZASP52-like |
cd23068 |
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ... |
269-308 |
7.52e-03 |
|
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467281 [Multi-domain] Cd Length: 82 Bit Score: 37.51 E-value: 7.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907082217 269 GLVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd23068 42 GLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLTVQ 81
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1303-1526 |
7.57e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1303 SEEQIRNKDEEIQQLRSKLEKVEKERNELRLSSDRLETRISELTSELtdeRNTGESASQLLDAETAERLRTekEMKELQT 1382
Cdd:COG3206 203 QKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL---GSGPDALPELLQSPVIQQLRA--QLAELEA 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1383 QYDALkkqmevmemevmearliraaeingevddddaggewRLKYERAVREVdftkKRLQQELEdkmEVEQQSRRQLERRL 1462
Cdd:COG3206 278 ELAEL-----------------------------------SARYTPNHPDV----IALRAQIA---ALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907082217 1463 GDLQADSDESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSeLSQAHEETQ 1526
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES-LLQRLEEAR 378
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1776-1990 |
7.59e-03 |
|
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: 41.86 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1776 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA----QASRDMAQMND------LQAQIEEsnKEKQELQ 1845
Cdd:pfam15818 21 EAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAvfkkQLQMKMCALEEekgkyqLATEIKE--KEIEGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1846 EKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFEKTQVKRLEN----LASR---LKETMEKLtEERDQRAAAEN 1918
Cdd:pfam15818 99 ETLKALQVSKYSLQKK------VSEMEQKLQLHLLAKEDHHKQLNEIEKyyatITGQfglVKENHGKL-EQNVQEAIQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1919 -REKEQNKRLQRQLRDTKEEM----SELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAF---KRIGDLQAAIEDE 1990
Cdd:pfam15818 172 kRLSALNKKQESEICSLKKELkkvtSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELelnKKINEEITHIQEE 251
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1589-1680 |
7.67e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1589 AKVKKQLRDLEAKVKDQEEELDEQagsiqMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQScqkKLKQMEVQLEE 1668
Cdd:cd16269 203 ERAKAEAAEQERKLLEEQQRELEQ-----KLEDQERSYEEHLRQLKEKMEEERENLLKEQERALES---KLKEQEALLEE 274
|
90
....*....|..
gi 1907082217 1669 EYEDKQKALREK 1680
Cdd:cd16269 275 GFKEQAELLQEE 286
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1793-1974 |
7.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1793 NEIQNRLEEDQEDMNELMKKHKAAVAQASRD----MAQMNDLQAQIEESNKEKQELQEKlqalQSQVEfleqsmvdkSLV 1868
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQlrkaLFELDKLQEELEQLREELEQAREE----LEQLE---------EEL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1869 SRQEAKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQLRDTKEEMSELARKEAEA 1948
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
170 180
....*....|....*....|....*.
gi 1907082217 1949 SRKKHELEMDLESLEAANQSLQADLK 1974
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQ 174
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1662-1975 |
7.81e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1662 MEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQRDFESEKrlrkDLKRTKALLADAQIMLDHLKNN-APSKREIAQLK 1740
Cdd:pfam03528 6 LQQRVAELEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE----DLKRQNAVLQEAQVELDALQNQlALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1741 NQLEESEFTCAAAV-KARKAMEVEMEDLHLQIDDIAKA-----KTALEEQLSR-------LQREKNEIQNRLEEDQEDMN 1807
Cdd:pfam03528 82 AVATVSENTKQEAIdEVKSQWQEEVASLQAIMKETVREyevqfHRRLEQERAQwnqyresAEREIADLRRRLSEGQEEEN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1808 ---------ELMKKHKAAVAQASRDMAQMNDLQAQIEESNKE-----KQELQEKLQALQSQVEFLEQSM----VDKSLVS 1869
Cdd:pfam03528 162 ledemkkaqEDAEKLRSVVMPMEKEIAALKAKLTEAEDKIKEleaskMKELNHYLEAEKSCRTDLEMYVavlnTQKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1870 RQEAKIR----ELETRLEFEKTQVKRL--------------ENLASRLKETMEKLTEERDQRAAAENREKEQNKRLQRQL 1931
Cdd:pfam03528 242 EDAEKLRkelhEVCHLLEQERQQHNQLkhtwqkandqflesQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRART 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1932 RDTKEEMSE-----------LARKEAEASRKKHELEMDLESLEAANQSLQADLKL 1975
Cdd:pfam03528 322 HKEKETLKSdrehtvsihavFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVL 376
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1765-1858 |
8.03e-03 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 40.76 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1765 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQMNDLQAQIEESNKekqEL 1844
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 1907082217 1845 QEKLQALQSQVEFL 1858
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| PDZ10_MUPP1-PDZ8_PATJ-like |
cd06673 |
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated ... |
258-307 |
8.25e-03 |
|
PDZ domain 10 of multi-PDZ-domain protein 1 (MUPP1), domain 8 of PATJ (protein-associated tight junction) and similar domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 10 of MUPP1, PDZ domain 8 of PATJ, and related domains. MUPP1 and PATJ serve as scaffolding proteins linking different proteins and protein complexes involved in the organization of tight junctions and epithelial polarity. MUPP1 contains an L27 (Lin-2 and Lin-7 binding) domain and 13 PDZ domains. PATJ (also known as INAD-like) contains an L27 domain and ten PDZ domains. MUPP1 and PATJ share several binding partners, including junctional adhesion molecules (JAM), zonula occludens (ZO)-3, Pals1 (protein associated with Lin-7), Par (partitioning defective)-6 proteins, and nectins (adherence junction adhesion molecules). PATJ lacks 3 PDZ domains seen in MUPP1: PDZ6, 9, and 13; consequently, MUPP1 PDZ7 and 8 align with PATJ PDZ6 and 7; and MUPP1 PDZ domains 10-12 align with PATJ PDZ domains 8-10. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MUPP1-like family PDZ10 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.
Pssm-ID: 467161 [Multi-domain] Cd Length: 86 Bit Score: 37.66 E-value: 8.25e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1907082217 258 EPGAGTKDlalG-LVPGDRLVEINGQNVENKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06673 37 EDGAAAKD---GrLWAGDQILEVNGEDLRKATHDEAINVLRQTPQKVRLLV 84
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1665-1877 |
8.31e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.05 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1665 QLEEEYEDKQKALREK-RELESKLSTLSDQVNQ---RDFESEKRLRKDLKRTKALLADAQIMLDhlKNNAPSKREIAQLK 1740
Cdd:pfam04012 15 EGLDKAEDPEKMLEQAiRDMQSELVKARQALAQtiaRQKQLERRLEQQTEQAKKLEEKAQAALT--KGNEELAREALAEK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1741 NQLEESEftcaaavkarKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedQEDMNELMKKH--KAAVA 1818
Cdd:pfam04012 93 KSLEKQA----------EALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLK--AAKAQEAVQTSlgSLSTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907082217 1819 QASRDMAQMNDLQAQIEESNkekqELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRE 1877
Cdd:pfam04012 161 SATDSFERIEEKIEEREARA----DAAAELASAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1682-1952 |
8.53e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 40.83 E-value: 8.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1682 ELESKLSTLSDQVNQRdfesEKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIAQLKNQLEESEftcaaavkarKAME 1761
Cdd:pfam04108 116 ILRDALKELIDELQAA----QESLDSDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLE----------EEMA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1762 VEMEDLHLQIDDIAKAKTALEEqlsrlqrEKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDMAQmndLQAQIEESNKEK 1841
Cdd:pfam04108 182 SLLESLTNHYDQCVTAVKLTEG-------GRAEMLEVLENDARELDDVVPELQDRLDEMENNYER---LQKLLEQKNSLI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1842 QELQEKLQalqsqvefleqsmvdkslvsrqeaKIRELETRLEFEKTQVKRLENLASRLKETMEKLTEE-RDQRAAAEN-- 1918
Cdd:pfam04108 252 DELLSALQ------------------------LIAEIQSRLPEYLAALKEFEERWEEEKETIEDYLSElEDLREFYEGfp 307
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907082217 1919 -----------REKEQNKRLQRQLRDTKEEMSELARKEAEAsRKK 1952
Cdd:pfam04108 308 saygsllleveRRREWAEKMKKILRKLAEELDRLQEEERKR-REK 351
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1508-1628 |
8.61e-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: 38.82 E-value: 8.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1508 EKKQRRFDSELSQAHEETQREKLQREKLQREKDML--------------LAEAFSLKQQMEEkdldiagFTQKVVSLEAE 1573
Cdd:pfam10473 2 EKKQLHVLEKLKESERKADSLKDKVENLERELEMSeenqelaileaensKAEVETLKAEIEE-------MAQNLRDLELD 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907082217 1574 LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE-QAGSIQMLEQAKLRLEM 1628
Cdd:pfam10473 75 LVTLRSEKENLTKELQKKQERVSELESLNSSLENLLEEkEQEKVQMKEESKTAVEM 130
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1507-1669 |
8.68e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1507 LEKKQRRFDSELSQAHEETQREKlqREKLQREKDmllaEAFSLKQQMEekdldiagftQKVVSLEAELQDISSQESKDEA 1586
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIK--KEALLEAKE----EIHKLRNEFE----------KELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1587 SLakvKKQLRDLEAKvkdqEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEME-----SRDE-------EVE-EARQ 1653
Cdd:PRK12704 97 NL---DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEakeilleKVEeEARH 169
|
170
....*....|....*.
gi 1907082217 1654 SCQKKLKQMEVQLEEE 1669
Cdd:PRK12704 170 EAAVLIKEIEEEAKEE 185
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1494-1679 |
8.74e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1494 KLHLEGQQVRNHELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQK-VVSLEA 1572
Cdd:pfam15709 337 RLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKqRLQLQA 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1573 ELQDISSQESKDEASLAKVKKQLRDLEAKvKDQEEELDEQAGSIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEAR 1652
Cdd:pfam15709 417 AQERARQQQEEFRRKLQELQRKKQQEEAE-RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAE 495
|
170 180
....*....|....*....|....*..
gi 1907082217 1653 QSCQKKLKQMEVQLEEEYEDKQKALRE 1679
Cdd:pfam15709 496 ERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
1762-1855 |
8.87e-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: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.72 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1762 VEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDmAQMNDLQAQIEESNKEK 1841
Cdd:smart00935 4 VDVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEK----LQKDAATLSEAARE-KKEKELQKKVQEFQRKQ 78
|
90
....*....|....
gi 1907082217 1842 QELQEKLQALQSQV 1855
Cdd:smart00935 79 QKLQQDLQKRQQEE 92
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1439-1619 |
9.02e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1439 RLQQELEDKMEVEQQSRRQLER---RLGDLQADSDESQRALQQLKKKCQRLTAELQ----DTKLHLEG-------QQVrn 1504
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEEltdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkVIKMYEKGgvcptctQQI-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1505 HELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLA---EAFSLKQQMEEKDLDIAGFTQKVVSLEAELQDISSQE 1581
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907082217 1582 SKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGSIQML 1619
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1815-1931 |
9.24e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 41.22 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1815 AAVAQASRDMAQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMvdkSLVSRQeakIRELETRLEfektqvkRLEN 1894
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAI---SQASRK---LRETQNTLN-------QLNK 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 1907082217 1895 LASRLKETMEKLteerdqraaaENREKEQNKRLQRQL 1931
Cdd:PRK11637 104 QIDELNASIAKL----------EQQQAAQERLLAAQL 130
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1456-1941 |
9.51e-03 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 40.97 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1456 RQLERRLGDLQAD-------SDESQRALQQLKKKCQRLTA--ELQDTKLHLEGQQVRN--HELEKKQRRFDSELSQAHEE 1524
Cdd:pfam15450 16 KQLEQWVADLQAEvvslrghKERCEHATLSLLRELLQVRAhvQLQDSELKQLRQEVQQaaRAPEKEALEFPGPQNQNQMQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1525 TQREKL--QREKLQREKDMLLAEAFSLKQQMEEKDLDIAGFTQKvVSLEAELQDISS---QESKDEASlAKVKKQLRDLE 1599
Cdd:pfam15450 96 ALDKRLveVREALTQIRRKQALQDSERKGAEQEANLRLTKLTGK-LKQEEQGREAACsalQKSQEEAS-QKVDHEVARMQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1600 AKVKDQEEE-----LDEQAGSIQMLEQAKLRLEmemERMRQTHSKEMESRDEEVEEARQSCQKklkqmevqLEEEYEDKQ 1674
Cdd:pfam15450 174 AQVTKLGEEmslrfLKREAKLCSFLQKSFLALE---KRMKASESTRLKAESSLREELEGRWQK--------LQELTEERL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1675 KALREKRELESklSTLSDQVnqrdfeseKRLRKDLKRTKALLADAQIMLDHLKNNAPSKREIaqlKNQLEESEFTCAAAV 1754
Cdd:pfam15450 243 RALQGQREQEE--GHLLEQC--------RGLDAAVVQLTKFVRQNQVSLNRVLLAEQKARDA---KGQLEESQAGELASY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1755 ------KARKAMEVEMEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN-------RLEEDQEDMNELMKKHKAAVAQAS 1821
Cdd:pfam15450 310 vqenleAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKDLSDhflalswRLDLQEQTLGLKLSEAKKEWEGAE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1822 RDmaQMNDLQAQIEESNKEKQELQEKLQALQSQVEFLEQSMV----DKSLVSRQEAKIRELET---RLE----FEKTQVK 1890
Cdd:pfam15450 390 RK--SLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVlhksDSDLKISAEGKAREFEVeamRQElaalLSSVQLL 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1907082217 1891 RLENLASRLKETMEKLTEERDQRAAAENREKE----QNKRLQRQLRDTKEEMSEL 1941
Cdd:pfam15450 468 KEGNPGRKIAEIQGKLATFQNQIIKLENSIQDnktiQNLKFNTETKLRTEEIATL 522
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1506-1752 |
9.71e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 41.28 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1506 ELEKKQRRFDSELSQAHEETQREKLQREKLQREKDMLLAEAFS-----LKQQMEEKDLDIAGFTQKVVSLEAELQDISSQ 1580
Cdd:pfam09731 230 NVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPvlkedNLLSNDDLNSLIAHAHREIDQLSKKLAELKKR 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1581 ESKDEA-SLAKVKKQLRDLEAKV-KDQEEELDEQAGSIQMLEQAKL-------RLEMEMERMRQTHSKEMESRDEEVEEA 1651
Cdd:pfam09731 310 EEKHIErALEKQKEELDKLAEELsARLEEVRAADEAQLRLEFEREReeiresyEEKLRTELERQAEAHEEHLKDVLVEQE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907082217 1652 rqscqkklkqMEVQLEEEYEDKQKALREKRELESKLSTLSDQVNQ--RDFESEKRLRKDLKRTKAL------LADAQIML 1723
Cdd:pfam09731 390 ----------IELQREFLQDIKEKVEEERAGRLLKLNELLANLKGleKATSSHSEVEDENRKAQQLwlaveaLRSTLEDG 459
|
250 260
....*....|....*....|....*....
gi 1907082217 1724 DHLKNNAPSKREIAQLKNQLEESEFTCAA 1752
Cdd:pfam09731 460 SADSRPRPLVRELKALKELASDDEVVKAA 488
|
|
| |
