|
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 ... |
419-1173 |
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: 1164.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 578
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAG-SVGGVLSVEKLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDE 658
Cdd:cd01386 160 LLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAESNSFGIVPLQKPEDKQKAAAAFSKLQAAMKTLGISEEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 659 QKACWFILAAIYHLGAAGATKEAaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRQGPEESGl 738
Cdd:cd01386 240 QRAIWSILAAIYHLGAAGATKAA-SAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGGPQQSTTSSGQESPARS- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 739 gDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGSARGASFEELCHNYTQDR 818
Cdd:cd01386 318 -SSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSITIVDTPGFQNPAHSGSQRGATFEDLCHNYAQER 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 819 LQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLARTDEARGLLWLLEEEALVPGASEDTLL 898
Cdd:cd01386 397 LQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQAPQQALVRSDLRDEDRRGLLWLLDEEALYPGSSDDTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 899 ERLFSYYGPQEGDkKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNPATQNAPRLLQDSQKKiisnlflgra 978
Cdd:cd01386 477 ERLFSHYGDKEGG-KGHSLLRRSEGPLQFVLGHLLGTNPVEYDVSGWLKAAKENPSAQNATQLLQESQKE---------- 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 979 gsatvlsgsiagleggsqlalrratsmrktfttgMAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGEp 1058
Cdd:cd01386 546 ----------------------------------TAAVKRKSPCLQIKFQVDALIDTLRRTGLHFVHCLLPQHNAGKDE- 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1059 rsassrrvsssseldlPSGDHCEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGR 1138
Cdd:cd01386 591 ----------------RSTSSPAAGDELLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGL 654
|
730 740 750
....*....|....*....|....*....|....*
gi 42794779 1139 NYIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd01386 655 NSEVADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
420-1173 |
1.54e-151 |
|
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: 483.25 E-value: 1.54e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd00124 2 AILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRsADLPPHVFAVADAAYRAMLRDGQNQSILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVFS-----VEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 573
Cdd:cd00124 82 ESGAGKTETTKLVLKYLAALSGSGSSKSSSsassiEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 574 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAEN---NVFGIVPLAKPEEKQKAAQQFSKLQAAMK 650
Cdd:cd00124 162 SIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYyylNDYLNSSGCDRIDGVDDAEEFQELLDALD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSF 729
Cdd:cd00124 242 VLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSaEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKPL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 730 RqgPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSS--QHSLCSMMIVDTPGFQNPEQggsargASF 807
Cdd:cd00124 322 T--VEQ------------AEDARDALAKALYSRLFDWLVNRINAALSPTdaAESTSFIGILDIFGFENFEV------NSF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 808 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLePPTDDSVAAVDQaSHQSLVRSLarTDEARgllwlleeea 887
Cdd:cd00124 382 EQLCINYANEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEG-KPLGILSLL--DEECL---------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 888 lVPGASEDTLLERLFSYYGPQEGDKKGQspllhSSKPHHFllGHSHGTNWVEYNVTGWLNYTKQNpatqnaprllqdsqk 967
Cdd:cd00124 448 -FPKGTDATFLEKLYSAHGSHPRFFSKK-----RKAKLEF--GIKHYAGDVTYDADGFLEKNKDT--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 968 kiisnlflgragsatvLSGSIAGLeggsqlaLRRATSMRKtfttgmaavkkkslciqmklQVDALIDTIKKSKLHFVHCF 1047
Cdd:cd00124 505 ----------------LPPDLVDL-------LRSGSQFRS--------------------QLDALMDTLNSTQPHFVRCI 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1048 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1127
Cdd:cd00124 542 KPNDEKKPG-----------------------------LFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRI 592
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 42794779 1128 LAPHLTKKHGRNYIVVDERRAveellECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd00124 593 LAPGATEKASDSKKAAVLALL-----LLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
400-1185 |
1.62e-118 |
|
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: 391.91 E-value: 1.62e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 400 NAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQ 479
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 480 TAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFS 557
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSG-SNTEVGSVED-QILESnpILEAFGNAKTLRNNNSSRFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 558 QILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVFgivpLAKPEEKQK 637
Cdd:smart00242 159 KFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKS-PEDYRY----LNQGGCLTV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 638 A----AQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 713
Cdd:smart00242 234 DgiddAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKEELSNAAELLGVDPEELEKAL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 714 fkhqhkggtLQRSTSFRQGPEESGLGdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 793
Cdd:smart00242 314 ---------TKRKIKTGGEVITKPLN-----VEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGSTYFIGVLDIYGF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 794 QNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEpptdDSVAAVD--QASHQSLVRSLa 871
Cdd:smart00242 380 EIFEVN------SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF----DNQDCIDliEKKPPGILSLL- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 872 rTDEARgllwlleeealVPGASEDTLLERLFSYYGPQEgdkkgqspllHSSKPH-----HFLLGHSHGTnwVEYNVTGWL 946
Cdd:smart00242 449 -DEECR-----------FPKGTDQTFLEKLNQHHKKHP----------HFSKPKkkgrtEFIIKHYAGD--VTYDVTGFL 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 947 nytKQN--PATQNAPRLLQDSQKKIISNLFlgragsatvlsGSIAGleggsqlalrRATSMRKTFTTGMaavkkkslciQ 1024
Cdd:smart00242 505 ---EKNkdTLSDDLIELLQSSKNPLIASLF-----------PSGVS----------NAGSKKRFQTVGS----------Q 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1025 MKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRTQLRGSRLLDA 1104
Cdd:smart00242 551 FKEQLNELMDTLNSTNPHFIRCIKP--------------------NEEKKP---------GDFDSSLVLHQLRYLGVLEN 601
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1105 MRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNyivvDERRAVEELLECLDLEKSSCCMGLSRVFFRAGTLARLEEQR 1184
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPD-TWPPWGG----DAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELR 676
|
.
gi 42794779 1185 D 1185
Cdd:smart00242 677 E 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
381-1905 |
9.56e-110 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 385.59 E-value: 9.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 381 KLDHDGAILDVDEDDVEKANAPSCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMH 460
Cdd:COG5022 42 KEDGESVSVKKKVLGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 461 MFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKwQALYT--L 538
Cdd:COG5022 122 SYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSSSTVEISSIEK-QILATnpI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 539 LEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL--- 615
Cdd:COG5022 201 LEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLqnp 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 616 ---NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQAAMKVLGISPDEQKACWFILAAIYHLG--AAGATKEaaeaGRKQFA 690
Cdd:COG5022 281 kdyIYLSQGGCDKIDGIDDAKE-------FKITLDALKTIGIDEEEQDQIFKILAAILHIGniEFKEDRN----GAAIFS 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 691 RHEWAQKAAYLLGCSLEELSSAIFKHQHKGG--TLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLV 768
Cdd:COG5022 350 DNSVLDKACYLLGIDPSLFVKWLVKRQIKTGgeWIVVPLNLEQ----------------ALAIRDSLAKALYSNLFDWIV 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 769 SLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFD 845
Cdd:COG5022 414 DRINKSLDHSAAASNFIGVLDIYGFEIFEKN------SFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEwsfIDYF 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 846 DLEPPTDdsvaavdqashqsLVRSLART-------DEARgllwlleeealVPGASEDTLLERLFSYYgPQEGDKKGQSPL 918
Cdd:COG5022 488 DNQPCID-------------LIEKKNPLgilslldEECV-----------MPHATDESFTSKLAQRL-NKNSNPKFKKSR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 919 LHSSKphhFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGRAgsatvlsgsiaglEGGSQLA 998
Cdd:COG5022 543 FRDNK---FVVKHYAGD--VEYDVEGFLDKNK-DPLNDDLLELLKASTNEFVSTLFDDEE-------------NIESKGR 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 999 LRRATSMRKTfttgmaavkkkslciqmklQVDALIDTIKKSKLHFVHCFLP--VAEGWageprsassrrvsssseldlps 1076
Cdd:COG5022 604 FPTLGSRFKE-------------------SLNSLMSTLNSTQPHYIRCIKPneEKSPW---------------------- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1077 gdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHlTKKHGRNYIVVDERRAVEELLECL 1156
Cdd:COG5022 643 ---------TFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPS-KSWTGEYTWKEDTKNAVKSILEEL 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1157 DLEKSSCCMGLSRVFFRAGTLARLEEQRDEQTSRNLTLFQAACRGYLARQHF-KKRKIQDlAIRCVQKNIKKNKGVKDWP 1235
Cdd:COG5022 713 VIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYlQALKRIK-KIQVIQHGFRLRRLVDYEL 791
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1236 WWKLFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEK----AEKERNELRLNSDRLESRISEltSELTDERNTGESASQL 1311
Cdd:COG5022 792 KWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekklRETEEVEFSLKAEVLIQKFGR--SLKAKKRFSLLKKETI 869
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1312 LDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDF----TKK 1387
Cdd:COG5022 870 YLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLeegpSIE 949
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1388 RLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRrfdsEL 1467
Cdd:COG5022 950 YVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPV----EV 1025
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1468 SQAHEEAQREKLQREKLQREKDMLLAEAFSLK--QQLEEKDmdiagftqKVVSLEAELQDIssqESKDEASLAKVKKQLR 1545
Cdd:COG5022 1026 AELQSASKIISSESTELSILKPLQKLKGLLLLenNQLQARY--------KALKLRRENSLL---DDKQLYQLESTENLLK 1094
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1546 DLEAK---VKDQEEELDEQAGTIQMLEQAKLRLEMEMERM--RQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYE 1620
Cdd:COG5022 1095 TINVKdleVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFlsQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPF 1174
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1621 D--KQKVLREKRELEGKLATLSDQVN--RRDFESEKRLRKDL----KRTKALLADAQLML-----------DHLKNSAPS 1681
Cdd:COG5022 1175 AalSEKRLYQSALYDEKSKLSSSEVNdlKNELIALFSKIFSGwprgDKLKKLISEGWVPTeystslkgfnnLNKKFDTPA 1254
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIakAKTALEEQLSRLQREKNEiqnRLEEDQEDMNELMKK 1761
Cdd:COG5022 1255 SMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVG--LFNALRTKASSLRWKSAT---EVNYNSEELDDWCRE 1329
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 HKAAVAQASRdlaqINDLQAQ--LEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRElETRLEFERTQVK 1839
Cdd:COG5022 1330 FEISDVDEEL----EELIQAVkvLQLLKDDLNKLDELLDACYSLNPAEIQNLKSRYDPADKENNLPK-EILKKIEALLIK 1404
|
1530 1540 1550 1560 1570 1580
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1840 RLESLASRLKENMEKLTEErdqriaaENREKEQNKRLQRQLRDTKEEMGELarkEAEASRKKHELE 1905
Cdd:COG5022 1405 QELQLSLEGKDETEVHLSE-------IFSEEKSLISLDRNSIYKEEVLSSL---SALLTKEKIALL 1460
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
408-1173 |
1.39e-109 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 365.83 E-value: 1.39e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 408 EDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLM 487
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 488 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGI-SGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDF 564
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSgSAGNVGRLEE-QILQSnpILEAFGNAKTVRNNNSSRFGKYIEIQF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 565 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL---------NHLAENNVFGIvplakpeek 635
Cdd:pfam00063 161 DAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLtnpkdyhylSQSGCYTIDGI--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 636 qKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKqFARHEWAQKAAYLLGCSLEELSSAIFK 715
Cdd:pfam00063 232 -DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAV-PDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 716 HQHKGGTLQRSTSfrQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQ 794
Cdd:pfam00063 310 RRIKTGRETVSKP--QNVEQ------------ANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIgVLDIYGFE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 795 NPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptDDSVAAVDQASHQSL-VRSLarT 873
Cdd:pfam00063 376 IFEKN------SFEQLCINYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDF----GDNQPCIDLIEKKPLgILSL--L 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 DEArgllwlleeeALVPGASEDTLLERLFSYYgpqegdkkGQSPLLHSSKPH---HFLLGHSHGTnwVEYNVTGWLNYTK 950
Cdd:pfam00063 444 DEE----------CLFPKATDQTFLDKLYSTF--------SKHPHFQKPRLQgetHFIIKHYAGD--VEYNVEGFLEKNK 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 951 qNPATQNAPRLLQDSQKKIISNLFLGRAgsatvLSGSIAGLEGGSQLALRRATSMRKtfTTGMaavkkkslciQMKLQVD 1030
Cdd:pfam00063 504 -DPLNDDLVSLLKSSSDPLLAELFPDYE-----TAESAAANESGKSTPKRTKKKRFI--TVGS----------QFKESLG 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1031 ALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQ 1110
Cdd:pfam00063 566 ELMKTLNSTNPHYIRCIKPNEKKRAG-----------------------------VFDNSLVLHQLRCNGVLEGIRIRRA 616
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1111 GYPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:pfam00063 617 GFPNRITFQEFVQRYRILAPKTWPK-----WKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
420-1173 |
2.07e-102 |
|
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: 344.83 E-value: 2.07e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPaVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01377 2 SVLHNLRERYYSDLIYTYSGLFCVAVNPyKRLP-IYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKW-----QALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 571
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKKgtledQILQAnpILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 572 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFgIVPLAKPEEKQKAAQQFSKLQAAMKV 651
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFF-LSQGELTIDGVDDAEEFKLTDEAFDI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 652 LGISPDEQKACWFILAAIYHLGAAGATKEaaeaGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRS 726
Cdd:cd01377 240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR----RREEQAEldgTEEADKAAHLLGVNSSDLLKALLKPRIKVGRewVTKG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 727 TSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQ----Npeqggsa 802
Cdd:cd01377 316 QNKEQ----------------VVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQYFIGVLDIAGFEifefN------- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 803 rgaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAF----DDLEPPTDdsvaavdqashqsLVRS-----LART 873
Cdd:cd01377 373 ---SFEQLCINYTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFidfgLDLQPTID-------------LIEKpnmgiLSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 DEargllwlleeEALVPGASEDTLLERLFSyygpQEGDKKGQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLnyTK-Q 951
Cdd:cd01377 437 DE----------ECVFPKATDKTFVEKLYS----NHLGKSKNFKKPKPKKSEaHFILKHYAGD--VEYNIDGWL--EKnK 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 952 NPATQNAPRLLQDSQKKIISNLFlgragsatvlsgSIAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDA 1031
Cdd:cd01377 499 DPLNENVVALLKKSSDPLVASLF------------KDYEESGGGGGKKKKKGGSFRT----VSQLHKEQL--------NK 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1032 LIDTIKKSKLHFVHCFLPVAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQG 1111
Cdd:cd01377 555 LMTTLRSTHPHFVRCIIPNEEKKPGK-----------------------------IDAPLVLHQLRCNGVLEGIRICRKG 605
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1112 YPDHMVFSEFRRRFDVLAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd01377 606 FPNRIIFAEFKQRYSILAPNAIPK-----GFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
419-1173 |
9.87e-91 |
|
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: 311.17 E-value: 9.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGI-SGNKVFSVE---KWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 572
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPgelERQLLQAnpILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 573 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF--GIVPLAkpeeKQKAAQQFSKLQAAMK 650
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsnGYIPIP----GQQDKDNFQETMEAMH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRSts 728
Cdd:cd14920 237 IMGFSHEEILSMLKVVSSVLQFGNISFKKE-RNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRdyVQKA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 729 frQGPEESGLGdgtgpklsalecLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSF 807
Cdd:cd14920 314 --QTKEQADFA------------VEALAKATYERLFRWLVHRINKALDRTKRQGASFIgILDIAGFEIFELN------SF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 808 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlleeEA 887
Cdd:cd14920 374 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGV--LALLDE----------EC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 888 LVPGASEDTLLERLFSYYGPQEGDKKGQSPllhsSKPHHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPRLLQDSQK 967
Cdd:cd14920 442 WFPKATDKTFVEKLVQEQGSHSKFQKPRQL----KDKADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVATLLHQSSD 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 968 KIISNLFlgRAGSATVlsgSIAGLEGGSQLALRRATSMRKTFTTGMAAVKKKSLciqmklqvDALIDTIKKSKLHFVHCF 1047
Cdd:cd14920 515 RFVAELW--KDVDRIV---GLDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESL--------TKLMATLRNTNPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1048 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1127
Cdd:cd14920 582 IPNHEKRAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 42794779 1128 LAPHLTKKhgrnyIVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14920 633 LTPNAIPK-----GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
419-1173 |
7.40e-86 |
|
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: 296.89 E-value: 7.40e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAG-----------ISGNKVFSV-EKWQALYT---LLEAFGNSPTIINGNATRFSQILSLD 563
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAskpkgsgavphPAVNPAVLIgELEQQLLQanpILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 564 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVF---GIVPLAKPEEkqkaAQ 640
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDD-VKSYAFlsnGSLPVPGVDD----YA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 641 QFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKG 720
Cdd:cd14911 236 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSM-KFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 721 GtlQRSTSFRQGPEESGLGdgtgpklsalecLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQG 799
Cdd:cd14911 315 G--RDFVTKAQTKEQVEFA------------VEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIgILDMAGFEIFELN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 800 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFD----DLEPPTDdsvaavdqashqslvrslaRTDE 875
Cdd:cd14911 381 ------SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIdfglDLQPTID-------------------LIDK 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 876 ARGLLWLLEEEALVPGASEDTLLERLFSYYG--PQ--EGDKKGQSpllhsskphHFLLGHSHGTnwVEYNVTGWLnYTKQ 951
Cdd:cd14911 436 PGGIMALLDEECWFPKATDKTFVDKLVSAHSmhPKfmKTDFRGVA---------DFAIVHYAGR--VDYSAAKWL-MKNM 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 952 NPATQNAPRLLQDSQKKIISNLFlgraGSATVLSGSIAGLeGGSQLALRRATSMRKTFTTgmaavkkkslciQMKLQVDA 1031
Cdd:cd14911 504 DPLNENIVSLLQGSQDPFVVNIW----KDAEIVGMAQQAL-TDTQFGARTRKGMFRTVSH------------LYKEQLAK 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1032 LIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQG 1111
Cdd:cd14911 567 LMDTLRNTNPNFVRCIIPNHEKRAG-----------------------------KIDAPLVLDQLRCNGVLEGIRICRQG 617
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1112 YPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14911 618 FPNRIPFQEFRQRYELLTPNVIPKG-----FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
419-1173 |
3.04e-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: 291.92 E-value: 3.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIA----GISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 572
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVAsshkGKKDTSITGELEKQLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 573 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNV--FGIVPLAkpeeKQKAAQQFSKLQAAMK 650
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFlsNGFVPIP----AAQDDEMFQETLEAMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGG--TLQRSTS 728
Cdd:cd14921 237 IMGFSEEEQLSILKVVSSVLQLGNIVFKKE-RNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGrdVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 729 FRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSF 807
Cdd:cd14921 316 KEQ----------------ADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLgILDIAGFEIFEVN------SF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 808 EELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQashQSLVRSLARTDEARGLLWLLEEEA 887
Cdd:cd14921 374 EQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDF---------GLDL---QPCIELIERPNNPPGVLALLDEEC 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 888 LVPGASEDTLLERLFSyygPQEGDKKGQSPLLHSSKPHHFLLghsHGTNWVEYNVTGWLNyTKQNPATQNAPRLLQDSQK 967
Cdd:cd14921 442 WFPKATDKSFVEKLCT---EQGNHPKFQKPKQLKDKTEFSII---HYAGKVDYNASAWLT-KNMDPLNDNVTSLLNASSD 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 968 KIISNLFLGragsatvlSGSIAGLEGGSQLALRRATSMRKTfTTGMAavkkKSLCIQMKLQVDALIDTIKKSKLHFVHCF 1047
Cdd:cd14921 515 KFVADLWKD--------VDRIVGLDQMAKMTESSLPSASKT-KKGMF----RTVGQLYKEQLGKLMTTLRNTTPNFVRCI 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1048 LPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDV 1127
Cdd:cd14921 582 IPNHEKRSG-----------------------------KLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 42794779 1128 LAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14921 633 LAANAIPKG-----FMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
419-1173 |
3.88e-83 |
|
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: 288.85 E-value: 3.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGIS------GNKVFS---VEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQA 567
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFktkkdqSSIALShgeLEK-QLLQAnpILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 568 GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQA 647
Cdd:cd14932 160 GYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDK--ELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 725
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKE-RNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRdyVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 STSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsarg 804
Cdd:cd14932 317 AQTQEQ----------------AEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlle 884
Cdd:cd14932 376 -SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGI--LALLDE--------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 885 eEALVPGASEDTLLERLfsyygpqeGDKKGQSPLLHSSKP----HHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPR 960
Cdd:cd14932 444 -ECWFPKATDKSFVEKV--------VQEQGNNPKFQKPKKlkddADFCIIHYAGK--VDYKANEWL-MKNMDPLNENVAT 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 961 LLQDSQKKIISNLFlgRAGSATVLSGSIAGLEGGSQLALRRATSMRKTFTTgmaavkkkslciQMKLQVDALIDTIKKSK 1040
Cdd:cd14932 512 LLNQSTDKFVSELW--KDVDRIVGLDKVAGMGESLHGAFKTRKGMFRTVGQ------------LYKEQLMNLMTTLRNTN 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1041 LHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSE 1120
Cdd:cd14932 578 PNFVRCIIPNHEKKAG-----------------------------KLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1121 FRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14932 629 FRQRYEILTPNAIPKG-----FMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
419-1173 |
9.75e-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: 281.48 E-value: 9.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKvfsvEKWQALY-------TLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 571
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESK----KKLGALEdqimqanPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 572 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDGTLRTELHLN------HLAENNVFGIvplakpeEKQKAAQQFSKL 645
Cdd:cd14929 157 SADIDIYLLEKSRVIFQQPGERNYHIFYQILS-GKKELRDLLLVSanpsdfHFCSCGAVAV-------ESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 646 QAAMKVLGISPDEQKACWFILAAIYHLG----AAGATKEAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAIFKHQHKGG 721
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGnmkfKQKPREEQLEADGT-----ENADKAAFLMGINSSELVKGLIHPRIKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 722 T--LQRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 799
Cdd:cd14929 304 NeyVTRSQNIEQVTYAVG----------------ALSKSIYERMFKWLVARINRVLDAKLSRQFFIGILDITGFEILDYN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 800 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE-LAFD---DLEpptddsvAAVDqashqsLVrslartDE 875
Cdd:cd14929 368 ------SLEQLCINFTNEKLQQFFNQHMFVLEQEEYRKEGIDwVSIDfglDLQ-------ACID------LI------EK 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 876 ARGLLWLLEEEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKPH------HFLLGHSHGTnwVEYNVTGWLNYT 949
Cdd:cd14929 423 PMGIFSILEEECMFPKATDLTFKTKLFDNH-------FGKSVHFQKPKPDkkkfeaHFELVHYAGV--VPYNISGWLEKN 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 950 KqNPATQNAPRLLQDSQKKIISNLFlgragSATVLSGSiaGLEGGSQlALRRATSMRKtfttgMAAVKKKSLciqmklqv 1029
Cdd:cd14929 494 K-DLLNETVVAVFQKSSNRLLASLF-----ENYISTDS--AIQFGEK-KRKKGASFQT-----VASLHKENL-------- 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1030 DALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYR 1109
Cdd:cd14929 552 NKLMTNLKSTAPHFVRCINPNVNKIPG-----------------------------VLDPYLVLQQLRCNGVLEGIRICR 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1110 QGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14929 603 EGFPNRLLYADFKQRYCILNPRTFPKSK----FVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
419-1173 |
1.82e-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: 280.83 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASI 575
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQGELERQLLQanpILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 576 QTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQAAMKVLGIS 655
Cdd:cd14919 161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDK--DMFQETMEAMRIMGIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 656 PDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRSTSFRQgp 733
Cdd:cd14919 239 EEEQMGLLRVISGVLQLGNIVFKKE-RNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRdyVQKAQTKEQ-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 734 eesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaSFEELCH 812
Cdd:cd14919 316 --------------ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIgILDIAGFEIFDLN------SFEQLCI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 813 NYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwlleeEALVPGA 892
Cdd:cd14919 376 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGI--LALLDE----------ECWFPKA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 893 SEDTLLERLFSYYGPQegdKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAPRLLQDSQKKIISN 972
Cdd:cd14919 444 TDKSFVEKVVQEQGTH---PKFQKPKQLKDKA-DFCIIHYAGK--VDYKADEWL-MKNMDPLNDNIATLLHQSSDKFVSE 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 973 LFlgRAGSATVLSGSIAGLeggSQLALRRATSMRKTFTTGMAAVKKKslciqmklQVDALIDTIKKSKLHFVHCFLPVAE 1052
Cdd:cd14919 517 LW--KDVDRIIGLDQVAGM---SETALPGAFKTRKGMFRTVGQLYKE--------QLAKLMATLRNTNPNFVRCIIPNHE 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1053 GWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHL 1132
Cdd:cd14919 584 KKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNS 634
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 42794779 1133 TKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14919 635 IPKG-----FMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
419-1173 |
1.31e-77 |
|
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: 272.71 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYT------------LLEAFGNSPTIINGNATRFSQILSLDFDQ 566
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVA--SSHKTKKDQNSLALSHgelekqllqanpILEAFGNAKTVKNDNSSRFGKFIRINFDV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 567 AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKaaQQFSKLQ 646
Cdd:cd15896 159 NGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDK--DLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 647 AAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQ 724
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKE-RHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRdyVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 725 RSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsar 803
Cdd:cd15896 316 KAQTQEQ----------------AEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIgILDIAGFEIFELN---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVrsLARTDEargllwll 883
Cdd:cd15896 376 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGI--LALLDE-------- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 884 eeEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKP----HHFLLGHSHGTnwVEYNVTGWLnYTKQNPATQNAP 959
Cdd:cd15896 444 --ECWFPKATDKSFVEKVLQ--------EQGTHPKFFKPKKlkdeADFCIIHYAGK--VDYKADEWL-MKNMDPLNDNVA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 960 RLLQDSQKKIISNLFLGragsatvlSGSIAGLEGGSQLA-LRRATSMRKTFTTGMAAVKKKslciqmklQVDALIDTIKK 1038
Cdd:cd15896 511 TLLNQSTDKFVSELWKD--------VDRIVGLDKVSGMSeMPGAFKTRKGMFRTVGQLYKE--------QLSKLMATLRN 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1039 SKLHFVHCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1118
Cdd:cd15896 575 TNPNFVRCIIPNHEKKAG-----------------------------KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 625
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1119 SEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd15896 626 QEFRQRYEILTPNAIPKG-----FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
419-1173 |
3.17e-75 |
|
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: 265.66 E-value: 3.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNkvfSVEKWQALYTL---------------LEAFGNSPTIINGNATRFSQILSLD 563
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDG---PGKKAQFLATKtggtledqiieanpaMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 564 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLN------HLAENNVFGIVPLAKPEEkqk 637
Cdd:cd14927 158 FGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmnpydyHFCSQGVTTVDNMDDGEE--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 638 aaqqFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATK----EAAEAGRKqfarhEWAQKAAYLLGCSLEELSSAI 713
Cdd:cd14927 235 ----LMATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQkqreEQAEADGT-----ESADKAAYLMGVSSADLLKGL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 714 FKHQHKGGtlQRSTSFRQGPEESGLGDGtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGF 793
Cdd:cd14927 306 LHPRVKVG--NEYVTKGQSVEQVVYAVG------------ALAKATYDRMFKWLVSRINQTLDTKLPRQFFIGVLDIAGF 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 794 QNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRT 873
Cdd:cd14927 372 EIFEFN------SFEQLCINFTNEKLQQFFNHHMFILEQEEYKREGIEWVFIDFGL---DLQACID------------LI 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 DEARGLLWLLEEEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKPH-------HFLLGHSHGTnwVEYNVTGWL 946
Cdd:cd14927 431 EKPLGILSILEEECMFPKASDASFKAKLYDNH-------LGKSPNFQKPRPDkkrkyeaHFEVVHYAGV--VPYNIVGWL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 947 NYTKqNPATQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgSIAGLEGGSQLALRRATSmrktFTTgMAAVKKKSLciqmk 1026
Cdd:cd14927 502 DKNK-DPLNETVVAIFQKSQNKLLATLYENYVGSD-----STEDPKSGVKEKRKKAAS----FQT-VSQLHKENL----- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1027 lqvDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMR 1106
Cdd:cd14927 566 ---NKLMTNLRATQPHFVRCIIP--------------------NETKTPG---------VMDPFLVLHQLRCNGVLEGIR 613
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1107 MYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14927 614 ICRKGFPNRILYADFKQRYRILNPSAIPDDK----FVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
419-1173 |
2.62e-73 |
|
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: 259.77 E-value: 2.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIaGISGNKVFSVEKW-----QALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 571
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV-GASKKTDEAAKSKgsledQVVQTnpVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 572 SASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNhlaeNNVFGIVPLAKPE---EKQKAAQQFSKLQAA 648
Cdd:cd14909 160 GADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLS----DNIYDYYIVSQGKvtvPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 649 MKVLGISPDEQKACWFILAAIYHLGaagaTKEAAEAGRKQFARH---EWAQKAAYLLGCSLEELSSAIFKHQHKGGTlqr 725
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMG----GMKFKQRGREEQAEQdgeEEGGRVSKLFGCDTAELYKNLLKPRIKVGN--- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 sTSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGGsarga 805
Cdd:cd14909 309 -EFVTQGRNVQQVTNSIG----------ALCKGVFDRLFKWLVKKCNETLDTQQKRQHFIGVLDIAGFEIFEYNG----- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 806 sFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 885
Cdd:cd14909 373 -FEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIDWAFIDFGM---DLLACID------------LIEKPMGILSILEE 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 886 EALVPGASEDTLLERLFSyygpqegDKKGQSPLLHSSKP-------HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNA 958
Cdd:cd14909 437 ESMFPKATDQTFSEKLTN-------THLGKSAPFQKPKPpkpgqqaAHFAIAHYAGC--VSYNITGWLEKNK-DPLNDTV 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 959 PRLLQDSQKKIISNLFLGRAGSatvlSGSIAGLEGGsqlalrratsmRKTFTTGMAAVKKkslciQMKLQVDALIDTIKK 1038
Cdd:cd14909 507 VDQFKKSQNKLLIEIFADHAGQ----SGGGEQAKGG-----------RGKKGGGFATVSS-----AYKEQLNSLMTTLRS 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1039 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1118
Cdd:cd14909 567 TQPHFVRCIIP--------------------NEMKQP-------GV--VDAHLVMHQLTCNGVLEGIRICRKGFPNRMMY 617
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1119 SEFRRRFDVLAPHLTKKHgrnyivVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14909 618 PDFKMRYKILNPAGIQGE------EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
419-1173 |
1.98e-72 |
|
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: 257.33 E-value: 1.98e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIA---------GISGNkvFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 569
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVAsspkgrkepGVPGE--LERQLLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 570 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQkaaQQFSKLQAAM 649
Cdd:cd14930 158 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER---ELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 650 KVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQRST 727
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRE-RNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRdyVQKAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 SFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsargaS 806
Cdd:cd14930 314 TKEQ----------------ADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFEIFQLN------S 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 807 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQashQSLVRSLARTDEARGLLWLLEEE 886
Cdd:cd14930 372 FEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDF---------GLDL---QPCIDLIERPANPPGLLALLDEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 887 ALVPGASEDTLLERLFSYYGPQegdKKGQSPLLHSSKPHHFLLghsHGTNWVEYNVTGWLnYTKQNPATQNAPRLLQDSQ 966
Cdd:cd14930 440 CWFPKATDKSFVEKVAQEQGGH---PKFQRPRHLRDQADFSVL---HYAGKVDYKANEWL-MKNMDPLNDNVAALLHQST 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 967 KKIISNLFLGRAGsatvlsgsIAGLEGGSQL--ALRRATSMRKTFTTgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1044
Cdd:cd14930 513 DRLTAEIWKDVEG--------IVGLEQVSSLgdGPPGGRPRRGMFRT-VGQLYKESL--------SRLMATLSNTNPSFV 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1045 HCFLPVAEGWAGeprsassrrvsssseldlpsgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1124
Cdd:cd14930 576 RCIVPNHEKRAG-----------------------------KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 626
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42794779 1125 FDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14930 627 YEILTPNAIPKG-----FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
420-1173 |
1.54e-69 |
|
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: 248.81 E-value: 1.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVA 571
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKKKDSKMKGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 572 SASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA---A 648
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILS----NKKPELIELLLITTNPYDYPFISQGEILVASIDDAEELLAtdsA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 649 MKVLGISPDEQKACWFILAAIYHLGaagaTKEAAEAGRKQFAR---HEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--L 723
Cdd:cd14913 238 IDILGFTPEEKSGLYKLTGAVMHYG----NMKFKQKQREEQAEpdgTEVADKTAYLMGLNSSDLLKALCFPRVKVGNeyV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 724 QRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsar 803
Cdd:cd14913 314 TKGQTVDQ----------------VHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHFIGVLDIAGFEIFEYN---- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLL 883
Cdd:cd14913 374 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGIFSIL 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 884 EEEALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLL 962
Cdd:cd14913 437 EEECMFPKATDTSFKNKLYDQHLGKSNNF--QKPKVVKGRAEaHFSLIHYAGT--VDYSVSGWLEKNK-DPLNETVVGLY 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 963 QDSQKKIISNLFLGRAGS-ATVLSGSIAGLEGGSqlalrratsmrktFTTgMAAVKKKSLciqmklqvDALIDTIKKSKL 1041
Cdd:cd14913 512 QKSSNRLLAHLYATFATAdADSGKKKVAKKKGSS-------------FQT-VSALFRENL--------NKLMSNLRTTHP 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1042 HFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEF 1121
Cdd:cd14913 570 HFVRCIIP--------------------NETKTPGA---------MEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1122 RRRFDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14913 621 KQRYRVLNASAIPE-GQ---FIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
420-1130 |
2.88e-69 |
|
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: 247.23 E-value: 2.88e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGISGnkvfSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 577
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSS----GIEN-EILQTnpILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 578 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGIVPLakpeekqKAAQQFSKLQAAMKV 651
Cdd:cd01383 155 YLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLksaseyKYLNQSNCLTIDGV-------DDAKKFHELKEALDT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 652 LGISPDEQKACWFILAAIYHLG---------AAGATKEAAEAgrkqfarhewAQKAAYLLGCSLEELSSAIFKHQHK--G 720
Cdd:cd01383 228 VGISKEDQEHIFQMLAAVLWLGnisfqvidnENHVEVVADEA----------VSTAASLLGCNANDLMLALSTRKIQagG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 721 GTLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQH-SLCSMMIVDTPGFQnpeqg 799
Cdd:cd01383 298 DKIVKKLTLQQ----------------AIDARDALAKAIYASLFDWLVEQINKSLEVGKRrTGRSISILDIYGFE----- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 800 gSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEpptdDSVAAVDQASHQSL-VRSLarTDEarg 878
Cdd:cd01383 357 -SFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYELDGIDWTKVDFE----DNQECLDLIEKKPLgLISL--LDE--- 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 879 llwlleeEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGWLNytkqnpatQNA 958
Cdd:cd01383 427 -------ESNFPKATDLTFANKLKQHLKSNSCFKGERGGA--------FTIRHYAGE--VTYDTSGFLE--------KNR 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 959 PRLLQDsqkkiISNLFLGRAGSATVLSGSIAGLEGGSQLALRRATSMRKTfttgmaavkKKSLCIQMKLQVDALIDTIKK 1038
Cdd:cd01383 482 DLLHSD-----LIQLLSSCSCQLPQLFASKMLDASRKALPLTKASGSDSQ---------KQSVATKFKGQLFKLMQRLEN 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1039 SKLHFVHCFLPVAEGWAGEprsassrrvsssSELDLpsgdhceagLLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVF 1118
Cdd:cd01383 548 TTPHFIRCIKPNNKQLPGV------------FDQDL---------VLQ--------QLRCCGVLEVVRISRSGYPTRMTH 598
|
730
....*....|..
gi 42794779 1119 SEFRRRFDVLAP 1130
Cdd:cd01383 599 QEFARRYGFLLP 610
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
420-1173 |
1.80e-68 |
|
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: 245.40 E-value: 1.80e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGIS---------GNKVFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 570
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGdrskkdqtpGKGTLEDQIIQA-NPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 571 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA--- 647
Cdd:cd14917 161 ASADIETYLLEKSRVIFQLKAERDYHIFYQILS----NKKPELLDMLLITNNPYDYAFISQGETTVASIDDAEELMAtdn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEwAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 725
Cdd:cd14917 237 AFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEE-ADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 STSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 805
Cdd:cd14917 316 GQNVQQVIYATG----------------ALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 806 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 885
Cdd:cd14917 374 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGM---DLQACID------------LIEKPMGIMSILEE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 886 EALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 964
Cdd:cd14917 439 ECMFPKATDMTFKAKLFDNHLGKSNNF--QKPRNIKGKPEaHFSLIHYAGT--VDYNIIGWLQKNK-DPLNETVVGLYQK 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 965 SQKKIISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1044
Cdd:cd14917 514 SSLKLLSNLFANYAGADAPIEKGKGKAKKGS------------SFQT-VSALHRENL--------NKLMTNLRSTHPHFV 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1045 HCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1124
Cdd:cd14917 573 RCIIP--------------------NETKSPG---------VMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 623
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42794779 1125 FDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14917 624 YRILNPAAIPE-GQ---FIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
419-1131 |
5.31e-68 |
|
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: 243.77 E-value: 5.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14883 1 EGINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIagisGNKVFSVEKwQAL--YTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd14883 81 ESGAGKTETTKLILQYLCAV----TNNHSWVEQ-QILeaNTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGT--LRTELHL---NHLAENNVFGIVPLAKPEEKQKaaqqFSKLQAAMKV 651
Cdd:cd14883 156 DYLLEQSRITFQAPGERNYHVFYQLLAGAKHSkeLKEKLKLgepEDYHYLNQSGCIRIDNINDKKD----FDHLRLAMNV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 652 LGISPDEQKACWFILAAIYHLGaaGATKEAAEAGRKQFAR--HEWAQKAAYLLGCSLEELSSA-IFKHQHKGGTLqrsTS 728
Cdd:cd14883 232 LGIPEEMQEGIFSVLSAILHLG--NLTFEDIDGETGALTVedKEILKIVAKLLGVDPDKLKKAlTIRQINVRGNV---TE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 729 FRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFE 808
Cdd:cd14883 307 IPLKVQE------------ARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNSRFIGVLDIFGFENFKVN------SFE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 809 ELCHNYTQDRLQRLFHERTFVQELERYKEENIELA---FDD-------LEPPTDDSVAAVDQASHqslvrslartdearg 878
Cdd:cd14883 369 QLCINYTNEKLHKFFNHYVFKLEQEEYEKEGINWShivFTDnqecldlIEKPPLGILKLLDEECR--------------- 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 879 llwlleeealVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSkphhFLLGHSHGTnwVEYNVTGWLNytkQNPATQ-- 956
Cdd:cd14883 434 ----------FPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTE----FGVKHYAGE--VTYTVQGFLD---KNKDTQqd 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 957 NAPRLLQDSQKKIISNLFLGRAgsatvlsgsiagleggsQLALRRATSMRKTFTTGMAAVKKK-SLCIQMKLQVDALIDT 1035
Cdd:cd14883 495 DLFDLMSRSKNKFVKELFTYPD-----------------LLALTGLSISLGGDTTSRGTSKGKpTVGDTFKHQLQSLVDV 557
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1036 IKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDH 1115
Cdd:cd14883 558 LSATQPWYVRCIKP--------------------NSLKEPN---------VFDDELVLAQLRYAGMLEIIRIRKEGFPIH 608
|
730
....*....|....*.
gi 42794779 1116 MVFSEFRRRFDVLAPH 1131
Cdd:cd14883 609 LTFKEFVDRYLCLDPR 624
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
419-1173 |
1.36e-66 |
|
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: 239.54 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGIS-----GNKVFSVEKWQAlYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 573
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGkqssdGKGSLEDQIIQA-NPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 574 SIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaennvfgiVPlaKPEEKQKAAQQFSKLQ------- 646
Cdd:cd14934 160 DIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLL-----------VP--NPKEYHWVSQGVTVVDnmddgee 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 647 -----AAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGG 721
Cdd:cd14934 227 lqitdVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREE-QAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 722 T--LQRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQG 799
Cdd:cd14934 306 NefVQKGQNMEQCNNSIG----------------ALGKAVYDKMFKWLVVRINKTLDTKMQRQFFIGVLDIAGFEIFEFN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 800 gsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDQashqslvrslarTDEARGL 879
Cdd:cd14934 370 ------SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKREGIEWVFIDFGL---DLQACIDL------------LEKPMGI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 880 LWLLEEEALVPGASEDTLLERLF--------SYYGPQEGDKKGQSPllhsskphHFLLGHSHGTnwVEYNVTGWLNYTKq 951
Cdd:cd14934 429 FSILEEQCVFPKATDATFKAALYdnhlgkssNFLKPKGGKGKGPEA--------HFELVHYAGT--VGYNITGWLEKNK- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 952 NPATQNAPRLLQDSQkKIISNLFLGRAGSAtvlsgsiagleGGSQLALRRATSMrktfttgmaavkkkSLCIQMKLQVDA 1031
Cdd:cd14934 498 DPLNETVVGLFQKSS-LGLLALLFKEEEAP-----------AGSKKQKRGSSFM--------------TVSNFYREQLNK 551
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1032 LIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQG 1111
Cdd:cd14934 552 LMTTLHSTAPHFVRCIVP---------------------------NEFKQSGV--VDAHLIMHQLACNGVLEGIRICRKG 602
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1112 YPDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14934 603 FPNRLQYPEFKQRYQVLNPNVIPQG-----FVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
421-1135 |
1.40e-66 |
|
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: 239.11 E-value: 1.40e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 421 VLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd01384 3 VLHNLKVRYELDEIYTYTGNILIAVNPfKRLPHLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 577
Cdd:cd01384 83 SGAGKTETTKMLMQYLAYMGGRAVTEGRSVEQ-QVLESnpLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 578 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGIVPLAKPEEkqkaaqqFSKLQAAMKV 651
Cdd:cd01384 162 YLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLkdpkqfHYLNQSKCFELDGVDDAEE-------YRATRRAMDV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 652 LGISPDEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKhqhkggtlqRSTSF 729
Cdd:cd01384 235 VGISEEEQDAIFRVVAAILHLGniEFSKGEEDDSSVPKDEKSEFHLKAAAELLMCDEKALEDALCK---------RVIVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 730 RQGPEESGLGdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQnpeqggSARGASFEE 809
Cdd:cd01384 306 PDGIITKPLD-----PDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNSKRLIGVLDIYGFE------SFKTNSFEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 810 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddlepptddsVAAVDQASHQSLVRS-----LARTDEArgllwlle 884
Cdd:cd01384 375 FCINLANEKLQQHFNQHVFKMEQEEYTKEEIDWSY----------IEFVDNQDVLDLIEKkpggiIALLDEA-------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 885 eeALVPGASEDTLLERLFSYYgpqEGDKKGQSPLLhssKPHHFLLGHSHGTnwVEYNVTGWLNYTKQN--PATQNaprLL 962
Cdd:cd01384 437 --CMFPRSTHETFAQKLYQTL---KDHKRFSKPKL---SRTDFTIDHYAGD--VTYQTDLFLDKNKDYvvAEHQA---LL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 963 QDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKtFTtgmaavkkkSLCIQMKLQVDALIDTIKKSKLH 1042
Cdd:cd01384 504 NASKCPFVAGLF--------------------PPLPREGTSSSSK-FS---------SIGSRFKQQLQELMETLNTTEPH 553
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1043 FVHCFLPVAEgwageprsassrrvsssseldLPSGDHCEAGLLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVFSEFR 1122
Cdd:cd01384 554 YIRCIKPNNL---------------------LKPGIFENANVLQ--------QLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
730
....*....|...
gi 42794779 1123 RRFDVLAPHLTKK 1135
Cdd:cd01384 605 DRFGLLAPEVLKG 617
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
420-1173 |
6.73e-64 |
|
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: 231.87 E-value: 6.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGI---------SGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 570
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIgdrskkenpNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 571 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA--- 647
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILS----NKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLAtds 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQR 725
Cdd:cd14916 238 AFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREE-QAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNeyVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 STSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 805
Cdd:cd14916 317 GQSVQQ----------------VYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFN------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 806 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPptdDSVAAVDqashqslvrslaRTDEARGLLWLLEE 885
Cdd:cd14916 375 SFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGM---DLQACID------------LIEKPMGIMSILEE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 886 EALVPGASEDTLLERLF-SYYGPQEGDKKGQSplLHSSKPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 964
Cdd:cd14916 440 ECMFPKASDMTFKAKLYdNHLGKSNNFQKPRN--VKGKQEAHFSLVHYAGT--VDYNILGWLEKNK-DPLNETVVGLYQK 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 965 SQKKIISNLFLGRAGSATvlsgsiaGLEGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1044
Cdd:cd14916 515 SSLKLMATLFSTYASADT-------GDSGKGKGGKKKGSSFQT-----VSALHRENL--------NKLMTNLKTTHPHFV 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1045 HCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1124
Cdd:cd14916 575 RCIIP---------------------------NERKAPGV--MDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 625
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42794779 1125 FDVLAPhLTKKHGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14916 626 YRILNP-AAIPEGQ---FIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
420-1128 |
1.15e-63 |
|
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: 231.11 E-value: 1.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAgISGNKVFSVEKWQALYT----------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 569
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIA-VTGDKKKEQQPGKMQGTledqiiqanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 570 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA-- 647
Cdd:cd14923 161 LASADIETYLLEKSRVTFQLSSERSYHIFYQIMS----NKKPELIDLLLISTNPFDFPFVSQGEVTVASIDDSEELLAtd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 -AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrS 726
Cdd:cd14923 237 nAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVG----N 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 727 TSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaS 806
Cdd:cd14923 312 EYVTKGQNVQQVTNSVG----------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------S 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 807 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEEE 886
Cdd:cd14923 376 LEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSILEEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 887 ALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQ 966
Cdd:cd14923 441 CMFPKATDTSFKNKLYDQHLGKSNNFQKPKPAKGKAEA-HFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQKSS 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 967 KKIISNLFLGRAGSAtvlsgsiAGLEGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFVHC 1046
Cdd:cd14923 517 LKLLSFLFSNYAGAE-------AGDSGGSKKGGKKKGSSFQT----VSAVFRENL--------NKLMTNLRSTHPHFVRC 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1047 FLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFD 1126
Cdd:cd14923 578 LIP--------------------NETKTPG---------VMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYR 628
|
..
gi 42794779 1127 VL 1128
Cdd:cd14923 629 IL 630
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
420-1128 |
3.13e-63 |
|
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: 230.00 E-value: 3.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAgISGNKV---FSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAG 568
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIA-VTGEKKkeeAASGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 569 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQA- 647
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMS----NKKPELIEMLLITTNPYDFAFVSQGEITVPSIDDQEELMAt 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 --AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--L 723
Cdd:cd14915 237 dsAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNeyV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 724 QRSTSFRQGPEESGlgdgtgpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsar 803
Cdd:cd14915 316 TKGQTVQQVYNSVG----------------ALAKAIYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLL 883
Cdd:cd14915 376 --SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSIL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 884 EEEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQ 963
Cdd:cd14915 439 EEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEA-HFSLVHYAGT--VDYNIAGWLDKNK-DPLNETVVGLYQ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 964 DSQKKIISNLFLGraGSATVLSGSiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHF 1043
Cdd:cd14915 515 KSGMKTLAFLFSG--GQTAEAEGG-----GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRSTHPHF 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1044 VHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1123
Cdd:cd14915 575 VRCLIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQ 625
|
....*
gi 42794779 1124 RFDVL 1128
Cdd:cd14915 626 RYKVL 630
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
420-1173 |
8.02e-63 |
|
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: 228.85 E-value: 8.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT----------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 569
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQGTledqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 570 VASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELhlnhLAENNVFGIVPLAKPEEKQKAAQQFSKLQA-- 647
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 -AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGT--LQ 724
Cdd:cd14910 238 sAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNeyVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 725 RSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 804
Cdd:cd14910 317 KGQTVQQ----------------VYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN----- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLE 884
Cdd:cd14910 376 -SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDF---------GMDLAACIELI------EKPMGIFSILE 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 885 EEALVPGASEDTLLERLFSYYgpqegdkKGQSPLLHSSKP------HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNA 958
Cdd:cd14910 440 EECMFPKATDTSFKNKLYEQH-------LGKSNNFQKPKPakgkveAHFSLIHYAGT--VDYNIAGWLDKNK-DPLNETV 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 959 PRLLQDSQKKIISNLFLGrAGSATVLSGsiagleGGSQLALRRATSMRKtfttgMAAVKKKSLciqmklqvDALIDTIKK 1038
Cdd:cd14910 510 VGLYQKSSMKTLALLFSG-AAAAEAEEG------GGKKGGKKKGSSFQT-----VSALFRENL--------NKLMTNLRS 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1039 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1118
Cdd:cd14910 570 THPHFVRCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILY 620
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1119 SEFRRRFDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14910 621 ADFKQRYKVLNASAIPE-GQ---FIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
419-1049 |
1.81e-62 |
|
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: 227.04 E-value: 1.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01378 1 EAINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYlatIAGISGNKVFSVE--KWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASAS 574
Cdd:cd01378 81 ESGAGKTEASKRIMQY---IAAVSGGSESEVErvKDMLLASnpLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 575 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVF---GIvplakpeekqKAAQQFSKL 645
Cdd:cd01378 158 ITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLqrpeqyYYYSKSGCFdvdGI----------DDAADFKEV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 646 QAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaaEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQR 725
Cdd:cd01378 228 LNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAED--EEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 ST-SFRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQNPEQGgsar 803
Cdd:cd01378 306 SVyEVPLNVEQ------------AAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIgVLDIYGFEIFEKN---- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELA----FD-----DL-EPPTDDSVAAVDQAShqslvrslart 873
Cdd:cd01378 370 --SFEQFCINYVNEKLQQIFIELTLKAEQEEYVREGIEWTpikyFNnkiicDLiEEKPPGIFAILDDAC----------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 deargllwlleeeALVPGASEDTLLERLfsyygpqegdkkgqspLLHSSKPHHFLLGHSHGTNW------------VEYN 941
Cdd:cd01378 437 -------------LTAGDATDQTFLQKL----------------NQLFSNHPHFECPSGHFELRrgefrikhyagdVTYN 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 942 VTGwlnYTKQNPAT--QNAPRLLQDSQKKIISNLFlgragsatvlsgsiagLEGGSQLALRRATsmrktfTTGMaavkkk 1019
Cdd:cd01378 488 VEG---FLDKNKDLlfKDLKELMQSSSNPFLRSLF----------------PEGVDLDSKKRPP------TAGT------ 536
|
650 660 670
....*....|....*....|....*....|
gi 42794779 1020 slciQMKLQVDALIDTIKKSKLHFVHCFLP 1049
Cdd:cd01378 537 ----KFKNSANALVETLMKKQPSYIRCIKP 562
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
421-1173 |
3.52e-62 |
|
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: 226.92 E-value: 3.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 421 VLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSS 500
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 501 GSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT--------LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVAS 572
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQGTLEdqiisanpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 573 ASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELhlnhLAENNVFGIVPLAKPEEKQKAAQQFSKLQA---AM 649
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEML----LITTNPYDYAFVSQGEITVPSIDDQEELMAtdsAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 650 KVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrSTSF 729
Cdd:cd14918 239 DILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVG----NEYV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 730 RQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEE 809
Cdd:cd14918 314 TKGQTVQQVYNAVG----------ALAKAVYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFN------SLEQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 810 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEEEALV 889
Cdd:cd14918 378 LCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPLGIFSILEEECMF 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 890 PGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKK 968
Cdd:cd14918 443 PKATDTSFKNKLYDQHLGKSANF--QKPKVVKGKAEaHFSLIHYAGT--VDYNITGWLDKNK-DPLNDTVVGLYQKSAMK 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 969 IISNLFLGRAGSATVLSGSIAGLEGGSqlalrratsmrkTFTTGMAAVKKkslciqmklQVDALIDTIKKSKLHFVHCFL 1048
Cdd:cd14918 518 TLASLFSTYASAEADSGAKKGAKKKGS------------SFQTVSALFRE---------NLNKLMTNLRSTHPHFVRCII 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1049 PvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1128
Cdd:cd14918 577 P--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVL 627
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 42794779 1129 APHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14918 628 NASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
420-1173 |
7.56e-62 |
|
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: 225.77 E-value: 7.56e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 569
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAvtgekkkeEITSGKMQGTLEDQIISAnpLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 570 VASASIQTMLLEKLRVARRPASEATFNVFYYLLAcgdgTLRTELHLNHLAENNVFGiVPLAKPEEKQKAA----QQFSKL 645
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITS----NKKPELIEMLLITTNPYD-YPFVSQGEISVASiddqEELMAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 646 QAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGtlqr 725
Cdd:cd14912 237 DSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREE-QAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVG---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 726 STSFRQGPEESGLGDGTGpklsalecleGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarga 805
Cdd:cd14912 312 NEYVTKGQTVEQVTNAVG----------ALAKAVYEKMFLWMVARINQQLDTKQPRQYFIGVLDIAGFEIFDFN------ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 806 SFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLepptddsvaAVDQASHQSLVrslartDEARGLLWLLEE 885
Cdd:cd14912 376 SLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDF---------GMDLAACIELI------EKPMGIFSILEE 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 886 EALVPGASEDTLLERLFSYYGPQEGDKkgQSPLLHSSKPH-HFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQD 964
Cdd:cd14912 441 ECMFPKATDTSFKNKLYEQHLGKSANF--QKPKVVKGKAEaHFSLIHYAGV--VDYNITGWLDKNK-DPLNETVVGLYQK 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 965 SQKKIISNLFLGragsATVLSGSIAGleGGSQLALRRATSMRKTfttgMAAVKKKSLciqmklqvDALIDTIKKSKLHFV 1044
Cdd:cd14912 516 SAMKTLAYLFSG----AQTAEGASAG--GGAKKGGKKKGSSFQT----VSALFRENL--------NKLMTNLRSTHPHFV 577
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1045 HCFLPvaegwageprsassrrvsssSELDLPSGdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRR 1124
Cdd:cd14912 578 RCIIP--------------------NETKTPGA---------MEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42794779 1125 FDVLAPHLTKKhGRnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14912 629 YKVLNASAIPE-GQ---FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
419-846 |
8.26e-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: 225.42 E-value: 8.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMS----RQDQS 493
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPyKSIPDLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSgvldPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 494 IILLGSSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYT------------------LLEAFGNSPTIINGNATR 555
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARIT--SGFAQGASGEGEAASEaieqtlgsledrvlssnpLLESFGNAKTLRNDNSSR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 556 FSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaENNVFGIVPLAK--PE 633
Cdd:cd14890 159 FGKFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKL----QTPVEYFYLRGEcsSI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 634 EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAI 713
Cdd:cd14890 235 PSCDDAKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLEDATTLQSLKLAAELLGVNEDALEKAL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 714 FKHQH--KGGTLQRstsfrqgPEESGLgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTP 791
Cdd:cd14890 315 LTRQLfvGGKTIVQ-------PQNVEQ---------ARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWGFIGVLDIY 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 792 GFQNPEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDD 846
Cdd:cd14890 379 GFEKFEWNT------FEQLCINYANEKLQRHFNQHMFEVEQVEYSNEGIDwqyITFND 430
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
419-1173 |
8.00e-60 |
|
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: 219.43 E-value: 8.00e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGisgnKVFSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG----QHSWIEQ-QILEAnpILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNH------LAENNVFGIvplakpeEKQKAAQQFSKLQAAMK 650
Cdd:cd01381 156 QYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDasdyyyLTQGNCLTC-------EGRDDAAEFADIRSAMK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEqkaCWFI---LAAIYHLGAAG------ATKEAAEagrkqFARHEWAQKAAYLLGCSLEELSSAIFKHQ--HK 719
Cdd:cd01381 229 VLMFTDEE---IWDIfklLAAILHLGNIKfeatvvDNLDASE-----VRDPPNLERAAKLLEVPKQDLVDALTTRTifTR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 720 GGTLQRSTSFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAL---KSSQHSLCSMMIVDTPGFQNP 796
Cdd:cd01381 301 GETVVSPLSAEQ----------------ALDVRDAFVKGIYGRLFIWIVNKINSAIykpRGTDSSRTSIGVLDIFGFENF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 797 EQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsVAAVDQASHQSLVrslart 873
Cdd:cd01381 365 EVN------SFEQLCINFANENLQQFFVRHIFKLEQEEYDKEGINwqhIEFVDNQDVLD--LIALKPMNIMSLI------ 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 DEargllwlleeEALVPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHHFLlghshGTnwVEYNVTGWLNytKQNP 953
Cdd:cd01381 431 DE----------ESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDLNTSFGINHFA-----GV--VFYDTRGFLE--KNRD 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 954 A-TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsQLALRRATSMRKtfttgmaavKKKSLCIQMKLQVDAL 1032
Cdd:cd01381 492 TfSADLLQLVQSSKNKFLKQLF---------------------NEDISMGSETRK---------KSPTLSSQFRKSLDQL 541
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1033 IDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPsgdhceaglLQLDVPLLRTQLRGSRLLDAMRMYRQGY 1112
Cdd:cd01381 542 MKTLSACQPFFVRCIKP--------------------NEYKKP---------MLFDRELCVRQLRYSGMMETIRIRKAGY 592
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1113 PDHMVFSEFRRRFDVLAPHLTKKHgrnyiVVDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd01381 593 PIRHTFEEFVERYRVLVPGIPPAH-----KTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
420-852 |
1.94e-59 |
|
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: 217.91 E-value: 1.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLaTIAGISGNKVFSvEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTML 579
Cdd:cd01379 82 SGAGKTESANLLVQQL-TVLGKANNRTLE-EKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 580 LEKLRVARRPASEATFNVFYYLLA-------CGDGTLRTELHLNHLAENNvfgiVPLAKPEEKQKAAQQFSKLQAAMKVL 652
Cdd:cd01379 160 LEKSRVVHQAIGERNFHIFYYIYAglaedkkLAKYKLPENKPPRYLQNDG----LTVQDIVNNSGNREKFEEIEQCFKVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 653 GISPDEQKACWFILAAIYHLGA---AGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ--HKGGTLQRST 727
Cdd:cd01379 236 GFTKEEVDSVYSILAAILHIGDiefTEVESNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSvvTRGETIIRNN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 SFRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNPEQGgsarg 804
Cdd:cd01379 316 TVEE----------------ATDARDAMAKALYGRLFSWIVNRINSLLKPDRSAsdePLSIGILDIFGFENFQKN----- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIEL---AFDDLEPPTD 852
Cdd:cd01379 375 -SFEQLCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVdliEYEDNRPLLD 424
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
419-1173 |
7.88e-59 |
|
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: 216.57 E-value: 7.88e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILL 497
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPyQWLPELYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 498 GSSGSGKTTSCQHLVQYLATIAGisGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 577
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAKCRT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 578 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAennVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPD 657
Cdd:cd14903 159 YLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANEC---AYTGANKTIKIEGMSDRKHFARTKEALSLIGVSEE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 658 EQKACWFILAAIYHLGAAGATKEAAEAGRKQFAR-HEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRSTSFRqgpees 736
Cdd:cd14903 236 KQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPgDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLK------ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 737 glgdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQ 816
Cdd:cd14903 310 --------KDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKMANHIGVLDIFGFEHFKHN------SFEQFCINYAN 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 817 DRLQRLFHERTFVQELERYKEENIELAFddlepptddsvaaVDQASHQSLvrsLARTDEARGLLWLLEEEALVPGASEDT 896
Cdd:cd14903 376 EKLQQKFTQDVFKTVQIEYEEEGIRWAH-------------IDFADNQDV---LAVIEDRLGIISLLNDEVMRPKGNEES 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 897 LLERLFSYYgpqeGDKKGQSPLLHSSKPhHFLLGHSHGTnwVEYNVTGWLNYTKQNpatqnaprLLQD-------SQKKI 969
Cdd:cd14903 440 FVSKLSSIH----KDEQDVIEFPRTSRT-QFTIKHYAGP--VTYESLGFLEKHKDA--------LLPDlsdlmrgSSKPF 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 970 ISNLFLGRAGSATVLSGSIAGLEGgsqlalRRATSMRKTFTTGMaavkkkslciQMKLQVDALIDTIKKSKLHFVHCFLP 1049
Cdd:cd14903 505 LRMLFKEKVESPAAASTSLARGAR------RRRGGALTTTTVGT----------QFKDSLNELMTTIRSTNVHYVRCIKP 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1050 VAEGWAGEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1129
Cdd:cd14903 569 NSIKSPTE-----------------------------LDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 42794779 1130 PhltkKHGRNYIVVDER-RAVEELLECLDLEKSSccMGLSRVFFR 1173
Cdd:cd14903 620 P----EGRNTDVPVAERcEALMKKLKLESPEQYQ--MGLTRIYFQ 658
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
420-846 |
1.17e-58 |
|
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: 215.48 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYG-ASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVfSVEKwQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-QVEE-KVLASnpIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISP 656
Cdd:cd01380 160 TYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGS-AEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 657 DEQKACWFILAAIYHLGAAgATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHK--GGTLQRSTSFRQgpe 734
Cdd:cd01380 239 EEQMEIFRILAAILHLGNV-EIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVtrSEVIVKPLTLQQ--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 735 esglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQ-HSLCSMM-IVDTPGFQNPEQGgsargaSFEELCH 812
Cdd:cd01380 315 -------------AIVARDALAKHIYAQLFDWIVDRINKALASPVkEKQHSFIgVLDIYGFETFEVN------SFEQFCI 375
|
410 420 430
....*....|....*....|....*....|....
gi 42794779 813 NYTQDRLQRLFHERTFVQELERYKEENIELAFDD 846
Cdd:cd01380 376 NYANEKLQQQFNQHVFKLEQEEYVKEEIEWSFID 409
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
420-1171 |
6.77e-58 |
|
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: 213.88 E-value: 6.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSE--KVMHMFKGCRRED----MAPHIYAVAQTAYRAMLMSR---- 489
Cdd:cd14901 2 SILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDetKEAYYEHGERRAAgerkLPPHVYAVADKAFRAMLFASrgqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 490 QDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKW----QALYT--LLEAFGNSPTIINGNATRFSQILSLD 563
Cdd:cd14901 82 CDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATEREnvrdRVLESnpILEAFGNARTNRNNNSSRFGKFIRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 564 FDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFS 643
Cdd:cd14901 162 FASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDRRDGVDDSVQYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 644 KLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTL 723
Cdd:cd14901 242 KTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAGGE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 724 QRSTSFrqgpeesglgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRALK--SSQHSLCSMMIVDTPGFQNPEQGgs 801
Cdd:cd14901 322 YITMPL--------------SVEQALLTRDVVAKTLYAQLFDWLVDRINESIAysESTGASRFIGIVDIFGFEIFATN-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 802 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddLEPPTDDSVAAVDQASHQSLVRSLartDEargllw 881
Cdd:cd14901 386 ----SLEQLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTF--VEYPNNDACVAMFEARPTGLFSLL---DE------ 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 882 lleeEALVPGASEDTLLErlfSYYgpqegDKKGQSPLLHSSKPHH----FLLGHSHGTnwVEYNVTGWLNYTKQNPATqN 957
Cdd:cd14901 451 ----QCLLPRGNDEKLAN---KYY-----DLLAKHASFSVSKLQQgkrqFVIHHYAGA--VCYATDGFCDKNKDHVHS-E 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 958 APRLLQDSqkkiiSNLFLgragSATVLSgsiagleggsqlalrratsmrktfttgmaavkkkslciQMKLQVDALIDTIK 1037
Cdd:cd14901 516 ALALLRTS-----SNAFL----SSTVVA--------------------------------------KFKVQLSSLLEVLN 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1038 KSKLHFVHCFLPVaegwageprsassrrvsssselDLPSGDhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMV 1117
Cdd:cd14901 549 ATEPHFIRCIKPN----------------------DVLSPS-------EFDAKRVLEQLRCSGVLEAVKISRSGYPVRFP 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1118 FSEFRRRFDVLAPHLTKKHGRNYIVVDERRAVEELLECLDLEKSSCCMGLSRVF 1171
Cdd:cd14901 600 HDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIEHLPPFQVGKTKVF 653
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
420-975 |
3.46e-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: 211.09 E-value: 3.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14897 2 TIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 578
Cdd:cd14897 82 ESGAGKTESTKYMIKHLMKLS--PSDDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLAcgdGTLRTELHLNHLAENNVFGIVPLA--------KPEEKQKAAQQFSKLQAAMK 650
Cdd:cd14897 160 LLEKSRVVHRGNGEKNFHIFYALFA---GMSRDRLLYYFLEDPDCHRILRDDnrnrpvfnDSEELEYYRQMFHDLTNIMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEQKACWFILAAIYHLgAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIF--KHQHKGGTLQRSTS 728
Cdd:cd14897 237 LIGFSEEDISVIFTILAAILHL-TNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALIsnVNTIRGERIQSWKS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 729 FRQgpeesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALKSSQ-----HSLCSMMIVDTPGFQNPEQGGsar 803
Cdd:cd14897 316 LRQ----------------ANDSRDALAKDLYSRLFGWIVGQINRNLWPDKdfqimTRGPSIGILDMSGFENFKINS--- 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAfdDLEPPTDDSVAAVDQASHQSLvrsLARTDEargllwll 883
Cdd:cd14897 377 ---FDQLCINLSNERLQQYFNDYVFPRERSEYEIEGIEWR--DIEYHDNDDVLELFFKKPLGI---LPLLDE-------- 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 884 eeEALVPGASEDTLLERLFSYYGPqegdkkgqSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLNYTKQNpATQNAPRLLQ 963
Cdd:cd14897 441 --ESTFPQSTDSSLVQKLNKYCGE--------SPRYVASPGNRVAFGIRHYAEQVTYDADGFLEKNRDN-LSSDIVGCLL 509
|
570
....*....|..
gi 42794779 964 DSQKKIISNLFL 975
Cdd:cd14897 510 NSNNEFISDLFT 521
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
419-1129 |
6.50e-57 |
|
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: 210.41 E-value: 6.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGIS-GNKVFSVEKwqaLYTLLEAFGNSPTIINGNATRFSQILSLDFdQAGQVASASIQT 577
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQtEDRLRQPED---VLPILESFGHAKTILNANASRFGQVLRLHL-QHGVIVGASVSH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 578 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHlAEN----NVFGIVPLAKPEEkqkaAQQFSKLQAAMKVLG 653
Cdd:cd14896 157 YLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQG-PETyyylNQGGACRLQGKED----AQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 654 ISPDEQKACWFILAAIYHLGA---AGATKEAAEAGrkqfARHEWA--QKAAYLLGCSLEELSSAIFKhqhkggtlqRSTS 728
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNicfSSSERESQEVA----AVSSWAeiHTAARLLQVPPERLEGAVTH---------RVTE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 729 FRQGPEESGLgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRAL--KSSQHSLCSMMIVDTPGFQnpeqggSARGAS 806
Cdd:cd14896 299 TPYGRVSRPL-----PVEGAIDARDALAKTLYSRLFTWLLKRINAWLapPGEAESDATIGVVDAYGFE------ALRVNG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 807 FEELCHNYTQDRLQRLFHERTFVQELERYKEEniELAFDDLEPPTDDSVAAVDQASHQSLVRSLartdeargllwllEEE 886
Cdd:cd14896 368 LEQLCINLASERLQLFSSQTLLAQEEEECQRE--LLPWVPIPQPPRESCLDLLVDQPHSLLSIL-------------DDQ 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 887 ALVPGASEDTLLERLFSYYGPQEGDKKGQSPLlhsskPhHFLLGHSHGTnwVEYNVTGWLNYTKQ--NPATQNaprLLQD 964
Cdd:cd14896 433 TWLSQATDHTFLQKCHYHHGDHPSYAKPQLPL-----P-VFTVRHYAGT--VTYQVHKFLNRNRDqlDPAVVE---MLAQ 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 965 SQKKIISNLFlGRAGSAtvlsgsiAGLE-GGSQLALRratsmrktfttgmaavkkkslcIQMKLQvdALIDTIKKSKLHF 1043
Cdd:cd14896 502 SQLQLVGSLF-QEAEPQ-------YGLGqGKPTLASR----------------------FQQSLG--DLTARLGRSHVYF 549
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1044 VHCFLPvaegwagEPRSassrrvsssseldLPsgdhceaGLlqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1123
Cdd:cd14896 550 IHCLNP-------NPGK-------------LP-------GL--FDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
....*.
gi 42794779 1124 RFDVLA 1129
Cdd:cd14896 601 RFGALG 606
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
420-1135 |
1.54e-55 |
|
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: 207.82 E-value: 1.54e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFK--------GCRREDMAPHIYAVAQTAYRAMLMS-R 489
Cdd:cd14902 2 ALLQALSERFEHDQIYTSIGDILVALNPlKPLPDLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKPeR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 490 QDQSIILLGSSGSGKTTSCQHLVQYLATI-----AGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSL 562
Cdd:cd14902 82 RNQSILVSGESGSGKTESTKFLMQFLTSVgrdqsSTEQEGSDAVEIGKRILQTnpILESFGNAQTIRNDNSSRFGKFIKI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 563 DFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAE---NNVFGIVPLAKPEEKQKAA 639
Cdd:cd14902 162 QFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKyelLNSYGPSFARKRAVADKYA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 640 QQFSKLQAAMKVLGISPDEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFKHQ 717
Cdd:cd14902 242 QLYVETVRAFEDTGVGELERLDIFKILAALLHLGnvNFTAENGQEDATAVTAASRFHLAKCAELMGVDVDKLETLLSSRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 718 HKGGtlQRSTSFRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVN---------RALKSSQHSLCSMMIV 788
Cdd:cd14902 322 IKAG--VEVMVLKLTPEQ------------AKEICGSLAKAIYGRLFTWLVRRLSdeinyfdsaVSISDEDEELATIGIL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 789 DTPGFQNPEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEPPtddsvaavDQASHQSLVr 868
Cdd:cd14902 388 DIFGFESLNRNG------FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGID--WKNISYP--------SNAACLALF- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 869 slarTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEgdkkgqspllhsskphHFLLGHSHGTnwVEYNVTGWLNy 948
Cdd:cd14902 451 ----DDKSNGLFSLLDQECLMPKGSNQALSTKFYRYHGGLG----------------QFVVHHFAGR--VCYNVEQFVE- 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 949 TKQNPATQNAPRLLQDSQKKIISNLFL-GRAGSATVLSGSiagleggsqlALRRATSMrktfttgmaaVKKKSLCIQMKL 1027
Cdd:cd14902 508 KNTDALPADASDILSSSSNEVVVAIGAdENRDSPGADNGA----------AGRRRYSM----------LRAPSVSAQFKS 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1028 QVDALIDTIKKSKLHFVHCFLPvaeGWAGEPRSassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRM 1107
Cdd:cd14902 568 QLDRLIVQIGRTEAHYVRCLKP---NEVKKPGI--------------------------FDRERMVEQMRSVGVLEAVRI 618
|
730 740
....*....|....*....|....*...
gi 42794779 1108 YRQGYPDHMVFSEFRRRFDVLAPHLTKK 1135
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKCFLSTR 646
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
420-1173 |
1.97e-55 |
|
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: 206.16 E-value: 1.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVM--HMFKGCRRedMAPHIYAVAQTAYRAMLMSRQDQSIILL 497
Cdd:cd14872 2 MIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMdqYMHKGPKE--MPPHTYNIADDAYRAMIVDAMNQSILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 498 GSSGSGKTTSCQHLVQYLATIAGISGNkvfsVEKWQALYT-LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd14872 80 GESGAGKTEATKQCLSFFAEVAGSTNG----VEQRVLLANpILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLnhlaeNNVFGIVPLAKPEEKQKA--AQQFSKLQAAMKVLGI 654
Cdd:cd14872 156 NYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGS-----SAAYGYLSLSGCIEVEGVddVADFEEVVLAMEQLGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 655 SPDEQKACWFILAAIYHLG----AAGATKEAAEAgrKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFR 730
Cdd:cd14872 231 DDADINNVMSLIAAILKLGniefASGGGKSLVSG--STVANRDVLKEVATLLGVDAATLEEAL---------TSRLMEIK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 731 QgpeesglGDGTGPKLSALECLEG---MAAGLYSELFTLLVSLVNRALKSSQHSL-CSMMIVDTPGFQNPEQGgsargaS 806
Cdd:cd14872 300 G-------CDPTRIPLTPAQATDAcdaLAKAAYSRLFDWLVKKINESMRPQKGAKtTFIGVLDIFGFEIFEKN------S 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 807 FEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsvaavdqashqsLVRSlaRTDearGLLWLL 883
Cdd:cd14872 367 FEQLCINFTNEKLQQHFNQYTFKLEEALYQSEGVKfehIDFIDNQPVLD-------------LIEK--KQP---GLMLAL 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 884 EEEALVPGASEDTLLERLfsyyGPQEGDKKGQSPLLHSSKPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQ 963
Cdd:cd14872 429 DDQVKIPKGSDATFMIAA----NQTHAAKSTFVYAEVRTSRTEFIVKHYAGD--VTYDITGFLEKNK-DTLQKDLYVLLS 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 964 DSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHF 1043
Cdd:cd14872 502 SSKNKLIAVLF--------------------PPSEGDQKTS-------------KVTLGGQFRKQLSALMTALNATEPHY 548
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1044 VHCFLPVAEGWAgeprsassrrvsssselDLPSGDHCeaglLQldvpllrtQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1123
Cdd:cd14872 549 IRCVKPNQEKRA-----------------RLFDGFMS----LE--------QLRYAGVFEAVKIRKTGYPFRYSHERFLK 599
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1124 RFDVLAPHLTKKHGRnyivvDERRAVEELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd14872 600 RYRFLVKTIAKRVGP-----DDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
416-858 |
2.84e-55 |
|
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: 205.48 E-value: 2.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 416 LNESSVLHTLRQRYGASLLHTYAGPS-LLVLGPRGAPAVYSEKVMHMFK-------GCRREDMAPHIYAVAQTAYRAMLM 487
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRLGSSaLVAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRMRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 488 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGIS--GNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFD 565
Cdd:cd14879 81 RSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSkkGTKL--SSQISAAEFVLDSFGNAKTLTNPNASRFGRYTELQFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 566 QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF---GIVPL-AKPEEKQkaAQQ 641
Cdd:cd14879 159 ERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLpLGPGSDD--AEG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 642 FSKLQAAMKVLGISPDEQKACWFILAAIYHLgaagatkeaaeaGRKQFA-----RHEWA--------QKAAYLLGCSLEE 708
Cdd:cd14879 237 FQELKTALKTLGFKRKHVAQICQLLAAILHL------------GNLEFTydhegGEESAvvkntdvlDIVAAFLGVSPED 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 709 LSSAI---FKHQHKggtlQRSTSFrqgpeesgLgdgtGPKLSAL--ECLegmAAGLYSELFTLLVSLVNRALKSSQHSLC 783
Cdd:cd14879 305 LETSLtykTKLVRK----ELCTVF--------L----DPEGAAAqrDEL---ARTLYSLLFAWVVETINQKLCAPEDDFA 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 784 SMM-IVDTPGFQNpeQGGSArGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAfddlEPPTDDSVAAV 858
Cdd:cd14879 366 TFIsLLDFPGFQN--RSSTG-GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVP----ATSYFDNSDCV 434
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
420-1130 |
1.23e-54 |
|
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: 204.16 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVM--HMFKGcrrEDMAPHIYAVAQTAYRAMLMSRQDQSIIL 496
Cdd:cd14888 2 SILHSLNLRFDIDEIYTFTGPILIAVNPfKTIPGLYSDEMLlkFIQPS---ISKSPHVFSTASSAYQGMCNNKKSQTILI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 497 LGSSGSGKTTSCQHLVQYLATiAGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQ-------- 566
Cdd:cd14888 79 SGESGAGKTESTKYVMKFLAC-AGSEDIKKRSLVEAQVLESnpLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskrmsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 567 -AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC----GDGTLRTELHLNHLAENNvfGIVPLAKPEEKQKAAQQ 641
Cdd:cd14888 158 dRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAareaKNTGLSYEENDEKLAKGA--DAKPISIDMSSFEPHLK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 642 FSKLQ--------------------AAMKVLGISPDEQKACWFILAAIYHLGAAG-ATKEAAEAGRKQFA-RHEWAQKAA 699
Cdd:cd14888 236 FRYLTksschelpdvddleefestlYAMQTVGISPEEQNQIFSIVAAILYLGNILfENNEACSEGAVVSAsCTDDLEKVA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 700 YLLGCSLEELSSAIFKHqhkggTLQRSTSFRQGPEESGlgdgtgpklSALECLEGMAAGLYSELFTLLVSLVNRAL-KSS 778
Cdd:cd14888 316 SLLGVDAEDLLNALCYR-----TIKTAHEFYTKPLRVD---------EAEDVRDALARALYSCLFDKVVERTNESIgYSK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 779 QHSLCSMMIVDTPGFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEPPTDDSVAAV 858
Cdd:cd14888 382 DNSLLFCGVLDIFGFE------CFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGIS--WNPLDFPDNQDCVDL 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 859 DQASHQSLvrsLARTDEargllwlleeEALVPGASEDTLLERLFSYYGpqeGDKKGQSPllhSSKPHHFLLGHSHGTnwV 938
Cdd:cd14888 454 LQEKPLGI---FCMLDE----------ECFVPGGKDQGLCNKLCQKHK---GHKRFDVV---KTDPNSFVIVHFAGP--V 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 939 EYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalrrATSMRKTFTTGMAAVKK 1018
Cdd:cd14888 513 KYCSDGFLEKNK-DQLSVDAQEVIKNSKNPFISNLF---------------------------SAYLRRGTDGNTKKKKF 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1019 KSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAgeprsassrrvsssSELDLPSgdhceagllqldvplLRTQLRG 1098
Cdd:cd14888 565 VTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVP--------------DLFDRIS---------------VNEQLKY 615
|
730 740 750
....*....|....*....|....*....|..
gi 42794779 1099 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1130
Cdd:cd14888 616 GGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
420-1133 |
2.46e-54 |
|
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: 203.10 E-value: 2.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14873 2 SIMYNLFQRYKRNQIYTYIGSILASVNPyQPIAGLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGIS-----GNKVFSVEkwQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQV 570
Cdd:cd14873 82 ESGAGKTESTKLILKFLSVISQQSlelslKEKTSCVE--QAILEsspIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 571 ASASIQTMLLEKLRVARRPASEATFNVFYYLLAcGDGTLRTELHLNHLAEN----NVFGIVPLAKPEEKqkaaQQFSKLQ 646
Cdd:cd14873 160 QGGRIVDYLLEKNRVVRQNPGERNYHIFYALLA-GLEHEEREEFYLSTPENyhylNQSGCVEDKTISDQ----ESFREVI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 647 AAMKVLGISPDEQKACWFILAAIYHLGAAgatkEAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRS 726
Cdd:cd14873 235 TAMEVMQFSKEEVREVSRLLAGILHLGNI----EFITAGGAQVSFKTALGRSAELLGLDPTQLTDAL---------TQRS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 727 TSFRqgpeesglGDGTGPKLS---ALECLEGMAAGLYSELFTLLVSLVNRALKSSQHsLCSMMIVDTPGFQNPEQGgsar 803
Cdd:cd14873 302 MFLR--------GEEILTPLNvqqAVDSRDSLAMALYARCFEWVIKKINSRIKGKED-FKSIGILDIFGFENFEVN---- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 804 gaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIElaFDDLEpptddsvaAVDQASHQSLVRS----LARTDEargl 879
Cdd:cd14873 369 --HFEQFNINYANEKLQEYFNKHIFSLEQLEYSREGLV--WEDID--------WIDNGECLDLIEKklglLALINE---- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 880 lwlleeEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKPHHFLLGHSHGTNWVEYNVTGWLnytKQNPAT--QN 957
Cdd:cd14873 433 ------ESHFPQATDSTLLEKLHS--------QHANNHFYVKPRVAVNNFGVKHYAGEVQYDVRGIL---EKNRDTfrDD 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 958 APRLLQDSQKKIISNLFlgragsatvlsgsiagleggsqlalRRATSMRKTFTTGMAAVKKK-SLCIQMKLQVDALIDTI 1036
Cdd:cd14873 496 LLNLLRESRFDFIYDLF-------------------------EHVSSRNNQDTLKCGSKHRRpTVSSQFKDSLHSLMATL 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1037 KKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHM 1116
Cdd:cd14873 551 SSSNPFFVRCIKPNMQ--------------------KMPD---------QFDQAVVLNQLRYSGMLETVRIRKAGYAVRR 601
|
730
....*....|....*..
gi 42794779 1117 VFSEFRRRFDVLAPHLT 1133
Cdd:cd14873 602 PFQDFYKRYKVLMRNLA 618
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
422-1129 |
7.88e-54 |
|
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: 201.53 E-value: 7.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 422 LHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSekVMHMFKGCRREDMA----PHIYAVAQTAYRAMLMSR----QDQ 492
Cdd:cd14892 4 LDVLRRRYERDAIYTFTADILISINPyKSIPLLYD--VPGFDSQRKEEATAssppPHVFSIAERAYRAMKGVGkgqgTPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 493 SIILLGSSGSGKTTSCQHLVQYLATIAGIsGNKVFSVEKWQALY-----------TLLEAFGNSPTIINGNATRFSQILS 561
Cdd:cd14892 82 SIVVSGESGAGKTEASKYIMKYLATASKL-AKGASTSKGAANAHesieecvllsnLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 562 LDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAEnnvFGIVPLAKPEEKQKA--A 639
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAES---FLFLNQGNCVEVDGVddA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 640 QQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRK-QFARHEWAQKAAYLLGCSLEELSSAIFKHQH 718
Cdd:cd14892 238 TEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFaQSADGVNVAKAAGLLGVDAAELMFKLVTQTT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 719 KGGtlqRSTSFRQ--GPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAlkSSQHSLCSMMIVDTP----- 791
Cdd:cd14892 318 STA---RGSVLEIklTARE------------AKNALDALCKYLYGELFDWLISRINAC--HKQQTSGVTGGAASPtfspf 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 792 -------GFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPPTDdsvaaVDQA 861
Cdd:cd14892 381 igildifGFE------IMPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDvsaIEFQDNQDCLD-----LIQK 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 862 SHQSLVRSLartdEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQ-EGDkkgqspllhsskphHFLLGHSHGTnwVEY 940
Cdd:cd14892 450 KPLGLLPLL----EEQMLLKRKTTDKQLLTIYHQTHLDKHPHYAKPRfECD--------------EFVLRHYAGD--VTY 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 941 NVTGWLnyTKQNPATQNAPRLLQDSQKKiisnlflgragsatvlsgsiagleggsqlalrratsmrktFTTgmaavkkks 1020
Cdd:cd14892 510 DVHGFL--AKNNDNLHDDLRDLLRSSSK----------------------------------------FRT--------- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1021 lciqmklQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssSELDLPSGDHCEagllqldvpLLRTQLRGSR 1100
Cdd:cd14892 539 -------QLAELMEVLWSTTPSYIKCIKP--------------------NNLKFPGGFSCE---------LVRDQLIYSG 582
|
730 740
....*....|....*....|....*....
gi 42794779 1101 LLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1129
Cdd:cd14892 583 VLEVVRIRREGFPIRRQFEEFYEKFWPLA 611
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
420-1130 |
7.18e-53 |
|
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: 198.63 E-value: 7.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14904 2 SILFNLKKRFAASKPYTYTNDIVIALNPyKWIDNLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGisGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 578
Cdd:cd14904 82 ESGAGKTETTKIVMNHLASVAG--GRKDKTIAKVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDE 658
Cdd:cd14904 160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQIPGLDDAKLFASTQKSLSLIGLDNDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 659 QKACWFILAAIYHLGAAGATKEAAEAGRKQfaRHEWAQKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFRQGPEESGL 738
Cdd:cd14904 240 QRTLFKILSGVLHLGEVMFDKSDENGSRIS--NGSQLSQVAKMLGLPTTRIEEAL---------CNRSVVTRNESVTVPL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 739 GdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALkSSQHSLCSMMI--VDTPGFQNPEQGGsargasFEELCHNYTQ 816
Cdd:cd14904 309 A-----PVEAEENRDALAKAIYSKLFDWMVVKINAAI-STDDDRIKGQIgvLDIFGFEDFAHNG------FEQFCINYAN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 817 DRLQRLFHERTFVQELERYKEENieLAFDDLEPPTDDSVAAVdqashqslvrslarTDEARGLLWLLEEEALVPGASEDT 896
Cdd:cd14904 377 EKLQQKFTTDVFKTVEEEYIREG--LQWDHIEYQDNQGIVEV--------------IDGKMGIIALMNDHLRQPRGTEEA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 897 LLERLFSYYGPQEGDKKGQSPllhSSKPHHFLLGHSHGTnwVEYNVTGWLNytKQNPATQN-APRLLQDSQKKIISNLFl 975
Cdd:cd14904 441 LVNKIRTNHQTKKDNESIDFP---KVKRTQFIINHYAGP--VTYETVGFME--KHRDTLQNdLLDLVLLSSLDLLTELF- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 976 graGSATVLSGSIAGLEGGSQLAlrratsmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWA 1055
Cdd:cd14904 513 ---GSSEAPSETKEGKSGKGTKA-------------------PKSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSP 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1056 GEprsassrrvsssseldlpsgdhceagllqLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1130
Cdd:cd14904 571 TE-----------------------------FDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
419-1173 |
1.39e-52 |
|
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: 197.67 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQaGQVASASIQTM 578
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRRNNLV--TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFEG-GVIVGAITSQY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTE---------LHLNHLAENNVFGivplakpeekQKAAQQFSKLQAAM 649
Cdd:cd01387 158 LLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKyglqeaekyFYLNQGGNCEIAG----------KSDADDFRRLLAAM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 650 KVLGISPDEQKACWFILAAIYHLG-------AAGATKEAAEAGRKqfARHEWaqkAAYLLGCSLEELSSAIfkhqhkggt 722
Cdd:cd01387 228 QVLGFSSEEQDSIFRILASVLHLGnvyfhkrQLRHGQEGVSVGSD--AEIQW---VAHLLQISPEGLQKAL--------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 723 LQRSTSFRQGPEESGLG-DgtgpklSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgs 801
Cdd:cd01387 294 TFKVTETRRERIFTPLTiD------QALDARDAIAKALYALLFSWLVTRVNAIVYSGTQDTLSIAILDIFGFEDLSEN-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 802 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LAFDDLEPptddsvaavdqashqsLVRSLARtdEARG 878
Cdd:cd01387 366 ----SFEQLCINYANENLQYYFNKHVFKLEQEEYIREQIDwteIAFADNQP----------------VINLISK--KPVG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 879 LLWLLEEEALVPGASEDTLLERLFSYYGPQEgdkkgqspllHSSKPH----HFLLGHSHGTNWveYNVTGWLNYTKqNPA 954
Cdd:cd01387 424 ILHILDDECNFPQATDHSFLEKCHYHHALNE----------LYSKPRmplpEFTIKHYAGQVW--YQVHGFLDKNR-DQL 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 955 TQNAPRLLQDSQKKIISNLFlgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAAVKKKSLCIQMKLQ--VDAL 1032
Cdd:cd01387 491 RQDVLELLVSSRTRVVAHLF--------------------SSHRAQTDKAPPRLGKGRFVTMKPRTPTVAARFQdsLLQL 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1033 IDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLlqLDVPLLRTQLRGSRLLDAMRMYRQGY 1112
Cdd:cd01387 551 LEKMERCNPWFVRCLKP---------------------------NHKKEPML--FDMDVVMAQLRYSGMLETIRIRKEGY 601
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1113 PDHMVFSEFRRRFDvlapHLTKKHGRNYIVVDERRAVeELLECLDLEKSSCCMGLSRVFFR 1173
Cdd:cd01387 602 PVRLPFQVFIDRYR----CLVALKLPRPAPGDMCVSL-LSRLCTVTPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
421-1128 |
1.83e-51 |
|
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: 194.35 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 421 VLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAML----MSRQDQSIIL 496
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 497 LGSSGSGKTTSCQHLVQYLATIAgiSGNKVFSVEKWQaLYTLLEAFGNSPTIINGNATRFSQILSLDFdQAGQVASASIQ 576
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC--RGNSQLEQQILQ-VNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGD-------GTLRTELH--LNHLAENNvfgivplakpEEKQKAAQQFSKLQA 647
Cdd:cd14889 159 EYLLEKSRVVHQDGGEENFHIFYYMFAGISaedrenyGLLDPGKYryLNNGAGCK----------REVQYWKKKYDEVCN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAYLLGCSLEELSsaifkhqhkgGTLQRST 727
Cdd:cd14889 229 AMDMVGFTEQEEVDMFTILAGILSLGNITFEMDDDEALKVENDSNGWLKAAAGQFGVSEEDLL----------KTLTCTV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 SFRQGPEESGLGDgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHS---LCSMMIVDTPGFQNPEQGgsarg 804
Cdd:cd14889 299 TFTRGEQIQRHHT----KQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSsveLREIGILDIFGFENFAVN----- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPPTDDSVAavdqashqSLVRSLARTDEargllw 881
Cdd:cd14889 370 -RFEQACINLANEQLQYFFNHHIFLMEQKEYKKEGIdwkEITYKDNKPILDLFLN--------KPIGILSLLDE------ 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 882 lleeEALVPGASEDTLLERLFSYYG--PQEGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGWLNYTKQN-PATQNA 958
Cdd:cd14889 435 ----QSHFPQATDESFVDKLNIHFKgnSYYGKSRSKSPK--------FTVNHYAGK--VTYNASGFLEKNRDTiPASIRT 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 959 prLLQDSQKKIISNLFLGRAGSATVLSGSIAGLEGGSQlalrratsmrktfttGMAAVKKKSLCIQMKLQVDALIDTIKK 1038
Cdd:cd14889 501 --LFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSD---------------NFNSTRKQSVGAQFKHSLGVLMEKMFA 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1039 SKLHFVHCFLPvaegwageprsassrrvsssSELDLPSgdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVF 1118
Cdd:cd14889 564 ASPHFVRCIKP--------------------NHVKVPG---------QLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
730
....*....|
gi 42794779 1119 SEFRRRFDVL 1128
Cdd:cd14889 615 AEFAERYKIL 624
|
|
| PDZ_MYO18-like |
cd06747 |
PDZ domain of MYO18A protein, and related domains; PDZ (PSD-95 (Postsynaptic density protein ... |
220-308 |
3.12e-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: 175.58 E-value: 3.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLRRTTMLDRGPE-GQACRRVVHFAEPGAGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06747 1 EITLKRQPTGDFGFSLRRGTIVERGPDdGQELKRTVHFAEPGAGTKNLATGLLPGDRLIEVNGVNVENASRDEIIEMIRK 80
|
90
....*....|
gi 42794779 299 SGDSVRLKVQ 308
Cdd:cd06747 81 SGDTVTLKVQ 90
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
420-1130 |
4.05e-51 |
|
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: 194.13 E-value: 4.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGS 499
Cdd:cd01385 2 TLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLATIAGISGNKvfSVEkwQALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd01385 82 SGSGKTESTNFLLHHLTALSQKGYGS--GVE--QTILGagpVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL------NHLAENNVFGivplakpEEKQKAAQQFSKLQAAMK 650
Cdd:cd01385 158 KYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLkqpedyHYLNQSDCYT-------LEGEDEKYEFERLKQAME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 651 VLGISPDEQKACWFILAAIYHLGaagatkeAAEAGRKQFARHEWAQKA--------AYLLGCSLEELSSAIF--KHQHKG 720
Cdd:cd01385 231 MVGFLPETQRQIFSVLSAVLHLG-------NIEYKKKAYHRDESVTVGnpevldiiSELLRVKEETLLEALTtkKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 721 GTLQRSTSFrqgPEesglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRAL---KSSQHSLC-SMMIVDTPGFQNP 796
Cdd:cd01385 304 ETLILPYKL---PE-------------AIATRDAMAKCLYSALFDWIVLRINHALlnkKDLEEAKGlSIGVLDIFGFEDF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 797 EQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEE-----NIELAfddlepptdDSVAAVDQASHQ--SLVRS 869
Cdd:cd01385 368 GNN------SFEQFCINYANEHLQYYFNQHIFKLEQEEYKKEgiswhNIEYT---------DNTGCLQLISKKptGLLCL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 870 LartDEargllwlleeEALVPGASEDTLLERLFS-------YYGPQEgdkkgqspllhssKPHHFLLGHSHGTnwVEYNV 942
Cdd:cd01385 433 L---DE----------ESNFPGATNQTLLAKFKQqhkdnkyYEKPQV-------------MEPAFIIAHYAGK--VKYQI 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 943 TGW----LNYTKQNPATqnaprLLQDSQKKIISNL-----------------FLGRAGSATVLSGSIAGLEGGSQLALRR 1001
Cdd:cd01385 485 KDFreknLDLMRPDIVA-----VLRSSSSAFVRELigidpvavfrwavlrafFRAMAAFREAGRRRAQRTAGHSLTLHDR 559
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1002 ATSMRktfttGMAAVKKKSLCIQMKLQV--DALIDTIKKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPsgdh 1079
Cdd:cd01385 560 TTKSL-----LHLHKKKKPPSVSAQFQTslSKLMETLGQAEPFFIRCIKSNAE--------------------KKP---- 610
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1080 ceaglLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1130
Cdd:cd01385 611 -----LRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLP 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
419-1128 |
8.41e-50 |
|
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: 189.86 E-value: 8.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRRE--------DMAPHIYAVAQTAYRAMLMSR 489
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPyKQIDNLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 490 QDQSIILLGSSGSGKTTSCQHLVQYLATiagISGNKVFSVEKWQALYT--------------------LLEAFGNSPTII 549
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQ---LSQQEQNSEEVLTLTSSiratskstksieqkilscnpILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 550 NGNATRFSQILSLDFD-QAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHL-NHLAENNVFgiv 627
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLkNQLSGDRYD--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 628 PLAKPE----EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARH-EWAQKAAYLL 702
Cdd:cd14907 235 YLKKSNcyevDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNkETLQIIAKLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 703 GCSLEELSSAIFKHQHKGGtlqrstsfrqgpeesglGDGTGPKLSALEC---LEGMAAGLYSELFTLLVSLVNRAL---- 775
Cdd:cd14907 315 GIDEEELKEALTTKIRKVG-----------------NQVITSPLSKKECinnRDSLSKELYDRLFNWLVERLNDTImpkd 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 776 ----KSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPT 851
Cdd:cd14907 378 ekdqQLFQNKYLSIGLLDIFGFEVFQNN------SFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLNQLSYTD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 852 DDSVAAVDQASHQSLVRSLartDEargllwlleeEALVPGASEDTLLERLFSyygpQEGDKKGQSPLLHSSKPhHFLLGH 931
Cdd:cd14907 452 NQDVIDLLDKPPIGIFNLL---DD----------SCKLATGTDEKLLNKIKK----QHKNNSKLIFPNKINKD-TFTIRH 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 932 SHGTnwVEYNVTGWL--NYTKQNPATQNaprLLQDSQKKIISNLFLGRAGSATVLSGSIAGleggsqlalrratsmrktf 1009
Cdd:cd14907 514 TAKE--VEYNIEGFRekNKDEISQSIIN---CIQNSKNRIISSIFSGEDGSQQQNQSKQKK------------------- 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1010 ttgmAAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAGLLQLDV 1089
Cdd:cd14907 570 ----SQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEK---------------------------KADLFIQGY 618
|
730 740 750
....*....|....*....|....*....|....*....
gi 42794779 1090 PLLrtQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVL 1128
Cdd:cd14907 619 VLN--QIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
420-838 |
1.87e-48 |
|
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: 185.14 E-value: 1.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd01382 2 TLLNNIRVRYSKDKIYTYVANILIAVNPyFDIPKLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAGISGNKVFS--VEKwqalYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQ 576
Cdd:cd01382 82 ESGAGKTESTKYILRYLTESWGSGAGPIEQriLEA----NPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENnvfgivplakpeekqkaAQQFSKLQAAMKVLGISP 656
Cdd:cd01382 158 HYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLDD-----------------VGDFIRMDKAMKKIGLSD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 657 DEQKACWFILAAIYHLG--AAGATKEAAEAGRKQFARHEWA-QKAAYLLGCSLEELSSAIfkhqhkggtlqrSTSFRQGP 733
Cdd:cd01382 221 EEKLDIFRVVAAVLHLGniEFEENGSDSGGGCNVKPKSEQSlEYAAELLGLDQDELRVSL------------TTRVMQTT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 734 EESGLGDGTGPKLSALECLEG---MAAGLYSELFTLLVSLVNRAL--KSSQHSLCsmmIVDTPGFQ----Npeqggsarg 804
Cdd:cd01382 289 RGGAKGTVIKVPLKVEEANNArdaLAKAIYSKLFDHIVNRINQCIpfETSSYFIG---VLDIAGFEyfevN--------- 356
|
410 420 430
....*....|....*....|....*....|....
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEE 838
Cdd:cd01382 357 -SFEQFCINYCNEKLQQFFNERILKEEQELYEKE 389
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
471-841 |
2.21e-46 |
|
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: 179.08 E-value: 2.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 471 APHIYAVAQTAYRAMLMSR---QDQSIILLGSSGSGKTTSCQHLVQYLAT-----IAGISGNKVFSVEKWQALYT----- 537
Cdd:cd14891 52 PPHPYAIAEMAYQQMCLGSgrmQNQSIVISGESGAGKTETSKIILRFLTTravggKKASGQDIEQSSKKRKLSVTslder 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 538 ------LLEAFGNSPTIINGNATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLR 610
Cdd:cd14891 132 lmdtnpILESFGNAKTLRNHNSSRFGKFMKLQFtKDKFKLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 611 TELHlnhlaennvfgivpLAKPEEKQKAAQ-------------QFSKLQAAMKVLGISPDEQKACWFILAAIYHLG---- 673
Cdd:cd14891 212 KELL--------------LLSPEDFIYLNQsgcvsddniddaaNFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGnief 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 674 -----AAGATKEAAEAGRKQFArhewaqKAAYLLGCSLEELSSAIfkhqhkggtLQRSTSFRqgpeesglGDGTGPKLSA 748
Cdd:cd14891 278 deedtSEGEAEIASESDKEALA------TAAELLGVDEEALEKVI---------TQREIVTR--------GETFTIKRNA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 749 LECL---EGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEqggsaRGASFEELCHNYTQDRLQRLFHE 825
Cdd:cd14891 335 REAVysrDAIAKSIYERLFLWIVQQINTSLGHDPDPLPYIGVLDIFGFESFE-----TKNDFEQLLINYANEALQATFNQ 409
|
410
....*....|....*.
gi 42794779 826 RTFVQELERYKEENIE 841
Cdd:cd14891 410 QVFIAEQELYKSEGID 425
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
420-1129 |
7.63e-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: 178.22 E-value: 7.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSekvMHMFkgcrREDM------APHIYAVAQTAYRAMLM----- 487
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPfKHIPGLYD---LHKY----REEMpgwtalPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 488 --SRQDQSIILLGSSGSGKTTSCQHLVQYLA-----TIAGISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQ 558
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskhTTATSSSKRRRAISGSELLSAnpILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 559 ILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNvFGIVPLAKPE 633
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQE-FQYISGGQCY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 634 EKQKAAQ---QFSKLQAAMKVLGISPDEQKACWFILAAIYHLG-----------------AAGATKEAAEAGRKQFARHE 693
Cdd:cd14895 234 QRNDGVRddkQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGnvlfvassedegeedngAASAPCRLASASPSSLTVQQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 694 WAQKAAYLLGCSLEELSSAIFKHQHKGGtlqrstsfrqgpeesglGDGTGPKLSALECLE---GMAAGLYSELFTLLVSL 770
Cdd:cd14895 314 HLDIVSKLFAVDQDELVSALTTRKISVG-----------------GETFHANLSLAQCGDardAMARSLYAFLFQFLVSK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 771 VNRALKSSQHSLCS-----------MMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEEN 839
Cdd:cd14895 377 VNSASPQRQFALNPnkaankdttpcIAVLDIFGFEEFEVN------QFEQFCINYANEKLQYQFIQDILLTEQQAHIEEG 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 840 IELAFDDLEpptDDSVAAVDQASHQSLVRSLarTDEargllwlleeEALVPGASEDTLLERLFSYY---GPQEGDKKGQS 916
Cdd:cd14895 451 IKWNAVDYE---DNSVCLEMLEQRPSGIFSL--LDE----------ECVVPKGSDAGFARKLYQRLqehSNFSASRTDQA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 917 PLLhsskphhFLLGHSHGTnwVEYNVTGWLNYTKQNPaTQNAPRLLQDSQKKIISNLFlgragsaTVLSGSIAGLEGGSQ 996
Cdd:cd14895 516 DVA-------FQIHHYAGA--VRYQAEGFCEKNKDQP-NAELFSVLGKTSDAHLRELF-------EFFKASESAELSLGQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 997 LALRRATSMRKTFTTGMaavkkkslciQMKLQVDALIDTIKKSKLHFVHCFLPVAEGWAGeprsassrrvsssseldlps 1076
Cdd:cd14895 579 PKLRRRSSVLSSVGIGS----------QFKQQLASLLDVVQQTQTHYIRCIKPNDESASD-------------------- 628
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1077 gdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLA 1129
Cdd:cd14895 629 ---------QFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
420-1146 |
4.20e-45 |
|
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: 174.72 E-value: 4.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF-------------KGcrREDMAPHIYAVAQTAYRAM 485
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPfQKLPGLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 486 LMSR----QDQSIILLGSSGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQALYTLLEAFGNSPTIINGNA 553
Cdd:cd14900 80 MLGLngvmSDQSILVSGESGSGKTESTKFLMEYLAQAGdnnlaasvSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 554 TRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLlacgdgtlrtelhlnhlaennvfgivpLAKPE 633
Cdd:cd14900 160 SRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEM---------------------------AIGAS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 634 EKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGaaGATKEAAEAGrkqfarHEWAQKAAYLLGCSLEELSSAI 713
Cdd:cd14900 213 EAARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIG--NLTFEHDENS------DRLGQLKSDLAPSSIWSRDAAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 714 FKHQHKGGTLQRSTS---FRQGPEESGLgdgtgpKLSALEC---LEGMAAGLYSELFTLLVSLVNRALK-----SSQHSL 782
Cdd:cd14900 285 TLLSVDATKLEKALSvrrIRAGTDFVSM------KLSAAQAnnaRDALAKALYGRLFDWLVGKMNAFLKmddssKSHGGL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 783 CSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafddlepptdDSVAAVDQAS 862
Cdd:cd14900 359 HFIGILDIFGFEVFPKN------SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDW----------KYVEFCDNQD 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 863 HQSLVrslarTDEARGLLWLLEEEALVPGASEDTLLERLFSyygpqegdKKGQSPLLHSSKPHH----FLLGHSHGTnwV 938
Cdd:cd14900 423 CVNLI-----SQRPTGILSLIDEECVMPKGSDTTLASKLYR--------ACGSHPRFSASRIQRarglFTIVHYAGH--V 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 939 EYNVTGWLNytkqnpatQNAPRLLQDsqkkiISNLFLGragsatvlsgsiagleggsqlalrratsmrktfttgmaavkk 1018
Cdd:cd14900 488 EYSTDGFLE--------KNKDVLHQE-----AVDLFVY------------------------------------------ 512
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1019 kslCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsGDHCEAGLLQLDVPLlrTQLRG 1098
Cdd:cd14900 513 ---GLQFKEQLTTLLETLQQTNPHYVRCLKP---------------------------NDLCKAGIYERERVL--NQLRC 560
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1099 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVL----APHLTKKHGrnYIVVDER 1146
Cdd:cd14900 561 NGVMEAVRVARAGFPIRLLHDEFVARYFSLarakNRLLAKKQG--TSLPDTD 610
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1224-1918 |
7.10e-42 |
|
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: 168.82 E-value: 7.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1224 NIKKNKGVKDWPWWKLFTTVRPLIEVQLSEEQIRNKDE-EIQQLRSKLEKAEKERNELrlnsdrlESRISELTSELtder 1302
Cdd:pfam01576 374 NLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEgQLQELQARLSESERQRAEL-------AEKLSKLQSEL---- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1303 ntgESASQLLDAETAERLRAEKEMKELQTQ-YDALKKQMEVMEMEVMEARLIRA--AEINGEVDDDDAGGEWRLKYERAV 1379
Cdd:pfam01576 443 ---ESVSSLLNEAEGKNIKLSKDVSSLESQlQDTQELLQEETRQKLNLSTRLRQleDERNSLQEQLEEEEEAKRNVERQL 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1380 REVDF----TKKRLQQEFEdKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE 1455
Cdd:pfam01576 520 STLQAqlsdMKKKLEEDAG-TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSN 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1456 LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSqeSKDEA 1535
Cdd:pfam01576 599 LEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVS--SKDDV 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 --SLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEV 1613
Cdd:pfam01576 677 gkNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEA 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLrKDLKRTKALLADAQLMLDHLKNS-----APSKREIAQL 1688
Cdd:pfam01576 757 ELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAV-KQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKL 835
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1689 KN------QLEESeftCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1762
Cdd:pfam01576 836 KNleaellQLQED---LAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRL 912
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1763 KAAVAQ---------ASRDLAQIND-LQAQLEEANKekqELQEKLQALQSQVEFLEqsmvdKSLVSRQEAKIRELETRLE 1832
Cdd:pfam01576 913 RKSTLQveqlttelaAERSTSQKSEsARQQLERQNK---ELKAKLQEMEGTVKSKF-----KSSIAALEAKIAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1833 FERtqvkRLESLASRLKENMEKLTEERDQRIAAENREKEQNK-----------RLQRQLRDTKEEMgelarKEAEASRKK 1901
Cdd:pfam01576 985 QES----RERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdqaekgnsrmkQLKRQLEEAEEEA-----SRANAARRK 1055
|
730
....*....|....*..
gi 42794779 1902 heLEMDLESLEAANQSL 1918
Cdd:pfam01576 1056 --LQRELDDATESNESM 1070
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
422-1173 |
4.63e-41 |
|
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: 164.05 E-value: 4.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 422 LHTLRQRYGA--------SLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQS 493
Cdd:cd14887 4 LENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRRSQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 494 IILLGSSGSGKTTSCQHLVQYLATIA----GISGNKVfsVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQ 569
Cdd:cd14887 84 ILISGESGAGKTETSKHVLTYLAAVSdrrhGADSQGL--EARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 570 VASASIQTMLLEKLRVARRPASEATFNVFYYLlaCGDGTLRTELHLNhlaennvfgivplakPEEKQKAAQQFSKLQAAM 649
Cdd:cd14887 162 LTRASVATYLLANERVVRIPSDEFSFHIFYAL--CNAAVAAATQKSS---------------AGEGDPESTDLRRITAAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 650 KVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARH-------EWAQKAAYLLgcSLEELSSAIFKHQHKGGT 722
Cdd:cd14887 225 KTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceETAADRSHSS--EVKCLSSGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 723 LQRSTSFRQGPEESGLGDGTGPKLSALEC--------LEGMAAG-------LYSELFTLLVSLVNRALKSSQHSLCSMMI 787
Cdd:cd14887 303 LKTVARLLGLPPGVEGEEMLRLALVSRSVretrsffdLDGAAAArdaacknLYSRAFDAVVARINAGLQRSAKPSESDSD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 788 VDTP--------------GFQNPEQGGSARgasFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDD 853
Cdd:cd14887 383 EDTPsttgtqtigildlfGFEDLRNHSKNR---LEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFSF 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 854 SVAAVDQASHQSlVRSLARTDEARGLLWLLEEEALVpgaSEDTLLERLFSYYGPQEGDKKGqSPLLHSSKphhfllghsh 933
Cdd:cd14887 460 PLASTLTSSPSS-TSPFSPTPSFRSSSAFATSPSLP---SSLSSLSSSLSSSPPVWEGRDN-SDLFYEKL---------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 934 gtnwvEYNVTGWLNYTKQNPAtqnaprlLQDSQKKIISNLFLGRA---------GSATVLSGSIAGLEGGSQLALRRATS 1004
Cdd:cd14887 525 -----NKNIINSAKYKNITPA-------LSRENLEFTVSHFACDVtydardfcrANREATSDELERLFLACSTYTRLVGS 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1005 MRKTFTTGMAAvKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPVAEGwageprsassrrvsssseldlpsgdhcEAGL 1084
Cdd:cd14887 593 KKNSGVRAISS-RRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQ---------------------------EAGI 644
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1085 LQLDvpLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHgrnyivVDERRAVEELLECLDLEKSSCC 1164
Cdd:cd14887 645 FEDA--YVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALREA------LTPKMFCKIVLMFLEINSNSYT 716
|
....*....
gi 42794779 1165 MGLSRVFFR 1173
Cdd:cd14887 717 FGKTKIFFR 725
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
420-1130 |
4.66e-40 |
|
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: 160.07 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFK--GCRRE-------DMAPHIYAVAQTAYRAMLM-SR 489
Cdd:cd14908 2 AILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSqgiespqALGPHVFAIADRSYRQMMSeIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 490 QDQSIILLGSSGSGKTTSCQHLVQYLATIA---------GISGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQIL 560
Cdd:cd14908 82 ASQSILISGESGAGKTESTKIVMLYLTTLGngeegapneGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSSRFGKFI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 561 SLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGivplakPEEKQKAAQ 640
Cdd:cd14908 162 ELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITGGLQL------PNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 641 -------------QFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAG--ATKEAAEAGRKQFARHEWAQKAAYLLGCS 705
Cdd:cd14908 236 ggapdlreftdedGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEfeSKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 706 LEELSSAIFKHQHKGGTLQRSTSFRqgPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALK--SSQHSLC 783
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLT--PHK------------AYDARDALAKTIYGALFLWVVATVNSSINweNDKDIRS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 784 SMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAFddLEPPTDDSVAAVDQASH 863
Cdd:cd14908 382 SVGVLDIFGFECFAHN------SFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAF--IEFPDNQDCLDTIQAKK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 864 QSLVRSLarTDEARGLLWlleeealvpgASEDTLLERLFSYYGPQEGDKKGQSPLLHSSKPHH----FLLGHSHGTnwVE 939
Cdd:cd14908 454 KGILTML--DDECRLGIR----------GSDANYASRLYETYLPEKNQTHSENTRFEATSIQKtkliFAVRHFAGQ--VQ 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 940 YNV-TGWLnytkqnpatqnaprllqDSQKKIISNlflgragSATVLsgsiagleggsqlalrratsmrktFTTGMaavkk 1018
Cdd:cd14908 520 YTVeTTFC-----------------EKNKDEIPL-------TADSL------------------------FESGQ----- 546
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1019 kslciQMKLQVDALIDTIKKSKLHFVHCFLPvaeGWAGEPRSASSRRvsssseldlpsgdhceagllqldvplLRTQLRG 1098
Cdd:cd14908 547 -----QFKAQLHSLIEMIEDTDPHYIRCIKP---NDAAKPDLVTRKR--------------------------VTEQLRY 592
|
730 740 750
....*....|....*....|....*....|..
gi 42794779 1099 SRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAP 1130
Cdd:cd14908 593 GGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP 624
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
419-831 |
6.48e-40 |
|
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: 159.60 E-value: 6.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMF---KGCRREDMAPHIYAVAQTAYRAMLMSRQDQSII 495
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 496 LLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSveKWQALYTLLEAFGNSPTIINGNATRFSQILSLDF-DQAGQVASAS 574
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDS--RFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKKHLTGAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 575 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVfgiVPLAKPEEKQKAA-----QQFSKLQAAM 649
Cdd:cd14878 159 IYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRY---LNQTMREDVSTAErslnrEKLAVLKQAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 650 KVLGISPDEQKACWFILAAIYHLGAAGATKeAAEAGRKQFARHEWAQKAAYLLGCSLEELSSAIFK--HQHKGGTLQRST 727
Cdd:cd14878 236 NVVGFSSLEVENLFVILSAILHLGDIRFTA-LTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTdiQYFKGDMIIRRH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 SFRQGPEESGLgdgtgpklsaleclegMAAGLYSELFTLLVSLVNRALKsSQHSLCSMM-----IVDTPGFQNPEQGgsa 802
Cdd:cd14878 315 TIQIAEFYRDL----------------LAKSLYSRLFSFLVNTVNCCLQ-SQDEQKSMQtldigILDIFGFEEFQKN--- 374
|
410 420
....*....|....*....|....*....
gi 42794779 803 rgaSFEELCHNYTQDRLQRLFHERTFVQE 831
Cdd:cd14878 375 ---EFEQLCVNMTNEKMHHYINEVLFLQE 400
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
420-1141 |
1.15e-39 |
|
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: 159.37 E-value: 1.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILL 497
Cdd:cd14906 2 IILNNLGKRYKSDSIYTYIGNVLISINPyKDISSIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIIIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 498 GSSGSGKTTSCQHLVQYLATIAGIS-------GNKVFSVEKwqALYT---LLEAFGNSPTIINGNATRFSQILSLDFDQA 567
Cdd:cd14906 82 GESGSGKTEASKTILQYLINTSSSNqqqnnnnNNNNNSIEK--DILTsnpILEAFGNSRTTKNHNSSRFGKFLKIEFRSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 568 -GQVASASIQTMLLEKLRVARRP-ASEATFNVFYYLLACGDGTLRTELHLNH--------LAENNVFGIV------PLAK 631
Cdd:cd14906 160 dGKIDGASIETYLLEKSRISHRPdNINLSYHIFYYLVYGASKDERSKWGLNNdpskyrylDARDDVISSFksqssnKNSN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 632 PEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEA--AEAGRKQFARHEWAQKAAYLLGCSLEEL 709
Cdd:cd14906 240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSdfSKYAYQKDKVTASLESVSKLLGYIESVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 710 SSAIFKHQHKGGTlqRSTSFRQgPEESGLGDGTGPKLSaleclegmaAGLYSELFTLLVSLVNR-----------ALKSS 778
Cdd:cd14906 320 KQALLNRNLKAGG--RGSVYCR-PMEVAQSEQTRDALS---------KSLYVRLFKYIVEKINRkfnqntqsndlAGGSN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 779 QHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELA---FDDleppTDDSV 855
Cdd:cd14906 388 KKNNLFIGVLDIFGFENLSSN------SLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSnsnFID----NKECI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 856 AAVDQASHQSLvrSLArTDEArgllwlleeeaLVPGASEDTLLERLFSYYgpqegdKKGQSPLLHSSKPHHFLLGHSHGT 935
Cdd:cd14906 458 ELIEKKSDGIL--SLL-DDEC-----------IMPKGSEQSLLEKYNKQY------HNTNQYYQRTLAKGTLGIKHFAGD 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 936 nwVEYNVTGWLNYTKQNPATqNAPRLLQDSQKKIISNLFLGRAGSATvlsgsiagleggsqlalrrATSMRKTFTTGMAA 1015
Cdd:cd14906 518 --VTYQTDGWLEKNRDSLYS-DVEDLLLASSNFLKKSLFQQQITSTT-------------------NTTKKQTQSNTVSG 575
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1016 vkkkslciQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvssSSELDLPSGDHCEagllqldvplLRTQ 1095
Cdd:cd14906 576 --------QFLEQLNQLIQTINSTSVHYIRCIKP-------------------NQTMDCNNFNNVH----------VLSQ 618
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 42794779 1096 LRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKKHGRNYI 1141
Cdd:cd14906 619 LRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPK 664
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
419-844 |
2.01e-38 |
|
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: 155.01 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRR-EDMAPHIYAVAQTAYRAMLMSRQ--DQSI 494
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPfKPVPQLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 495 ILLGSSGSGKTTSCQHLVQYLATIAG----ISGNKVFSVEKWQALYT--LLEAFGNSPTIINGNATRFSQILSLDFDQAG 568
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAsptsWESHKIAERIEQRILNSnpVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 569 QVASASIQTMLLEKLRVARRPASEATFNVFYYLLacgDGTLRTELHLNHLAENNVFGIVPlakPEEKQKAAQQFSKLQAA 648
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQIC---KGASADERLQWHLPEGAAFSWLP---NPERNLEEDCFEVTREA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 649 MKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFA--RHEWAQKAAYLLGCSLEELSSAIFKHQHKGGTLQRs 726
Cdd:cd14880 235 MLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMddTKESVRTSALLLKLPEDHLLETLQIRTIRAGKQQQ- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 727 tSFRQgpeesglgdgtgpKLSALEC---LEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMM-IVDTPGFQN-PEQggs 801
Cdd:cd14880 314 -VFKK-------------PCSRAECdtrRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIgLLDVYGFESfPEN--- 376
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 42794779 802 argaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELAF 844
Cdd:cd14880 377 ----SLEQLCINYANEKLQQHFVAHYLRAQQEEYAVEGLEWSF 415
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
420-855 |
5.71e-38 |
|
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: 152.36 E-value: 5.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPrgAPAVYSEKVMHMFKGCRREdMAPHIYAVAQTAYRAMLMSrQDQSIILLGS 499
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNP--YETIYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 500 SGSGKTTSCQHLVQYLatIAGISGNKvfSVEK-WQALYTLLEAFGNSPTIINGNATRFSQILSLDFDqaGQVASASIQTM 578
Cdd:cd14898 78 SGSGKTENAKLVIKYL--VERTASTT--SIEKlITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITGAKFETY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVFGIVPLakpeekqkaAQQFSKLQAAMKVLGISpdE 658
Cdd:cd14898 152 LLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFIDTSSTAGNKESIVQL---------SEKYKMTCSAMKSLGIA--N 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 659 QKACWFILAAIYHLGAAGATKEaaeaGRKQFARHEWAQKAAYLLGCSLEELSSAIFKH--QHKGGTLQRSTSFRQgpees 736
Cdd:cd14898 221 FKSIEDCLLGILYLGSIQFVND----GILKLQRNESFTEFCKLHNIQEEDFEESLVKFsiQVKGETIEVFNTLKQ----- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 737 glgdgtgpklsALECLEGMAAGLYSELFTLLVSLVNRALK-SSQHSLCsmmIVDTPGFQNPEQGGsargasFEELCHNYT 815
Cdd:cd14898 292 -----------ARTIRNSMARLLYSNVFNYITASINNCLEgSGERSIS---VLDIFGFEIFESNG------LDQLCINWT 351
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 42794779 816 QDRLQRLFHERTFVQELERYKEENIElaFDDLEPPTDDSV 855
Cdd:cd14898 352 NEKIQNDFIKKMFRAKQGMYKEEGIE--WPDVEFFDNNQC 389
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
385-1049 |
1.27e-36 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 150.95 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 385 DGAILDVDEDDVEKANAP-SCDRLEDLASLVYLNESSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFK 463
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 464 GCRR-EDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLAtiAGISGNKVFSVEK--WQAlYTLLE 540
Cdd:PTZ00014 155 DAKDsDKLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLKIQNaiMAA-NPVLE 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 541 AFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAE 620
Cdd:PTZ00014 232 AFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 621 ----NN----VFGIVPlakpeekqkaAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLG-------AAGATKEAAEAG 685
Cdd:PTZ00014 312 ykyiNPkcldVPGIDD----------VKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGnveiegkEEGGLTDAAAIS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 686 RKQFarhEWAQKAAYLLGCSLEELS-SAIFKHQHKGGtlQRSTSFRQGPEESGLgdgtgpKLSaleclegMAAGLYSELF 764
Cdd:PTZ00014 382 DESL---EVFNEACELLFLDYESLKkELTVKVTYAGN--QKIEGPWSKDESEML------KDS-------LSKAVYEKLF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 765 TLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIelaf 844
Cdd:PTZ00014 444 LWIIRNLNATIEPPGGFKVFIGMLDIFGFEVFKNN------SLEQLFINITNEMLQKNFVDIVFERESKLYKDEGI---- 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 845 ddlepptddSVAAVDQASHQSLVRSLarTDEARGLLWLLEEEALVPGASEDTLLERLFSYYGPQEGDKKGQspllhSSKP 924
Cdd:PTZ00014 514 ---------STEELEYTSNESVIDLL--CGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAK-----VDSN 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 925 HHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIAgleggsqlalrrats 1004
Cdd:PTZ00014 578 KNFVIKHTIGD--IQYCASGFLFKNK-DVLRPELVEVVKASPNPLVRDLFEG----VEVEKGKLA--------------- 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 42794779 1005 mrktfttgmaavKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLP 1049
Cdd:PTZ00014 636 ------------KGQLIGSQFLNQLDSLMSLINSTEPHFIRCIKP 668
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
419-1125 |
6.78e-34 |
|
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: 141.39 E-value: 6.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF----------KGCRREDMAPHIYAVAQTAYRAMLM 487
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPfQDLPQLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 488 SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALYT---------------LLEAFGNSPTIINGN 552
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPASpsrttieeqvlqsnpILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 553 ATRFSQILSLDF-DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLA----CGDGTLRTELHLNHLAEN-NVFGI 626
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSadnnCVSKEQKQVLALSGGPQSfRLLNQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 627 VPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAA-----------GATKEAAEAGRKQFARHEWA 695
Cdd:cd14899 241 SLCSKRRDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVdfeqiphkgddTVFADEARVMSSTTGAFDHF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 696 QKAAYLLGCSLEELSSAIFKHQhkggtLQRSTSFRQGPEESGLGDGTGPKLSaLEClegmaaglYSELFTLLVSLVNRAL 775
Cdd:cd14899 321 TKAAELLGVSTEALDHALTKRW-----LHASNETLVVGVDVAHARNTRNALT-MEC--------YRLLFEWLVARVNNKL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 776 K---------------SSQHSLCSMMIVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI 840
Cdd:cd14899 387 QrqasapwgadesdvdDEEDATDFIGLLDIFGFEDMAEN------SFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 841 ELAFDDLEpptdDSVAAVDQASHQSLvrslartdearGLLWLLEEEALVPGASEDTLLERlfsYYgpQEGDKKGQSPLLH 920
Cdd:cd14899 461 RWSFVDFP----NNRACLELFEHRPI-----------GIFSLTDQECVFPQGTDRALVAK---YY--LEFEKKNSHPHFR 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 921 SS----KPHHFLLGHSHGTnwVEYNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLflgRAGSATVLSGSIAGLEGGSQ 996
Cdd:cd14899 521 SApliqRTTQFVVAHYAGC--VTYTIDGFLAKNK-DSFCESAAQLLAGSSNPLIQAL---AAGSNDEDANGDSELDGFGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 997 LALRRATSmrktfttgmaAVKKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlps 1076
Cdd:cd14899 595 RTRRRAKS----------AIAAVSVGTQFKIQLNELLSTVRATTPRYVRCIKP--------------------------- 637
|
730 740 750 760
....*....|....*....|....*....|....*....|....*....
gi 42794779 1077 GDHCEAGLLQldVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRF 1125
Cdd:cd14899 638 NDSHVGSLFQ--STRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
419-1131 |
6.03e-33 |
|
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: 138.57 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKGCRRE----------DMAPHIYAVAQTAYRAMLMS 488
Cdd:cd14893 1 NVALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREQtplyekdtvnDAPPHVFALAQNALRCMQDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 489 RQDQSIILLGSSGSGKTTSCQHLVQYLATIA--------GISGNKVFSVEKWQAL--YTLLEAFGNSPTIINGNATRFSQ 558
Cdd:cd14893 81 GEDQAVILLGGMGAGKSEAAKLIVQYLCEIGdeteprpdSEGASGVLHPIGQQILhaFTILEAFGNAATRQNRNSSRFAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 559 ILSLDFDQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLAC--GDGTLRTELHLNHLAENnvFGIVPLAKPEEKQ 636
Cdd:cd14893 161 MISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGvqHDPTLRDSLEMNKCVNE--FVMLKQADPLATN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 637 KA--AQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEWAQKAAyllGCSLEELSSAIF 714
Cdd:cd14893 239 FAldARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQ---SCALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 715 -KHQHKGGTLQRSTSFRQGPEESGLGDGTGPKLSALECLEGMAA------GLYSELFTLLVSLVN--------RALKS-- 777
Cdd:cd14893 316 aAKLLEVEPVVLDNYFRTRQFFSKDGNKTVSSLKVVTVHQARKArdtfvrSLYESLFNFLVETLNgilggifdRYEKSni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 778 ---SQhslcSMMIVDTPGFQN--PEQGGsargasFEELCHNYTQDRLQRLFHERTFVQELERYKEE------------NI 840
Cdd:cd14893 396 vinSQ----GVHVLDMVGFENltPSQNS------FDQLCFNYWSEKVHHFYVQNTLAINFSFLEDEsqqvenrltvnsNV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 841 ELAFDD---LEPPTDDSVAAVDQASHQSLVRS----------LARTDEARGLLWlleeealvPGASEDTLLERLfsyygp 907
Cdd:cd14893 466 DITSEQekcLQLFEDKPFGIFDLLTENCKVRLpndedfvnklFSGNEAVGGLSR--------PNMGADTTNEYL------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 908 qeGDKKGQSPLlhsskphhFLLGHSHGTnwVEYNVTGwlnYTKQNPATQNA--PRLLQDSQkkiisNLFLGRAGSATVLS 985
Cdd:cd14893 532 --APSKDWRLL--------FIVQHHCGK--VTYNGKG---LSSKNMLSISStcAAIMQSSK-----NAVLHAVGAAQMAA 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 986 GSIAglEGGSQLALRRATS--MRKTFTTGMAAVK-KKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsas 1062
Cdd:cd14893 592 ASSE--KAAKQTEERGSTSskFRKSASSARESKNiTDSAATDVYNQADALLHALNHTGKNFLVCIKP------------- 656
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1063 srrvssssELDLPSGdhceagllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPH 1131
Cdd:cd14893 657 --------NETLEEG--------VFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYKNVCGH 709
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1263-1951 |
2.72e-32 |
|
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: 137.89 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1263 IQQLRSKLEKAEKERNELRLNSDRLESRISELTSE---LTDERNTGESASQLL----DAETAERLR----AEKEMKELQT 1331
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerLRREREKAERYQALLkekrEYEGYELLKekeaLERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1332 QYDALKKQMEVMEMEVM------EARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTK-KRLQQEFEDKLEVEQQNK 1404
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrlEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKL 1484
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1485 QREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDE-------ASLAKVKKQLRDLEAKVKDQEEE 1557
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEwkleqlaADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQAGTIQMLEqAKLRLEMEMERMRQTHSKEMESRDEEV---------------------------------EEARQSC 1604
Cdd:TIGR02169 485 LSKLQRELAEAE-AQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvvedDAVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1605 QKKLKQME----------------------------------VQLEEEYEDKQK-VLR---------EKRELEGK--LAT 1638
Cdd:TIGR02169 564 IELLKRRKagratflplnkmrderrdlsilsedgvigfavdlVEFDPKYEPAFKyVFGdtlvvedieAARRLMGKyrMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1639 LSDQ--------------------VNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSA--------PSKREIAQLKN 1690
Cdd:TIGR02169 644 LEGElfeksgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelsDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1691 QLEESEFTcAAAVKAR--------KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEI-----QNRLEEDQEDMNE 1757
Cdd:TIGR02169 724 EIEQLEQE-EEKLKERleeleedlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSK 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1758 LMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLE----F 1833
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKE------IENLNGKKEELEEELEeleaA 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1834 ERTQVKRLESLAS---RLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS------------ 1898
Cdd:TIGR02169 877 LRDLESRLGDLKKerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeelsledv 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1899 -RKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMESDENEDLINS 1951
Cdd:TIGR02169 957 qAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKlEEERKAILERIEE 1011
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
420-1129 |
3.50e-32 |
|
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: 135.25 E-value: 3.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKvMHMFKGCR-REDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQE-FHAKYRCKsRSDNAPHIFSVADSAYQDMLHHEEPQHIILSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAgiSGNKVfSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 578
Cdd:cd14882 81 ESYSGKTTNARLLIKHLCYLG--DGNRG-ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTLRteLHLNHLAENNVFGIVPLAKPEEKQKA----------AQQFSKLQAA 648
Cdd:cd14882 158 QLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNR--LKEYNLKAGRNYRYLRIPPEVPPSKLkyrrddpegnVERYKEFEEI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 649 MKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAgrkQFARHEWAQKAAYLLGCSLEELSSAIFKH-QHKGGTLQRSt 727
Cdd:cd14882 236 LKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGYA---ELENTEIASRVAELLRLDEKKFMWALTNYcLIKGGSAERR- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 sfRQGPEEsglgdgtgpklsALECLEGMAAGLYSELFTLLVSLVN------RALKSSQHSLcsmMIVDTPGFQNPEQGGs 801
Cdd:cd14882 312 --KHTTEE------------ARDARDVLASTLYSRLVDWIINRINmkmsfpRAVFGDKYSI---SIHDMFGFECFHRNR- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 802 argasFEELCHNYTQDRLQRLFHERTFVQELERYKEENI----------ELAFDDLEPPTDDSVAAVDQASHQslvrsla 871
Cdd:cd14882 374 -----LEQLMVNTLNEQMQYHYNQRIFISEMLEMEEEDIptinlrfydnKTAVDQLMTKPDGLFYIIDDASRS------- 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 872 rtdeargllwlleeealvpGASEDTLLERLfsyygpqegdKKGQSPLLHSSKPHHFLLGHshgtnwveynVTGWLNYTKQ 951
Cdd:cd14882 442 -------------------CQDQNYIMDRI----------KEKHSQFVKKHSAHEFSVAH----------YTGRIIYDAR 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 952 NPATQN----APRL---LQDSQKKIISNLFlgragsatvlsgsiagleGGSQlaLRRATSMRKTFttgmaavKKKSLCIQ 1024
Cdd:cd14882 483 EFADKNrdfvPPEMietMRSSLDESVKLMF------------------TNSQ--VRNMRTLAATF-------RATSLELL 535
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1025 MKLQVDAlidtiKKSKLHFVHCFLPVAEgwageprsassrrvsssselDLPSGDHCEagllqldvpLLRTQLRGSRLLDA 1104
Cdd:cd14882 536 KMLSIGA-----NSGGTHFVRCIRSDLE--------------------YKPRGFHSE---------VVRQQMRALAVLDT 581
|
730 740
....*....|....*....|....*
gi 42794779 1105 MRMYRQGYPDHMVFSEFRRRFDVLA 1129
Cdd:cd14882 582 AKARQKGFSYRIPFQEFLRRYQFLA 606
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1247-1962 |
7.12e-31 |
|
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: 133.26 E-value: 7.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEM 1326
Cdd:TIGR02168 225 LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1327 KELQTQYDALKKQMEV--MEMEVMEARLIRAAEIngevddddaggEWRLKYERAVREVDFtkkrlqQEFEDKLEVEQQNK 1404
Cdd:TIGR02168 305 QILRERLANLERQLEEleAQLEELESKLDELAEE-----------LAELEEKLEELKEEL------ESLEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQR--E 1482
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQAelE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1483 KLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEskdeASLAKVKKQLRDLEAKVKDQEEELDEQA 1562
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1563 GTIQMLEQ-----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEG 1634
Cdd:TIGR02168 520 GILGVLSElisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1635 KLATLSDQVnrrdfESEKRLRKDLKrtkALLA------DAQLMLDHLKNSAPSKReIAQLKNQLEESEFTCAAAVKARKA 1708
Cdd:TIGR02168 600 FLGVAKDLV-----KFDPKLRKALS---YLLGgvlvvdDLDNALELAKKLRPGYR-IVTLDGDLVRPGGVITGGSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1709 ----MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1784
Cdd:TIGR02168 671 sileRRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1785 EANKEKQELQEKLQALQSQVEFLEQSMV-DKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRI 1863
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAeAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1864 AAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED-EMES 1942
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRElESKR 910
|
730 740
....*....|....*....|
gi 42794779 1943 DENEDLINSEGDSDVDSELE 1962
Cdd:TIGR02168 911 SELRRELEELREKLAQLELR 930
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1261-1938 |
8.42e-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: 132.99 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1261 EEI-QQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDErntgESASQLLDAEtaeRLRAEKEMKELQTQYDALKKQ 1339
Cdd:pfam01576 74 EEIlHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEE----EAARQKLQLE---KVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1340 MEVMEMEVMEARLiRAAEINGEVDDDDAG----GEWRLKYERAVREVDftkKRLQQEFEDKLEVEQqNKRQLERRLGDLQ 1415
Cdd:pfam01576 147 NSKLSKERKLLEE-RISEFTSNLAEEEEKakslSKLKNKHEAMISDLE---ERLKKEEKGRQELEK-AKRKLEGESTDLQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1416 ADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEA 1495
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1496 FSLKQQLEEkdmdiagfTQKVVSLEAELQdissqeSKDEASLAKVKK-----------QLRDLEAKVKDQEEELDEQagt 1564
Cdd:pfam01576 302 EALKTELED--------TLDTTAAQQELR------SKREQEVTELKKaleeetrsheaQLQEMRQKHTQALEELTEQ--- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1565 iqmLEQAKlRLEMEMERMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS- 1640
Cdd:pfam01576 365 ---LEQAK-RNKANLEKAKQALESENAELQAELrtlQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQs 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1641 --DQVNRRDFESEK---RLRKDLKRTKALLADAQLML-------------------------DHLKNSAPSKREI----- 1685
Cdd:pfam01576 441 elESVSSLLNEAEGkniKLSKDVSSLESQLQDTQELLqeetrqklnlstrlrqledernslqEQLEEEEEAKRNVerqls 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1686 ------AQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----------KNEIQNRLE 1749
Cdd:pfam01576 521 tlqaqlSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElddllvdldhQRQLVSNLE 600
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1750 EDQEDMNELMKKHKAAVAQAS--RDLAQIN---------DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM--VDKSL 1816
Cdd:pfam01576 601 KKQKKFDQMLAEEKAISARYAeeRDRAEAEareketralSLARALEEALEAKEELERTNKQLRAEMEDLVSSKddVGKNV 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1817 VSRQEAKiRELETRLEFERTQVKRLESLAS-------RLKENMEKLTEERDQRIAAENREKEQNKR-LQRQLRDTKEEMG 1888
Cdd:pfam01576 681 HELERSK-RALEQQVEEMKTQLEELEDELQatedaklRLEVNMQALKAQFERDLQARDEQGEEKRRqLVKQVRELEAELE 759
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1889 ELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1938
Cdd:pfam01576 760 DERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKD 809
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
421-841 |
1.56e-30 |
|
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: 130.39 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 421 VLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKGCRRE-----DMAPHIYAVAQTAYRAMLMSRQDQSI 494
Cdd:cd14886 3 VIDILRDRFAKDKIYTYAGKLLVALNPfKQIRNLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 495 ILLGSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQALytLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASAS 574
Cdd:cd14886 83 IVSGESGAGKTETAKQLMNFFAYGHSTSSTDVQSLILGSNP--LLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 575 IQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENNVF--GIVPLAKPEEKQKaaqQFSKLQAAMKVL 652
Cdd:cd14886 161 ITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLnaSKCYDAPGIDDQK---EFAPVRSQLEKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 653 gISPDEQKACWFILAAIYHLG--------AAGATKEAAEAGRKQFarhewaQKAAYLLGCSLEELSSAIfkhqhkggtLQ 724
Cdd:cd14886 238 -FSKNEIDSFYKCISGILLAGniefseegDMGVINAAKISNDEDF------GKMCELLGIESSKAAQAI---------IT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 725 RSTSFRQGPEESGLgdgtgPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 804
Cdd:cd14886 302 KVVVINNETIISPV-----TQAQAEVNIRAVAKDLYGALFELCVDTLNEIIQFDADARPWIGILDIYGFEFFERN----- 371
|
410 420 430
....*....|....*....|....*....|....*..
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE 841
Cdd:cd14886 372 -TYEQLLINYANERLQQYFINQVFKSEIQEYEIEGID 407
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1386-1937 |
2.19e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.60 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1386 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1465
Cdd:COG1196 223 KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR 1545
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1546 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKV 1625
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE-LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1626 LREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLD-----HLKNSAPSKREIAQLKNQLEESEFTCA 1700
Cdd:COG1196 462 LELLAELLEEAALLEAALAELL-EELAEAAARLLLLLEAEADYEGFLEgvkaaLLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1701 AAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQ 1780
Cdd:COG1196 541 EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1781 AQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD 1860
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1861 QRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1937
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
419-1130 |
2.10e-29 |
|
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: 126.52 E-value: 2.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVmhmFKGCrredmapHIYAVAQTAYRAML-MSRQDQSIILL 497
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLV---IKKC-------HISGVAENALDRIKsMSSNAESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 498 GSSGSGKTTSCQHLVQYLATiagiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQT 577
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS----QPKSKVTTKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 578 MLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLaeNNVFGIVPLAKPEEKQKAAQQFSKLQAAMKVLGISPD 657
Cdd:cd14874 147 VPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGL--QKFFYINQGNSTENIQSDVNHFKHLEDALHVLGFSDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 658 EQKACWFILAAIYHLG--------AAGATKEAAEAGrkQFARHEWaqkAAYLLGCSLEELSSAIFKHQHKGGTLQRStsf 729
Cdd:cd14874 225 HCISIYKIISTILHIGniyfrtkrNPNVEQDVVEIG--NMSEVKW---VAFLLEVDFDQLVNFLLPKSEDGTTIDLN--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 730 rqgpeesglgdgtgpklSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSlCSMMIVDTPGFQNPEQGGsargasFEE 809
Cdd:cd14874 297 -----------------AALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHT-GVISILDHYGFEKYNNNG------VEE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 810 LCHNYTQDRLQRLFHERTFVQELERYKEENIELAFDDLEPPTDDSVAAVDQASHQSLVRSLarTDEARgllwlleeealV 889
Cdd:cd14874 353 FLINSVNERIENLFVKHSFHDQLVDYAKDGISVDYKVPNSIENGKTVELLFKKPYGLLPLL--TDECK-----------F 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 890 PGASEDTLLERL------FSYYGPQEGDKKGQspllhsskphhFLLGHSHGTNWveYNVTGWLNYTKQNpATQNAPRLLQ 963
Cdd:cd14874 420 PKGSHESYLEHCnlnhtdRSSYGKARNKERLE-----------FGVRHCIGTTW--YNVTDFFSRNKRI-ISLSAVQLLR 485
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 964 DSQKKIISNLFLGRAGSATVLSGSIAgleggsQLALRRATSmrktfttgmaavkkkslciqmklqvdaLIDTIKKSKLHF 1043
Cdd:cd14874 486 SSKNPIIGLLFESYSSNTSDMIVSQA------QFILRGAQE---------------------------IADKINGSHAHF 532
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1044 VHCflpvaegwageprsassrrvsssseldLPSGDHCEAGllQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRR 1123
Cdd:cd14874 533 VRC---------------------------IKSNNERQPK--KFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFAR 583
|
....*..
gi 42794779 1124 RFDVLAP 1130
Cdd:cd14874 584 QYRCLLP 590
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1266-1951 |
4.63e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.98 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1266 LRSKLEKAEKERNELRLNSDRLESRISELtseltdERNTGESASQlldAETAERLRaekemkELQTQYDALKKQMEVMEM 1345
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLEDILGEL------ERQLEPLERQ---AEKAERYR------ELKEELKELEAELLLLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1346 EVMEARLIRAAEINGEVDDDDAggewRLKYERAVREVDFTKKRLQ-QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRA 1424
Cdd:COG1196 235 RELEAELEELEAELEELEAELE----ELEAELAELEAELEELRLElEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1425 LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEE 1504
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1505 KDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ 1584
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1585 THSKEMESRDEEVEEARQscQKKLKQMEVQLEEEYEDK-QKVLREKRELEGKLATLSDQVNRRDfesEKRLRKDLkrtkA 1663
Cdd:COG1196 471 EAALLEAALAELLEELAE--AAARLLLLLEAEADYEGFlEGVKAALLLAGLRGLAGAVAVLIGV---EAAYEAAL----E 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1664 LLADAQLMLDHLKNSAPSKREIAQLK-NQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKN 1742
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKaAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1743 EIQNRLEEDQEDM-NELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEklqalqsqvefleqsmvdkslvsRQE 1821
Cdd:COG1196 622 LLGRTLVAARLEAaLRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL-----------------------EAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1822 AKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrkK 1901
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALE---E 755
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1902 HELEMDLESLEAANQSLQADLklafKRIGDL-QAAIE--DEME------SDENEDLINS 1951
Cdd:COG1196 756 LPEPPDLEELERELERLEREI----EALGPVnLLAIEeyEELEerydflSEQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1253-1953 |
4.75e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 127.48 E-value: 4.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1332
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKKQMevmemevmearliraAEINGEVDdddaggewrlkyeravrevdftkkrlqqEFEDKLEVEQQNKRQLERRLG 1412
Cdd:TIGR02168 339 LAELEEKL---------------EELKEELE----------------------------SLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1413 DLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQR--EKLQREKDM 1490
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI----EELLKKLEEAELKELQAelEELEEELEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1491 LLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ 1570
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQAR----LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1571 -----AKLRLEMEM---ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ 1642
Cdd:TIGR02168 528 lisvdEGYEAAIEAalgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1643 VnrrdfESEKRLRKDLkrtKALLA------DAQLMLDHLKNSAPS-------------------------------KREI 1685
Cdd:TIGR02168 608 V-----KFDPKLRKAL---SYLLGgvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssilerRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1686 AQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA 1765
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1766 VAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKS-LVSRQEAKIRELETRLEFERTQVKRLESL 1844
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaELTLLNEEAANLRERLESLERRIAATERR 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1845 ASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKL 1924
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
730 740 750
....*....|....*....|....*....|
gi 42794779 1925 AFKRIGDLQAAIED-EMESDENEDLINSEG 1953
Cdd:TIGR02168 920 LREKLAQLELRLEGlEVRIDNLQERLSEEY 949
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
472-1135 |
5.27e-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: 125.69 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 472 PHIYAVAQTAYRAMLM-SRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGI-SGN--------KVFSVEKWQAlyTLLEA 541
Cdd:cd14875 56 PHIWQVAHKAFNAIFVqGLGNQSVVISGESGSGKTENAKMLIAYLGQLSYMhSSNtsqrsiadKIDENLKWSN--PVMES 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 542 FGNSPTIINGNATRFSQILSLDFDQA-GQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGD-------GTLRTEL 613
Cdd:cd14875 134 FGNARTVRNDNSSRFGKYIKLYFDPTsGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSpeekkelGGLKTAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 614 HLNHLAENNVFgiVPLAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaaeagrkQFARHE 693
Cdd:cd14875 214 DYKCLNGGNTF--VRRGVDGKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-------QNDKAQ 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 694 WAQKAAYLLGCSLEELSSAIFKHQHkggtLQRS-----TSFRQGPEESGLGDgtgpklsalecleGMAAGLYSELFTLLV 768
Cdd:cd14875 285 IADETPFLTACRLLQLDPAKLRECF----LVKSktslvTILANKTEAEGFRN-------------AFCKAIYVGLFDRLV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 769 SLVNRALKSSQH-SLCSMM-IVDTPGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIE---LA 843
Cdd:cd14875 348 EFVNASITPQGDcSGCKYIgLLDIFGFENFTRN------SFEQLCINYANESLQNHYNKYTFINDEEECRREGIQipkIE 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 844 FddlePPTDDSVAAVDQAShqslVRSLARTDEargllwlleeEALVPGASEDTLLERLFSYYGpqegdkkGQSPLL---H 920
Cdd:cd14875 422 F----PDNSECVNMFDQKR----TGIFSMLDE----------ECNFKGGTTERFTTNLWDQWA-------NKSPYFvlpK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 921 SSKPHHFllGHSHGTNWVEYNVTGWLNytKQNPA-TQNAPRLLQDSQKKIISNLFLGRAGSAtvlsgsiagleggsqlal 999
Cdd:cd14875 477 STIPNQF--GVNHYAAFVNYNTDEWLE--KNTDAlKEDMYECVSNSTDEFIRTLLSTEKGLA------------------ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1000 RRatsmrktfttgmaavkKKSLCIQMKLQVDALIDTIKKSKLHFVHCFLPvaegwageprsassrrvsssseldlpsgdH 1079
Cdd:cd14875 535 RR----------------KQTVAIRFQRQLTDLRTELESTETQFIRCIKP-----------------------------N 569
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1080 CEAGLLQLDVPLLRTQLRGSRLLDAMRMYRQGYPDHMVFSEFRRRFDVLAPHLTKK 1135
Cdd:cd14875 570 MEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTAS 625
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
421-1049 |
3.10e-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: 123.17 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 421 VLHTLRQRYGASLLHTYAGPSLLVLGP---------------RGAPAVysekvmhmfkgcrrEDMAPHIYAVAQTAYRAM 485
Cdd:cd14876 3 VLDFLKHRYLKNQIYTTADPLLVAINPfkdlgnatdewirkyRDAPDL--------------TKLPPHVFYTARRALENL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 486 LMSRQDQSIILLGSSGSGKTTSCQHLVQYLAtiAGISGNKVFSVEKW-QALYTLLEAFGNSPTIINGNATRFSQILSLDF 564
Cdd:cd14876 69 HGVNKSQTIIVSGESGAGKTEATKQIMRYFA--SAKSGNMDLRIQTAiMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 565 DQAGQVASASIQTMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLNHLAENN--------VFGIVPLAkpeekq 636
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKflnpkcldVPGIDDVA------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 637 kaaqQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAGATKEaAEAGRKQFARHEWAQKAAYLLGCSL-----EELSS 711
Cdd:cd14876 221 ----DFEEVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK-TEQGVDDAAAISNESLEVFKEACSLlfldpEALKR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 712 AIF-KHQHKGGtlQRSTSFRQGPEESGLgdgtgpKLSaleclegMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDT 790
Cdd:cd14876 296 ELTvKVTKAGG--QEIEGRWTKDDAEML------KLS-------LAKAMYDKLFLWIIRNLNSTIEPPGGFKNFMGMLDI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 791 PGFQNPEQGgsargaSFEELCHNYTQDRLQRLFHERTFVQELERYKEENI---ELAFDDLEPPTD------DSVAAV--D 859
Cdd:cd14876 361 FGFEVFKNN------SLEQLFINITNEMLQKNFIDIVFERESKLYKDEGIptaELEYTSNAEVIDvlcgkgKSVLSIleD 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 860 QAshqslvrsLArtdeargllwlleeealvPGASEdtllERLFSYYGPQEGDKKGQSPLLHSSKpHHFLLGHSHGTnwVE 939
Cdd:cd14876 435 QC--------LA------------------PGGSD----EKFVSACVSKLKSNGKFKPAKVDSN-INFIVVHTIGD--IQ 481
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 940 YNVTGWLNYTKqNPATQNAPRLLQDSQKKIISNLFLGragsATVLSGSIA-GLEGGSQLalrratsMRktfttgmaavkk 1018
Cdd:cd14876 482 YNAEGFLFKNK-DVLRAELVEVVQASTNPVVKALFEG----VVVEKGKIAkGSLIGSQF-------LK------------ 537
|
650 660 670
....*....|....*....|....*....|.
gi 42794779 1019 kslciqmklQVDALIDTIKKSKLHFVHCFLP 1049
Cdd:cd14876 538 ---------QLESLMGLINSTEPHFIRCIKP 559
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1238-1922 |
9.51e-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: 122.98 E-value: 9.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1238 KLFTTVRPLIEVQLSEEQIRNKDEEiqQLRSKLEKA----EKERNELRLNSDRLESRISELTSELTDERNTGESASQLLD 1313
Cdd:pfam01576 176 KSLSKLKNKHEAMISDLEERLKKEE--KGRQELEKAkrklEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1314 AETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIR----------AAEINGEVDDDDAGGEWRLKYERAVREVd 1383
Cdd:pfam01576 254 EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRrdlgeelealKTELEDTLDTTAAQQELRSKREQEVTEL- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1384 ftKKRLQQE---FEDKL-EVEQQNKRQLErrlgDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK 1459
Cdd:pfam01576 333 --KKALEEEtrsHEAQLqEMRQKHTQALE----ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1460 QRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAK 1539
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLN 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1540 VKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEY 1619
Cdd:pfam01576 487 LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK-KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1620 EDKQKVLREKRELEGKLATLS-DQVNRRDFES--EKRLRK---DLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQL 1692
Cdd:pfam01576 566 AAYDKLEKTKNRLQQELDDLLvDLDHQRQLVSnlEKKQKKfdqMLAEEKAISARYAEERDRAEAEAREKETRAlSLARAL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1693 EESEFTCAAAVKARKAMEVEIEDLHLQIDDIAK-------AKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA 1765
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKDDVGKnvhelerSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1766 VAQASRdlaqinDLQAQlEEANKEKQelqeklQALQSQVefleqsmvdkslvsrqeakiRELETRLEFERTQvkrlESLA 1845
Cdd:pfam01576 726 KAQFER------DLQAR-DEQGEEKR------RQLVKQV--------------------RELEAELEDERKQ----RAQA 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1846 SRLKENMEKLTEERDQRIAAENREKE----QNKRLQRQLRDTKEEMGE--LARKEAEASRKkhELEMDLESLEAANQSLQ 1919
Cdd:pfam01576 769 VAAKKKLELDLKELEAQIDAANKGREeavkQLKKLQAQMKDLQRELEEarASRDEILAQSK--ESEKKLKNLEAELLQLQ 846
|
...
gi 42794779 1920 ADL 1922
Cdd:pfam01576 847 EDL 849
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1391-1976 |
2.27e-27 |
|
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: 122.09 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1391 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1470
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1471 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEA--------------S 1536
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqletlrskvaqlelQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1537 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEM---------------ESRDEEVEEAR 1601
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqeelerleealEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1602 QSCQKK-------------LKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVN-RRDFES--EKRLRKDL------- 1658
Cdd:TIGR02168 475 QALDAAerelaqlqarldsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvDEGYEAaiEAALGGRLqavvven 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1659 ----KRTKALLADAQ------LMLDHLKNSAPSKREIAQLKNQlEESEFTCAAAVKARKAMEVEIEDL--HLQI-DDIAK 1725
Cdd:TIGR02168 555 lnaaKKAIAFLKQNElgrvtfLPLDSIKGTEIQGNDREILKNI-EGFLGVAKDLVKFDPKLRKALSYLlgGVLVvDDLDN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1726 A----------------------------KTALEEQLSRLQREKN--EIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ 1775
Cdd:TIGR02168 634 AlelakklrpgyrivtldgdlvrpggvitGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1776 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSL-VSRQEAKIRELETRLEFERTQVKRLEslasrlkENMEK 1854
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeLTELEAEIEELEERLEEAEEELAEAE-------AEIEE 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1855 LTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQA 1934
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 42794779 1935 A---IEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNK 1976
Cdd:TIGR02168 867 LieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
420-860 |
4.42e-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: 119.63 E-value: 4.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMF-------KGCRREDMAPHIYAVAQTAYRAMLMSRQD 491
Cdd:cd14884 2 NVLQNLKNRYLKNKIYTFHASLLLALNPyKPLKELYDQDVMNVYlhkksnsAASAAPFPKAHIYDIANMAYKNMRGKLKR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 492 QSIILLGSSGSGKTTSCQHLVQYLATIAGISgNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQ----- 566
Cdd:cd14884 82 QTIVVSGHSGSGKTENCKFLFKYFHYIQTDS-QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 567 ----AGQVASASIQTMLLEKLRVARRPASEATFNVFYYLL-ACGDgtlrTELHLNHLAEN-NVFGIVPLAK--------- 631
Cdd:cd14884 161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLrGLSD----EDLARRNLVRNcGVYGLLNPDEshqkrsvkg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 632 ------------PEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYHLGAAgATKEAAEagrkqfarhewaqkaa 699
Cdd:cd14884 237 tlrlgsdsldpsEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNR-AYKAAAE---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 700 yLLGCSLEELSSAIfkhqhKGGTLQRSTSFRQGPEEsglgdgtgpKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQ 779
Cdd:cd14884 300 -CLQIEEEDLENVI-----KYKNIRVSHEVIRTERR---------KENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCK 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 780 HSLCSM------------MIVDTPGFQnpeqggSARGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIeLAFDDL 847
Cdd:cd14884 365 EKDESDnediysineaiiSILDIYGFE------ELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENI-ICCSDV 437
|
490
....*....|...
gi 42794779 848 EPPTDDSVAAVDQ 860
Cdd:cd14884 438 APSYSDTLIFIAK 450
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
419-974 |
2.52e-25 |
|
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: 113.96 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 419 SSVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYsekvMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLatIAGISGNKVFSVEKWQALYtLLEAFGNSPTIINGNATRFSQILSLDFDQAGQVASASIQTM 578
Cdd:cd14937 77 ESGSGKTEASKLVIKYY--LSGVKEDNEISNTLWDSNF-ILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSSSIEIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 579 LLEKLRVARRPASEATFNVFYYLLACGDGTL------RTELHLNHLAENNVfgIVPlakpeeKQKAAQQFSKLQAAMKVL 652
Cdd:cd14937 154 LLENIRVVSQEEEERGYHIFYQIFNGMSQELknkykiRSENEYKYIVNKNV--VIP------EIDDAKDFGNLMISFDKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 653 GISpDEQKACWFILAAIYHLG-------AAGATKEAAEAGRKQFarhEWAQKAAYLLGCSLEEL-SSAIFKHQhkgGTLQ 724
Cdd:cd14937 226 NMH-DMKDDLFLTLSGLLLLGnveyqeiEKGGKTNCSELDKNNL---ELVNEISNLLGINYENLkDCLVFTEK---TIAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 725 RSTSFRQGPEESglgdgtgpklsaLECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLCSMMIVDTPGFQNPEQGgsarg 804
Cdd:cd14937 299 QKIEIPLSVEES------------VSICKSISKDLYNKIFSYITKRINNFLNNNKELNNYIGILDIFGFEIFSKN----- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 805 aSFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafDDLEPPTDDSVaaVDQASHQSLVRSLARtDEARGllwlle 884
Cdd:cd14937 362 -SLEQLLINIANEEIHSIYLYIVYEKETELYKAEDILI--ESVKYTTNESI--IDLLRGKTSIISILE-DSCLG------ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 885 eealvPGASEDTLLERLFSYYGPQEGDKKGQSPLLHSskphhFLLGHShgTNWVEYNVTGWLNYTKQNPATqNAPRLLQD 964
Cdd:cd14937 430 -----PVKNDESIVSVYTNKFSKHEKYASTKKDINKN-----FVIKHT--VSDVTYTITNFISKNKDILPS-NIVRLLKV 496
|
570
....*....|
gi 42794779 965 SQKKIISNLF 974
Cdd:cd14937 497 SNNKLVRSLY 506
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1248-1862 |
1.81e-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: 112.46 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1327
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQMEVMEMEVMEARlIRAAEINGEVD--DDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKleveQQNKR 1405
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLE-ARLERLEDRRErlQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1406 QLERRLGDLQADSEESQRALQQLKKKCQRLTAE---LQDTKLHLEGQQ--VRNHELEKKQR-----------RFDSELSQ 1469
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSegVKALLKNQSGLsgilgvlseliSVDEGYEA 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1470 AHEEAQREKLQREKLQREKDMLLAEAFsLKQ-----------------QLEEKDMDI-------AGFTQKVVSLEAELQD 1525
Cdd:TIGR02168 538 AIEAALGGRLQAVVVENLNAAKKAIAF-LKQnelgrvtflpldsikgtEIQGNDREIlkniegfLGVAKDLVKFDPKLRK 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1526 --------------------------------------------ISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1561
Cdd:TIGR02168 617 alsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1562 AGTIQMLEQAKLRLEMEME-------RMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE 1628
Cdd:TIGR02168 697 EKALAELRKELEELEEELEqlrkeleELSRQISalrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1629 KRELEGKLATLSDQVNR--RDFESEKR----LRKDLKRTKALLADAQLML-DHLKNSAPSKREIAQLKNQLEESEFTCAA 1701
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQlkEELKALREaldeLRAELTLLNEEAANLRERLeSLERRIAATERRLEDLEEQIEELSEDIES 856
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1702 AVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA---VAQASRDLAQI-N 1777
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELrekLAQLELRLEGLeV 936
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1778 DLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslVSRQEAKI--------------RELETRLEFERTQVKRLES 1843
Cdd:TIGR02168 937 RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR--LKRLENKIkelgpvnlaaieeyEELKERYDFLTAQKEDLTE 1014
|
730
....*....|....*....
gi 42794779 1844 LASRLKENMEKLTEERDQR 1862
Cdd:TIGR02168 1015 AKETLEEAIEEIDREARER 1033
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1173-1956 |
3.02e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 112.16 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1173 RAGTLARLEEQRDEQTSRNLTLF---QAACRGYLARQHFKKRKIQDlAIRCVQ----KNIKKNKGVKDWPWWKLFTTVRP 1245
Cdd:PTZ00121 1135 KAEDARKAEEARKAEDAKRVEIArkaEDARKAEEARKAEDAKKAEA-ARKAEEvrkaEELRKAEDARKAEAARKAEEERK 1213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1246 LIEVQLSEEQIR----NKDEEIQQLRSKLEKAEKERNE---LRLNSDRLESRISELTSELTDERNTGESASQLLDAETAE 1318
Cdd:PTZ00121 1214 AEEARKAEDAKKaeavKKAEEAKKDAEEAKKAEEERNNeeiRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1319 RLRAEKEMKELqtqyDALKKQMEVMEMEVMEARliRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLE 1398
Cdd:PTZ00121 1294 EAKKAEEKKKA----DEAKKKAEEAKKADEAKK--KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1399 VEQQNKRQLERRLGDLQADSEESQRAlQQLKKKCQRLTAELQDTKlHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQR 1476
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKaeEKKKADEAKKKAEEAKK 1445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1477 EKLQREKLQREKdmllaEAFSLKQQLEEKDmdiagftqkvvsleaelqdiSSQESKDEASLAKVKKQLRDLEAKVKDQEE 1556
Cdd:PTZ00121 1446 ADEAKKKAEEAK-----KAEEAKKKAEEAK--------------------KADEAKKKAEEAKKADEAKKKAEEAKKKAD 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1557 ELDEQAGTIQMLEQAKlrlEMEMERMRQTHSKEMESRdeEVEEARQSCQKKlKQMEVQLEEEY---EDKQKVLREKRELE 1633
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAK---KAEEAKKADEAKKAEEAK--KADEAKKAEEKK-KADELKKAEELkkaEEKKKAEEAKKAEE 1574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1634 GKL-----ATLSDQVNRRDFESEKRLRKDLKRTKALLA----DAQLMLDHLKNSAPSKREIAQLKNQLEES--------- 1695
Cdd:PTZ00121 1575 DKNmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEkkkaeelkk 1654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1696 ---EFTCAAAVKARKAME--VEIEDLHLQIDDIAKAktalEEQLSRLQREK---NEIQNRLEEDQEDMNELMKKHKAAVA 1767
Cdd:PTZ00121 1655 aeeENKIKAAEEAKKAEEdkKKAEEAKKAEEDEKKA----AEALKKEAEEAkkaEELKKKEAEEKKKAEELKKAEEENKI 1730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTqVKRLESLASR 1847
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK-IKDIFDNFAN 1809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1848 LKE---------NMEKLTE--ERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQ 1916
Cdd:PTZ00121 1810 IIEggkegnlviNDSKEMEdsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADE 1889
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 42794779 1917 SLQADLKlafkrigDLQAAIEDEMESDENEDLINSEGDSD 1956
Cdd:PTZ00121 1890 IEKIDKD-------DIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1248-1969 |
1.71e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.46 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRL--ESRISELTSELTDERNTgESASQLLDAETAERLRAEKE 1325
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKaeDARKAEEARKAEDAKRV-EIARKAEDARKAEEARKAED 1174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1326 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggewRLKYERAVREVdftkkrlqQEFEDKLEVEQQnKR 1405
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKAEELRKAEDARKAEAAR--------------KAEEERKAEEA--------RKAEDAKKAEAV-KK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1406 QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK--QRRFDSELSQAHEEAQREKLQREK 1483
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKaeEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1484 LQREKdmllAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQA 1562
Cdd:PTZ00121 1312 EEAKK----ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKA 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1563 GTIQMLEQAKLRLEMEMERMRQTHSKEMESRdeEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ 1642
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKADELKKAAAAKK--KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1643 VNRRDFESEKRLRKDLKR----TKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCA-AAVKARKAMEVEIEDLH 1717
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKkadeAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAkKAEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1718 LQIDDIAKA---KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQ 1794
Cdd:PTZ00121 1546 KKADELKKAeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1795 EKLQALQSQVEFLEQSMVDKslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1874
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEE---KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1875 RLQR-------------QLRDTKEE----MGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1937
Cdd:PTZ00121 1703 KAEElkkkeaeekkkaeELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
730 740 750
....*....|....*....|....*....|...
gi 42794779 1938 DEM-ESDENEDLINSEGDSDVDSELEDRVDGVK 1969
Cdd:PTZ00121 1783 EELdEEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1374-1899 |
3.89e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.84 E-value: 3.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1374 KYERAVREVDFTKKRLQqEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN 1453
Cdd:PRK03918 225 KLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1454 hELEKKQRRFDSELSQAHEEAQ--REKLQ-REKLQREKDMLLAEAFSLKQQLEEKDMDIAGFtQKVVSLEAELQDISSQE 1530
Cdd:PRK03918 304 -EYLDELREIEKRLSRLEEEINgiEERIKeLEEKEERLEELKKKLKELEKRLEELEERHELY-EEAKAKKEELERLKKRL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1531 SkdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSK----EMESRDEEVEEARQSCQK 1606
Cdd:PRK03918 382 T--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1607 KLKQMEVQLEEEYEDKQKVLREKRELEGKLatlsdqvnrrdfESEKRLRKDLKrtkalladaqlMLDHLKN--SAPSKRE 1684
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVL------------KKESELIKLKE-----------LAEQLKEleEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1685 IAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHlQIDDIAKAKTALEEQLSRLQREKNEIQNRL--------EEDQEDMN 1756
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfesvEELEERLK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1757 ELMKKH------KAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLvSRQEAKIRELETR 1830
Cdd:PRK03918 596 ELEPFYneylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYLELSRE 674
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1831 LEFERTQVKRLESLASRLKENMEKLTEERDQRiaaeNREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1899
Cdd:PRK03918 675 LAGLRAELEELEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKALERVEELREKVKKYKALLKE 739
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
420-848 |
5.27e-23 |
|
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: 106.72 E-value: 5.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP-RGAPAVYSEKVMHMFKgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLG 498
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPlRYLPFLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 499 SSGSGKTTSCQHLVQYLATIAgisgnkvFSVEKWQALYTL-----LEAFGNSPTIINGNATRFSQILSLDFDQAGQVASA 573
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTD-------LSRSKYLRDYILesgiiLESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 574 SIQTMLLEKLRVARRPASEATFNVFYYLLacgDGTLRTELHLNHLAENNVF------GIVPLAKPEEKqkaaQQFSKLQA 647
Cdd:cd14905 153 KLYSYFLDENRVTYQNKGERNFHIFYQFL---KGITDEEKAAYQLGDINSYhylnqgGSISVESIDDN----RVFDRLKM 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 648 AMKVLGISPDEQKACWFILAAIYHLGAAGATKEAAEAGRKQFARHEwaqkaayllgcsleelssaifkhqhkggTLQRST 727
Cdd:cd14905 226 SFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNGKTEVKDRTLIE----------------------------SLSHNI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 728 SFRQGPEESGL-GDGTGPKLSALECLEGMAAGLYSELFTLLVSLVNRALKSSQHSLcSMMIVDTPGFQNPEQGGsargas 806
Cdd:cd14905 278 TFDSTKLENILiSDRSMPVNEAVENRDSLARSLYSALFHWIIDFLNSKLKPTQYSH-TLGILDLFGQESSQLNG------ 350
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 42794779 807 FEELCHNYTQDRLQRLFHERTFVQELERYKEENI----ELAFDDLE 848
Cdd:cd14905 351 YEQFSINFLEERLQQIYLQTVLKQEQREYQTERIpwmtPISFKDNE 396
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1390-1975 |
1.45e-22 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 105.49 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1390 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQR--RFDSEL 1467
Cdd:TIGR04523 35 EKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN---------DKLKKNKDKinKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1468 SQAHEEAQREKLQREKLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKdeaslakVKKQLRDL 1547
Cdd:TIGR04523 106 SKINSEIKNDKEQKNKLEVELN-------KLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-------LKKQKEEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1548 EAKVKDQEEELDEQAGTIQMLEQAKLRLEMEM---ERMRQTHsKEMESRDEEVEEARQSCQKKLKQmevqLEEEYEDKQK 1624
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKN-KSLESQISELKKQNNQLKDNIEK----KQQEINEKTT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1625 VLREKRElegKLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESeftCAAAVK 1704
Cdd:TIGR04523 247 EISNTQT---QLNQLKDE-QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKS------EISDLNNQKEQD---WNKELK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 AR-KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKN-------EIQNRLEEDQEDMnELMKKHKAAVAQASRDL-AQ 1775
Cdd:TIGR04523 314 SElKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEI-EKLKKENQSYKQEIKNLeSQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1776 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KSLVSRQ--------------EAKIRELETRLEFERTQVKR 1840
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERlKETIIKNnseikdltnqdsvkELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1841 LESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1920
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1921 DLKLAF--KRIGDLQAAIEDEMESDENEDLINSEGDSDVDsELEDRVDGVKSWLSKN 1975
Cdd:TIGR04523 553 ELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELID-QKEKEKKDLIKEIEEK 608
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1248-1830 |
1.51e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 105.79 E-value: 1.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1327
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREvdftkkrlQQEFEDKLEVEQQNKRQL 1407
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE--------LLEALRAAAELAAQLEEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1408 ERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQRE 1487
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1488 KDMLLAEAFSLKQQLEEKDmdiaGFTQKVVSLEAELQdissqeskdEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQM 1567
Cdd:COG1196 486 LAEAAARLLLLLEAEADYE----GFLEGVKAALLLAG---------LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIV 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1568 LEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRD 1647
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1648 FESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEIEDLHLQIDDIAKAK 1727
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL---EELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1728 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK----AAVAQASRDLAQINDLQAQLEEANK--------------E 1789
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEReiealgpvnllaieE 789
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 42794779 1790 KQELQEKLQALQSQVEFLEQSMvdKSLVSRqeakIRELETR 1830
Cdd:COG1196 790 YEELEERYDFLSEQREDLEEAR--ETLEEA----IEEIDRE 824
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1248-1877 |
3.02e-22 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 104.33 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMK 1327
Cdd:TIGR04523 111 EIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQMEVMEMEVMEARLIRAaEINgevddddaggewrlKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQL 1407
Cdd:TIGR04523 191 KIKNKLLKLELLLSNLKKKIQKNKSLES-QIS--------------ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1408 E----------RRLGDLQADSEESQRALQQLKKKCQRLTAELQDtkLHLEGQQVRNHEL-------EKKQRRFDSELSQA 1470
Cdd:TIGR04523 256 NqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD--LNNQKEQDWNKELkselknqEKKLEEIQNQISQN 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1471 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagftqkvvslEAELQDISSQESKDEASLAKVKKQLRDLEAK 1550
Cdd:TIGR04523 334 NKIISQLNEQISQLKKELTNSESENSEKQRELEEK--------------QNEIEKLKKENQSYKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1551 VKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEE---EYED 1621
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseiKDLTNQDSVKELIIKNLDNTRESLETQLKVlsrSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1622 -KQKVLREKRELEGKLATLsDQVNRRDFESEKRLrKDLKRTKALLADAQLMLDHLKNSApsKREIAQLKNQLEESEFTca 1700
Cdd:TIGR04523 480 iKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKV-KDLTKKISSLKEKIEKLESEKKEK--ESKISDLEDELNKDDFE-- 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1701 aavkarkameveiedlhLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQ 1780
Cdd:TIGR04523 554 -----------------LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1781 AQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEA--KIRELETRL-EFERTQVKRLESLASRLKEN 1851
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketIKEIRNKWPEIikKIKESKTKIdDIIELMKDWLKELSLHYKKY 696
|
650 660
....*....|....*....|....*...
gi 42794779 1852 MEKLTEERDQRIAAENRE--KEQNKRLQ 1877
Cdd:TIGR04523 697 ITRMIRIKDLPKLEEKYKeiEKELKKLD 724
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1404-1937 |
3.32e-21 |
|
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: 101.79 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREK 1483
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1484 LQREKDMllaeafslkqqleekdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1563
Cdd:pfam01576 150 LSKERKL----------------------------LEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1564 TIQMLEQAKLRLEMEMERMRQTHSkEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDqv 1643
Cdd:pfam01576 202 GRQELEKAKRKLEGESTDLQEQIA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE-- 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1644 nrrDFESEKRLRKDLKRTK-----ALLADAQLMLDHLKNSAP-----SKR--EIAQLKNQLEESEFTCAAAVKA-RKAME 1710
Cdd:pfam01576 279 ---DLESERAARNKAEKQRrdlgeELEALKTELEDTLDTTAAqqelrSKReqEVTELKKALEEETRSHEAQLQEmRQKHT 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1711 VEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqasrdlAQINDLQAQLEEANKEK 1790
Cdd:pfam01576 356 QALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE-------GQLQELQARLSESERQR 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1791 QELQEKLQALQSQVEFLeqsmvdKSLVSRQEAKIRELEtrlefertqvKRLESLASRLKENMEKLTEERDQRIAAENR-- 1868
Cdd:pfam01576 429 AELAEKLSKLQSELESV------SSLLNEAEGKNIKLS----------KDVSSLESQLQDTQELLQEETRQKLNLSTRlr 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 1869 --EKEQNKrLQRQLRDTKEEMGELAR-------KEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1937
Cdd:pfam01576 493 qlEDERNS-LQEQLEEEEEAKRNVERqlstlqaQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYD 569
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1244-1962 |
1.15e-20 |
|
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: 100.05 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1244 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTseLTDERNTGESASQLLDAETAERLRAE 1323
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL--YLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1324 KEMKELQTQYDALKKQMEVMemevmearLIRAAEINGEVDDDDAGGEWRLKYERAVREvdfTKKRLQQEFEDKLEVEQQN 1403
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKE--------NKEEEKEKKLQEEELKLLAKEEEELKSELL---KLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREK 1483
Cdd:pfam02463 323 KKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1484 LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAG 1563
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1564 TIQMLEQAKLRLEMEMeRMRQTHSKEMESRDEEV---EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS 1640
Cdd:pfam02463 483 QEQLELLLSRQKLEER-SQKESKARSGLKVLLALikdGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1641 DQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLH--- 1717
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKesa 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1718 ------------LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1785
Cdd:pfam02463 642 kakesglrkgvsLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1786 ANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA 1865
Cdd:pfam02463 722 LLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1866 ENRE--KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGdLQAAIEDEMESD 1943
Cdd:pfam02463 802 ELRAleEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL-LQELLLKEEELE 880
|
730
....*....|....*....
gi 42794779 1944 ENEDLINSEGDSDVDSELE 1962
Cdd:pfam02463 881 EQKLKDELESKEEKEKEEK 899
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1520-1963 |
1.23e-20 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 99.86 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1520 EAELQDISSQESKDEASLAKVKKQLRDLEAKVkdqeEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS----------KE 1589
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKH----QQLCEEKNALQEQLQAETELCAEAEEMRARLAarkqeleeilHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1590 MESRDEEVEEARQSCQ---KKLKQ----MEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTK 1662
Cdd:pfam01576 80 LESRLEEEEERSQQLQnekKKMQQhiqdLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLE-DQNSKLSKERKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1663 ALLAD--AQL--------MLDHLKNSAPSKreIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEE 1732
Cdd:pfam01576 159 ERISEftSNLaeeeekakSLSKLKNKHEAM--ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1733 QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVE-FLEQSM 1811
Cdd:pfam01576 237 QLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEdTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1812 VDKSLVSRQEAKIRELETRLEFE-RTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGEL 1890
Cdd:pfam01576 317 AQQELRSKREQEVTELKKALEEEtRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1891 ARKEAEASRKKHELEMDLESLEA-ANQSLQADLKLAfKRIGDLQAAIED---EMESDENEDLINSEGDSDVDSELED 1963
Cdd:pfam01576 397 QQAKQDSEHKRKKLEGQLQELQArLSESERQRAELA-EKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQD 472
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1478-1937 |
1.94e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 98.98 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1478 KLQREKLQREKDMLLAEAfSLKQQLEEKDmdiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEaKVKDQEEE 1557
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTE-NIEELIKEKE-------KELEEVLREINEISSELPELREELEKLEKEVKELE-ELKEEIEE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQagtIQMLEQAKLRLEmemERMRQTHS--KEMESRDEEVEEARQSCqKKLKQMEVQLEEEYEDKQKVLREKRELEGK 1635
Cdd:PRK03918 243 LEKE---LESLEGSKRKLE---EKIRELEEriEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1636 LATLSDQVN--RRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEseftcaaaVKARKAMEvEI 1713
Cdd:PRK03918 316 LSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER--------LKKRLTGL-TP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1714 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmKKHKAAVAQASRDLAQ------INDLQAQLEEAN 1787
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRELTEehrkelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1788 KEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEA---KIRELETRL-------------EFERT---------QVKRLE 1842
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKElaeQLKELEEKLkkynleelekkaeEYEKLkekliklkgEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1843 SLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQ----LRDTKEEMGELA---RKEAEASRKKHELEMDLESLEaan 1915
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyNEYLELKDAEKELEREEKELK--- 622
|
490 500
....*....|....*....|..
gi 42794779 1916 qSLQADLKLAFKRIGDLQAAIE 1937
Cdd:PRK03918 623 -KLEEELDKAFEELAETEKRLE 643
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1353-1946 |
4.39e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1353 IRAAEINGEVDDDDA---------GGEwrlKYERA-------VREVDFTKKRLQQEFEDKLEVEQQNKRQlERRLGDLQA 1416
Cdd:PRK03918 132 IRQGEIDAILESDESrekvvrqilGLD---DYENAyknlgevIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1417 DSEESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDMLLA 1493
Cdd:PRK03918 208 EINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIREL-EERIEELKKEIEELEEKVKELK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1494 EAfslkQQLEEKDMDIAGFTQKVVSleaELQDISSQESKDEASLAKVKKQLRDLE---AKVKDQEEELDEQAGTIQMLEQ 1570
Cdd:PRK03918 287 EL----KEKAEEYIKLSEFYEEYLD---ELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEKRLEELEE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1571 AKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRrdFES 1650
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGLTPEKL----EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE--LKK 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1651 EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEftcAAAVKARKAMEVEIEDLHLQidDIAKAKTAL 1730
Cdd:PRK03918 434 AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLR---KELRELEKVLKKESELIKLK--ELAEQLKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1731 EEQLSRLQREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQS 1810
Cdd:PRK03918 509 EEKLKKYNLEELE---KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1811 MVDKSlvsrqEAKIRELETRLEfERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGEl 1890
Cdd:PRK03918 586 SVEEL-----EERLKELEPFYN-EYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE- 658
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1891 aRKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEdEMESDENE 1946
Cdd:PRK03918 659 -EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKE 712
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
450-568 |
5.35e-20 |
|
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: 89.33 E-value: 5.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 450 APAVYSEKVMHMFKGCRREDMAPHIYAVAQTAYRAMLMSRQDQSIILLGSSGSGKTTSCQHLVQYLATIAGISGNK---- 525
Cdd:cd01363 11 LPIYRDSKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVAFNGINKgete 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 526 ---------VFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQAG 568
Cdd:cd01363 91 gwvylteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAG 142
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1522-1898 |
1.16e-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: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1522 ELQDISSQESKDEASLAK---VKKQLRDLEAKVkdqeEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1598
Cdd:TIGR02169 161 EIAGVAEFDRKKEKALEEleeVEENIERLDLII----DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1599 EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQlmldhlkns 1678
Cdd:TIGR02169 237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE--------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1679 apskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL 1758
Cdd:TIGR02169 308 ----RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1759 MKKHKAAVaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQV 1838
Cdd:TIGR02169 384 RDELKDYR-------EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI------EAKINELEEEKEDKALEI 450
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1839 KRLESLASRLKENMEKLTEERDQRiaaenreKEQNKRLQRQLRDTKEemgELARKEAEAS 1898
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDL-------KEEYDRVEKELSKLQR---ELAEAEAQAR 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1649-1979 |
1.36e-19 |
|
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: 96.28 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1649 ESEKRLRK---DLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAA-----AVKARKAMEVEIEDLHLQI 1720
Cdd:TIGR02168 176 ETERKLERtreNLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVlrleeLREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1721 DDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNEL----------MKKHKAAVAQASRDL----AQINDLQAQLEEA 1786
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALaneisrleqqKQILRERLANLERQLeeleAQLEELESKLDEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1787 NKEKQELQEKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEferTQVKRLESLASRLKENMEKLTEERDQRIAAE 1866
Cdd:TIGR02168 336 AEELAELEEKLEELKEELESLEA------ELEELEAELEELESRLE---ELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1867 NREKEQNKRLQRQLRDTKEEMGELARKE-AEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIeDEMESDEN 1945
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELA 485
|
330 340 350
....*....|....*....|....*....|....
gi 42794779 1946 EDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPS 1979
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
420-1146 |
5.79e-19 |
|
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: 93.64 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGP---RGAPAVYSEKvmhmfkgcRREDMAPHIYAVAQTAYRAMLMSRQDQSIIL 496
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPyrdVGNPLTLTST--------RSSPLAPQLLKVVQEAVRQQSETGYPQAIIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 497 LGSSGSGKTTSCQHLVQYLATIAGiSGNKVFSVEKWQALYTLLEAFGNSPTIINGNATRFSQILSLDFDQaGQVASASIQ 576
Cdd:cd14881 74 SGTSGSGKTYASMLLLRQLFDVAG-GGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTD-GALYRTKIH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 577 TMLLEKLRVARRPASEATFNVFYYLLACGDGTLRTELHLN--------HLAENNVFgivplakpEEKQKAAQQFSKLQAA 648
Cdd:cd14881 152 CYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgyspanlrYLSHGDTR--------QNEAEDAARFQAWKAC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 649 MKVLGISpdeqkacwF-----ILAAIYHLG----AAGATKEAAEAGRKQFarhewaQKAAYLLGCSleelSSAIFKhqhk 719
Cdd:cd14881 224 LGILGIP--------FldvvrVLAAVLLLGnvqfIDGGGLEVDVKGETEL------KSVAALLGVS----GAALFR---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 720 gGTLQRSTSFRQGPEESgLGDgtgPKLSALEClEGMAAGLYSELFTLLVSLVNrALKSSQHSLC------SMMIVDTPGF 793
Cdd:cd14881 282 -GLTTRTHNARGQLVKS-VCD---ANMSNMTR-DALAKALYCRTVATIVRRAN-SLKRLGSTLGthatdgFIGILDMFGF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 794 QNPeqggsaRGASFEELCHNYTQDRLQRLFHERTFVQELERYKEENIELafdDLEPPTDDSVAAVDqashqsLVRSLaRT 873
Cdd:cd14881 355 EDP------KPSQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQC---EVEVDYVDNVPCID------LISSL-RT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 874 dearGLLWLLEEEALVPGASEdtllerlfSYYGPQEGDKKgQSPLLHSSKPHH---FLLGHSHGTnwVEYNVTGWLnytk 950
Cdd:cd14881 419 ----GLLSMLDVECSPRGTAE--------SYVAKIKVQHR-QNPRLFEAKPQDdrmFGIRHFAGR--VVYDASDFL---- 479
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 951 qnpatqnaprllqDSQKKIISNlflgragsatvlsgsiagleggSQLALRRATSMRKTFTTGMAavkkkslciQMKLQVD 1030
Cdd:cd14881 480 -------------DTNRDVVPD----------------------DLVAVFYKQNCNFGFATHTQ---------DFHTRLD 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1031 ALIDTIKKSKLHFVHCflpvaegwageprsassrrvsssseldLPSGDHCEAGllQLDVPLLRTQLRGSRLLDAMRMYRQ 1110
Cdd:cd14881 516 NLLRTLVHARPHFVRC---------------------------IRSNTTETPN--HFDRGTVVRQIRSLQVLETVNLMAG 566
|
730 740 750
....*....|....*....|....*....|....*.
gi 42794779 1111 GYPDHMVFSEFRRRFDVLAPHLTKKHGRNYIVVDER 1146
Cdd:cd14881 567 GYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCA 602
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1262-1886 |
6.32e-19 |
|
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: 94.27 E-value: 6.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1262 EIQQLRSKLEK--AEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETaERLRAEKEM-------KELQTQ 1332
Cdd:TIGR00618 197 ELLTLRSQLLTlcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLkqlrariEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKR---------------LQQEFEDKL 1397
Cdd:TIGR00618 276 EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAahvkqqssieeqrrlLQTLHSQEI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1398 EVEQQNKRQ------------LERRLGDLQADSEESQRALQQLKKKCQRLTAE-------------LQDTKLHLEGQQVR 1452
Cdd:TIGR00618 356 HIRDAHEVAtsireiscqqhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREqatidtrtsafrdLQGQLAHAKKQQEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1453 NHELEKKQRRFDSElsQAHEEAQREKLQREKLQ--REKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISS-- 1528
Cdd:TIGR00618 436 QQRYAELCAAAITC--TAQCEKLEKIHLQESAQslKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhp 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1529 -QESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRD---EEVEEARQSC 1604
Cdd:TIGR00618 514 nPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNrskEDIPNLQNIT 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1605 QKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRK-DLKRTKALLADAQLMLDHLKNSAPSKR 1683
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLtALHALQLTLTQERVREHALSIRVLPKE 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1684 EIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHK 1763
Cdd:TIGR00618 674 LLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1764 AAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFErTQVKRLES 1843
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE-TLVQEEEQ 832
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 42794779 1844 LASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEE 1886
Cdd:TIGR00618 833 FLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1388-1893 |
7.75e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 93.83 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1388 RLQQEFEDKLEVEQQNKRQLERR--LGDLQADSEESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNHELEKKQRRFDS 1465
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIelLEPIRELAERYAAARERLA------ELEYLRAALRLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQREKLQREKDMLLAEAFS--------LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASL 1537
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1538 AKVKKQLRDLEAKVKDQEEELDEQA----GTIQMLEQAKLRLEMEMERMRQTHSkemeSRDEEVEEARQSCQKKLKQME- 1612
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALaeaeAALRDLRRELRELEAEIASLERRKS----NIPARLLALRDALAEALGLDEa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1613 --------VQLEEEYEDKQ----KVLR-EKREL---EGKLATLSDQVNRRDFesekRLRKDLKRTKALLADAQLMLDHlK 1676
Cdd:COG4913 459 elpfvgelIEVRPEEERWRgaieRVLGgFALTLlvpPEHYAAALRWVNRLHL----RGRLVYERVRTGLPDPERPRLD-P 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1677 NSAPSKREIAQ------LKNQLEES-EFTCAAAVKA----RKAMEVE-----IEDLHlQIDD--------------IAKA 1726
Cdd:COG4913 534 DSLAGKLDFKPhpfrawLEAELGRRfDYVCVDSPEElrrhPRAITRAgqvkgNGTRH-EKDDrrrirsryvlgfdnRAKL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1727 KtALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAA------------VAQASRDLAQINDLQAQLEEANKEKQELQ 1794
Cdd:COG4913 613 A-ALEAELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidVASAEREIAELEAELERLDASSDDLAALE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1795 EKLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFERTQVK----RLESLASRLKENMEKLTEERDQRIAAENREK 1870
Cdd:COG4913 692 EQLEELEAELEELEE------ELDELKGEIGRLEKELEQAEEELDelqdRLEAAEDLARLELRALLEERFAAALGDAVER 765
|
570 580
....*....|....*....|...
gi 42794779 1871 EQNKRLQRQLRDTKEEMGELARK 1893
Cdd:COG4913 766 ELRENLEERIDALRARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1242-1801 |
8.88e-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: 93.59 E-value: 8.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1242 TVRPLIEVQLSEEQIRNKD--EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAER 1319
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAEtrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1320 LRAEKEMKELQTQYDALKKQMEVMEMEVMEARlIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLE- 1398
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLK-EEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQg 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1399 ----------VEQQNKRQLERRLGD-LQA----DSEESQRALQQLK-KKCQRLT---------AELQDTKLHLEGQQ--- 1450
Cdd:TIGR02169 523 vhgtvaqlgsVGERYATAIEVAAGNrLNNvvveDDAVAKEAIELLKrRKAGRATflplnkmrdERRDLSILSEDGVIgfa 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1451 -----------------------VRNHELEKKQ-------------------------RRFDSELSQAHEEAQREKLQR- 1481
Cdd:TIGR02169 603 vdlvefdpkyepafkyvfgdtlvVEDIEAARRLmgkyrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLREr 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1482 -EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE 1560
Cdd:TIGR02169 683 lEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1561 QAGTIQMLEQ--AKLRLEMEMERMRQTHSKEMESRDE--EVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1636
Cdd:TIGR02169 763 LEARIEELEEdlHKLEEALNDLEARLSHSRIPEIQAElsKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1637 ATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQLEESEftcaaavKARKAMEVEIED 1715
Cdd:TIGR02169 843 IDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRlGDLKKERDELEAQLRELE-------RKIEELEAQIEK 914
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1716 LHLQIDDIAKAKTALEEQLSRLQREKNEIQnrlEEDQEDMN-ELMKKHKAAVAQASRDLAQINDLQAQ-LEEANKEKQEL 1793
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE---EIPEEELSlEDVQAELQRVEEEIRALEPVNMLAIQeYEEVLKRLDEL 991
|
....*...
gi 42794779 1794 QEKLQALQ 1801
Cdd:TIGR02169 992 KEKRAKLE 999
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1253-1924 |
2.14e-18 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 92.09 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSE---LTDERNTGESASQLLDaETAERlRAEKEMKel 1329
Cdd:pfam05483 98 EAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLK-ETCAR-SAEKTKK-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1330 qTQYDALKKQMEVMEMEVMEARLIRAAEingevddddaggEWRLKYERAVREVDFtkkRLQQEFEDKLEVEQQNKRQL-- 1407
Cdd:pfam05483 174 -YEYEREETRQVYMDLNNNIEKMILAFE------------ELRVQAENARLEMHF---KLKEDHEKIQHLEEEYKKEInd 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1408 ---------------ERRLGDLQADSEESQRALQQLKKKCQ--------------RLTAELQDTKLHLEGQQVRNHELEK 1458
Cdd:pfam05483 238 kekqvsllliqitekENKMKDLTFLLEESRDKANQLEEKTKlqdenlkeliekkdHLTKELEDIKMSLQRSMSTQKALEE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1459 KQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagftqkvvsLEAELQDISSQESKDEASLA 1538
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL-------------LRTEQQRLEKNEDQLKIITM 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1539 KVKKQLRDLE--AKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthSKEMESRDEEVEEARQSCQKKLKQMEVQLE 1616
Cdd:pfam05483 385 ELQKKSSELEemTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKI----AEELKGKEQELIFLLQAREKEIHDLEIQLT 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1617 EEYEDKQKVLREKRELEGKLatlsdqvnrrdfESEKrlrkdLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEse 1696
Cdd:pfam05483 461 AIKTSEEHYLKEVEDLKTEL------------EKEK-----LKNIELTAHCDKLLLENKELTQEASDMTLELKKHQED-- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1697 ftcaaaVKARKAMEveiEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMNELMKKHKAAVAQASRD 1772
Cdd:pfam05483 522 ------IINCKKQE---ERMLKQIENLEEKEMNLRDELESVREEfiqkGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1773 LAQINDLQAQLEEANKEKQELQEKLQALQsqveflEQSMVDKSLVSRQEAKIRELEtrLEFERTQVKRLESLASRLKE-- 1850
Cdd:pfam05483 593 ENKCNNLKKQIENKNKNIEELHQENKALK------KKGSAENKQLNAYEIKVNKLE--LELASAKQKFEEIIDNYQKEie 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1851 ----NMEKLTEERDQRIA----AENREKEQNKRLQRQL------------------RDTKEEMGELARKEAEASRKKHEL 1904
Cdd:pfam05483 665 dkkiSEEKLLEEVEKAKAiadeAVKLQKEIDKRCQHKIaemvalmekhkhqydkiiEERDSELGLYKNKEQEQSSAKAAL 744
|
730 740
....*....|....*....|
gi 42794779 1905 EMDLESLEAANQSLQADLKL 1924
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLEI 764
|
|
| PDZ_canonical |
cd00136 |
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ... |
220-308 |
7.88e-18 |
|
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: 79.89 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLRRTTMLDRGPegqacrrVVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd00136 1 TVTLEKDPGGGLGFSIRGGKDGGGGI-------FVSRVEPG-GPAARDGRLRVGDRILEVNGVSLEGLTHEEAVELLKSA 72
|
....*....
gi 42794779 300 GDSVRLKVQ 308
Cdd:cd00136 73 GGEVTLTVR 81
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1250-1961 |
1.97e-17 |
|
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: 89.41 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1250 QLSEEQIRNKDEEIQQLRSKLEKAEKERNELrLNSDRLESRISEltseltDERNTGESASQLLDAEtaeRLRAEKEMKEL 1329
Cdd:pfam15921 99 ELHEKQKFYLRQSVIDLQTKLQEMQMERDAM-ADIRRRESQSQE------DLRNQLQNTVHELEAA---KCLKEDMLEDS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1330 QTQYDALKKQMEVMEMEVMEAR--LIRAAEINGE-VDDDDAGGEWRLK-----YERAVREVD----FTKKRLQqEFEDKL 1397
Cdd:pfam15921 169 NTQIEQLRKMMLSHEGVLQEIRsiLVDFEEASGKkIYEHDSMSTMHFRslgsaISKILRELDteisYLKGRIF-PVEDQL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1398 EV---EQQNK-----RQLERRLGDLQADSEESQRALQQlKKKCQRLTAELQDTKLHLEGQQVRNH---------ELEKKQ 1460
Cdd:pfam15921 248 EAlksESQNKielllQQHQDRIEQLISEHEVEITGLTE-KASSARSQANSIQSQLEIIQEQARNQnsmymrqlsDLESTV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1461 RRFDSELSQAheeaqrEKLQREKLQR-EKDMLLAEAfSLKQQLEEKDMdiagFTQKVVSLEAELQDISSQESKDEASLAK 1539
Cdd:pfam15921 327 SQLRSELREA------KRMYEDKIEElEKQLVLANS-ELTEARTERDQ----FSQESGNLDDQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1540 VKKQLRDLeakvkdqeeeLDEQAGTiqmleqaklrlEMEMERMRqthsKEMESRDEEVeearQSCQKKLKQMEVQLEEEY 1619
Cdd:pfam15921 396 EKEQNKRL----------WDRDTGN-----------SITIDHLR----RELDDRNMEV----QRLEALLKAMKSECQGQM 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1620 EDKQKVLREKRELEGKLATLSDQVnrrdfESEKRLrkdLKRTKALLADAQLMLDHlknsapSKREIAQLKNQLEESE--- 1696
Cdd:pfam15921 447 ERQMAAIQGKNESLEKVSSLTAQL-----ESTKEM---LRKVVEELTAKKMTLES------SERTVSDLTASLQEKErai 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1697 -FTCAAAVKARKAMEVEIEDL-HLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEEDQEDMNELmkkhkaaVAQASRDL 1773
Cdd:pfam15921 513 eATNAEITKLRSRVDLKLQELqHLKNEGDHLRNVQTECEALKLQmAEKDKVIEILRQQIENMTQL-------VGQHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 AQINDLQAQLE-EANKEKQELQEKlqalqsqvefleqsmvdKSLVSRQEAKIRELETRL-EFERTQVKRLESLASRLKEn 1851
Cdd:pfam15921 586 GAMQVEKAQLEkEINDRRLELQEF-----------------KILKDKKDAKIRELEARVsDLELEKVKLVNAGSERLRA- 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1852 MEKLTEERDQRI-------AAENREKEQNKRLQRQLRDTKEEMGELARK-EAEASRKKHELEM---DLESLEAAN----- 1915
Cdd:pfam15921 648 VKDIKQERDQLLnevktsrNELNSLSEDYEVLKRNFRNKSEEMETTTNKlKMQLKSAQSELEQtrnTLKSMEGSDghamk 727
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1916 --QSLQADLKLAFKRIGDLQAAI---EDEMESDENEDLINSEGDSDVDSEL 1961
Cdd:pfam15921 728 vaMGMQKQITAKRGQIDALQSKIqflEEAMTNANKEKHFLKEEKNKLSQEL 778
|
|
| PDZ_NHERF-like |
cd06768 |
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ... |
219-307 |
2.78e-17 |
|
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: 78.25 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGdFGFSLRRttmlDRGPEGQACRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06768 1 RLCHLVKGPEG-YGFNLHA----EKGRPGHFIREV----DPG-SPAERA-GLKDGDRLVEVNGENVEGESHEQVVEKIKA 69
|
....*....
gi 42794779 299 SGDSVRLKV 307
Cdd:cd06768 70 SGNQVTLLV 78
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
420-602 |
5.06e-17 |
|
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: 87.58 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 420 SVLHTLRQRYGASLLHTYAGPSLLVLGPRGAPAVYSEKVMHMFKgCRR--EDMAPHIYAVAQTAYRAMLMSRQDQSIILL 497
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYK-CIDciEDLSLNEYHVVHNALKNLNELKRNQSIIIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 498 GSSGSGKTTSCQHLVQYLATIAGISGNKVFSVEKWQAL---------------------YTLLEAFGNSPTIINGNATRF 556
Cdd:cd14938 81 GESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEEDnihneentdyqfnmsemlkhvNVVMEAFGNAKTVKNNNSSRF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 42794779 557 SQILSLDFDQAgQVASASIQTMLLEKLRVARRPASEATFNVFYYLL 602
Cdd:cd14938 161 SKFCTIHIENE-EIKSFHIKKFLLDKERLINRKANENSFNIFYYII 205
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1248-1912 |
7.24e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.00 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESasqlLDAET---AERLRAEK 1324
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1325 EMK-ELQTQYDALKKQMEVMEMEVmearliraAEINGEVDdddaggewRLKYERAVREVDFTK-KRLQQEFEDKLEVEQQ 1402
Cdd:TIGR04523 117 EQKnKLEVELNKLEKQKKENKKNI--------DKFLTEIK--------KKEKELEKLNNKYNDlKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1403 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTaELQDTKLHLEGQqvrNHELEKKQRRFDSELSQAHEEAQREKLQRE 1482
Cdd:TIGR04523 181 EKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQ---NNQLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1483 KLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEEE 1557
Cdd:TIGR04523 257 QLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQNQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQAGTIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLA 1637
Cdd:TIGR04523 330 ISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1638 TLSDQVNRRD-----FESEKR-LRKDLKRTKALLADaqlmldhlknsapSKREIAQLKNQleeseftcaaavkarkamev 1711
Cdd:TIGR04523 402 NQEKLNQQKDeqikkLQQEKElLEKEIERLKETIIK-------------NNSEIKDLTNQ-------------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1712 eIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdlaqindlqaQLEEANKEKQ 1791
Cdd:TIGR04523 449 -DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEKK 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1792 ELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKR--LESLASRLKENMEKLTEERDQRIAAENR 1868
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1869 ------EKEQNKR---------------LQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLE 1912
Cdd:TIGR04523 587 kqelidQKEKEKKdlikeieekekkissLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1466-1872 |
9.06e-17 |
|
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: 87.05 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQR--EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1543
Cdd:TIGR02169 666 ILFSRSEPAELQRLRErlEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthskEMESRDEEVEEARQScqkklkqmevqleeeyedKQ 1623
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL------EARLSHSRIPEIQAE------------------LS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1624 KVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLmldhlkNSAPSKREIAQLKNQLEEseftcaaav 1703
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEY-LEKEIQELQEQRIDLKE------QIKSIEKEIENLNGKKEE--------- 865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1704 karkaMEVEIEDLHLQIDDiakaktaLEEQLSRLQREKNEIQNRLEEDQEDMNELMkkhkaavAQASRDLAQINDLQAQL 1783
Cdd:TIGR02169 866 -----LEEELEELEAALRD-------LESRLGDLKKERDELEAQLRELERKIEELE-------AQIEKKRKRLSELKAKL 926
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1784 EEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELE-----TRLEFERTQVKRLEslasrLKENMEKLTEE 1858
Cdd:TIGR02169 927 EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlAIQEYEEVLKRLDE-----LKEKRAKLEEE 1001
|
410
....*....|....*..
gi 42794779 1859 RDQ---RIAAENREKEQ 1872
Cdd:TIGR02169 1002 RKAileRIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1401-1789 |
1.26e-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: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1401 QQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQ 1480
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1481 REKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASlaKVKKQLRDLEAKVKDQEEELDE 1560
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELS--KLEEEVSRIEARLREIEQKLNR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1561 QAGTIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLEE------EYEDKQKVLREKR-ELE 1633
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRI--------DLKEQIKSIEKEIENLNGKKEELEEELEEleaalrDLESRLGDLKKERdELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1634 GKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEEseftcaaAVKARKAMEVEI 1713
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLED-------VQAELQRVEEEI 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1714 EDLH----LQIDD---IAKAKTALEEQLSRLQREKNEIQNRLEE-DQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1785
Cdd:TIGR02169 968 RALEpvnmLAIQEyeeVLKRLDELKEKRAKLEEERKAILERIEEyEKKKREVFMEAFEAINENFNEIFAELSGGTGELIL 1047
|
....
gi 42794779 1786 ANKE 1789
Cdd:TIGR02169 1048 ENPD 1051
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1627-1968 |
1.91e-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: 86.28 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1627 REKRELEGKLATLS--DQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcaAAVK 1704
Cdd:TIGR02169 153 VERRKIIDEIAGVAefDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGY--ELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAV--------AQASRDLAQI 1776
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVkekigeleAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1777 NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSL--------VSRQEAKIRELETRLEFERTQVKRLESLASRL 1848
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1849 KENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKR 1928
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1929 IGDLQA---AIEDEMESDENEdLINSE-----------GDSDVDSELEDRVDGV 1968
Cdd:TIGR02169 471 LYDLKEeydRVEKELSKLQRE-LAEAEaqaraseervrGGRAVEEVLKASIQGV 523
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1261-1923 |
2.09e-16 |
|
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: 85.46 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1261 EEIQQLRSKLEKAEKERNEL--RLNSDR------------LESRISELTSELTDERNTGESasqlLDAET---AERLRAE 1323
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLdkNLNKDEekinnsnnkikiLEQQIKDLNDKLKKNKDKINK----LNSDLskiNSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1324 KEMK-ELQTQYDALKKQMEVMEMEVmearliraAEINGEVDdddaggewRLKYERAVREVDFTK-KRLQQEFEDKLEVEQ 1401
Cdd:TIGR04523 116 KEQKnKLEVELNKLEKQKKENKKNI--------DKFLTEIK--------KKEKELEKLNNKYNDlKKQKEELENELNLLE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1402 QNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTaELQDTKLHLEGQqvrNHELEKKQRRFDSELSQAHEEAQREKLQR 1481
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQ---NNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1482 EKLQREKDmllaeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQES-----KDEASLAKVKKQLRDLEAKVKDQEE 1556
Cdd:TIGR04523 256 NQLKDEQN-------KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1557 ELDEQAGTIQMLEQAKLRLEMEmermRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1636
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKE----LTNSESENSEKQRELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1637 ATLSDQVNRRD-----FESEKR-LRKDLKRTKALLADaqlmldhlknsapSKREIAQLKNQleeseftcaaavkarkame 1710
Cdd:TIGR04523 401 QNQEKLNQQKDeqikkLQQEKElLEKEIERLKETIIK-------------NNSEIKDLTNQ------------------- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1711 veIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKKHKaavaqasrdlaqindlqaQLEEANKEK 1790
Cdd:TIGR04523 449 --DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQK---ELKSKEK------------------ELKKLNEEK 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1791 QELQEKLQALQSQVEFLEQSMVD-KSLVSRQEAKIRELETRLEFERTQVKR--LESLASRLKENMEKLTEERDQRIAAen 1867
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKDDFELKKenLEKEIDEKNKEIEELKQTQKSLKKK-- 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1868 rekeqNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLK 1923
Cdd:TIGR04523 584 -----QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1435-1935 |
4.63e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 84.05 E-value: 4.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1435 LTAELQDTKLHLEGQQVRNHELEKKQRRfdsELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQ 1514
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELK---ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1515 KVvsleaELQDISSQESKDEASLAKVKKQLRDLEAkvkdQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRD 1594
Cdd:COG4717 124 LL-----QLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1595 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQvnrrdfesekrlrKDLKRTKALLADAQLMLdh 1674
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-------------ERLKEARLLLLIAAALL-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1675 lknsapskrEIAQLKNQLEESEFTCAAAVKARKAMeveiedLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQED 1754
Cdd:COG4717 260 ---------ALLGLGGSLLSLILTIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1755 MNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKlQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFE 1834
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE-ELEQEIAALLAEAGVED------EEELRAALEQAEEY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1835 RTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQnkRLQRQLRDTKEEMGELARKEAEASRKKHELEMD--LESLE 1912
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELE--ELEEELEELEEELEELREELAELEAELEQLEEDgeLAELL 475
|
490 500
....*....|....*....|...
gi 42794779 1913 AANQSLQADLKLAFKRIGDLQAA 1935
Cdd:COG4717 476 QELEELKAELRELAEEWAALKLA 498
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1244-1960 |
5.92e-16 |
|
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: 84.71 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1244 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKER---------NELRLNSDRLESR---ISELTSELTD-ERNTGESASQ 1310
Cdd:TIGR00606 351 RLQLQADRHQEHIRARDSLIQSLATRLELDGFERgpfserqikNFHTLVIERQEDEaktAAQLCADLQSkERLKQEQADE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1311 LLDAETA-------ERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVR--- 1380
Cdd:TIGR00606 431 IRDEKKGlgrtielKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQnek 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1381 -EVDFTKKRLQQEFE-----------------DKLEVEQQ--------------------NKRQLERRLGDLQADSEESQ 1422
Cdd:TIGR00606 511 aDLDRKLRKLDQEMEqlnhhtttrtqmemltkDKMDKDEQirkiksrhsdeltsllgyfpNKKQLEDWLHSKSKEINQTR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1423 RALQQLKKKCQRLtaELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHE-EAQREKLQREKLQREKDMLLAEAFSLKQ- 1500
Cdd:TIGR00606 591 DRLAKLNKELASL--EQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQf 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1501 --QLEEKDMDIAGFTQKVVSLEAELQDISsqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEME 1578
Cdd:TIGR00606 669 itQLTDENQSCCPVCQRVFQTEAELQEFI---SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKE 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1579 MERMR---QTHSKEMESRDEEVE-------------EARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLS-D 1641
Cdd:TIGR00606 746 IPELRnklQKVNRDIQRLKNDIEeqetllgtimpeeESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvQ 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1642 QVNRRDFESEKRLRK---DLKRTKALLADAQLMLDHLKNSApskreiaqlkNQLEESEFTCAAAVKARKAME-------V 1711
Cdd:TIGR00606 826 QVNQEKQEKQHELDTvvsKIELNRKLIQDQQEQIQHLKSKT----------NELKSEKLQIGTNLQRRQQFEeqlvelsT 895
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1712 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASRDL--------------- 1773
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDIenkiqdgkddylkqk 975
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 -AQINDLQAQLEEANKEKQELQEKLQALQSQVE---FLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLasRLK 1849
Cdd:TIGR00606 976 eTELNTVNAQLEECEKHQEKINEDMRLMRQDIDtqkIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVL--QMK 1053
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1850 ENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrKKHELEMDLESLEAANQSL--------QAD 1921
Cdd:TIGR00606 1054 QEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEE--KYREMMIVMRTTELVNKDLdiyyktldQAI 1131
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 42794779 1922 LKLAFKRIGDLQAAIEDEMESDEN-EDLINSEGDSDVDSE 1960
Cdd:TIGR00606 1132 MKFHSMKMEEINKIIRDLWRSTYRgQDIEYIEIRSDADEN 1171
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1318-1956 |
7.02e-16 |
|
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: 84.25 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1318 ERLRAEKEM---KELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERA---VREVDFTKKRLQQ 1391
Cdd:pfam02463 154 RRLEIEEEAagsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1392 EFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1471
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1472 EEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLaKVKKQLRDLEAKV 1551
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK-KLESERLSSAAKL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1552 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRE 1631
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1632 LEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREI-AQLKNQLEESEFTCAAAVKARK--A 1708
Cdd:pfam02463 470 SEDLLKETQLVKLQEQ-LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGrIISAHGRLGDLGVAVENYKVAIstA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1709 MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVAQASRDLAQINDLQAQLE 1784
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleiDPILNLAQLDKATLEADEDDKRAKVVEGI 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1785 EANKEKQELQEKLQALQSQVefLEQSMVDKSLVSRQEAKIRELETRlefERTQVKRLESLASRLKENMEKLTEERDQRIA 1864
Cdd:pfam02463 629 LKDTELTKLKESAKAKESGL--RKGVSLEEGLAEKSEVKASLSELT---KELLEIQELQEKAESELAKEEILRRQLEIKK 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1865 AENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDE 1944
Cdd:pfam02463 704 KEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKT 783
|
650
....*....|..
gi 42794779 1945 NEDLINSEGDSD 1956
Cdd:pfam02463 784 EKLKVEEEKEEK 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1246-1887 |
7.20e-16 |
|
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: 84.25 E-value: 7.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1246 LIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAErlraEKE 1325
Cdd:pfam02463 376 LAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTE----EKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1326 MKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFE--DKLEVEQQN 1403
Cdd:pfam02463 452 ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggRIISAHGRL 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEEAQREKLQREK 1483
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLK---LPLKSIAVLEIDPILNLAQL 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1484 LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE------SKDEASLAKVKKQLRDLEAKVKDQEEE 1557
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEeglaekSEVKASLSELTKELLEIQELQEKAESE 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQAGTIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLA 1637
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREK-EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1638 TLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLH 1717
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1718 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA------QASRDLAQINDLQAQLEEANKEKQ 1791
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEekkeleEESQKLNLLEEKENEIEERIKEEA 927
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1792 ELQEKLQALQsqvefLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKE 1871
Cdd:pfam02463 928 EILLKYEEEP-----EELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEE 1002
|
650
....*....|....*.
gi 42794779 1872 QNKRLQRQLRDTKEEM 1887
Cdd:pfam02463 1003 EKKKLIRAIIEETCQR 1018
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1247-1790 |
1.13e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.19 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLES---------RISELTSELTDERNTGE-------SASQ 1310
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEkrlsrleEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1311 LLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREVDFTKKRLQ 1390
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELE----------RLKKRLTGLTPEKLEKELE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1391 QEFEDKLEVEQQnKRQLERRLGDLQADSEESQRALQQLKK---KCQRLTAELQDtklhlegqqvrnHELEKKQRRFDSEL 1467
Cdd:PRK03918 395 ELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEELKKakgKCPVCGRELTE------------EHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1468 SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMdiagfTQKVVSLEAELQDISSQE-SKDEASLAKVKKQLRD 1546
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL-----AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1547 LEAKVKDQEEELDEQagtiqmleqaklrlememermrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEE----YEDK 1622
Cdd:PRK03918 537 LKGEIKSLKKELEKL--------------------------EELKKKLAELEKKLDELEEELAELLKELEELgfesVEEL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1623 QKVLREKRELEGKLATLSDQvnRRDFESEKRLRKDLKRTkalLADAQLMLDHLKNSAPSKR-EIAQLKNQLEESEFTCAA 1701
Cdd:PRK03918 591 EERLKELEPFYNEYLELKDA--EKELEREEKELKKLEEE---LDKAFEELAETEKRLEELRkELEELEKKYSEEEYEELR 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1702 AVKARKAMEV-----EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ--NRLEEDQEDMNELMKKHKAAVAQASrdLA 1774
Cdd:PRK03918 666 EEYLELSRELaglraELEELEKRREEIKKTLEKLKEELEEREKAKKELEklEKALERVEELREKVKKYKALLKERA--LS 743
|
570
....*....|....*..
gi 42794779 1775 QINDLQAQL-EEANKEK 1790
Cdd:PRK03918 744 KVGEIASEIfEELTEGK 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1500-1945 |
1.96e-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: 82.80 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1500 QQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAsLAKVKKQLRDLE-----AKVKDQEEELDEQAGTIQmleqaklr 1574
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAER-YKELKAELRELElallvLRLEELREELEELQEELK-------- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1575 lemEMERMRQTHSKEMESRDEEVEEARqscqkkLKQMEvqLEEEYEDKQKVL----REKRELEGKLATLSdqvnrrdfES 1650
Cdd:TIGR02168 250 ---EAEEELEELTAELQELEEKLEELR------LEVSE--LEEEIEELQKELyalaNEISRLEQQKQILR--------ER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1651 EKRLRKDLKRTKALLADAQLMLDHLK-NSAPSKREIAQLKNQLEeseftcaaavkarkameveiedlhlqiddiakaktA 1729
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAeELAELEEKLEELKEELE-----------------------------------S 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1730 LEEQLSRLQREKNEIQNRLEEDQEDMNELmkkhKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQ 1809
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETL----RSKVAQLEL---QIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1810 SMvdkslvsrQEAKIRELETRLEfertqvkrleslasRLKENMEKLTEERDQRIAAEnrekeqnKRLQRQLRDTKEEMGE 1889
Cdd:TIGR02168 429 KL--------EEAELKELQAELE--------------ELEEELEELQEELERLEEAL-------EELREELEEAEQALDA 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1890 LARKEAEASRKKHELEMDLESLEAANQSLQAdLKLAFKRIGDLQAAIEDEMESDEN 1945
Cdd:TIGR02168 480 AERELAQLQARLDSLERLQENLEGFSEGVKA-LLKNQSGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1247-1593 |
2.40e-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: 82.41 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNE-------LRLNSDRLESRISELTSELTDERNTGESASQLLDAETAER 1319
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISAlrkdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1320 LRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDD-DDAGGEWRLKYERAVREVDFTKKRLqQEFEDKLE 1398
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALRE--------ALDELRAELTLlNEEAANLRERLESLERRIAATERRL-EDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1399 VEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1478
Cdd:TIGR02168 849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE 928
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1479 LQREKLQREKDmllaeafSLKQQLEEKdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK------ 1552
Cdd:TIGR02168 929 LRLEGLEVRID-------NLQERLSEE-------------YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvn 988
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 42794779 1553 --------DQEEELDEQAGTIQMLEQAKLRLEMEMERMrqthSKEMESR 1593
Cdd:TIGR02168 989 laaieeyeELKERYDFLTAQKEDLTEAKETLEEAIEEI----DREARER 1033
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1254-1741 |
3.83e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 81.35 E-value: 3.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELtseltderntgESASQLLDAEtAERLRAEKEMKELQTQY 1333
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----------EKLLQLLPLY-QELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1334 DALKKQMEVMEmevmearliraaeingevddddaggEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD 1413
Cdd:COG4717 149 EELEERLEELR-------------------------ELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1414 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQvrnhelekkqrrfdselsqaheeaqreklQREKLQREKDMLLA 1493
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-----------------------------LEERLKEARLLLLI 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1494 EA-----FSLKQQLEEKDMDIAGFTQKVVSLeaeLQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1568
Cdd:COG4717 255 AAallalLGLGGSLLSLILTIAGVLFLVLGL---LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1569 EQAKL-RLEMEMERMRQTHSKEMESRDEE----VEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQV 1643
Cdd:COG4717 332 PDLSPeELLELLDRIEELQELLREAEELEeelqLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1644 NRR--------DFESEKRLRKDLKRTKALLADAQLMLDHLknsapsKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEI 1713
Cdd:COG4717 412 EELlgeleellEALDEEELEEELEELEEELEELEEELEEL------REELAELEAELEqlEEDGELAELLQELEELKAEL 485
|
490 500
....*....|....*....|....*...
gi 42794779 1714 EDLHLQIDDIAKAKTALEEQLSRLQREK 1741
Cdd:COG4717 486 RELAEEWAALKLALELLEEAREEYREER 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1414-1859 |
8.95e-15 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1414 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheEAQREKLQREKLQREKdmlLA 1493
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--EAELEELREELEKLEK---LL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1494 EAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEskdeaslakvkKQLRDLEAKVKDQEEELDEQagtiqmLEQAKL 1573
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLEELEERLEELRELE-----------EELEELEAELAELQEELEEL------LEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1574 RLEMEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMEVQLEEeYEDKQKVLREKRELEGK------------------ 1635
Cdd:COG4717 189 ATEEELQDLAEEL-EELQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEArlllliaaallallglgg 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1636 ------------------LATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLK-----NSAPSKREIAQLKNQL 1692
Cdd:COG4717 267 sllsliltiagvlflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLaalglPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1693 EESEFTCAAAVKARKamEVEIEDLHLQIDDI-AKAKTALEEQLSRL---QREKNEIQNRLEEDQEDMNELMKKHKAAVAQ 1768
Cdd:COG4717 347 EELQELLREAEELEE--ELQLEELEQEIAALlAEAGVEDEEELRAAleqAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1769 ASRD--LAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkSLVSRQEAKIRELETRLEFERTQVKRLESLAS 1846
Cdd:COG4717 425 LDEEelEEELEELEEELEELEEELEELREELAELEAELEQLEED----GELAELLQELEELKAELRELAEEWAALKLALE 500
|
490
....*....|...
gi 42794779 1847 RLKENMEKLTEER 1859
Cdd:COG4717 501 LLEEAREEYREER 513
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1248-1798 |
9.38e-15 |
|
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: 80.55 E-value: 9.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKE-RNELRLNSDRLESRISELTSELTderntgESASQLLDAETaERLRAEKEM 1326
Cdd:pfam15921 300 QLEIIQEQARNQNSMYMRQLSDLESTVSQlRSELREAKRMYEDKIEELEKQLV------LANSELTEART-ERDQFSQES 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1327 KELQTQYdalkkQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERavREVDFTKKRLQQEFEDKLEVEQQNKRQ 1406
Cdd:pfam15921 373 GNLDDQL-----QKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLR--RELDDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1407 LERRLGDLQADSEESQRA------LQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEEAQR 1476
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVssltaqLESTKEMLRKVVEELTAKKMTLESSERTvsdlTASLQEKERAIEATNAEITKLRSR 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1477 EKLQREKLQR---EKDMLL---AEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAK 1550
Cdd:pfam15921 526 VDLKLQELQHlknEGDHLRnvqTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLE 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1551 VKDQEEELDEQAGTIQMLEQAKLRLEMEM--------ERMRQTHSKEMEsRDEEVEEARqSCQKKLKQmevqLEEEYEDK 1622
Cdd:pfam15921 606 LQEFKILKDKKDAKIRELEARVSDLELEKvklvnagsERLRAVKDIKQE-RDQLLNEVK-TSRNELNS----LSEDYEVL 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1623 QKVLREKRElEGKLATlsdqvnrrdfeseKRLRKDLKRTKAlladaqlmldhlknsapskrEIAQLKNQLEESEFTCAAA 1702
Cdd:pfam15921 680 KRNFRNKSE-EMETTT-------------NKLKMQLKSAQS--------------------ELEQTRNTLKSMEGSDGHA 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1703 VKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSR-------LQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ 1775
Cdd:pfam15921 726 MKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNankekhfLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
570 580
....*....|....*....|...
gi 42794779 1776 INDLQAQLEEANKEKQELQEKLQ 1798
Cdd:pfam15921 806 VANMEVALDKASLQFAECQDIIQ 828
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1257-1844 |
1.00e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.08 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1257 RNKDEEIQQLRSKLEkaEKERNEL--RLNSdrLESRISELTSELTDERNTGESASQLLDaETAERLraeKEMKELQTQYD 1334
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLheRLNG--LESELAELDEEIERYEEQREQARETRD-EADEVL---EEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1335 ALKkqmevmemevmearliraAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFED---KLEVEQQNKRQLERRL 1411
Cdd:PRK02224 255 TLE------------------AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDllaEAGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1412 GDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDml 1491
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE-- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1492 laeafSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD-------QEEELDEQAGT 1564
Cdd:PRK02224 395 -----ELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1565 IQMLEQAKLRLEMEMERMRQTHskemESRDEEVEEArqscqKKLKQMEVQLEEeyedkqkvLREKRELEGKLatLSDQVN 1644
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEV----EEVEERLERA-----EDLVEAEDRIER--------LEERREDLEEL--IAERRE 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1645 RRDfesEKRLRKDLKRTKAlladaqlmlDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-------IEDLH 1717
Cdd:PRK02224 531 TIE---EKRERAEELRERA---------AELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKErieslerIRTLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1718 LQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH-KAAVAQASRDLAQINDLQAQLEEankEKQELQEK 1796
Cdd:PRK02224 599 AAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEE---KLDELREE 675
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 42794779 1797 LQALQSQVEFLEQSMvdkslvsrqeAKIRELETRLEFERTQVKRLESL 1844
Cdd:PRK02224 676 RDDLQAEIGAVENEL----------EELEELRERREALENRVEALEAL 713
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1300-1890 |
2.87e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1300 DERNTGESASQLLDaETAERLRAEKEMKELQTQYDALKKqmevmeMEVMEARLIRAAEINGEVDDDDAggewRLKYERAV 1379
Cdd:COG4913 219 EEPDTFEAADALVE-HFDDLERAHEALEDAREQIELLEP------IRELAERYAAARERLAELEYLRA----ALRLWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1380 REVDFTKKRLQQEfEDKLEVEQQNKRQLERRLGDLQADSEESQRA--------LQQLKKKCQRLTAELQDTKLHLEGQQV 1451
Cdd:COG4913 288 RRLELLEAELEEL-RAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1452 R----NHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDIs 1527
Cdd:COG4913 367 LlaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL- 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1528 sqeskdeasLAKVKKQLRDLEA---------KVKDQEEE--------LDEQAGTI-----------QMLEQAKLRLEMEM 1579
Cdd:COG4913 446 ---------RDALAEALGLDEAelpfvgeliEVRPEEERwrgaiervLGGFALTLlvppehyaaalRWVNRLHLRGRLVY 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1580 ERMRQTHSKEMESRDEE------------------------------VEEARQ----------SCQKKL------KQMEV 1613
Cdd:COG4913 517 ERVRTGLPDPERPRLDPdslagkldfkphpfrawleaelgrrfdyvcVDSPEElrrhpraitrAGQVKGngtrheKDDRR 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEY------EDKQKVLREKR-ELEGKLATLSDQVNRRdfeseKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIA 1686
Cdd:COG4913 597 RIRSRYvlgfdnRAKLAALEAELaELEEELAEAEERLEAL-----EAELDALQERREALQRLAEYSWDEIDVASAEREIA 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1687 QLKNQ---LEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnelmkkhk 1763
Cdd:COG4913 672 ELEAElerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------------- 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1764 aavAQASRDLAQINDLQAQLEEANKEKQE------LQEKLQALQSQVEFLEQSMVDK--SLVSRQEAKIRELETRLEFER 1835
Cdd:COG4913 739 ---AEDLARLELRALLEERFAAALGDAVErelrenLEERIDALRARLNRAEEELERAmrAFNREWPAETADLDADLESLP 815
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1836 TQVKRLESL-ASRLKENMEKLteeRDQRIAAENREKEQ-NKRLQRQLRDTKEEMGEL 1890
Cdd:COG4913 816 EYLALLDRLeEDGLPEYEERF---KELLNENSIEFVADlLSKLRRAIREIKERIDPL 869
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1378-1913 |
5.43e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 77.77 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1378 AVREVDFTKKRLQQEFEDklEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELE 1457
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1458 kkqrrfdsELSQAHEEAQREKLQREklqREKDMLLAEAFSLKQQLEEkdmdiagftqkvvsLEAELQDISSQESKDEASL 1537
Cdd:PRK02224 255 --------TLEAEIEDLRETIAETE---REREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1538 AKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQaklrlemEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLEE 1617
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNE-------EAESLRED-ADDLEERAEELREEAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1618 EYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSApskREIAQLKNQ------ 1691
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE-LREERDELREREAELEATLRTARERV---EEAEALLEAgkcpec 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1692 ---LEESEFTCAAAVK--ARKAMEVEIEDLHLQIDDI------AKAKTALEEQLSRLQREKNEIQ-------NRLEEDQE 1753
Cdd:PRK02224 458 gqpVEGSPHVETIEEDreRVEELEAELEDLEEEVEEVeerlerAEDLVEAEDRIERLEERREDLEeliaerrETIEEKRE 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1754 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdKSLVSRQEAKIRELETRLEf 1833
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI---RTLLAAIADAEDEIERLRE- 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1834 ertqvkRLESLASRLKENMEKLTEERDQR--IAAENRE------KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE 1905
Cdd:PRK02224 614 ------KREALAELNDERRERLAEKRERKreLEAEFDEarieeaREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVE 687
|
....*...
gi 42794779 1906 MDLESLEA 1913
Cdd:PRK02224 688 NELEELEE 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1682-1862 |
6.78e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 75.57 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1761
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 --------------HKAAVAQASRDL-----------AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVD-KS 1815
Cdd:COG4942 113 lyrlgrqpplalllSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAAlEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42794779 1816 LVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQR 1862
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1724-1953 |
7.69e-14 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 75.57 E-value: 7.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1724 AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1803
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1804 VEFLEQ---SMVDKSLVSRQEAKIREL---ETRLEFERTqVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQ 1877
Cdd:COG4942 99 LEAQKEelaELLRALYRLGRQPPLALLlspEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1878 RQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEG 1953
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1253-1734 |
1.22e-13 |
|
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: 76.75 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDernTGESASQLldaETAERLrAEKEMKELQTQ 1332
Cdd:pfam01576 628 EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDD---VGKNVHEL---ERSKRA-LEQQVEEMKTQ 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKKQMEVMEMevmeARL-----IRAAEINGEVD---DDDAGGEWRLKYERAVREvdftkkrLQQEFEDKLEVEQQ-- 1402
Cdd:pfam01576 701 LEELEDELQATED----AKLrlevnMQALKAQFERDlqaRDEQGEEKRRQLVKQVRE-------LEAELEDERKQRAQav 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1403 -NKRQLERRLGDLQADSEESQR----ALQQLKK---KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEA 1474
Cdd:pfam01576 770 aAKKKLELDLKELEAQIDAANKgreeAVKQLKKlqaQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDL 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1475 QREKLQREKLQREKDmllaeafslkqqleekdmdiagftqkvvsleaELQDISSQESKDEASLAKVKkqlRDLEAKVKDQ 1554
Cdd:pfam01576 850 AASERARRQAQQERD--------------------------------ELADEIASGASGKSALQDEK---RRLEARIAQL 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1555 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEmESRDEEVEEARQSCQKKLKQMEVQL-EEEYEDKQKVLREKRELE 1633
Cdd:pfam01576 895 EEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAE-RSTSQKSESARQQLERQNKELKAKLqEMEGTVKSKFKSSIAALE 973
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1634 GKLATLSDQVnrrdfESEKRLR----KDLKRTKALLADAQLMLDHLKNSAPSKREIA--------QLKNQLEESEFTCAA 1701
Cdd:pfam01576 974 AKIAQLEEQL-----EQESRERqaanKLVRRTEKKLKEVLLQVEDERRHADQYKDQAekgnsrmkQLKRQLEEAEEEASR 1048
|
490 500 510
....*....|....*....|....*....|...
gi 42794779 1702 AVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1734
Cdd:pfam01576 1049 ANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1385-1944 |
2.19e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.16 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1385 TKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEES---QRALQQLKKKCQRLTA-----ELQDTKLHLEGQQVRNHEL 1456
Cdd:TIGR00618 219 ERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQlkkQQLLKQLRARIEELRAqeavlEETQERINRARKAAPLAAH 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1457 EKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQ--LEEKDMDIAGFTQKVVSLEAELQDISSQESKDE 1534
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQrrLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1535 ASLAKVKKQLRDLEAKVK---DQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLkQM 1611
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTSAFRDLQGQLAHAK----KQQELQQRYAELCAAAITCTA-QC 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1612 EVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRL-------RKDLKRTKALLADAQLMLDHLKNSAPSKR- 1683
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLlelqeepCPLCGSCIHPNPARQDIDNPGPLTRRMQRg 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1684 --EIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmnELMKK 1761
Cdd:TIGR00618 534 eqTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSE---AEDML 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 HKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ--------------------- 1820
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVlpkellasrqlalqkmqseke 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1821 ------------EAKIRELETRLEFERTQVKRLESLASRLKENME-----------KLTEERDQRIAAENREKEQN---- 1873
Cdd:TIGR00618 691 qltywkemlaqcQTLLRELETHIEEYDREFNEIENASSSLGSDLAaredalnqslkELMHQARTVLKARTEAHFNNneev 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1874 --------------KRLQRQLRDTKEEMGELARKEAE--ASRKKHELEMDLESLEAANQSLQADLKLAFKriGDLQAAIE 1937
Cdd:TIGR00618 771 taalqtgaelshlaAEIQFFNRLREEDTHLLKTLEAEigQEIPSDEDILNLQCETLVQEEEQFLSRLEEK--SATLGEIT 848
|
....*..
gi 42794779 1938 DEMESDE 1944
Cdd:TIGR00618 849 HQLLKYE 855
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1254-1738 |
2.54e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntGESASQLLDAETAERLRAEKEMKELQTQY 1333
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLL--AEAGLDDADAEAVEARREELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1334 DALKKQMEVMEMEVMEARLIRAAEingevDDDDAGGEWRLKYERAVREVDFTKKRLqQEFEDKLEVEQQNKRQLERRLGD 1413
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDAD-----DLEERAEELREEAAELESELEEAREAV-EDRREEIEELEEEIEELRERFGD 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1414 LQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRnheLEKKQRRFDS----ELSQAHEEAQR-EKLQREKLQREK 1488
Cdd:PRK02224 403 APVDLGNAEDFLEELREERDELREREAELEATLRTARER---VEEAEALLEAgkcpECGQPVEGSPHvETIEEDRERVEE 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1489 dmLLAEAFSLKQQLEEKDMDIagftqkvvsleAELQDISSQESKDEaslaKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1568
Cdd:PRK02224 480 --LEAELEDLEEEVEEVEERL-----------ERAEDLVEAEDRIE----RLEERREDLEELIAERRETIEEKRERAEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1569 EQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE------------EEYEDKQKVLREKRElegKL 1636
Cdd:PRK02224 543 RERAAELEAEAEEKREA-AAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllaaiADAEDEIERLREKRE---AL 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1637 ATLSDQvnRRDFESEKRLRK-------DLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavKARKAM 1709
Cdd:PRK02224 619 AELNDE--RRERLAEKRERKreleaefDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ----------AEIGAV 686
|
490 500
....*....|....*....|....*....
gi 42794779 1710 EVEIEDLhlqiDDIAKAKTALEEQLSRLQ 1738
Cdd:PRK02224 687 ENELEEL----EELRERREALENRVEALE 711
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1254-2003 |
2.56e-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: 76.03 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAErLRAEKEMkELQTQY 1333
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE-KRDELNG-ELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1334 DALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVD-FTKK--RLQQEFED-KLEVEQQNKRQLER 1409
Cdd:pfam12128 315 AAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKaLTGKhqDVTAKYNRrRSKIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1410 RLGDLQADSEESQRALQQLKKKCQRLTAELqdtklhlegqqvrNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKD 1489
Cdd:pfam12128 395 IKDKLAKIREARDRQLAVAEDDLQALESEL-------------REQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1490 MLLaeafslkqQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDE-------QA 1562
Cdd:pfam12128 462 LLL--------QLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpQA 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1563 GTIQmleqAKLRLEMEM--ERMRQTHSKEMESR---DEEVEEARQSCQKKLKQMEVQLEE----EYEDKQKVLREKRE-L 1632
Cdd:pfam12128 534 GTLL----HFLRKEAPDweQSIGKVISPELLHRtdlDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEELRERLDkA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1633 EGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAqlmLDHLKNSapsKREIAQLKNQLEESEFTCAAAVKARKAMEVE 1712
Cdd:pfam12128 610 EEALQSAREKQAAAE-EQLVQANGELEKASREETFA---RTALKNA---RLDLRRLFDEKQSEKDKKNKALAERKDSANE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 iedlhlQIDDIAKAKTALEeqlsrlqrekNEIQNRLEEDQEDMNElmkkHKAAVAQASRDLaqINDLQAQLEEANKEKQE 1792
Cdd:pfam12128 683 ------RLNSLEAQLKQLD----------KKHQAWLEEQKEQKRE----ARTEKQAYWQVV--EGALDAQLALLKAAIAA 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1793 LQEKLQALQSQVEF-----LEQSMVDKSLVSRQEAKIRELETRLEfertQVKRLESLASRLKENMEKLTEERDQRIAAEN 1867
Cdd:pfam12128 741 RRSGAKAELKALETwykrdLASLGVDPDVIAKLKREIRTLERKIE----RIAVRRQEVLRYFDWYQETWLQRRPRLATQL 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1868 REKEQNkrlQRQLRDtkeemgELARKEAEASRKKHELEMDLESLEAANQSLQADLklafKRIGDLQAAIEDEMESDENED 1947
Cdd:pfam12128 817 SNIERA---ISELQQ------QLARLIADTKLRRAKLEMERKASEKQQVRLSENL----RGLRCEMSKLATLKEDANSEQ 883
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1948 LinsegdsdvDSELEDRVDGVKSWLSKNKGPSKAAS-----DDGSLKS---SSPTSYWKSLAPD 2003
Cdd:pfam12128 884 A---------QGSIGERLAQLEDLKLKRDYLSESVKkyvehFKNVIADhsgSGLAETWESLREE 938
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1711-1872 |
6.32e-13 |
|
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: 70.34 E-value: 6.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1711 VEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQ---EDMNELMKKHKAAVAQASrdlAQINDLQAQLEEAN 1787
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKtelEDLEKEIKRLELEIEEVE---ARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1788 KEKQelqekLQALQSQVEFLEQsmvdksLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAEN 1867
Cdd:COG1579 87 NNKE-----YEALQKEIESLKR------RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*
gi 42794779 1868 REKEQ 1872
Cdd:COG1579 156 AELEE 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1467-1669 |
8.20e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1467 LSQAHEEAQREKlQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRD 1546
Cdd:COG4942 16 AAQADAAAEAEA-ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1547 LEAKVKDQEEELDEQAGTIQML-EQAKLRLEM------EMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEY 1619
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLspedflDAVRRLQYLKYLAPARREQAEELRAD-LAELAALRAELEAER 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1620 EDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQ 1669
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1697-1917 |
1.56e-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: 71.72 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1697 FTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQI 1776
Cdd:COG4942 13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1777 NDLQAQLEEankEKQELQEKLQALQ---------------SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRL 1841
Cdd:COG4942 93 AELRAELEA---QKEELAELLRALYrlgrqpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1842 ESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQS 1917
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1429-1971 |
3.63e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 72.18 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1429 KKKCQRLTAELQDTKlHLEGQQVRNHELEKKQRRFDS------ELSQAHEEAQREKLQREKLQREKDMLLAEafsLKQQL 1502
Cdd:pfam12128 217 RLNRQQVEHWIRDIQ-AIAGIMKIRPEFTKLQQEFNTlesaelRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1503 EEKDMDIagftqkvvsleaelqdissQESKDEASLakvkkQLRDLEAKVKDQEEEL---DEQAGTIQMLEQAKLRLEMEM 1579
Cdd:pfam12128 293 RTLDDQW-------------------KEKRDELNG-----ELSAADAAVAKDRSELealEDQHGAFLDADIETAAADQEQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1580 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFES-EKRLRKDL 1658
Cdd:pfam12128 349 LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQAlESELREQL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1659 KRTKALLADAQLM----LDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQL 1734
Cdd:pfam12128 429 EAGKLEFNEEEYRlksrLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQ---SELRQARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1735 SRLQREK---NEIQNRLEEDQE-------DMNELMKKHKAAVAQ-----ASRDLAQINDLQAQLEEANKeKQELQeklqa 1799
Cdd:pfam12128 506 EALRQASrrlEERQSALDELELqlfpqagTLLHFLRKEAPDWEQsigkvISPELLHRTDLDPEVWDGSV-GGELN----- 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1800 LQSQVEFLEQSMVDKSLVSRQEAKIR--ELETRLEFERTQVKRLESLASRLKENMEKLT-EERDQRIAAENREKEQnKRL 1876
Cdd:pfam12128 580 LYGVKLDLKRIDVPEWAASEEELRERldKAEEALQSAREKQAAAEEQLVQANGELEKASrEETFARTALKNARLDL-RRL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1877 ---QRQLRDTKEEMGELARKEAEASRKK--HELEMDLESLEAANQSLQADLKLAfkRIGDLQAAIEDEMESDENEDLINS 1951
Cdd:pfam12128 659 fdeKQSEKDKKNKALAERKDSANERLNSleAQLKQLDKKHQAWLEEQKEQKREA--RTEKQAYWQVVEGALDAQLALLKA 736
|
570 580
....*....|....*....|
gi 42794779 1952 EGDSdVDSELEDRVDGVKSW 1971
Cdd:pfam12128 737 AIAA-RRSGAKAELKALETW 755
|
|
| PDZ_SHANK1_3-like |
cd06746 |
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ... |
219-307 |
4.85e-12 |
|
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: 64.15 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGdFGFSLRRT---------TMLDRGPEGQACRRVvhfaEPGaGTKDLAlGLVPGDRLVEINGHNVESKSR 289
Cdd:cd06746 7 RTVVLQKGDKG-FGFVLRGAkavgpilefTPTPAFPALQYLESV----DPG-GVADKA-GLKKGDFLLEINGEDVVKASH 79
|
90
....*....|....*...
gi 42794779 290 DEIVEMIRQSGDSVRLKV 307
Cdd:cd06746 80 EQVVNLIRQSGNTLVLKV 97
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1248-1868 |
5.44e-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: 71.41 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRN-KDEEIQQLRSKLEKAEKERNELRLNSDRL--------------ESRISELTSELTD--ERNTGESASQ 1310
Cdd:pfam12128 323 ELEALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLkaltgkhqdvtakyNRRRSKIKEQNNRdiAGIKDKLAKI 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1311 lldAETAERLRAEKEmKELQTQYDALKKQMEVMEMEVMEARL---IRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKK 1387
Cdd:pfam12128 403 ---REARDRQLAVAE-DDLQALESELREQLEAGKLEFNEEEYrlkSRLGELKLRLNQATATPELLLQLENFDERIERARE 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1388 RLQQEFedkleveqQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRfDSEL 1467
Cdd:pfam12128 479 EQEAAN--------AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAP-DWEQ 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1468 SQAhEEAQREKLQREKLQREKDMLLAEA----FSLKQQLEEkdMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1543
Cdd:pfam12128 550 SIG-KVISPELLHRTDLDPEVWDGSVGGelnlYGVKLDLKR--IDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQ 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQ 1623
Cdd:pfam12128 627 LVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1624 KVLREkrelegklATLSDQVNRRDFESEKRLRkdLKRTKALLADAQlmldhlknsAPSKREIAQLKNQLEESEFTCAAAV 1703
Cdd:pfam12128 707 EQKRE--------ARTEKQAYWQVVEGALDAQ--LALLKAAIAARR---------SGAKAELKALETWYKRDLASLGVDP 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1704 KARKAMEVEIEDLHLQIDDIAKAKTALEE----QLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDL 1779
Cdd:pfam12128 768 DVIAKLKREIRTLERKIERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEME 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1780 QAQLEEANKEKQELQEKLQALQSQVEFLeqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1859
Cdd:pfam12128 848 RKASEKQQVRLSENLRGLRCEMSKLATL-----------KEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHF 916
|
....*....
gi 42794779 1860 DQRIAAENR 1868
Cdd:pfam12128 917 KNVIADHSG 925
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1478 |
8.66e-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: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1252 SEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELtderntgESASQLLDAETAERLRAEKEMKELQT 1331
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-------RALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1332 QYDALKKQmevmemevmEARLIRAAEINGEVD--------DDDAGGEWRLKYERAVREVDftKKRLQQEFEDKLEVEQQN 1403
Cdd:COG4942 98 ELEAQKEE---------LAELLRALYRLGRQPplalllspEDFLDAVRRLQYLKYLAPAR--REQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1404 KRQLERR--LGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAHEEAQREK 1478
Cdd:COG4942 167 AELEAERaeLEALLAELEEERAALEALKAERQKLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1262-1799 |
8.89e-12 |
|
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: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1262 EIQQLRSKLEKAEKERNELRLNSDR----LESRISELTSELTDERNTGE------SASQLLDAETAERLRAEKEMKELQT 1331
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRarieLEKKASALKRQLDRESDRNQelqkriRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1332 QY-DALKKQMEVMEMEVMEARLIRAAeINGEVddddagGEWRLKYERAVREVDFTKKRLQqEFEDKLEVEQQNKRQLERR 1410
Cdd:pfam05557 83 KYlEALNKKLNEKESQLADAREVISC-LKNEL------SELRRQIQRAELELQSTNSELE-ELQERLDLLKAKASEAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1411 LGDLQADSEESQRALQQLKKKCQRLTAELQDTKL--HLEGQQVRNHELEKKQRRFDSELSQAHE--------EAQREKLQ 1480
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIvkNSKSELARIPELEKELERLREHNKHLNEnienklllKEEVEDLK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1481 ReKLQREKDMLlAEAFSL---KQQLEEK-------DMD--------------IAGFTQKVVSLEAELQDISSQESKDEAS 1536
Cdd:pfam05557 235 R-KLEREEKYR-EEAATLeleKEKLEQElqswvklAQDtglnlrspedlsrrIEQLQQREIVLKEENSSLTSSARQLEKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1537 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ------------THSKEMESRDEEVEEARQSC 1604
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAilesydkeltmsNYSPQLLERIEEAEDMTQKM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1605 QKKLKQMEVQLEeeyedkqKVLREKRELEGKLATLSDQVnrrdfesekrlrkDLKRTKALLADaqlmldhlknSAPSKRE 1684
Cdd:pfam05557 393 QAHNEEMEAQLS-------VAEEELGGYKQQAQTLEREL-------------QALRQQESLAD----------PSYSKEE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1685 IAQLKNQLEESEFTCAAAVKARKAMEVEIED--------------LHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEE 1750
Cdd:pfam05557 443 VDSLRRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKK 522
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 42794779 1751 DQEDMNELMKKHKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQA 1799
Cdd:pfam05557 523 LEDDLEQVLRLPETTSTMNFK---EVLDLRKELESAELKNQRLKEVFQA 568
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1390-1811 |
1.11e-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: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1390 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRrfdsELSQ 1469
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHE-------ELEEKYK----ELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1470 AHEEaqreklqrekLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEA 1549
Cdd:pfam07888 109 SSEE----------LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1550 KVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDeeveearqSCQKKLKQMEVQLEEEYEDKQKVLREK 1629
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT--------TAHRKEAENEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1630 RELEGKLATLSDQVNRRDfesekrlrkdlkRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAAVKA-RKA 1708
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRD------------RTQAELHQARLQAAQLTL------QLADASLALREGRARWAQERETlQQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1709 MEVEIEDLHLQIDDIAKAKTALEEQlsRLQREKNEIqnrleedqedmnELMKKHKAAVAQASRDLAQINDLQAQLEEANK 1788
Cdd:pfam07888 313 AEADKDRIEKLSAELQRLEERLQEE--RMEREKLEV------------ELGREKDCNRVQLSESRRELQELKASLRVAQK 378
|
410 420
....*....|....*....|...
gi 42794779 1789 EKQELQEKLQALQSQVEFLEQSM 1811
Cdd:pfam07888 379 EKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PDZ |
smart00228 |
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ... |
218-309 |
1.73e-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: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 218 LRELELQRRPTGdFGFSLRRTTMLDRGPEgqacrrVVHFAEPGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:smart00228 2 PRLVELEKGGGG-LGFSLVGGKDEGGGVV------VSSVVPGSPAAKA---GLRVGDVILEVNGTSVEGLTHLEAVDLLK 71
|
90
....*....|..
gi 42794779 298 QSGDSVRLKVQP 309
Cdd:smart00228 72 KAGGKVTLTVLR 83
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1719-1952 |
1.99e-11 |
|
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: 69.70 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1719 QIDDIAKAK-----TALEEQ--LSRLQREKNEIQNRLEEDQEDM-------NELMK-----KHKAAVAQASRDL------ 1773
Cdd:TIGR02168 145 KISEIIEAKpeerrAIFEEAagISKYKERRKETERKLERTRENLdrledilNELERqlkslERQAEKAERYKELkaelre 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 --------------AQINDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLVSRQE------AKIRELETRL 1831
Cdd:TIGR02168 225 lelallvlrleelrEELEELQEELKEAEEELEELTAELQELEEKLEELrlEVSELEEEIEELQKelyalaNEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1832 EFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1911
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 42794779 1912 EAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSE 1952
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1576-1916 |
2.68e-11 |
|
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: 69.00 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1576 EMEMERMRQTH---SKEMESRD--EEVEEARQScqkklkQMEVQLEEEYEDKQKVLREKRELEgklaTLSDQVNRRDFES 1650
Cdd:pfam17380 295 KMEQERLRQEKeekAREVERRRklEEAEKARQA------EMDRQAAIYAEQERMAMERERELE----RIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1651 --EKRLRKDLKRTKALladAQLMLDHLKNSAPSKREI-AQLKNQLEESEftcaaavKARKAMEVEIEDLHLQiddiAKAK 1727
Cdd:pfam17380 365 irQEEIAMEISRMREL---ERLQMERQQKNERVRQELeAARKVKILEEE-------RQRKIQQQKVEMEQIR----AEQE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1728 TALEEQLSRLQREKNEIQNRLEEDqedmnELMKKHkaavaqasrdlaQINDLQAQLEEANKEKQELqEKLQALQSQVEFL 1807
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLE-----EQERQQ------------QVERLRQQEEERKRKKLEL-EKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMVDKSLVSRQEAKIRELETRLEFERtqvkrleslasRLKENMEKLTEERDQRIAAENREKEQN----KRLQRQLRDT 1883
Cdd:pfam17380 493 RRKILEKELEERKQAMIEEERKRKLLEK-----------EMEERQKAIYEEERRREAEEERRKQQEmeerRRIQEQMRKA 561
|
330 340 350
....*....|....*....|....*....|....*
gi 42794779 1884 KEEMGEL--ARKEAEASRKKHELEMDLESLEAANQ 1916
Cdd:pfam17380 562 TEERSRLeaMEREREMMRQIVESEKARAEYEATTP 596
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1727-1942 |
2.78e-11 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 67.55 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1727 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMkkhkaavaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEf 1806
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN--------------EEYNELQAELEALQAEIDKLQAEIAEAEAEIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1807 LEQSMVDKSLVS--RQEAKIRELETRLEfertqVKRLESLASRLkENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTK 1884
Cdd:COG3883 83 ERREELGERARAlyRSGGSVSYLDVLLG-----SESFSDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 1885 EemgELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMES 1942
Cdd:COG3883 157 A---ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1373-1925 |
5.87e-11 |
|
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: 67.92 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1373 LKYERAVREVDFTKKRLQQEfedKLEVEQQNKRQLERRLGDLQaDSEESQRALQQL----KKKCQRLTAELQDTKLHLEG 1448
Cdd:pfam10174 41 LKKERALRKEEAARISVLKE---QYRVTQEENQHLQLTIQALQ-DELRAQRDLNQLlqqdFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1449 QQVRNHELEKKQRRFDSELSQAHEE------AQREKL--QREKLQREKDMLLAEAFSLKQQLEEKDMD--IAGFTQKVVS 1518
Cdd:pfam10174 117 NFRRLQSEHERQAKELFLLRKTLEEmelrieTQKQTLgaRDESIKKLLEMLQSKGLPKKSGEEDWERTrrIAEAEMQLGH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1519 LEAELQDISSQESKDEASLaKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVE 1598
Cdd:pfam10174 197 LEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1599 --EARQSCQKKLKQMEVQLEEEYEDKQKvlrEKRELEGKLATLSDQV--NRRDFE--------SEKR----------LRK 1656
Cdd:pfam10174 276 qmEVYKSHSKFMKNKIDQLKQELSKKES---ELLALQTKLETLTNQNsdCKQHIEvlkesltaKEQRaailqtevdaLRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1657 DLKRTKALLADAQLMLDHLKNSAPSKR-EIAQLKNQLEeseftcaaaVKARKAMEVE--IEDLHLQIDDIAKAKTALEEQ 1733
Cdd:pfam10174 353 RLEEKESFLNKKTKQLQDLTEEKSTLAgEIRDLKDMLD---------VKERKINVLQkkIENLQEQLRDKDKQLAGLKER 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1734 LSRLQREKNEIQNRL---EE---DQEDMNELMKKHKAAVAQASRDlaqindlqaQLEEANKEKQELQEKLQALQSQVEFL 1807
Cdd:pfam10174 424 VKSLQTDSSNTDTALttlEEalsEKERIIERLKEQREREDRERLE---------ELESLKKENKDLKEKVSALQPELTEK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMVD-----KSLVSR---QEAKIRELETRLEFERTQVKRLESLASRLKEnmekltEERDQRIAAENREKEQNkrLQRq 1879
Cdd:pfam10174 495 ESSLIDlkehaSSLASSglkKDSKLKSLEIAVEQKKEECSKLENQLKKAHN------AEEAVRTNPEINDRIRL--LEQ- 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 42794779 1880 lrdtkeemgELARKEAEASRKKHELEMDLESL-EAANQSLQADLKLA 1925
Cdd:pfam10174 566 ---------EVARYKEESGKAQAEVERLLGILrEVENEKNDKDKKIA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1401-1624 |
1.06e-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: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1401 QQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAheEAQREKLQ 1480
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL--EKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1481 REKLQREKDM--LLAEAFSLKQQLEEKD-MDIAGFTQKVVSLEAeLQDISSQeskDEASLAKVKKQLRDLEAKVKDQEEE 1557
Cdd:COG4942 97 AELEAQKEELaeLLRALYRLGRQPPLALlLSPEDFLDAVRRLQY-LKYLAPA---RREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQAGTIQMLEQAKLRLEMEMERMRQT---HSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQK 1624
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLlarLEKELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1714-1919 |
1.14e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 66.96 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1714 EDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQAsrdlaQINDLQAQLEEANKEKQEL 1793
Cdd:COG3206 164 QNLELRREEARKALEFLEEQL-------PELRKELEEAEAALEEFRQKNGLVDLSE-----EAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1794 QEKLQALQSQVEFLEQSM----------VDKSLVSRQEAKIRELETRLEFERT-------QVKRLESLASRLKENMEKLT 1856
Cdd:COG3206 232 RAELAEAEARLAALRAQLgsgpdalpelLQSPVIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEA 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1857 EERDQRIAAENRE-KEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQ 1919
Cdd:COG3206 312 QRILASLEAELEAlQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1253-1716 |
1.38e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 66.86 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKD-EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDE-----------RNTGESASQLLDAETAERL 1320
Cdd:COG4913 329 EAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASaeefaalraeaAALLEALEEELEALEEALA 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1321 RAEKEMKELQTQYDALKKQMEV---------MEMEVMEARLIRAAEING----------EVDDDDAggEWRL-------- 1373
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASlerrksnipARLLALRDALAEALGLDEaelpfvgeliEVRPEEE--RWRGaiervlgg 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1374 ---------KYERAVRE-VDFTKKRLQQEFE--------------------DKLEVEQQN-----KRQLERRLGDLQADS 1418
Cdd:COG4913 487 faltllvppEHYAAALRwVNRLHLRGRLVYErvrtglpdperprldpdslaGKLDFKPHPfrawlEAELGRRFDYVCVDS 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1419 EEsqralqQLKKKCQRLTAELQ----------DTKLHLEGQQV-------RNHELEKKQRRFDSELSQAHEEAQREKLQR 1481
Cdd:COG4913 567 PE------ELRRHPRAITRAGQvkgngtrhekDDRRRIRSRYVlgfdnraKLAALEAELAELEEELAEAEERLEALEAEL 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1482 EKLQRekdmlLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDIssqeSKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1561
Cdd:COG4913 641 DALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELDEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1562 AGTIQMLEQAKLRLEMEMERMRQTHSkemESRDEEVEEARQSCQKKLKQmeVQLEEEYEDKQKVLREKRE-LEGKLATLS 1640
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLE---AAEDLARLELRALLEERFAA--ALGDAVERELRENLEERIDaLRARLNRAE 786
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1641 DQVNR------RDFESEKRlrkDLKRTKALLADAQLMLDHLKNSA-PSKRE-IAQLKNQLEESEFT--CAAAVKARKAME 1710
Cdd:COG4913 787 EELERamrafnREWPAETA---DLDADLESLPEYLALLDRLEEDGlPEYEErFKELLNENSIEFVAdlLSKLRRAIREIK 863
|
....*.
gi 42794779 1711 VEIEDL 1716
Cdd:COG4913 864 ERIDPL 869
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1239-1941 |
1.47e-10 |
|
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: 66.90 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1239 LFTTVRPLIEVQLSEEQIRNKDEEIQQLRSKLEKA--------EKERNELRLNS--DRLESRISELTSELtDERN--TGE 1306
Cdd:COG3096 294 LFGARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhlNLVQTALRQQEkiERYQEDLEELTERL-EEQEevVEE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1307 SASQLLDAEtAERLRAEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEINGEVD-DDDAGGEWrlkyera 1378
Cdd:COG3096 373 AAEQLAEAE-ARLEAAEEEVDSLKSQladyqqaLDVQ--QTRAIQYQQAVQALEKARALCGLPDlTPENAEDY------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1379 vrevdftkkrlQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKkcqrLTAELQDTKLHLEGQQV-RNHELE 1457
Cdd:COG3096 443 -----------LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCK----IAGEVERSQAWQTARELlRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1458 KKQRRFDSELSQAHEEAQREKLQREKLQRekdmlLAEAF--SLKQQLEEKDMdiagFTQKVVSLEAELQDISSQESKDEA 1535
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAER-----LLEEFcqRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 SLAKVKKQLRDLEAKVKdqeeELDEQAGTIQMLEQAKLRLememermrQTHSKEMESRDEEVEEARQSCQKKLKQMEVQL 1615
Cdd:COG3096 579 QRSELRQQLEQLRARIK----ELAARAPAWLAAQDALERL--------REQSGEALADSQEVTAAMQQLLEREREATVER 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1616 EEEYEDKQKVLREKREL-------EGKLATLSDQVN-------RRDFESEKR---------LRK-----DLKRTKALLAD 1667
Cdd:COG3096 647 DELAARKQALESQIERLsqpggaeDPRLLALAERLGgvllseiYDDVTLEDApyfsalygpARHaivvpDLSAVKEQLAG 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1668 AQLMLDHL----------KNSAPSKRE-----IAQLKN-QLEESEFTcAAAVKARKAMEVEIEDLHLQIDDIAK--AKTA 1729
Cdd:COG3096 727 LEDCPEDLyliegdpdsfDDSVFDAEEledavVVKLSDrQWRYSRFP-EVPLFGRAAREKRLEELRAERDELAEqyAKAS 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1730 L----------------------------EEQLSRLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLAQINDLQA 1781
Cdd:COG3096 806 FdvqklqrlhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQ----EQQLRQQLDQLKEQLQLLNKLLP 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1782 QLEEANKEkqELQEKLQALQSQVEFLEQsmvDKSLVSRQEAKIRELETRL----------EFERTQVKRLESLASRLKEN 1851
Cdd:COG3096 882 QANLLADE--TLADRLEELREELDAAQE---AQAFIQQHGKALAQLEPLVavlqsdpeqfEQLQADYLQAKEQQRRLKQQ 956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1852 MEKLTEERDQR----------IAAENRekEQNKRLQRQLRDTKEEMGElARKEAEASRKKHE----LEMDLES-LEAANQ 1916
Cdd:COG3096 957 IFALSEVVQRRphfsyedavgLLGENS--DLNEKLRARLEQAEEARRE-AREQLRQAQAQYSqynqVLASLKSsRDAKQQ 1033
|
810 820
....*....|....*....|....*
gi 42794779 1917 SLQAdlklAFKRIGDLQAAIEDEME 1941
Cdd:COG3096 1034 TLQE----LEQELEELGVQADAEAE 1054
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1254-1870 |
1.80e-10 |
|
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: 66.61 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEE-IQQLRSKLEKAEKERNELRLNSD--RLESRISELTSELTDERNTGESASQLLDaETAErlrAEKEmkelQ 1330
Cdd:TIGR01612 1135 EEIKKKSENyIDEIKAQINDLEDVADKAISNDDpeEIEKKIENIVTKIDKKKNIYDEIKKLLN-EIAE---IEKD----K 1206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1331 TQYDALKKQMEVMEMEVMEARLiraaeinGEVDDDDAGGEWRLK-YERAVREVDFTKKRlQQEFEDKLEVEQQNKRQLEr 1409
Cdd:TIGR01612 1207 TSLEEVKGINLSYGKNLGKLFL-------EKIDEEKKKSEHMIKaMEAYIEDLDEIKEK-SPEIENEMGIEMDIKAEME- 1277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1410 rlgdlqadseesQRALQQLKKKCQRLTAELQDTKLhlegQQVRNHELEKKQRRF-DSELSQAHEEAQREKLQREKLQREK 1488
Cdd:TIGR01612 1278 ------------TFNISHDDDKDHHIISKKHDENI----SDIREKSLKIIEDFSeESDINDIKKELQKNLLDAQKHNSDI 1341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1489 DMLLAEAFSLKQQLEEKDM-----DIAGFTQKVvslEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdQEEELDEQ-- 1561
Cdd:TIGR01612 1342 NLYLNEIANIYNILKLNKIkkiidEVKEYTKEI---EENNKNIKDELDKSEKLIKKIKDDINLEECKSK-IESTLDDKdi 1417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1562 AGTIQMLEQAKLRLEMEmERMRQTHSKEMESRDEEV-------EEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEG 1634
Cdd:TIGR01612 1418 DECIKKIKELKNHILSE-ESNIDTYFKNADENNENVlllfkniEMADNKSQHILKIKKDNATNDHDFNINELKEHIDKSK 1496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1635 KLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEE--SEFTCAAAVKARKAMEVE 1712
Cdd:TIGR01612 1497 GCKDEADK-NAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIIIKEIKDahKKFILEAEKSEQKIKEIK 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLHLQiDDIAKA----KTALEEQLSrlqrekneIQNrLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAqleeaNK 1788
Cdd:TIGR01612 1576 KEKFRIE-DDAAKNdksnKAAIDIQLS--------LEN-FENKFLKISDIKKKINDCLKETESIEKKISSFSI-----DS 1640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1789 EKQELQEKLQALQSQVEFLEQsmvdkslVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENR 1868
Cdd:TIGR01612 1641 QDTELKENGDNLNSLQEFLES-------LKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
..
gi 42794779 1869 EK 1870
Cdd:TIGR01612 1714 EE 1715
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1248-1828 |
2.42e-10 |
|
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: 65.91 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGEsasqlLDAETAERLRAEKE-M 1326
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVD-----LKLQELQHLKNEGDhL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1327 KELQTQYDALKKQMEVMEMEVMEAR--LIRAAEINGEvDDDDAGGewrLKYERAVREVDFTKKRLQ-QEFEDKLEVEQQN 1403
Cdd:pfam15921 544 RNVQTECEALKLQMAEKDKVIEILRqqIENMTQLVGQ-HGRTAGA---MQVEKAQLEKEINDRRLElQEFKILKDKKDAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQADS-------EESQRALQQLKKKCQRLTAELQDTKLHLEG---------QQVRN--HELEKKQRRFDS 1465
Cdd:pfam15921 620 IRELEARVSDLELEKvklvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSlsedyevlkRNFRNksEEMETTTNKLKM 699
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE---------------------AELQ 1524
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEeamtnankekhflkeeknklsQELS 779
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1525 DISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD-------EQAGTIQMLEQAKLRLEM-------EMERMRQTHSKEM 1590
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDkaslqfaECQDIIQRQEQESVRLKLqhtldvkELQGPGYTSNSSM 859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1591 ESR-DEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE--KRELEGKLATLSDQVNRRDFESEKRlRKDLKRTKALLAD 1667
Cdd:pfam15921 860 KPRlLQPASFTRTHSNVPSSQSTASFLSHHSRKTNALKEdpTRDLKQLLQELRSVINEEPTVQLSK-AEDKGRAPSLGAL 938
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1668 AQLMLDHLKNSAPSKREIAQLKNQLE----ESEFTCAAAVKARKAMevEIEDLHLQIDDIAKAKTALEEQLSR---LQRE 1740
Cdd:pfam15921 939 DDRVRDCIIESSLRSDICHSSSNSLQtegsKSSETCSREPVLLHAG--ELEDPSSCFTFPSTASPSVKNSASRsfhSSPK 1016
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1741 KNEIQNRLEEDQEDMNELMKKHKAAVAQASRDlaQINDLQAQ-LEEANKEKQELQEKLQALQSQVEFLE---QSMvdKSL 1816
Cdd:pfam15921 1017 KSPVHSLLTSSAEGSIGSSSQYRSAKTIHSPD--SVKDSQSLpIETTGKTCRKLQNRLESLQTLVEDLQlknQAM--SSM 1092
|
650
....*....|..
gi 42794779 1817 VSRQEAKIRELE 1828
Cdd:pfam15921 1093 IRNQEKRIQKVK 1104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1248-1526 |
2.56e-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: 65.86 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAE---- 1323
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAElskl 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1324 -KEMKELQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQqEFEDKLEVEQQ 1402
Cdd:TIGR02169 804 eEEVSRIEARLREIEQKLNRLTLEKEYLE----KEIQELQEQRI---DLKEQIKSIEKEIENLNGKKE-ELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1403 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVR----NHELEKKQRRFDSELSQAHEEAQREK 1478
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKlealEEELSEIEDPKGEDEEIPEEELSLED 955
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1479 LQREKLQREKDMLLAEAFSLK--QQLEEKDMDIAGFTQKVVSLEAELQDI 1526
Cdd:TIGR02169 956 VQAELQRVEEEIRALEPVNMLaiQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1515-1921 |
2.56e-10 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 65.53 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1515 KVVSLEAELQDISSQESKDEASLakvKKQLRDLEAKVKDQEEELDEQAgtiqmleQAKLRLEMEMERMRQTHSKEMESRD 1594
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEH---KRARIELEKKASALKRQLDRES-------DRNQELQKRIRLLEKREAEAEEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1595 EEVEEARQscQKKLKQMEVQLEEEYEDKQKVLRE-KRELEGKLATLSDQVNRRDFEsekrlrkdLKRTKALLADAQLMLD 1673
Cdd:pfam05557 73 EQAELNRL--KKKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELE--------LQSTNSELEELQERLD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1674 HLKNSApskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEdlhLQIDDIAKAKTALEEQLS--RLQREkneiQNRLEED 1751
Cdd:pfam05557 143 LLKAKA---SEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQ---SQEQDSEIVKNSKSELARipELEKE----LERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1752 QEDMNELMKKH---KAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQ-----------------ALQSQVEFLEQSm 1811
Cdd:pfam05557 213 NKHLNENIENKlllKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQswvklaqdtglnlrspeDLSRRIEQLQQR- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1812 vDKSLVSRQ-----------------EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERD-QRIAAENREKEQN 1873
Cdd:pfam05557 292 -EIVLKEENssltssarqlekarrelEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgYRAILESYDKELT 370
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1874 -KRLQRQLRDTKEEMGELARK-EAEASRKKHELEMDLESLEAANQSLQAD 1921
Cdd:pfam05557 371 mSNYSPQLLERIEEAEDMTQKmQAHNEEMEAQLSVAEEELGGYKQQAQTL 420
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1614-1960 |
2.61e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 64.54 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQlmldhlknsapskREIAQLKNQLE 1693
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAR-------------EELEQLEEELE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1694 ESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1773
Cdd:COG4372 70 QAR-------SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1853
Cdd:COG4372 143 SEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1854 KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQ 1933
Cdd:COG4372 223 AKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLL 302
|
330 340
....*....|....*....|....*..
gi 42794779 1934 AAIEDEMESDENEDLINSEGDSDVDSE 1960
Cdd:COG4372 303 NLAALSLIGALEDALLAALLELAKKLE 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1595-1820 |
2.82e-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: 64.40 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1595 EEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESE------KRLRKDLKRTKALLADA 1668
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaelAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1669 QLMLDHLKNSAPSKREIAQLKNQLEESEFtcAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQ--- 1745
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEall 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1746 NRLEEDQEDMNELMKKHKAAVAQASRDLAQindLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQ 1820
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAE---LAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1465-1811 |
4.02e-10 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 64.86 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1465 SELSQAHEEAQREKLQREKLQRE--KDmLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS---LEAE--LQDISSQE 1530
Cdd:PRK04778 129 QELLESEEKNREEVEQLKDLYRElrKS-LLANRFSfgpaldeLEKQLENLEEEFSQFVELTESgdyVEAReiLDQLEEEL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1531 SKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSK---EMESRD-EEVEEARQ 1602
Cdd:PRK04778 208 AALEQIMEEIPELLKELQTELPDQLQEL--KAGYRELVEEgyhlDHLDIEKEIQDLKEQIDEnlaLLEELDlDEAEEKNE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1603 SCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ----------------VNRRDFESEKRLRKDLKRTKALLa 1666
Cdd:PRK04778 286 EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQnkelkeeidrvkqsytLNESELESVRQLEKQLESLEKQY- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1667 daqlmLDHLKNSAPSKREIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQN 1746
Cdd:PRK04778 365 -----DEITERIAEQEIAYSELQEELEEIL-------KQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNKLHEIKR 432
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1747 RLE--------EDQEDMNELMKKHkaaVAQASRDLAQ----INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1811
Cdd:PRK04778 433 YLEksnlpglpEDYLEMFFEVSDE---IEALAEELEEkpinMEAVNRLLEEATEDVETLEEETEELVENATLTEQLI 506
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1377-1925 |
4.09e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 65.36 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1377 RAVREVDFTKKRLQQEFEDKLEVEQQNKRQ------LERRLGDLQADSEESQRALQQLKKKCQRLTA------ELQDTkl 1444
Cdd:PRK04863 534 RAERLLAEFCKRLGKNLDDEDELEQLQEELearlesLSESVSEARERRMALRQQLEQLQARIQRLAArapawlAAQDA-- 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1445 hlegqqvrnheLEKKQRRFDSEL--SQAHEEAQREKLQREK-LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLeA 1521
Cdd:PRK04863 612 -----------LARLREQSGEEFedSQDVTEYMQQLLEREReLTVERDELAARKQALDEEIERLSQPGGSEDPRLNAL-A 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1522 E------LQDISSQESKDEA-----------------SLAKVKKQLRDLEAKVKD----------------QEEELDE-- 1560
Cdd:PRK04863 680 ErfggvlLSEIYDDVSLEDApyfsalygparhaivvpDLSDAAEQLAGLEDCPEDlyliegdpdsfddsvfSVEELEKav 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1561 --QAGTIQML---------------EQaklRLEmEMERMRQTHSKEMESRDEEVeearQSCQKKLKQME--------VQL 1615
Cdd:PRK04863 760 vvKIADRQWRysrfpevplfgraarEK---RIE-QLRAEREELAERYATLSFDV----QKLQRLHQAFSrfigshlaVAF 831
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1616 EEEYEDKQKVLREKR-ELEGKLATLSDQvnrrdfesEKRLRKDLKRTKALLADAQLMLDHLKNSAPSK--REIAQLKNQL 1692
Cdd:PRK04863 832 EADPEAELRQLNRRRvELERALADHESQ--------EQQQRSQLEQAKEGLSALNRLLPRLNLLADETlaDRVEEIREQL 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1693 EESEFtcAAAVKARKAMEVEiedlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE---DMNELM-KKHKAAVAQ 1768
Cdd:PRK04863 904 DEAEE--AKRFVQQHGNALA------QLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQqafALTEVVqRRAHFSYED 975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1769 ASRDLAQINDLQAQLEEANKEKQELQEKL--QALQSQVEFLEQSMVDKSLVSRQEAKireLETRLEFERtqvkRLESLAS 1846
Cdd:PRK04863 976 AAEMLAKNSDLNEKLRQRLEQAEQERTRAreQLRQAQAQLAQYNQVLASLKSSYDAK---RQMLQELKQ----ELQDLGV 1048
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1847 RLKENME-KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEmdlESLEAANQSLQADLKLA 1925
Cdd:PRK04863 1049 PADSGAEeRARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR---EQVVNAKAGWCAVLRLV 1125
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1379-1984 |
5.10e-10 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 64.92 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1379 VREVDFTKKRLQQEfedKLEVEQQNKR--QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHEL 1456
Cdd:PRK01156 182 ISNIDYLEEKLKSS---NLELENIKKQiaDDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1457 EKKQRRFDSELSQAHE----EAQREKLQREKLQREKDMLLaEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQEsK 1532
Cdd:PRK01156 259 KTAESDLSMELEKNNYykelEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ-K 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1533 DEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLE---MEMERMRQTHS---KEMESRDEEVEEARQSCQK 1606
Cdd:PRK01156 337 DYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEeysKNIERMSAFISeilKIQEIDPDAIKKELNEINV 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1607 KLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQ----VNRRDFESEK--RLRKDLKRTKALLADAqlmLDHLKNSAP 1680
Cdd:PRK01156 417 KLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpVCGTTLGEEKsnHIINHYNEKKSRLEEK---IREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1681 S----KREIAQLKNQLEESEFT-CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIqnrLEEDQEDM 1755
Cdd:PRK01156 494 DidekIVDLKKRKEYLESEEINkSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED---LDSKRTSW 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1756 NELMkkhkaavaqASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvSRQEAKIRELETRLEFER 1835
Cdd:PRK01156 571 LNAL---------AVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDK---------SYIDKSIREIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1836 TQVKRLESLasrlkenmeklteerdqriaaenreKEQNKRLQRQLRDTKEEmgelarkeaeaSRKKHELEMDLESLEAAN 1915
Cdd:PRK01156 633 NKYNEIQEN-------------------------KILIEKLRGKIDNYKKQ-----------IAEIDSIIPDLKEITSRI 676
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1916 QSLQADLKLAFKRigdLQAAIEDEMESDENEDLINSEgdsdvDSELEDRVDGVKSWLSKNKGPSKAASD 1984
Cdd:PRK01156 677 NDIEDNLKKSRKA---LDDAKANRARLESTIEILRTR-----INELSDRINDINETLESMKKIKKAIGD 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1592-1944 |
7.31e-10 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 7.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1592 SRDEEVEEARqscqkklkqmEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLM 1671
Cdd:pfam01576 1 TRQEEEMQAK----------EEELQKVKERQQKAESELKELEKKHQQLCEEKN--------ALQEQLQAETELCAEAEEM 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1672 LDHLKNSAPSKREIAQ-LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL-------------------- 1730
Cdd:pfam01576 63 RARLAARKQELEEILHeLESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvtteakikkleedill 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1731 -EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQE--------------LQE 1795
Cdd:pfam01576 143 lEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQElekakrklegestdLQE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1796 KLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQ----VKRLESLASRLKENMEKLTEERDQRIAAEnreke 1871
Cdd:pfam01576 223 QIAELQAQIAELRAQL------AKKEEELQAALARLEEETAQknnaLKKIRELEAQISELQEDLESERAARNKAE----- 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1872 qnkrlqRQLRDTKEEMGELarkeaeasrkKHELEMDLESlEAANQSLQADLKlafKRIGDLQAAIEDEMESDE 1944
Cdd:pfam01576 292 ------KQRRDLGEELEAL----------KTELEDTLDT-TAAQQELRSKRE---QEVTELKKALEEETRSHE 344
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1390-1698 |
8.00e-10 |
|
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: 63.99 E-value: 8.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1390 QQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQrltaELQDTKLHLEGQQVRNHELEKK------QRRF 1463
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAR----EVERRRKLEEAEKARQAEMDRQaaiyaeQERM 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1464 DSELSQAHEEAQREKLQREkLQREKDMLLAEAFSLKQQLEEKDMDiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQ 1543
Cdd:pfam17380 343 AMERERELERIRQEERKRE-LERIRQEEIAMEISRMRELERLQME---RQQKNERVRQELEAARKVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELDEQagtIQMLEQAKLRlemEMERMRQTHSKEMES----RDEEVEEARQSCQKKLKQMEVQLEEEY 1619
Cdd:pfam17380 419 KVEMEQIRAEQEEARQRE---VRRLEEERAR---EMERVRLEEQERQQQverlRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1620 ----------EDKQKVLREKR-------ELEGKLATLSDQVNRRDFESEKRLRKDLKRTKAL------LADAQLMLDHLK 1676
Cdd:pfam17380 493 rrkilekeleERKQAMIEEERkrkllekEMEERQKAIYEEERRREAEEERRKQQEMEERRRIqeqmrkATEERSRLEAME 572
|
330 340
....*....|....*....|..
gi 42794779 1677 NSAPSKREIAQLKNQLEESEFT 1698
Cdd:pfam17380 573 REREMMRQIVESEKARAEYEAT 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1261-1518 |
9.54e-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: 62.86 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1261 EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQM 1340
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1341 EVMEMEVmeARLIRAAEINGEVDdddaggewrlkyeravrevdftkkrlqqefEDKLEVEQQNKRQLERRLGDLQADSEE 1420
Cdd:COG4942 100 EAQKEEL--AELLRALYRLGRQP------------------------------PLALLLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1421 SQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQ 1500
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250
....*....|....*...
gi 42794779 1501 QLEEKDMDIAGFTQKVVS 1518
Cdd:COG4942 228 LIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1253-1798 |
1.01e-09 |
|
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: 63.97 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1332
Cdd:pfam05483 274 EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDAlkkqmevmeMEVMEARLIRAAEINGEVDDDdaggewRLKyeraVREVDFTKKRLQQE----FEDKLEVEQQNKRQLE 1408
Cdd:pfam05483 354 FEA---------TTCSLEELLRTEQQRLEKNED------QLK----IITMELQKKSSELEemtkFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1409 RRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREK 1488
Cdd:pfam05483 415 AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1489 DMLLAEAFSLKQqlEEKDMdiagftqkVVSLEAELQDISSQESKDEASLAKVkKQLRDLEAKVKDQEEELDEQagTIQML 1568
Cdd:pfam05483 495 DKLLLENKELTQ--EASDM--------TLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELESVREE--FIQKG 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1569 EQAKLRLEMEMERMRQThSKEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKVLREKRELEGK-LATLSDQVNR 1645
Cdd:pfam05483 562 DEVKCKLDKSEENARSI-EYEVLKKEKQMKILENKCNNLKKQIENKNKniEELHQENKALKKKGSAENKqLNAYEIKVNK 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1646 RDFEsekrlrkdlkrtkalLADAQLMLDHLKNSAPSKREIAQLknqleeSEFTCAAAVKARKAMEVEIEDLHLQIDDIAK 1725
Cdd:pfam05483 641 LELE---------------LASAKQKFEEIIDNYQKEIEDKKI------SEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1726 AKTAleEQLSRLQREKNEIQNRLEEDQEDM----NELMKKHKAAVA---QASRDLAQINDLQAQLEEANKEKQELQEKLQ 1798
Cdd:pfam05483 700 HKIA--EMVALMEKHKHQYDKIIEERDSELglykNKEQEQSSAKAAleiELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1250-1772 |
1.08e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.98 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1250 QLSEEQiRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESR-------ISELTSELTDERNTGESASQLLDAETAE-RLR 1321
Cdd:pfam15921 367 QFSQES-GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSEcQGQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1322 AEKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAeingeVDDDDAGgewRLKYERAVREVDFTKKRLQQEfEDKLEVEQ 1401
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKV-----VEELTAK---KMTLESSERTVSDLTASLQEK-ERAIEATN 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1402 QNKRQLERR----LGDLQADSEESQRaLQQLKKKCQRLTAEL--QDTKLHLEGQQVRNhelekkQRRFDSELSQAHEEAQ 1475
Cdd:pfam15921 517 AEITKLRSRvdlkLQELQHLKNEGDH-LRNVQTECEALKLQMaeKDKVIEILRQQIEN------MTQLVGQHGRTAGAMQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1476 REKLQREKLQREKDMLLAEAFSLKqqlEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQE 1555
Cdd:pfam15921 590 VEKAQLEKEINDRRLELQEFKILK---DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR 666
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1556 EELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS-------------------------------C 1604
Cdd:pfam15921 667 NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghamkvamgmqkqitakrgqidaL 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1605 QKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKrLRKDLKRTKALLADAQLMLDHLKNSAPSKRE 1684
Cdd:pfam15921 747 QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEV-LRSQERRLKEKVANMEVALDKASLQFAECQD 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1685 IAQLKNQ---------------LEESEFTCAAAVKARKAMEVEIEDLHLQIddiaKAKTALEEQLSRLQREKNEIQnrlE 1749
Cdd:pfam15921 826 IIQRQEQesvrlklqhtldvkeLQGPGYTSNSSMKPRLLQPASFTRTHSNV----PSSQSTASFLSHHSRKTNALK---E 898
|
570 580
....*....|....*....|...
gi 42794779 1750 EDQEDMNELMKKHKAAVAQASRD 1772
Cdd:pfam15921 899 DPTRDLKQLLQELRSVINEEPTV 921
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1246-1603 |
1.64e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1246 LIEVQLSEEQIRNKDEEIQQLRSKLEKaEKERNElrlnsdRLESRISELTSELTDERntgesasqlldaetAERLRAEKE 1325
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEK-LKERLE------ELEEDLSSLEQEIENVK--------------SELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1326 MKELQTQYDALKKQMEVMEMEVMEARLiraAEINGEVDDDDaggEWRLKYERAVREVDFTKKRLQQEfedkLEVEQQNKR 1405
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLE---EEVSRIEARLREIEQKLNRLTLE----KEYLEKEIQ 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1406 QLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQ 1485
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1486 REKDMLLAEAFSLKQQLEEkdmdiagftqkvvsLEAELQDISSqESKDEASLAKVKKQLRDLEAKVKDQEeelDEQAGTI 1565
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSE--------------IEDPKGEDEE-IPEEELSLEDVQAELQRVEEEIRALE---PVNMLAI 978
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 42794779 1566 QMLEQAKLRL-EMEMERMR-QTHSKEMESRDEEVEEARQS 1603
Cdd:TIGR02169 979 QEYEEVLKRLdELKEKRAKlEEERKAILERIEEYEKKKRE 1018
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1370-1738 |
2.44e-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: 63.05 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1370 EWRLKYERAV--REVDFTKKRLQQEFEDKL-----EVEQQNKRqlERRLG-DLQADSEESQRALQ--QLKKKCQRLTAEL 1439
Cdd:COG3096 279 ERRELSERALelRRELFGARRQLAEEQYRLvemarELEELSAR--ESDLEqDYQAASDHLNLVQTalRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1440 QDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDML-------------LAEAfslKQQLEEKD 1506
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQqtraiqyqqavqaLEKA---RALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1507 MDIAGF--------------TQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-AKVKDQEEELDEQAGTIQMLEQA 1571
Cdd:COG3096 434 LTPENAedylaafrakeqqaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVErSQAWQTARELLRRYRSQQALAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1572 KLRLEMEMERMRQthskeMESRDEEVEEARQSCQKKLKQmEVQLEEEYEDKQKvlrekrELEGKLATLSDQVNRrdfESE 1651
Cdd:COG3096 514 LQQLRAQLAELEQ-----RLRQQQNAERLLEEFCQRIGQ-QLDAAEELEELLA------ELEAQLEELEEQAAE---AVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1652 KR--LRKDLKRTKALLADaqlmldhLKNSAPSKREIAQLKNQLEE---SEFTCAAAVKArkAMEVEIEDLH---LQIDDI 1723
Cdd:COG3096 579 QRseLRQQLEQLRARIKE-------LAARAPAWLAAQDALERLREqsgEALADSQEVTA--AMQQLLEREReatVERDEL 649
|
410
....*....|....*
gi 42794779 1724 AKAKTALEEQLSRLQ 1738
Cdd:COG3096 650 AARKQALESQIERLS 664
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1686-1950 |
3.39e-09 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 60.70 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1686 AQLKNQLEESEFTCAAAVKARKAM-EVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnELMKKHKA 1764
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED------ELNLRTSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1765 AvaqasrdlAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslvsrQEAKIRELETRLEFERTQVkrlESL 1844
Cdd:pfam00038 102 E--------NDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN---------HEEEVRELQAQVSDTQVNV---EMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1845 ASRLKENMEKLTEERDQ--RIAAENRE------KEQNKRLQRQ-------LRDTKEEMGELarkeaeaSRKKHELEMDLE 1909
Cdd:pfam00038 162 AARKLDLTSALAEIRAQyeEIAAKNREeaeewyQSKLEELQQAaarngdaLRSAKEEITEL-------RRTIQSLEIELQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1910 SLEAANQSLQA-----------DLKLAFKRIGDLQAA---IEDEMES--DENEDLIN 1950
Cdd:pfam00038 235 SLKKQKASLERqlaeteeryelQLADYQELISELEAElqeTRQEMARqlREYQELLN 291
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1682-1898 |
3.74e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 61.96 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEftcaAAVKARKAmEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedMNELMKK 1761
Cdd:COG3206 181 EEQLPELRKELEEAE----AALEEFRQ-KNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 HKAAVAQASRDlAQINDLQAQLEEANKEKQELQEKL-------QALQSQVEFLEQSmvdksLVSRQEAKIRELETRLEFE 1834
Cdd:COG3206 252 GPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQ-----LQQEAQRILASLEAELEAL 325
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1835 RTQVKRLESLASRLKENMEKLTEERDQRiaaenrekeqnKRLQRQLRDTKEEMGELARKEAEAS 1898
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELEAEL-----------RRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1740-1939 |
4.15e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1740 EKNEIQNRLEEDQEDMNELMKKHKAAV-AQASRD-LAQINDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdkslv 1817
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEdAREQIElLEPIRELAERYAAARERLAELEYLRAALRLW-------------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1818 sRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQ-RIAAENREKEQNKRLQRQLRDTKEEMGELARKEAE 1896
Cdd:COG4913 285 -FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 42794779 1897 ASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDE 1939
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1623-1799 |
4.37e-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: 59.17 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1623 QKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAA 1702
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELE-DELAALEARLEAAKTELEDLEKEIKRLEL------EIEEVEARIKKYEEQLGNV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1703 VKAR--KAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdlaqinDLQ 1780
Cdd:COG1579 86 RNNKeyEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELA----------ELE 155
|
170
....*....|....*....
gi 42794779 1781 AQLEEANKEKQELQEKLQA 1799
Cdd:COG1579 156 AELEELEAEREELAAKIPP 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1678-1874 |
5.30e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.61 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1678 SAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1757
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1758 L---MKKHKAAV-----------------------AQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1811
Cdd:COG3883 91 RaraLYRSGGSVsyldvllgsesfsdfldrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1812 VD-KSLVSRQEAKIRELETRlefERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1874
Cdd:COG3883 171 AElEAQQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| PDZ7_MUPP1-PD6_PATJ-like |
cd06671 |
PDZ domain 7 of multi-PDZ-domain protein 1 (MUPP1), PDZ domain 6 of PATJ (protein-associated ... |
219-310 |
6.68e-09 |
|
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: 55.02 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGDFGFSL---RrtTMLDRGPEGQACRRVV--HFAE-PGAGTKDLalgLVPGDRLVEINGHNVESKSRDEI 292
Cdd:cd06671 3 RRVELWREPGKSLGISIvggR--VMGSRLSNGEEIRGIFikHVLEdSPAGRNGT---LKTGDRILEVNGVDLRNATHEEA 77
|
90
....*....|....*...
gi 42794779 293 VEMIRQSGDSVRLKVQPI 310
Cdd:cd06671 78 VEAIRNAGNPVVFLVQSL 95
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1454-1812 |
7.20e-09 |
|
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: 60.64 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1454 HELEKKQRRFDSELSQ--AHEEAQREKLQ--REKLQREKDMLLAEAFS-------LKQQLEEKDMDIAGFTQKVVS---L 1519
Cdd:pfam06160 96 DDIEEDIKQILEELDEllESEEKNREEVEelKDKYRELRKTLLANRFSygpaideLEKQLAEIEEEFSQFEELTESgdyL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1520 EAE--LQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELdeQAGTIQMLEQ----AKLRLEMEMERMRQTHSKEMES- 1592
Cdd:pfam06160 176 EARevLEKLEEETDALEELMEDIPPLYEELKTELPDQLEEL--KEGYREMEEEgyalEHLNVDKEIQQLEEQLEENLALl 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1593 ---RDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQvnrrdfesEKRLRKDLKRTK------- 1662
Cdd:pfam06160 254 enlELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ--------NKELKEELERVQqsytlne 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1663 ---ALLADAQLMLDHLknsapsKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALE-------E 1732
Cdd:pfam06160 326 nelERVRGLEKQLEEL------EKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRkdelearE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1733 QLSRLQREKNEIQNRLEEDQ-----EDMNELMKKHKAAVAQASRDLAQ----INDLQAQLEEANKEKQELQEKLQALQSQ 1803
Cdd:pfam06160 400 KLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLADELNEvplnMDEVNRLLDEAQDDVDTLYEKTEELIDN 479
|
....*....
gi 42794779 1804 VEFLEQSMV 1812
Cdd:pfam06160 480 ATLAEQLIQ 488
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1706-1920 |
7.37e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 7.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1706 RKAMEVEIEDLHLQIDDIAKAKTALE---EQLSRLQ--REKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQ--IND 1778
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEdarEQIELLEpiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEaeLEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1779 LQAQLEEANKEKQELQEKLQALQSQVEFLEQSM--VDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKenmekLT 1856
Cdd:COG4913 300 LRAELARLEAELERLEARLDALREELDELEAQIrgNGGDRLEQLEREIERLERELEERERRRARLEALLAALG-----LP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1857 EERDQRIAAENREkeqnkRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1920
Cdd:COG4913 375 LPASAEEFAALRA-----EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1683-1861 |
7.92e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 58.40 E-value: 7.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1683 REIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkh 1762
Cdd:COG1579 17 SELDRLEHRLKELP-------AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1763 kaavaqasRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFERtqvKRLE 1842
Cdd:COG1579 86 --------RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEE------LAELEAELAELEAELEEKK---AELD 148
|
170
....*....|....*....
gi 42794779 1843 SLASRLKENMEKLTEERDQ 1861
Cdd:COG1579 149 EELAELEAELEELEAEREE 167
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1248-1941 |
1.12e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.74 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNEL---------RLNS-----------DRLESRISELTSELTDERNTGES 1307
Cdd:PRK04863 294 ELYTSRRQLAAEQYRLVEMARELAELNEAESDLeqdyqaasdHLNLvqtalrqqekiERYQADLEELEERLEEQNEVVEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1308 ASQLLDAETAERLRAEKEMKELQTQ-------YDALkkQMEVMEMEVMEARLIRAAEING--EVDDDDAGGewrlkyera 1378
Cdd:PRK04863 374 ADEQQEENEARAEAAEEEVDELKSQladyqqaLDVQ--QTRAIQYQQAVQALERAKQLCGlpDLTADNAED--------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1379 vrevdftkkrLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKK---KCQRLTA--ELQDTKLHLEGQQVRN 1453
Cdd:PRK04863 443 ----------WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKiagEVSRSEAwdVARELLRRLREQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1454 HELEKKQRRFdSELSQAHEEAQR-EKLQREKLQREKDMLLAEAFsLKQQLEEkdmdiagftqkvvsLEAELQDISSQesk 1532
Cdd:PRK04863 513 EQLQQLRMRL-SELEQRLRQQQRaERLLAEFCKRLGKNLDDEDE-LEQLQEE--------------LEARLESLSES--- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1533 deaslakvKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRdEEVEEARQSCQKKLKQME 1612
Cdd:PRK04863 574 --------VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDS-QDVTEYMQQLLERERELT 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1613 VQLEEEYEDKQKVLREKRELEG-------KLATLSDQVN-------RRDFESEkrlrkDLKRTKAL------------LA 1666
Cdd:PRK04863 645 VERDELAARKQALDEEIERLSQpggsedpRLNALAERFGgvllseiYDDVSLE-----DAPYFSALygparhaivvpdLS 719
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1667 DAQLMLDHLKNSAPSKREIAQLKNQLEES-----EFTCAAAVK-----------------ARKAMEVEIEDLHLQIDDIA 1724
Cdd:PRK04863 720 DAAEQLAGLEDCPEDLYLIEGDPDSFDDSvfsveELEKAVVVKiadrqwrysrfpevplfGRAAREKRIEQLRAEREELA 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1725 K--AKTA--------LEEQLSR--------------------LQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLA 1774
Cdd:PRK04863 800 EryATLSfdvqklqrLHQAFSRfigshlavafeadpeaelrqLNRRRVELERALADHESQ----EQQQRSQLEQAKEGLS 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1775 QINDLQAQL-----EEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLK 1849
Cdd:PRK04863 876 ALNRLLPRLnlladETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAK 955
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1850 ENMEKLTE--ERDQRIAAENREK--EQNKRLQRQLRdtkeemGELARKEAEASRKKHELEMDLESLEAANQsLQADLKLA 1925
Cdd:PRK04863 956 QQAFALTEvvQRRAHFSYEDAAEmlAKNSDLNEKLR------QRLEQAEQERTRAREQLRQAQAQLAQYNQ-VLASLKSS 1028
|
810
....*....|....*.
gi 42794779 1926 FKRIGDLQAAIEDEME 1941
Cdd:PRK04863 1029 YDAKRQMLQELKQELQ 1044
|
|
| PDZ_FRMPD1_3_4-like |
cd06769 |
PDZ domain of FERM and PDZ domain-containing protein 1 (FRMPD1), FRMPD3, FRMPD4, and related ... |
220-307 |
1.12e-08 |
|
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: 53.79 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLrrttmldrGPEGQACRRVVHFAEPGAGTkdlalgLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd06769 1 TVEIQRDAVLGFGFVA--------GSERPVVVRSVTPGGPSEGK------LLPGDQILKINNEPVEDLPRERVIDLIREC 66
|
....*...
gi 42794779 300 GDSVRLKV 307
Cdd:cd06769 67 KDSIVLTV 74
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1396-1881 |
1.35e-08 |
|
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: 60.22 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1396 KLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqVRNHELEKKQRRfdSELSQAHEEAQ 1475
Cdd:pfam10174 276 QMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIE---VLKESLTAKEQR--AAILQTEVDAL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1476 REKL------------QREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDissqesKDeaslakvkKQ 1543
Cdd:pfam10174 351 RLRLeekesflnkktkQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD------KD--------KQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQsCQKKLKQMEVQLEEEYEDKQ 1623
Cdd:pfam10174 417 LAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKK-ENKDLKEKVSALQPELTEKE 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1624 KVLREKRELEGKLAtlSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAV 1703
Cdd:pfam10174 496 SSLIDLKEHASSLA--SSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1704 KARKAMEVE-----IEDLHLQIDDIAKAKTALEEQLSRLQREkneiQNRLEEDQEDMNELMKKHKAAVAQASR---DLAQ 1775
Cdd:pfam10174 574 SGKAQAEVErllgiLREVENEKNDKDKKIAELESLTLRQMKE----QNKKVANIKHGQQEMKKKGAQLLEEARrreDNLA 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1776 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKS--LVSRQEAKIRELETRLEFER-----------TQVKRLE 1842
Cdd:pfam10174 650 DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKQeallaaisekdANIALLE 729
|
490 500 510
....*....|....*....|....*....|....*....
gi 42794779 1843 SLASRLKENMEKlteerdqrIAAENREKEqnkRLQRQLR 1881
Cdd:pfam10174 730 LSSSKKKKTQEE--------VMALKREKD---RLVHQLK 757
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1754-1996 |
2.09e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1754 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEf 1833
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-------------AEIAEAEAEIE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1834 erTQVKRLESLASRLKEN------MEKLTEERD-----QRIAAENREKEQNKRLQRQLRDTKEEmgeLARKEAEASRKKH 1902
Cdd:COG3883 83 --ERREELGERARALYRSggsvsyLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAE---LEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1903 ELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELEDRVDGVKSWLSKNKGPSKAA 1982
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
250
....*....|....
gi 42794779 1983 SDDGSLKSSSPTSY 1996
Cdd:COG3883 238 AAAAAAASAAGAGA 251
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1390-1803 |
2.29e-08 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 59.27 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1390 QQEFEDklEVEQQNkrqLERRLGDLQADSEESQRALQQLKkkcQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQ 1469
Cdd:pfam05667 219 AQEWEE--EWNSQG---LASRLTPEEYRKRKRTKLLKRIA---EQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTT 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1470 AHEEAQREKLQR-EKLQREKDMLLAEAFSLKQQLEEKDMDIAGfTQKVVSLEAELQDISSqeskdeaSLAKVKKQLRDLE 1548
Cdd:pfam05667 291 DTGLTKGSRFTHtEKLQFTNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLES-------SIQELEKEIKKLE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1549 AKVKDQEEELDEQAGTIQMLEQaklrlemEMERMRQTHsKEMESRDEEVEEARQSCQKKLKQMeVQLEEEYEDKQKVLRE 1628
Cdd:pfam05667 363 SSIKQVEEELEELKEQNEELEK-------QYKVKKKTL-DLLPDAEENIAKLQALVDASAQRL-VELAGQWEKHRVPLIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1629 krelegKLATLSDQVNRRDFESEKRLR--KDLK-RTKALLADAQlmldhlknsapSKRE-IAQLKNQLEE-------SEF 1697
Cdd:pfam05667 434 ------EYRALKEAKSNKEDESQRKLEeiKELReKIKEVAEEAK-----------QKEElYKQLVAEYERlpkdvsrSAY 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1698 TcaaavkaRKAMEVeIEDLHLQIDDIAKaktALEEQLSrLQREKNEIQNRLEEDQEDMNELM---KKHKAAVAQASRDLA 1774
Cdd:pfam05667 497 T-------RRILEI-VKNIKKQKEEITK---ILSDTKS-LQKEINSLTGKLDRTFTVTDELVfkdAKKDESVRKAYKYLA 564
|
410 420 430
....*....|....*....|....*....|....*.
gi 42794779 1775 QINDLQAQL----EEANK---EKQELQEKLQALQSQ 1803
Cdd:pfam05667 565 ALHENCEQLiqtvEETGTimrEIRDLEEQIETESGK 600
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1624-1907 |
2.38e-08 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 59.26 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1624 KVLREK-RELEGKLATLSDQVN--RRDFESEKRLRKDL-KRTKALLADAQLMLDHLKNSAPS-KREIAQLKNQLEEseft 1698
Cdd:PHA02562 170 KLNKDKiRELNQQIQTLDMKIDhiQQQIKTYNKNIEEQrKKNGENIARKQNKYDELVEEAKTiKAEIEELTDELLN---- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1699 caaavkarkaMEVEIEDLHLQIDDIAKAKTALEEQLSRLQR-----EKNEIQNRLEEDQEDMNELMKKHKAavaqasrdl 1773
Cdd:PHA02562 246 ----------LVMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyEKGGVCPTCTQQISEGPDRITKIKD--------- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 aQINDLQAQLEEANKEKQELQEKLqalqsqVEFLEQSMvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENME 1853
Cdd:PHA02562 307 -KLKELQHSLEKLDTAIDELEEIM------DEFNEQSK-----------KLLELKNKISTNKQSLITLVDKAKKVKAAIE 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1854 KLTEERdqriaaenrekeqnkrlqrqlRDTKEEMGELARKEAEASRKKHELEMD 1907
Cdd:PHA02562 369 ELQAEF---------------------VDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1246-1639 |
2.43e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1246 LIEVQLsEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgESASQLLDAETaerlRAEKE 1325
Cdd:pfam07888 31 LLQNRL-EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELK---EELRQSREKHE----ELEEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1326 MKELQTQYDALKKQMevmemevmearliraaeingevdddDAGGEWRLKYERAVREVDFTKKRLQQ---EFEDKLEVEQQ 1402
Cdd:pfam07888 103 YKELSASSEELSEEK-------------------------DALLAQRAAHEARIRELEEDIKTLTQrvlERETELERMKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1403 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHeeaQREKlqre 1482
Cdd:pfam07888 158 RAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAH---RKEA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1483 klqrEKDMLLAEAFSLKQQLEEKDmdiagftQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQA 1562
Cdd:pfam07888 231 ----ENEALLEELRSLQERLNASE-------RKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGR 299
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1563 GTIQMlEQAKLRLEMEMERMR-QTHSKEMESRDEEVEEARQSCQKklkqMEVQLEEEYEDKQKVLRE-KRELEGKLATL 1639
Cdd:pfam07888 300 ARWAQ-ERETLQQSAEADKDRiEKLSAELQRLEERLQEERMEREK----LEVELGREKDCNRVQLSEsRRELQELKASL 373
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1253-1750 |
2.59e-08 |
|
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: 59.07 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNE-------LRLNSDRLESRISELTSELTderntgesasqlldaetaerlRAEKE 1325
Cdd:pfam10174 246 ERNIRDLEDEVQMLKTNGLLHTEDREEeikqmevYKSHSKFMKNKIDQLKQELS---------------------KKESE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1326 MKELQTQYDALK------KQMEVMEMEVMEARLIRAAEINGEVDdddaggEWRLKYERavrevdftKKRLQQEFEDKLEV 1399
Cdd:pfam10174 305 LLALQTKLETLTnqnsdcKQHIEVLKESLTAKEQRAAILQTEVD------ALRLRLEE--------KESFLNKKTKQLQD 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1400 EQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAhEEAQREK- 1478
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL-EEALSEKe 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1479 --LQREKLQREKD--MLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ 1554
Cdd:pfam10174 450 riIERLKEQREREdrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQK 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1555 EEE---LDEQAGTIQMLEQA---------KLR-LEMEMERMRQTHSKEMESRD------EEVEEARQSCQKKLKQMEVQL 1615
Cdd:pfam10174 530 KEEcskLENQLKKAHNAEEAvrtnpeindRIRlLEQEVARYKEESGKAQAEVErllgilREVENEKNDKDKKIAELESLT 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1616 EEEYEDKQKVLREKRELE-----GKLATLSDQVNRRDFESEK--------------RLRKDLKRTKALLADAQLMLD--- 1673
Cdd:pfam10174 610 LRQMKEQNKKVANIKHGQqemkkKGAQLLEEARRREDNLADNsqqlqleelmgaleKTRQELDATKARLSSTQQSLAekd 689
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 1674 -HLKNSAPSKREiaQLKNQLEESEFTCAAAVKARKAmevEIEDLHLQiddIAKAKTALEEQLSrLQREKNEIQNRLEE 1750
Cdd:pfam10174 690 gHLTNLRAERRK--QLEEILEMKQEALLAAISEKDA---NIALLELS---SSKKKKTQEEVMA-LKREKDRLVHQLKQ 758
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1424-1804 |
3.07e-08 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 58.76 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1424 ALQQLKKKCQRLT-AELQDTKLHLEGQQVRNhELEKKQRRFDSEL-SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQ 1501
Cdd:pfam15964 333 AYEQVKQAVQMTEeANFEKTKALIQCEQLKS-ELERQKERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQN 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1502 LEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ-----AGTIQMLEQA----- 1571
Cdd:pfam15964 412 VAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEhreyrTKTGRQLEIKdqeie 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1572 KLRLEMEMERMRqthskeMESRDEEVEEARQSCQK---KLKQMEVQLEEEYEDKQKVlreKRELEGKLATLSDQVNRRDF 1648
Cdd:pfam15964 492 KLGLELSESKQR------LEQAQQDAARAREECLKlteLLGESEHQLHLTRLEKESI---QQSFSNEAKAQALQAQQREQ 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1649 ESEKRLR-------KDLKRTKALLADAQLMLDHLKnsapskREIAQLKNQLEEseftcaAAVKARKAME---VEIEDLHL 1718
Cdd:pfam15964 563 ELTQKMQqmeaqhdKTVNEQYSLLTSQNTFIAKLK------EECCTLAKKLEE------ITQKSRSEVEqlsQEKEYLQD 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1719 QIDDIAKAKTALEEQLSRLQREKNEIQNRLEEdqedmnelMKKHKAAVAQasrDLAQINDLQAQLEeanKEKQELQEKLQ 1798
Cdd:pfam15964 631 RLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ--------LDKHCQATAQ---QLVQLLSKQNQLF---KERQNLTEEVQ 696
|
....*.
gi 42794779 1799 ALQSQV 1804
Cdd:pfam15964 697 SLRSQV 702
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1453-1923 |
3.16e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.98 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1453 NHELEKKQRRFDsELSQAHEeaqreklqreklqREKDMLLAEAFSLKQQLEEKDMDiagftqkvvslEAELQDISSQESK 1532
Cdd:pfam15921 84 SHQVKDLQRRLN-ESNELHE-------------KQKFYLRQSVIDLQTKLQEMQME-----------RDAMADIRRRESQ 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1533 DEASLA-KVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQM 1611
Cdd:pfam15921 139 SQEDLRnQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1612 EVQLeeeyedkQKVLREKRE----LEGKLATLSDQVNRRDFESEKR----LRKDLKRTKALLADAQLMLDHLKNSAPSKR 1683
Cdd:pfam15921 219 GSAI-------SKILRELDTeisyLKGRIFPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSAR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1684 EIAQ-LKNQLEesefTCAAAVKARKAMEVEiedlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1762
Cdd:pfam15921 292 SQANsIQSQLE----IIQEQARNQNSMYMR------QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEA 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1763 KAAVAQASRDLAQIND-LQAQLEEANKEKQELQ-EKLQalqsqvefleqsmvDKSLVSRQEAK---IRELETRLEFERTQ 1837
Cdd:pfam15921 362 RTERDQFSQESGNLDDqLQKLLADLHKREKELSlEKEQ--------------NKRLWDRDTGNsitIDHLRRELDDRNME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1838 VKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKeemgELARKEAEASRKKhelEMDLESLEAANQS 1917
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTK----EMLRKVVEELTAK---KMTLESSERTVSD 500
|
....*.
gi 42794779 1918 LQADLK 1923
Cdd:pfam15921 501 LTASLQ 506
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1248-1643 |
3.36e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSK-------LEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDA------ 1314
Cdd:PRK02224 378 AVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpec 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1315 ----ETAERLRAEKEMKElqtqydalkkqmevmemevmearliRAAEINGEVDDddaggewrLKYERAVREVDFTKKRLQ 1390
Cdd:PRK02224 458 gqpvEGSPHVETIEEDRE-------------------------RVEELEAELED--------LEEEVEEVEERLERAEDL 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1391 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegqqvrnhelekkqrrfdSELSQA 1470
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKR---------------------EAAAEA 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1471 HEEAQREKLQREKLQREKDMLLAEAFSLkQQLEEKDMDIAGFTQKVVSLEAELQDIssQESKDEAslakvKKQLRDLEAK 1550
Cdd:PRK02224 564 EEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREAL--AELNDER-----RERLAEKRER 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1551 VKDQEEELDEQAgtIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLE--EEYEDKQKVLRE 1628
Cdd:PRK02224 636 KRELEAEFDEAR--IEEAREDKERAEEYLE--------QVEEKLDELREERDDLQAEIGAVENELEelEELRERREALEN 705
|
410
....*....|....*
gi 42794779 1629 KRElegKLATLSDQV 1643
Cdd:PRK02224 706 RVE---ALEALYDEA 717
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1466-1656 |
3.37e-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: 56.47 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQlR 1545
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1546 DLEAKVKdqeeELDEQAGTIQMLEQAKLRLEMEMErmrqthskEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKv 1625
Cdd:COG1579 90 EYEALQK----EIESLKRRISDLEDEILELMERIE--------ELEEELAELEAELAELEAELEEKKAELDEELAELEA- 156
|
170 180 190
....*....|....*....|....*....|.
gi 42794779 1626 lrEKRELEGKLATLSDQVNRRDFESEKRLRK 1656
Cdd:COG1579 157 --ELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| 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 |
3.74e-08 |
|
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: 52.62 E-value: 3.74e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42794779 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06734 45 LKVGDRILAVNGISILNLSHGDIVNLIKDSGLSVTLTIVP 84
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1713-1901 |
4.01e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.23 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQE 1792
Cdd:COG1340 3 TDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1793 LQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF-----------ERTQVKRLESLASRLK--ENMEKLTEER 1859
Cdd:COG1340 83 LNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWrqqtevlspeeEKELVEKIKELEKELEkaKKALEKNEKL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 42794779 1860 DQRIAAENREKEQNKRLQRQLRDTKEEMGEL------ARKEAEASRKK 1901
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELheemieLYKEADELRKE 210
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1373-1962 |
4.10e-08 |
|
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: 58.90 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1373 LKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgQQVR 1452
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLN-QEKT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1453 NHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESK 1532
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1533 DEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQME 1612
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1613 VQLEEEYEDkqkVLREKRELEGKLATLSDQVNRR---------------------------------DFESEKRL----- 1654
Cdd:TIGR00606 504 KSLQNEKAD---LDRKLRKLDQEMEQLNHHTTTRtqmemltkdkmdkdeqirkiksrhsdeltsllgYFPNKKQLedwlh 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1655 --RKDLKRTKALLADAQL-------MLDHLKNSAPSKRE---------------------IAQLKNQLEESEFTCAAAVK 1704
Cdd:TIGR00606 581 skSKEINQTRDRLAKLNKelasleqNKNHINNELESKEEqlssyedklfdvcgsqdeesdLERLKEEIEKSSKQRAMLAG 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEVEIEDLHLQ-------IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQA-------S 1770
Cdd:TIGR00606 661 ATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLApgrqsiiD 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1771 RDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL-------EQSMVDKSLVSRQEAKIRELETRLEferTQVKRLES 1843
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTImpeeesaKVCLTDVTIMERFQMELKDVERKIA---QQAAKLQG 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1844 L-ASRLKENMEKLTEERDQRIAAENREKEQNKRL----QRQLRDTKEEMGELARKE---AEASRKKHELEMDLESLEAAN 1915
Cdd:TIGR00606 818 SdLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLiqdqQEQIQHLKSKTNELKSEKlqiGTNLQRRQQFEEQLVELSTEV 897
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 42794779 1916 QSLQADLKLAFKRIGDLQAAIEDEMEsdENEDLINSEGDSDVDSELE 1962
Cdd:TIGR00606 898 QSLIREIKDAKEQDSPLETFLEKDQQ--EKEELISSKETSNKKAQDK 942
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1238-1642 |
5.66e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.19 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1238 KLFTTVRPLIEVQLSEEQIRNKDE--------EIQQLRSKLEKAEKERNELRLNSDRLESRISElTSELTDERNTGESAS 1309
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEdqlkiitmELQKKSSELEEMTKFKNNKEVELEELKKILAE-DEKLLDEKKQFEKIA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1310 QLLDAETAERL----RAEKEMKELQTQYDALKKQMEVMemevmearLIRAAEINGEVDDDdaggewRLKYERAVREVD-- 1383
Cdd:pfam05483 432 EELKGKEQELIfllqAREKEIHDLEIQLTAIKTSEEHY--------LKEVEDLKTELEKE------KLKNIELTAHCDkl 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1384 -FTKKRLQQEFEDK-LEVEQQNKrqlerrlgDLQADSEESQRALQQLKkkcqrlTAELQDTKLHLEGQQVRNhELEKKQR 1461
Cdd:pfam05483 498 lLENKELTQEASDMtLELKKHQE--------DIINCKKQEERMLKQIE------NLEEKEMNLRDELESVRE-EFIQKGD 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1462 RFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE----AELQDISSQE---SKDE 1534
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEikvNKLE 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1535 ASLAKVKKQL--------RDLEAKVKDQEEELDE-QAGTIQMLEQAKLRLEME-------------MERMRQTHSKEMES 1592
Cdd:pfam05483 643 LELASAKQKFeeiidnyqKEIEDKKISEEKLLEEvEKAKAIADEAVKLQKEIDkrcqhkiaemvalMEKHKHQYDKIIEE 722
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1593 RDEEV-----EEARQSCQKKLKQMEV------------QLEEEYEDKQKVLREKRElegKLATLSDQ 1642
Cdd:pfam05483 723 RDSELglyknKEQEQSSAKAALEIELsnikaellslkkQLEIEKEEKEKLKMEAKE---NTAILKDK 786
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1625-1964 |
6.84e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1625 VLREKRELEGKLATLSDQVNRRDfesEKRLRKDLKRTKALLADAQLMLDHLKnsapSKREIAqlKNQLEESEFTCAAAVK 1704
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKE---EKDLHERLNGLESELAELDEEIERYE----EQREQA--RETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKamevEIEDLHLQIDDIAKAKTALEeqlsrlqREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1784
Cdd:PRK02224 249 RRE----ELETLEAEIEDLRETIAETE-------REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1785 EANKEKQELQEklqalqsqvefleqsmvdkslvsrqeakireletRLEFERTQVKRLESLASRLKENMEKLTEERDQ-RI 1863
Cdd:PRK02224 318 ELEDRDEELRD----------------------------------RLEECRVAAQAHNEEAESLREDADDLEERAEElRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1864 AAENREKE-QNKRlqRQLRDTKEEMGELaRKEAEASRKKHE-LEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1941
Cdd:PRK02224 364 EAAELESElEEAR--EAVEDRREEIEEL-EEEIEELRERFGdAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
330 340 350
....*....|....*....|....*....|....
gi 42794779 1942 S-DENEDLINS----------EGDSDVDSELEDR 1964
Cdd:PRK02224 441 RvEEAEALLEAgkcpecgqpvEGSPHVETIEEDR 474
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1177-1593 |
8.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1177 LARLEEQRDEQTSRNLTLFQAacRGYLARQHFKKRKIQDLAIRCVQKNIKKNKGVKDWPWWKLFTTVRP-LIEVQLSEEQ 1255
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1256 IRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELT-SELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYD 1334
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1335 ALKKQMEVMEMEVMEARLIRAAEINGEV------DDDDAGGEWRLK---------------YERAVREVDFTKKRLQQEF 1393
Cdd:COG4717 231 QLENELEAAALEERLKEARLLLLIAAALlallglGGSLLSLILTIAgvlflvlgllallflLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHE---LEKKQRRFDSELSQA 1470
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIaalLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1471 HEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAgfTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLE-- 1548
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEEELEELREELAELEAELEQLEed 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1549 -------AKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESR 1593
Cdd:COG4717 469 gelaellQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1350-1881 |
8.08e-08 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 57.44 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1350 ARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFE-DKLEVEQQNKRQLERRLGDLQADSEESQRALQQL 1428
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDREsDRNQELQKRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1429 KKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDML---LAEAFSLKQQLEEK 1505
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLkakASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1506 DMDIAGFTQKVVSLEAELQdisSQESkDEASLAKVKKQLR---DLEAKVKDQEEE---LDEQAGTIQMLEQAKLRLEMEM 1579
Cdd:pfam05557 162 QSSLAEAEQRIKELEFEIQ---SQEQ-DSEIVKNSKSELAripELEKELERLREHnkhLNENIENKLLLKEEVEDLKRKL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1580 ERMRQTHSK--EMESRDEEVEEARQScQKKLKQME-------VQLEEEYEDKQKvlREKRELEGKLATLSD----QVNRR 1646
Cdd:pfam05557 238 EREEKYREEaaTLELEKEKLEQELQS-WVKLAQDTglnlrspEDLSRRIEQLQQ--REIVLKEENSSLTSSarqlEKARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1647 DFESEKR--------LRKDLKRTKALLADAQlmldhlKNSAPSKREIAQLKNQLE--ESEFTCAAAVKARKAMEVEIEDL 1716
Cdd:pfam05557 315 ELEQELAqylkkiedLNKKLKRHKALVRRLQ------RRVLLLTKERDGYRAILEsyDKELTMSNYSPQLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1717 hlqIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNelMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEK 1796
Cdd:pfam05557 389 ---TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1797 LQALQSQVEFLEQSMvDKSLVSRQEAKIRELETRLEFERT--QVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNK 1874
Cdd:pfam05557 464 KNELEMELERRCLQG-DYDPKKTKVLHLSMNPAAEAYQQRknQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF 542
|
....*..
gi 42794779 1875 RLQRQLR 1881
Cdd:pfam05557 543 KEVLDLR 549
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1247-1771 |
8.78e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 8.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLES------RISELTSELTDERNTG--------------- 1305
Cdd:PRK01156 225 IEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMeleknnYYKELEERHMKIINDPvyknrnyindyfkyk 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1306 ---ESASQLL---DAETAERLRAEKEMKELQTQYDA-LKKQMevmemevmearliRAAEINGEVDDDDaggEWRLKYERA 1378
Cdd:PRK01156 305 ndiENKKQILsniDAEINKYHAIIKKLSVLQKDYNDyIKKKS-------------RYDDLNNQILELE---GYEMDYNSY 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1379 VREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGD---LQADSEESQRALQQLKKKCQRLTA----------ELQDTKLH 1445
Cdd:PRK01156 369 LKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDpdaIKKELNEINVKLQDISSKVSSLNQriralrenldELSRNMEM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1446 LEGQQV----RNHELEKKQRR----FDSELSQAHEEAQREKLQREKLQREKDMLLaeafSLKQQLEEKDMD-IAGFTQKV 1516
Cdd:PRK01156 449 LNGQSVcpvcGTTLGEEKSNHiinhYNEKKSRLEEKIREIEIEVKDIDEKIVDLK----KRKEYLESEEINkSINEYNKI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1517 VSLEAELQDissqeskDEASLAKVKKQlrdleakvKDQEEELDEQAGTIQmLEQAKLRLEMEMERMRQTHSKEME---SR 1593
Cdd:PRK01156 525 ESARADLED-------IKIKINELKDK--------HDKYEEIKNRYKSLK-LEDLDSKRTSWLNALAVISLIDIEtnrSR 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1594 DEEVEEARQSCQKKLKQMEVQLEeeyEDKQKVLREKRELEGKLATLSDQVNrrDFESEKRLRKDLKRTkalladaqlmLD 1673
Cdd:PRK01156 589 SNEIKKQLNDLESRLQEIEIGFP---DDKSYIDKSIREIENEANNLNNKYN--EIQENKILIEKLRGK----------ID 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1674 HLKNSAPSKREIAQLKNQLeeseftcaaAVKARKaMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1753
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEI---------TSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINE 723
|
570
....*....|....*...
gi 42794779 1754 DMnELMKKHKAAVAQASR 1771
Cdd:PRK01156 724 TL-ESMKKIKKAIGDLKR 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1735-1976 |
1.13e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1735 SRLQREKNEIQNRLEEDQEDMNELmkkhkaavaqasRDLaqINDLQAQLE----EANK-EK-QELQEKLQALQSQVEFLe 1808
Cdd:COG1196 168 SKYKERKEEAERKLEATEENLERL------------EDI--LGELERQLEplerQAEKaERyRELKEELKELEAELLLL- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1809 qsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMG 1888
Cdd:COG1196 233 --------------KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1889 ELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELEDRVDGV 1968
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
....*...
gi 42794779 1969 KSWLSKNK 1976
Cdd:COG1196 379 EELEELAE 386
|
|
| PDZ |
pfam00595 |
PDZ domain; PDZ domains are found in diverse signaling proteins. |
220-308 |
1.15e-07 |
|
PDZ domain; PDZ domains are found in diverse signaling proteins.
Pssm-ID: 395476 [Multi-domain] Cd Length: 81 Bit Score: 51.13 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLRRttMLDRGPEGQACRRVVHFaepGAGTKDlalGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:pfam00595 1 QVTLEKDGRGGLGFSLKG--GSDQGDPGIFVSEVLPG---GAAEAG---GLKVGDRILSINGQDVENMTHEEAVLALKGS 72
|
....*....
gi 42794779 300 GDSVRLKVQ 308
Cdd:pfam00595 73 GGKVTLTIL 81
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1459-1917 |
1.16e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.22 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1459 KQRRFDSELSQahEEAQREKLQREKLQREKdmLLAEAFSLKQQLEekdmdiagftqkvvSLEAELQDISSQESKDEAS-- 1536
Cdd:PRK01156 136 GQGEMDSLISG--DPAQRKKILDEILEINS--LERNYDKLKDVID--------------MLRAEISNIDYLEEKLKSSnl 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1537 -LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMermrqthsKEMESRDEEVeearqscqkklKQMEVQL 1615
Cdd:PRK01156 198 eLENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSAL--------NELSSLEDMK-----------NRYESEI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1616 EEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRkDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEE- 1694
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-DYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKd 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1695 -SEFTcaaavkarkAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1773
Cdd:PRK01156 338 yNDYI---------KKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIK 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 AQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM-----------------VDKSL---------VSRQEAKIREL 1827
Cdd:PRK01156 409 KELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMemlngqsvcpvcgttlgEEKSNhiinhynekKSRLEEKIREI 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1828 EtrleferTQVKRLESLASRLKENMEKLTEERDQRIAAENRekeQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE-M 1906
Cdd:PRK01156 489 E-------IEVKDIDEKIVDLKKRKEYLESEEINKSINEYN---KIESARADLEDIKIKINELKDKHDKYEEIKNRYKsL 558
|
490
....*....|.
gi 42794779 1907 DLESLEAANQS 1917
Cdd:PRK01156 559 KLEDLDSKRTS 569
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1460-1935 |
1.40e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 56.98 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1460 QRRFDSELSQAHEEAQREKLQREKLQREKDMllAEAFSLKQQLEEKDMDIAGFTQKVVSLEAEL---QDISSQESKDEAS 1536
Cdd:TIGR00606 172 KQKFDEIFSATRYIKALETLRQVRQTQGQKV--QEHQMELKYLKQYKEKACEIRDQITSKEAQLessREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1537 LAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLE 1616
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1617 EEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRlrkDLKRTKALLadaQLMLDHLKNSAPSKREI----------- 1685
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR---DSLIQSLAT---RLELDGFERGPFSERQIknfhtlvierq 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1686 ---AQLKNQLeESEFTCAAAVKARKAMEVEIE------DLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE--- 1753
Cdd:TIGR00606 404 edeAKTAAQL-CADLQSKERLKQEQADEIRDEkkglgrTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQElrk 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1754 DMNELMKKHKAAVAQASrdLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEF 1833
Cdd:TIGR00606 483 AERELSKAEKNSLTETL--KKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1834 ERTQVKRLESLASRLKENMEKLTEERDQriaAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHEL--EMDLESL 1911
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQ---TRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdVCGSQDE 637
|
490 500
....*....|....*....|....
gi 42794779 1912 EAANQSLQADLKLAFKRIGDLQAA 1935
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAMLAGA 661
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1629-1894 |
1.64e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 56.84 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1629 KRELEGKLATLSDQvnrRDFESEKRLrkdlkrTKALLADAQLMLDHLKNSapsKREIAQLKNQLEEseftcaAAVKARKA 1708
Cdd:PRK11281 38 EADVQAQLDALNKQ---KLLEAEDKL------VQQDLEQTLALLDKIDRQ---KEETEQLKQQLAQ------APAKLRQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1709 MEvEIEDlhLQIDDIAKAKTALEEQ-LSRLQREKNEIQNRLEEDQEDMNEL----------MKKHKAAVAQASRDLAQIN 1777
Cdd:PRK11281 100 QA-ELEA--LKDDNDEETRETLSTLsLRQLESRLAQTLDQLQNAQNDLAEYnsqlvslqtqPERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1778 DLQAQLEEANK-----EKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELET----RLEferTQVKRLESLAS-- 1846
Cdd:PRK11281 177 NLLKGGKVGGKalrpsQRVLLQAEQALLNAQNDLQRKSLEGNTQLQDLLQKQRDYLTariqRLE---HQLQLLQEAINsk 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1847 RLKENMEKLTEERDQRIAAEN-------REKEQNKRLQRQLRDTKEEMGELARKE 1894
Cdd:PRK11281 254 RLTLSEKTVQEAQSQDEAARIqanplvaQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| PDZ_SNX27-like |
cd23070 |
PDZ domain of sorting nexin-27 (SNX27), and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-307 |
1.75e-07 |
|
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: 50.87 E-value: 1.75e-07
10 20 30
....*....|....*....|....*....|....*....
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd23070 53 GVRKGDRILEVNGVNVEGATHKQVVDLIKSGGDELTLTV 91
|
|
| PDZ_tamalin_CYTIP-like |
cd06713 |
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ... |
219-307 |
2.27e-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: 50.31 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGDFGF-------------SLRRTTMLDRgpegqacrrvVHFAEPGagtkDLAlGLVPGDRLVEINGHNVE 285
Cdd:cd06713 4 RTIILEKQDNETFGFeiqtyglhhknsnEVEMCTYVCR----------VHEDSPA----YLA-GLTAGDVILSVNGVSVE 68
|
90 100
....*....|....*....|..
gi 42794779 286 SKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06713 69 GASHQEIVELIRSSGNTLRLET 90
|
|
| 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 |
3.53e-07 |
|
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: 49.50 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 222 ELQRRPTGdFGFSLRRTTMLDRGPegqacRRVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQSG 300
Cdd:cd06735 5 ELERGPKG-FGFSIRGGREYNNMP-----LYVLRLAEDGPAQRD---GrLRVGDQILEINGESTQGMTHAQAIELIRSGG 75
|
....*....
gi 42794779 301 DSVRLKVQP 309
Cdd:cd06735 76 SVVRLLLRR 84
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1534-1896 |
3.61e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1534 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQThskemesrdeeveEARQSCQKKLK 1609
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqaASDHLNLVQTALRQQ-------------EKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1610 QMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVnrrdfesekrlrkdlKRTKALLADAQLMLDHLKnsapsKREIA--Q 1687
Cdd:PRK04863 359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEV---------------DELKSQLADYQQALDVQQ-----TRAIQyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1688 LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSrlqrekneiqnrleedqedmneLMKKHKAAVA 1767
Cdd:PRK04863 419 AVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLS----------------------VAQAAHSQFE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 QASRDLAQINDlQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASR 1847
Cdd:PRK04863 477 QAYQLVRKIAG-EVSRSEAWDVARELLRRLREQRHLAEQLQQ----------LRMRLSELEQRLRQQQRAERLLAEFCKR 545
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1848 LK------ENMEKLTEERDQRIAAENREK----EQNKRLQRQLRDTKEEMGELARKEAE 1896
Cdd:PRK04863 546 LGknlddeDELEQLQEELEARLESLSESVsearERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| cpPDZ_CPP-like |
cd06782 |
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ... |
269-309 |
3.99e-07 |
|
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: 49.79 E-value: 3.99e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:cd06782 31 GIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLTIRR 72
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1723-1969 |
4.01e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1723 IAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQS 1802
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1803 QVEfleqsmVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRD 1882
Cdd:COG4372 88 QLQ------AAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1883 TKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSELE 1962
Cdd:COG4372 162 LQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
....*..
gi 42794779 1963 DRVDGVK 1969
Cdd:COG4372 242 LELEEDK 248
|
|
| PDZ3_Dlg1-2-4-like |
cd06795 |
PDZ domain 3 of human discs large homolog 1 (Dlg1), Dlg2, and Dlg4, Drosophila disc large (Dlg) ... |
219-312 |
4.70e-07 |
|
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: 49.66 E-value: 4.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGdFGFSLRRttmldrGPEGQACrrVVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06795 3 RKIVLHKGSTG-LGFNIVG------GEDGEGI--FISFILAG-GPADLSGELRRGDQILSVNGVDLRNATHEQAAAALKN 72
|
90
....*....|....
gi 42794779 299 SGDSVRLKVQPIPE 312
Cdd:cd06795 73 AGQTVTIIAQYKPE 86
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1253-1906 |
5.35e-07 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 55.22 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNkdeEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESasqllDAETAERLRAEKEMKELQTQ 1332
Cdd:PTZ00440 793 ENKISN---DINILKENKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPT-----EDENLNLKELEKEFNENNQI 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKKQMEvmemevmearliraaEINGEVDdddaggewrlkyerAVREVDFTKKRL---QQEFEDKLEVEQQNKRQLER 1409
Cdd:PTZ00440 865 VDNIIKDIE---------------NMNKNIN--------------IIKTLNIAINRSnsnKQLVEHLLNNKIDLKNKLEQ 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1410 RLGDLQADS----EESQRALQQLKKKCQRLTAELQDTK---LHLEGQQVRNHeLEKKQRRFDSELSQAHEEAQREKLQRE 1482
Cdd:PTZ00440 916 HMKIINTDNiiqkNEKLNLLNNLNKEKEKIEKQLSDTKinnLKMQIEKTLEY-YDKSKENINGNDGTHLEKLDKEKDEWE 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1483 KLQREKDMLLAEAFSLKQQ-------------------LEEKDMDIAGFTQKVVSLEAELQD-ISSQESKDEASL---AK 1539
Cdd:PTZ00440 995 HFKSEIDKLNVNYNILNKKiddlikkqhddiielidklIKEKGKEIEEKVDQYISLLEKMKTkLSSFHFNIDIKKyknPK 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1540 VKKQLRDLEAKVKDQEEELDEQagtiqmleqaklrlEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMevqlEEEY 1619
Cdd:PTZ00440 1075 IKEEIKLLEEKVEALLKKIDEN--------------KNKLIEIKNKSHEHVVNADKEKNKQTEHYNKKKKSL----EKIY 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1620 EDKQKVLREKRELEGKLATLSDqVNRRDFESEKrlrkdlkrtkalladaqLMLDHLKNsapskreiaQLKNQLEESeftc 1699
Cdd:PTZ00440 1137 KQMEKTLKELENMNLEDITLNE-VNEIEIEYER-----------------ILIDHIVE---------QINNEAKKS---- 1185
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1700 aaavkarKAMEVEIEDLHLQIDDIaKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA--AVAQASRDLAQI- 1776
Cdd:PTZ00440 1186 -------KTIMEEIESYKKDIDQV-KKNMSKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGlkGEANRSTNVDELk 1257
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1777 ---NDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTQ--VKRLESLASR 1847
Cdd:PTZ00440 1258 eikLQVFSYLQQVIKENNKMENALHEIKNMYEFLISIDSEKILKeilnSTKKAEEFSNDAKKELEKTDnlIKQVEAKIEQ 1337
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1848 LKENMEKLTE-ERDQRIAAENREKEQnkrLQRQLRDTKEEMGELArKEAEASRKKHELEM 1906
Cdd:PTZ00440 1338 AKEHKNKIYGsLEDKQIDDEIKKIEQ---IKEEISNKRKEINKYL-SNIKSNKEKCDLHV 1393
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1765-1949 |
6.13e-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: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1765 AVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLES- 1843
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALE-------------ARLEAAKTELEDLEKEIKRLELe 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1844 ---LASRLKENMEKLTEERDQR-IAAENREKEQNKRLQRQLRD-TKEEMGELARKEAEASRKKHELEM---DLESLEAAN 1915
Cdd:COG1579 68 ieeVEARIKKYEEQLGNVRNNKeYEALQKEIESLKRRISDLEDeILELMERIEELEEELAELEAELAEleaELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|....
gi 42794779 1916 QSLQADLKlafKRIGDLQAAIEdEMESDENEDLI 1949
Cdd:COG1579 148 DEELAELE---AELEELEAERE-ELAAKIPPELL 177
|
|
| PDZ_Par6-like |
cd06718 |
PDZ domain of partitioning defective 6 (Par6), Drosophila Rho GTPase-activating protein 100F ... |
219-297 |
6.26e-07 |
|
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: 49.10 E-value: 6.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 219 RELELQRRPTGDFGFSLRRTTMLDRGPeGQACRRVVhfaePGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06718 1 RRVELIKPPGKPLGFYIRDGNGVERVP-GIFISRLV----LG-SLADSTGLLAVGDEILEVNGVEVTGKSLDDVTDMMV 73
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1394-1947 |
6.62e-07 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 54.81 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQ----LERRlGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNH-ELEKKQRRFDSELS 1468
Cdd:PRK10246 232 EKQLLTAQQQQQQslnwLTRL-DELQQEASRRQQALQQALAAEEKAQPQLAALSLAQPARQLRPHwERIQEQSAALAHTR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1469 QAHEE---------AQREKLqREKLQREKDMLLAEAFSLKQQLEEKDMdIAGFTQKVVSLEAELqdisSQESKDEASLAK 1539
Cdd:PRK10246 311 QQIEEvntrlqstmALRARI-RHHAAKQSAELQAQQQSLNTWLAEHDR-FRQWNNELAGWRAQF----SQQTSDREQLRQ 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1540 VKKQLRDLEAKVKDQEE-----ELDEQAGTI-QMLEQAKLRlememERMRQTHSK--EMESRDEEVEEARQSCQKKLKQM 1611
Cdd:PRK10246 385 WQQQLTHAEQKLNALPAitltlTADEVAAALaQHAEQRPLR-----QRLVALHGQivPQQKRLAQLQVAIQNVTQEQTQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1612 EVQLEEeyedKQKVLREKRELEGKLATLSDQvnrrdfesEKRLrKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLK-- 1689
Cdd:PRK10246 460 NAALNE----MRQRYKEKTQQLADVKTICEQ--------EARI-KDLEAQRAQLQAGQPCPLCGSTSHPAVEAYQALEpg 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1690 -NQLEeseftcaaavkaRKAMEVEIEDLHlqiDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEdmneLMKKHKAAVAQ 1768
Cdd:PRK10246 527 vNQSR------------LDALEKEVKKLG---EEGAALRGQLDALTKQLQRDESEAQSLRQEEQA----LTQQWQAVCAS 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1769 ASRDLAQINDLQAQLEEANKEKQELQE--KLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVK-RLESLA 1845
Cdd:PRK10246 588 LNITLQPQDDIQPWLDAQEEHERQLRLlsQRHELQGQIA-------------AHNQQIIQYQQQIEQRQQQLLtALAGYA 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1846 SRLKENMEKLT--EERDQRIAAENREKEQNKRLQRQ------LRDTKEEMGELARKEAEAS----RKKHElemDLESLEA 1913
Cdd:PRK10246 655 LTLPQEDEEASwlATRQQEAQSWQQRQNELTALQNRiqqltpLLETLPQSDDLPHSEETVAldnwRQVHE---QCLSLHS 731
|
570 580 590
....*....|....*....|....*....|....
gi 42794779 1914 ANQSLQADLKLAFKRIGDLQAAIEDEMESDENED 1947
Cdd:PRK10246 732 QLQTLQQQDVLEAQRLQKAQAQFDTALQASVFDD 765
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1536-1880 |
6.93e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.53 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 SLAKVKKQLrdleAKVKDQEEELDEQAGTIQMLEQAKLRLEmemerMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQL 1615
Cdd:PRK11281 37 TEADVQAQL----DALNKQKLLEAEDKLVQQDLEQTLALLD-----KIDRQKEETEQLKQQLAQA----PAKLRQAQAEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1616 EEEYEDKQKVLREK------RELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLMLDHLKN--SAPSKReIAQ 1687
Cdd:PRK11281 104 EALKDDNDEETRETlstlslRQLESRLAQTLDQLQ--------NAQNDLAEYNSQLVSLQTQPERAQAalYANSQR-LQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1688 LKNQLEESEFTCAAAVKARKAM-EVEIEDLHLQID-------------DIAKAKTAL-EEQLSRLQREKNEIQN-----R 1747
Cdd:PRK11281 175 IRNLLKGGKVGGKALRPSQRVLlQAEQALLNAQNDlqrkslegntqlqDLLQKQRDYlTARIQRLEHQLQLLQEainskR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1748 LEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQL--------EEANK-EKQELQEKLQ---ALQSQVEFLEQSMVDK- 1814
Cdd:PRK11281 255 LTLSEKTVQEAQSQDEAARIQANPLVAQELEINLQLsqrllkatEKLNTlTQQNLRVKNWldrLTQSERNIKEQISVLKg 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1815 SLV-SR----------QEAKIREL-----ETRLE-FE----RTQVKRLESLASRL--KENMEKLTEERDQ--RIAAENRE 1869
Cdd:PRK11281 335 SLLlSRilyqqqqalpSADLIEGLadriaDLRLEqFEinqqRDALFQPDAYIDKLeaGHKSEVTDEVRDAllQLLDERRE 414
|
410
....*....|...
gi 42794779 1870 --KEQNKRLQRQL 1880
Cdd:PRK11281 415 llDQLNKQLNNQL 427
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1253-1885 |
7.60e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.52 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKaekernelrlnsdrLESRISELTSELtderntgESASQLLDAETAERLRAEKEMKELQTQ 1332
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIAD--------------DEKSHSITLKEI-------ERLSIEYNNAMDDYNNLKSALNELSSL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKkqmevmemevmearliraaeingevddddaggewrlKYERAVREVDftkKRLQQEFEDKLEVEQQNKRqLERRLG 1412
Cdd:PRK01156 248 EDMKN------------------------------------RYESEIKTAE---SDLSMELEKNNYYKELEER-HMKIIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1413 DLQADSEESQRALQQLKKKCQRLTAELQDtklhLEGQQVRNHELEKKQrrfdSELSQAHEEAQREKLQREKLQREKDMLL 1492
Cdd:PRK01156 288 DPVYKNRNYINDYFKYKNDIENKKQILSN----IDAEINKYHAIIKKL----SVLQKDYNDYIKKKSRYDDLNNQILELE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1493 AEAF---SLKQQLEEKDMDIAGFTQKVVSLEAElqdISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLE 1569
Cdd:PRK01156 360 GYEMdynSYLKSIESLKKKIEEYSKNIERMSAF---ISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALR 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1570 QAKLRLEMEMErMRQTHSK----EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATL-SDQVN 1644
Cdd:PRK01156 437 ENLDELSRNME-MLNGQSVcpvcGTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEIN 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1645 R-----RDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPS-KREIAQLKNqleeSEFTCAAAVKArkamEVEIEDLHL 1718
Cdd:PRK01156 516 KsineyNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKR----TSWLNALAVIS----LIDIETNRS 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1719 QIDDIAKaktaleeQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEeankekqELQEKLQ 1798
Cdd:PRK01156 588 RSNEIKK-------QLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIE-------KLRGKID 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1799 ALQSQVEFLEQSMVDKSLVSrqeAKIRELETRLEFERTQVKRLESLASRLKENMEKL---TEERDQRIAAENREKEQNKR 1875
Cdd:PRK01156 654 NYKKQIAEIDSIIPDLKEIT---SRINDIEDNLKKSRKALDDAKANRARLESTIEILrtrINELSDRINDINETLESMKK 730
|
650
....*....|
gi 42794779 1876 LQRQLRDTKE 1885
Cdd:PRK01156 731 IKKAIGDLKR 740
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1734-1948 |
7.64e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 7.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1734 LSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvd 1813
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK---- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1814 kslvsrqeakireletrLEFERTQVKRLESLASRLKENMEKLtEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARK 1893
Cdd:COG4717 124 -----------------LLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQ 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1894 EAEASRKK-HELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDL 1948
Cdd:COG4717 186 LSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1666-1893 |
8.23e-07 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 53.93 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1666 ADAQL-MLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAK------TALEEQLSRLQ 1738
Cdd:COG0497 140 PDAQReLLDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAAAlqpgeeEELEEERRRLS 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1739 R-EK-----NEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFleqsmv 1812
Cdd:COG0497 220 NaEKlrealQEALEALSGGEGGALDLLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRYLDSLEF------ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1813 dkslvsrQEAKIRELETRLEfertqvkRLESLASRLKENMEKLTEERD---QRIAA-ENREkEQNKRLQRQLRDTKEEMG 1888
Cdd:COG0497 294 -------DPERLEEVEERLA-------LLRRLARKYGVTVEELLAYAEelrAELAElENSD-ERLEELEAELAEAEAELL 358
|
....*
gi 42794779 1889 ELARK 1893
Cdd:COG0497 359 EAAEK 363
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1260-1475 |
8.44e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1260 DEEIQQLRSKLEKAEKERNELRLNSDrlesriseltseLTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALKKQ 1339
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEFRQKNG------------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1340 mevmemevmearLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQ------QEFEDKL-EVEQQNKRQLERRLG 1412
Cdd:COG3206 249 ------------LGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTpnhpdvIALRAQIaALRAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1413 DLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSeLSQAHEEAQ 1475
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES-LLQRLEEAR 378
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1314-1562 |
9.24e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 9.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1314 AETAERLRAEKEMKELQTQYDALKKQMEVMEMevmearliRAAEINGEVDDDDaggewrlkyeravREVDFTKKRLqQEF 1393
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKK--------EEKALLKQLAALE-------------RRIAALARRI-RAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLtAELQDTKLHLEGQQVRnhELEKKQRRFDSELSQAHEE 1473
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFL--DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1474 AQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKD 1553
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
....*....
gi 42794779 1554 QEEELDEQA 1562
Cdd:COG4942 232 LEAEAAAAA 240
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1572-1893 |
1.00e-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: 52.89 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1572 KLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLsdqvnrrdfesE 1651
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASL-----------E 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1652 KRLRkDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcaAAVKARKaMEVEIEDLHLQIDDIAKAKTALE 1731
Cdd:pfam15905 129 KQLL-ELTRVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKE--VMAKQEG-MEGKLQVTQKNLEHSKGKVAQLE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1732 EQLSRLQREKNEiqnrleedqedmnelmkkHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM 1811
Cdd:pfam15905 205 EKLVSTEKEKIE------------------EKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1812 vdkslvsrqEAKIRELETRLEFERTQVKRLESlasrLKENMEKLTEERDQRIAAENREkeqnkrLQRQLRDTKEEMGELA 1891
Cdd:pfam15905 267 ---------EEKEQELSKQIKDLNEKCKLLES----EKEELLREYEEKEQTLNAELEE------LKEKLTLEEQEHQKLQ 327
|
..
gi 42794779 1892 RK 1893
Cdd:pfam15905 328 QK 329
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1713-1954 |
1.11e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLhLQI------DDIAKAKT-ALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAqasrdlaqinDLQAQLEE 1785
Cdd:PHA02562 156 VEDL-LDIsvlsemDKLNKDKIrELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1786 ANKEKQELQEKLQALQSQVEFLEQSMVDkslVSRQEAKIRELETRLefeRTQVKRLESLASRLKENMEKLT-----EERD 1860
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIED---PSAALNKLNTAAAKI---KSKIEQFQKVIKMYEKGGVCPTctqqiSEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1861 QRIAAEnreKEQNKRLQRQLRDTKEEMGELARKE---AEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIE 1937
Cdd:PHA02562 299 DRITKI---KDKLKELQHSLEKLDTAIDELEEIMdefNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFV 375
|
250 260
....*....|....*....|..
gi 42794779 1938 DEMES-----DENEDLINSEGD 1954
Cdd:PHA02562 376 DNAEElaklqDELDKIVKTKSE 397
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1579-1803 |
1.11e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1579 MERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEeYEDKQKVL---REKRELEGKLATLSDQVNRrdfesekrLR 1655
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-FRQKNGLVdlsEEAKLLLQQLSELESQLAE--------AR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1656 KDLKRTKALLADAQLMLDHLKNSAPSKRE---IAQLKNQLEESEFTCAAAVK-------ARKAMEVEIEDLHLQIDD-IA 1724
Cdd:COG3206 233 AELAEAEARLAALRAQLGSGPDALPELLQspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQeAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1725 KAKTALEEQLSRLQREKNEIQNRLEEdqedmnelmkkHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1803
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQ-----------LEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1253-1922 |
1.58e-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: 53.80 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQ 1332
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1333 YDALKKQmeVMEMEVMEARLIRAAEINGEvddddaggewRLKYERAVREvdFTKKRLQQEFEDKLEVEQ--QNKRQLE-- 1408
Cdd:COG3096 594 IKELAAR--APAWLAAQDALERLREQSGE----------ALADSQEVTA--AMQQLLEREREATVERDElaARKQALEsq 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1409 -RRLgdLQADSEESQRaLQQLkkkCQRLTAEL-----QDTKLH-------LEGQQ-----VRNHELEKKQ---------- 1460
Cdd:COG3096 660 iERL--SQPGGAEDPR-LLAL---AERLGGVLlseiyDDVTLEdapyfsaLYGPArhaivVPDLSAVKEQlagledcped 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1461 --------RRFDSELSQAHEE--------------------------AQREKlQREKLQREKDML---LAEAFSLKQQLE 1503
Cdd:COG3096 734 lyliegdpDSFDDSVFDAEELedavvvklsdrqwrysrfpevplfgrAAREK-RLEELRAERDELaeqYAKASFDVQKLQ 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1504 EKDMDIAGF--TQKVVSLEAElqdissqeskDEASLAKVKKQLRDLEAKVKDQEEELDEQAgtiQMLEQAKLRLEMEMER 1581
Cdd:COG3096 813 RLHQAFSQFvgGHLAVAFAPD----------PEAELAALRQRRSELERELAQHRAQEQQLR---QQLDQLKEQLQLLNKL 879
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1582 MRQTHSKEMESRDEEVEEARQscqkklkqmevQLEEEYEDKQKVLREK---RELEGKLATLsdqvnRRDFESEKRLRKDL 1658
Cdd:COG3096 880 LPQANLLADETLADRLEELRE-----------ELDAAQEAQAFIQQHGkalAQLEPLVAVL-----QSDPEQFEQLQADY 943
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1659 KRTKALLADAQLMLDHLKNsapskreiaqlknqleeseftcaaaVKARKAmeveiedlHLQIDD---IAKAKTALEEQLs 1735
Cdd:COG3096 944 LQAKEQQRRLKQQIFALSE-------------------------VVQRRP--------HFSYEDavgLLGENSDLNEKL- 989
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1736 rlqREKNEiqnRLEEDQEDMNELMKKHKAAVAQASRDLAqinDLQAQLEEANKEKQELQEKLQALQSQVeflEQSMVDKS 1815
Cdd:COG3096 990 ---RARLE---QAEEARREAREQLRQAQAQYSQYNQVLA---SLKSSRDAKQQTLQELEQELEELGVQA---DAEAEERA 1057
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1816 LVSRQE---------AKIRELETRLEFERTQvkrLESLASRLKENMEKLTEERDQRIAAenreKEQNKRLQRQLRDTKEE 1886
Cdd:COG3096 1058 RIRRDElheelsqnrSRRSQLEKQLTRCEAE---MDSLQKRLRKAERDYKQEREQVVQA----KAGWCAVLRLARDNDVE 1130
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 42794779 1887 ----MGELARKEAEASRkkhelEMDLESLEAANQSlQADL 1922
Cdd:COG3096 1131 rrlhRRELAYLSADELR-----SMSDKALGALRLA-VADN 1164
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1305-1657 |
1.68e-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: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1305 GESASQLLDAETAERLRAEKEMKELQTQYDALKKQMEVMEMEVMEARLIRaaeingEVDDDDaggewrLKYERAVREVDf 1384
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA------EYSWDE------IDVASAEREIA- 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1385 tkkRLQQEFEDkLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQR--- 1461
Cdd:COG4913 672 ---ELEAELER-LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARlel 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1462 --RFDSELSQAHEEAQREKLqREKLQREKDMLLAEAFSLKQQLEEK--------DMDIAGFTQKVVSLE---AELQDISS 1528
Cdd:COG4913 748 raLLEERFAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAmrafnrewPAETADLDADLESLPeylALLDRLEE 826
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1529 QEskdeasLAKVKKQLRDLEAKVKDQE-----EELDEQAGTI--------QMLEQAK------LRLEMEmermrqthske 1589
Cdd:COG4913 827 DG------LPEYEERFKELLNENSIEFvadllSKLRRAIREIkeridplnDSLKRIPfgpgryLRLEAR----------- 889
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1590 mESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVL---------REKRELEGKLATLSDQVNRRDFESEKRLRKD 1657
Cdd:COG4913 890 -PRPDPEVREFRQELRAVTSGASLFDEELSEARFAALkrlierlrsEEEESDRRWRARVLDVRNHLEFDAEEIDRED 965
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1593-1921 |
1.73e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1593 RDEEVEEArQSCQKKLKQMEVQLEEEYEDKqkvlrekRELEGKLATLSdqvnrrdfESEKRLRKDLKRTKALLADAQLML 1672
Cdd:PRK04863 281 RRVHLEEA-LELRRELYTSRRQLAAEQYRL-------VEMARELAELN--------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1673 DHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKA----KTALEEQLSRLQREKNEIQnRL 1748
Cdd:PRK04863 345 RQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyQQALDVQQTRAIQYQQAVQ-AL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1749 EEDQEdMNELMKkhkAAVAQASRDLAQindLQAQLEEANKEKQELQEKL---QALQSQVEF---LEQSMVDKslVSRQEA 1822
Cdd:PRK04863 424 ERAKQ-LCGLPD---LTADNAEDWLEE---FQAKEQEATEELLSLEQKLsvaQAAHSQFEQayqLVRKIAGE--VSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1823 K--IRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqriaAENREKEQNKRLQRQLRDtkeemgelarkEAEASRK 1900
Cdd:PRK04863 495 WdvARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQR----AERLLAEFCKRLGKNLDD-----------EDELEQL 559
|
330 340
....*....|....*....|.
gi 42794779 1901 KHELEMDLESLEAANQSLQAD 1921
Cdd:PRK04863 560 QEELEARLESLSESVSEARER 580
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1585-1904 |
1.86e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.30 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1585 THSKEMESRD---------EEVEEARQSCQKKLKQMEVQLEE------------EYEDKQKVLREKRELEGKLATLSDQV 1643
Cdd:pfam12128 188 MHSKEGKFRDvksmivailEDDGVVPPKSRLNRQQVEHWIRDiqaiagimkirpEFTKLQQEFNTLESAELRLSHLHFGY 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1644 NrrdfESEKRLRKDLKRTKALLADAQLMLDHLKNsapskrEIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDI 1723
Cdd:pfam12128 268 K----SDETLIASRQEERQETSAELNQLLRTLDD------QWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1724 AKAKTALE-EQLSRLQREKNEIQNRLEEDQEDMNELMKKHKA----AVAQASRDLAQIND-LQAQLEEANKEKQELQEKL 1797
Cdd:pfam12128 338 DIETAAADqEQLPSWQSELENLEERLKALTGKHQDVTAKYNRrrskIKEQNNRDIAGIKDkLAKIREARDRQLAVAEDDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1798 QALQSQV-EFLEQSMVDKSLVSRQ-EAKIRELETRL------EFERTQVKRLESLASRLKENMEKLTEER----DQRIAA 1865
Cdd:pfam12128 418 QALESELrEQLEAGKLEFNEEEYRlKSRLGELKLRLnqatatPELLLQLENFDERIERAREEQEAANAEVerlqSELRQA 497
|
330 340 350
....*....|....*....|....*....|....*....
gi 42794779 1866 ENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHEL 1904
Cdd:pfam12128 498 RKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL 536
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1261-1813 |
1.94e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.98 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1261 EEIQQLRSKLEKAEKERNELRLNSDRLES---RISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQTQYDALK 1337
Cdd:PRK01156 173 DVIDMLRAEISNIDYLEEKLKSSNLELENikkQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKN 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1338 KqmEVMEMEVMEARLIRAAEINGEVddddAGGEWRLKyERAVREVDFTKKRLQQEFEDKLEVEqqNKRQLERRLGDLQAD 1417
Cdd:PRK01156 253 R--YESEIKTAESDLSMELEKNNYY----KELEERHM-KIINDPVYKNRNYINDYFKYKNDIE--NKKQILSNIDAEINK 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1418 SEESQRALQQLKK------KCQRLTAELQDTKLHLEGQQ------VRNHELEKKQRRfdselsqahEEAQREKLQREKLQ 1485
Cdd:PRK01156 324 YHAIIKKLSVLQKdyndyiKKKSRYDDLNNQILELEGYEmdynsyLKSIESLKKKIE---------EYSKNIERMSAFIS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1486 REKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLR------DL-EAKVKDQEEEL 1558
Cdd:PRK01156 395 EILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLgEEKSNHIINHY 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1559 DEQAGTiqmLEQAKLRLEMEMERM--RQTHSKEMESR--DEEVEEARQScQKKLKQMEVQLEEeYEDKQKVLREKrelEG 1634
Cdd:PRK01156 475 NEKKSR---LEEKIREIEIEVKDIdeKIVDLKKRKEYleSEEINKSINE-YNKIESARADLED-IKIKINELKDK---HD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1635 KLATLSDQVNRRDFESekrlrKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavKARKAMEVEIE 1714
Cdd:PRK01156 547 KYEEIKNRYKSLKLED-----LDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLE----------SRLQEIEIGFP 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1715 DLHLQIDDIAKAktaLEEQLSRLQREKNEIQNR-------------LEEDQEDMNELMKKHKAAVAQASRDLAQINDLQA 1781
Cdd:PRK01156 612 DDKSYIDKSIRE---IENEANNLNNKYNEIQENkilieklrgkidnYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRK 688
|
570 580 590
....*....|....*....|....*....|..
gi 42794779 1782 QLEEANKEKQELQEKLQALQSQVEFLEQSMVD 1813
Cdd:PRK01156 689 ALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| PDZ4_Scribble-like |
cd06701 |
PDZ domain 4 of Drosophila Scribble, human Scribble homolog, and related domains; PDZ (PSD-95 ... |
218-307 |
2.41e-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: 47.61 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 218 LRELELQRRPTGDFGFSLR------RTTMLDRGPEGQACRRVVHfaePGAGTKDlalG-LVPGDRLVEINGHNVESKSRD 290
Cdd:cd06701 4 LQELTIVKEPGEKLGISIRggakghAGNPLDPTDEGIFISKINP---DGAAARD---GrLKVGQRILEVNGQSLLGATHQ 77
|
90
....*....|....*..
gi 42794779 291 EIVEMIRQSGDSVRLKV 307
Cdd:cd06701 78 EAVRILRSVGDTLTLLV 94
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1605-1917 |
2.51e-06 |
|
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: 52.45 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1605 QKKLKQMEVQLEE---EYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPS 1681
Cdd:pfam09731 124 QEKEKALEEVLKEaisKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAME--VEIEDLHLQIDDIAKAKTALEEQLSRLQREK--NEIQNRLEEDQEDMNE 1757
Cdd:pfam09731 204 QSEEEAAPPLLDAAPETPPKLPEHLDNVEekVEKAQSLAKLVDQYKELVASERIVFQQELVSifPDIIPVLKEDNLLSND 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1758 lmkKHKAAVAQASRDLAQindLQAQLEEanKEKQELQEKLQALQSQVEFLEQSmvDKSLVSRQEAKIRELET--RLEFER 1835
Cdd:pfam09731 284 ---DLNSLIAHAHREIDQ---LSKKLAE--LKKREEKHIERALEKQKEELDKL--AEELSARLEEVRAADEAqlRLEFER 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1836 TQVKRLESLASRLKENMEKLTEERDQRIaaENREKEQNKRLQR-QLRDTKEEMgelARKEAEASRKKHELEMDLESLEAA 1914
Cdd:pfam09731 354 EREEIRESYEEKLRTELERQAEAHEEHL--KDVLVEQEIELQReFLQDIKEKV---EEERAGRLLKLNELLANLKGLEKA 428
|
...
gi 42794779 1915 NQS 1917
Cdd:pfam09731 429 TSS 431
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1405-1561 |
2.79e-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: 50.69 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDtklhlegqqvrnheLEKKQRRFDSELSQAHEEAQR--EKLQRE 1482
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELED--------------LEKEIKRLELEIEEVEARIKKyeEQLGNV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1483 KLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ 1561
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1428-1704 |
3.01e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 52.32 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1428 LKKKCQRLTAELQ--DTKLHLEGQQVrnheleKKQRRFDSELsqaheeaqrEKLQREKLQREKDM---LLAEAFSLKQQL 1502
Cdd:PHA02562 172 NKDKIRELNQQIQtlDMKIDHIQQQI------KTYNKNIEEQ---------RKKNGENIARKQNKydeLVEEAKTIKAEI 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1503 EEkdmdiagftqkvvsLEAELQDISSQESKDEASLAKVKKQLRDLEAKVK--DQEEELDEQAGT----IQMLEQAKLRLE 1576
Cdd:PHA02562 237 EE--------------LTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfQKVIKMYEKGGVcptcTQQISEGPDRIT 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1577 MEMERMrqthsKEMESRDEEVEEARQScqkklkqmEVQLEEEYEDKQKVLRE-KRELEGKLATLSDQVNrrdfeSEKRLR 1655
Cdd:PHA02562 303 KIKDKL-----KELQHSLEKLDTAIDE--------LEEIMDEFNEQSKKLLElKNKISTNKQSLITLVD-----KAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 42794779 1656 KDLKRTKALLADaqlmldhlknsapSKREIAQLKNQLEESEFTCAAAVK 1704
Cdd:PHA02562 365 AAIEELQAEFVD-------------NAEELAKLQDELDKIVKTKSELVK 400
|
|
| PDZ_SYNJ2BP-like |
cd06709 |
PDZ domain of synaptojanin-2-binding protein (SYNJ2BP), and related domains; PDZ (PSD-95 ... |
220-308 |
3.07e-06 |
|
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: 46.90 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGdFGFSLRRTTMLDRGPEGQACRrVVHFAEPGAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06709 2 EITLKRGPSG-LGFNIVGGTDQPYIPNDSGIY-VAKIKEDGAAAID---GrLQEGDKILEINGQSLENLTHQDAVELFRN 76
|
90
....*....|
gi 42794779 299 SGDSVRLKVQ 308
Cdd:cd06709 77 AGEDVKLKVQ 86
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1555-1911 |
3.98e-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: 51.82 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1555 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS------KEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLRE 1628
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREqwerqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1629 K--------------RELEGKLATLSDQVNRRDFESEkRLRKDLKRTKALLADAQlmldhlknsapskREIAQLKNQLEE 1694
Cdd:pfam07888 117 KdallaqraaheariRELEEDIKTLTQRVLERETELE-RMKERAKKAGAQRKEEE-------------AERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1695 SEFTCaaavkarKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLA 1774
Cdd:pfam07888 183 TEEEL-------RSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1775 QINDLQAQLEEANKEKQEL-QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERtqvKRLESLASRLKENME 1853
Cdd:pfam07888 256 LGEELSSMAAQRDRTQAELhQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADK---DRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1854 KLTEERDQRIAAE---NREKEQNKrlqRQLRDTKEEMGELARKEAEASRKKHELEMDLESL 1911
Cdd:pfam07888 333 RLQEERMEREKLEvelGREKDCNR---VQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1544-1906 |
4.11e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 51.07 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQE--EELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEd 1621
Cdd:pfam13868 8 LRELNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1622 KQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKAlladaqlmldhlknsapsKREIAQLKNQLEESeftcaa 1701
Cdd:pfam13868 87 QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQL------------------REEIDEFNEEQAEW------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1702 avKARKAMEVEIEDLHLQ--IDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDL 1779
Cdd:pfam13868 143 --KELEKEEEREEDERILeyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1780 QAQLEEANKEKQELQEKLQALQSQVEFleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEER 1859
Cdd:pfam13868 221 QKEREEAEKKARQRQELQQAREEQIEL------------KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 42794779 1860 DQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEM 1906
Cdd:pfam13868 289 LEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1394-1798 |
4.51e-06 |
|
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: 51.94 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQ--------RALQQLKKKCQRLTAELQDTKlhlegqqvrNHELEKKQRrfdS 1465
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKhtqnvalnKKLSDIKTEYLYELNVLKEKS---------EAELTSKTK---K 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQREKLQREKDMLLAEA-FSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESkdEASLAKVKKQL 1544
Cdd:NF033838 122 ELDAAFEQFKKDTLEPGKKVAEATKKVEEAeKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1545 RDLEAKVKDQEEELDEQAGTIQMLEQAKlrlememermrqthskemESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQK 1624
Cdd:NF033838 200 PRDEEKIKQAKAKVESKKAEATRLEKIK------------------TDREKAEEEAKRRADAKLKEAVEKNVATSEQDKP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1625 VLREKRELEGKLATlsdqvnrrdfesekrlrKDLKRTKALLADAQLMLDHLKN-SAPSKREIAQLKNQLEESEftcaaav 1703
Cdd:NF033838 262 KRRAKRGVLGEPAT-----------------PDKKENDAKSSDSSVGEETLPSpSLKPEKKVAEAEKKVEEAK------- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1704 kaRKAMEVEIED-----------LHLQiddIAKAKTALEE-QLSRLQREKNEIQNrleedQEDMNELMKKHKAAVAQASR 1771
Cdd:NF033838 318 --KKAKDQKEEDrrnyptntyktLELE---IAESDVKVKEaELELVKEEAKEPRN-----EEKIKQAKAKVESKKAEATR 387
|
410 420
....*....|....*....|....*..
gi 42794779 1772 dLAQINDLQAQLEEANKEKQELQEKLQ 1798
Cdd:NF033838 388 -LEKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| PDZ2_L-delphilin-like |
cd06744 |
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
224-308 |
4.84e-06 |
|
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: 46.11 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 224 QRRPTGDFGFSLRrttmldrgpeGQAcrrVVHF--AEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGD 301
Cdd:cd06744 4 VYRGNGSFGFTLR----------GHA---PVYIesVDPG-SAAERA-GLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGS 68
|
....*..
gi 42794779 302 SVRLKVQ 308
Cdd:cd06744 69 MPTLVVE 75
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1594-1913 |
4.90e-06 |
|
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: 51.22 E-value: 4.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1594 DEEVEEARQScQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRrdfesekrLRKDLKRTKALLADAQLMLD 1673
Cdd:pfam19220 37 EAILRELPQA-KSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEE--------LVARLAKLEAALREAEAAKE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1674 HLKnsapskREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALE-------EQLSRLQREKNEIQN 1746
Cdd:pfam19220 108 ELR------IELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEgelatarERLALLEQENRRLQA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1747 RLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQelqeklqalqsqvefleqsmvdkslvsRQEAKIRE 1826
Cdd:pfam19220 182 LSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERE---------------------------RAEAQLEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1827 LETRLEFERT-QVKRLESLASRLKENMEKLTEERDqriaaenrekeqnkrlqrQLRDTKEEMGELARKEAEASRKKHELE 1905
Cdd:pfam19220 235 AVEAHRAERAsLRMKLEALTARAAATEQLLAEARN------------------QLRDRDEAIRAAERRLKEASIERDTLE 296
|
....*...
gi 42794779 1906 MDLESLEA 1913
Cdd:pfam19220 297 RRLAGLEA 304
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1744-1938 |
5.10e-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: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1744 IQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKE----KQELQEKLQALQSQVEFLEQSMVD------ 1813
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRElesrVAELKEELRQSREKHEELEEKYKElsasse 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1814 -----KSLVSRQ----EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQriaaenrEKEQNKRLQRQLRDTK 1884
Cdd:pfam07888 112 elseeKDALLAQraahEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKE-------EEAERKQLQAKLQQTE 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1885 EEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIED 1938
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEE 238
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1434-1808 |
5.47e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1434 RLTAELQDTKLHLEGQQVRNHELEKKQrrfDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFT 1513
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAAL---SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1514 QKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMErMRQTHSKEMESR 1593
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIA-EREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1594 DEEVEEARQSCQKKLKQMEVQleEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLD 1673
Cdd:COG4372 159 LESLQEELAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1674 HLKNSAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQE 1753
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIE-ELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALED 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1754 DMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLE 1808
Cdd:COG4372 316 ALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1376-1734 |
5.61e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.06 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1376 ERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERrlgdLQADSEESQRALQQLKKKCQRLTAELQdtklhlegqqvrnhE 1455
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQ----LEEELEQARSELEQLEEELEELNEQLQ--------------A 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1456 LEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEA 1535
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 SLAKVKKQlrDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHS--KEMESRDEEVEEARQSCQKKLKQMEV 1613
Cdd:COG4372 172 ELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLeaKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLE 1693
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 42794779 1694 ESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1734
Cdd:COG4372 330 LALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PDZ1_PTPN13_FRMPD2-like |
cd06694 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13),FERM and PDZ ... |
258-305 |
5.71e-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: 5.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 42794779 258 EPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRL 305
Cdd:cd06694 38 IPG-GPADKDGRIKPGDRIIAINGQSLEGKTHHAAVEIIQNAPDKVEL 84
|
|
| PDZ4_PTPN13-like |
cd06696 |
PDZ domain 4 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
220-307 |
6.16e-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: 46.15 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLRRTTMldrgPEGQACRRVVHfaEPgagtkdlALG---LVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06696 5 EVTLTKSEKGSLGFTVTKGKD----DNGCYIHDIVQ--DP-------AKSdgrLRPGDRLIMVNGVDVTNMSHTEAVSLL 71
|
90
....*....|.
gi 42794779 297 RQSGDSVRLKV 307
Cdd:cd06696 72 RAAPKEVTLVL 82
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
538-819 |
6.33e-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: 51.67 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 538 LLEAFGNSPTIINGNATRFSQILSLDF-----DQAGQVASASIQTMLLEKLRVARRPASEA------TFNVFYYLLACGD 606
Cdd:cd14894 255 VLEAFGHATTSMNLNSSRFGKMTTLQVafglhPWEFQICGCHISPFLLEKSRVTSERGRESgdqnelNFHILYAMVAGVN 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 607 G-----TLRTELHLNHL----------AENNVFGIVplAKPEEKQKAAQQFSKLQAAMKVLGISPDEQKACWFILAAIYH 671
Cdd:cd14894 335 AfpfmrLLAKELHLDGIdcsaltylgrSDHKLAGFV--SKEDTWKKDVERWQQVIDGLDELNVSPDEQKTIFKVLSAVLW 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 672 LGaaGATKEAAEAGRKQFARHEWA----QKAAYLLGC-SLEELSSAIFKhqhKGGTLQRSTSFRQGPEESGLGDGTGPKL 746
Cdd:cd14894 413 LG--NIELDYREVSGKLVMSSTGAlnapQKVVELLELgSVEKLERMLMT---KSVSLQSTSETFEVTLEKGQVNHVRDTL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 747 SALeclegmaagLYSELFTLLVSLVNRALKSS-------QHSLCS----------MMIVDTPGFQNPEQGgsargaSFEE 809
Cdd:cd14894 488 ARL---------LYQLAFNYVVFVMNEATKMSalstdgnKHQMDSnasapeavslLKIVDVFGFEDLTHN------SLDQ 552
|
330
....*....|
gi 42794779 810 LCHNYTQDRL 819
Cdd:cd14894 553 LCINYLSEKL 562
|
|
| PDZ4_GRIP1-2-like |
cd06686 |
PDZ domain 4 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
220-308 |
6.39e-06 |
|
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: 46.57 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLR----RTTMLDRGPegqacrrVVHFAEPGAGTKDLALgLVPGDRLVEINGHNVESKSRDEIVEM 295
Cdd:cd06686 9 EVILRGDPLKGFGIQLQggvfATETLSSPP-------LISFIEPDSPAERCGV-LQVGDRVLSINGIPTEDRTLEEANQL 80
|
90
....*....|...
gi 42794779 296 IRQSGDSVRLKVQ 308
Cdd:cd06686 81 LRDSASKVTLEIE 93
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1449-1923 |
6.55e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 51.75 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1449 QQVRNHELEKKQRRFDS--ELSQAHEEAQR----EKLQREKLQREkdmLLAEAFSLKQQLeekDMDIAGFTQKVVSleae 1522
Cdd:NF041483 76 QLLRNAQIQADQLRADAerELRDARAQTQRilqeHAEHQARLQAE---LHTEAVQRRQQL---DQELAERRQTVES---- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1523 lqDISSQESKDEASLAKVKKQLRDLeakvkdqeeeLDE-QAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEE-- 1599
Cdd:NF041483 146 --HVNENVAWAEQLRARTESQARRL----------LDEsRAEAEQALAAARAEAERLAEEARQRLGSEAESARAEAEAil 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1600 --ARQSCQKKLKQMEVQLEEEyEDKQKVLR-----EKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLML 1672
Cdd:NF041483 214 rrARKDAERLLNAASTQAQEA-TDHAEQLRsstaaESDQARRQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1673 DHLKNSAPS---------KREIAQLKNQ-LEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEE--QLSRLQRE 1740
Cdd:NF041483 293 AKQLASAESaneqrtrtaKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTaaQLAKAART 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1741 KNEIQNRLEEDQEDM-----NELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQ--------ELQEKLQALQSQVEFL 1807
Cdd:NF041483 373 AEEVLTKASEDAKATtraaaEEAERIRREAEAEADRLRGEAADQAEQLKGAAKDDTkeyraktvELQEEARRLRGEAEQL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMVDKSLVSRQEAKireletrlefeRTQVKRLESLASRLKENMEKLTEERDQ--RIAAENREKEQNKRLQR--QLRDT 1883
Cdd:NF041483 453 RAEAVAEGERIRGEAR-----------REAVQQIEEAARTAEELLTKAKADADElrSTATAESERVRTEAIERatTLRRQ 521
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 42794779 1884 KEEMGELARKEAEasRKKHELEMDLESLEAANQSLQADLK 1923
Cdd:NF041483 522 AEETLERTRAEAE--RLRAEAEEQAEEVRAAAERAARELR 559
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1396-1771 |
6.74e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.67 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1396 KLEVEQQNKRQLERRLGDLQADSEESQRA----LQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAH 1471
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKalfeLDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1472 EEAQREKLQREKLQREKDMLLAEAFSLKQQLEEkdmdiagFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKV 1551
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEE-------LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1552 KDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARqscqkklkqmEVQLEEEYEDKQKVLREKRE 1631
Cdd:COG4372 160 ESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLI----------ESLPRELAEELLEAKDSLEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1632 LEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEV 1711
Cdd:COG4372 230 KLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1712 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASR 1771
Cdd:COG4372 310 IGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1531-1646 |
6.76e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 51.30 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1531 SKDEASLAKVkkqLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRqthskemESRDEEVEEARQSCQKKLKQ 1610
Cdd:COG1193 510 GEESIDVEKL---IEELERERRELEEEREEAERLREELEKLREELEEKLEELE-------EEKEEILEKAREEAEEILRE 579
|
90 100 110
....*....|....*....|....*....|....*....
gi 42794779 1611 MEVQLEE---EYEDKQKVLREKRELEGKLATLSDQVNRR 1646
Cdd:COG1193 580 ARKEAEElirELREAQAEEEELKEARKKLEELKQELEEK 618
|
|
| PDZ2-PTPN13_FRMPD2-like |
cd06792 |
PDZ domain 2 of tyrosine kinase PTPN13, FERM and PDZ domain-containing protein 2 (FRMPD2), and ... |
273-308 |
7.00e-06 |
|
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: 46.05 E-value: 7.00e-06
10 20 30
....*....|....*....|....*....|....*.
gi 42794779 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06792 51 GDRLLEVNGVSLEGVTHKQAVECLKNAGQVVTLVLE 86
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1534-1894 |
8.87e-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: 51.11 E-value: 8.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1534 EASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQ----AKLRLEMEMERMRQThsKEMESRDEEVEEArqscqkklk 1609
Cdd:COG3096 291 RRELFGARRQLAEEQYRLVEMARELEELSARESDLEQdyqaASDHLNLVQTALRQQ--EKIERYQEDLEEL--------- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1610 qmEVQLEEEyedkqkvlrekrelEGKLATLSDQVNRRDFESEkRLRKDLKRTKALLADAQLMLDHLKNSAPSKReiaQLK 1689
Cdd:COG3096 360 --TERLEEQ--------------EEVVEEAAEQLAEAEARLE-AAEEEVDSLKSQLADYQQALDVQQTRAIQYQ---QAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1690 NQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqedmneLMKKHKAAVA-- 1767
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE--------LVCKIAGEVErs 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 ----QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQvefleqsmvdkslvSRQEAKIRELETRLEFERTQVKRLES 1843
Cdd:COG3096 492 qawqTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQ--------------QNAERLLEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1844 LASRLKENMEKLTEErdqriAAENREkeQNKRLQRQLRDTKEEMGELARKE 1894
Cdd:COG3096 558 LLAELEAQLEELEEQ-----AAEAVE--QRSELRQQLEQLRARIKELAARA 601
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1487-1877 |
8.93e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.11 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1487 EKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEAS-------LAKVKKQLR-------------D 1546
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDyqaasdhLNLVQTALRqqekieryqadleE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1547 LEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMR-------------QTHSKEMESRDEEVEEARQSCQK---KLKQ 1610
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKsqladyqqaldvqQTRAIQYQQAVQALERAKQLCGLpdlTADN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1611 MEVQLEEeYEDKQKVLREK-RELEGKLATLSDQVNRRD--FESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREiAQ 1687
Cdd:PRK04863 440 AEDWLEE-FQAKEQEATEElLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQL-QQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1688 LKNQLEESEftcaaavkarkameveiEDLHLQiddiakaktaleEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAava 1767
Cdd:PRK04863 518 LRMRLSELE-----------------QRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEA--- 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 qasrdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRLEFERTQV-------KR 1840
Cdd:PRK04863 566 -------RLESLSESVSEARERRMALRQQLEQLQARIQRLAA----------RAPAWLAAQDALARLREQSgeefedsQD 628
|
410 420 430
....*....|....*....|....*....|....*..
gi 42794779 1841 LESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQ 1877
Cdd:PRK04863 629 VTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1249-1644 |
1.39e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1249 VQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRIseltseLTDERNTGESASQLldaetaerlraEKEMKE 1328
Cdd:PRK04778 114 LDLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSL------LANRFSFGPALDEL-----------EKQLEN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1329 LQTQYDalkkqmevmemevmearliRAAEINGEVDDDDAggewRLKYERAVREVDFTK----------KRLQQEFEDKLE 1398
Cdd:PRK04778 177 LEEEFS-------------------QFVELTESGDYVEA----REILDQLEEELAALEqimeeipellKELQTELPDQLQ 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1399 VEQQNKRQLER---RLGDLQADSEesqraLQQLKKKCQRLTAELQDtkLHLEGQQVRNHELEKK--------QRRFDSEl 1467
Cdd:PRK04778 234 ELKAGYRELVEegyHLDHLDIEKE-----IQDLKEQIDENLALLEE--LDLDEAEEKNEEIQERidqlydilEREVKAR- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1468 SQAHEEAQREKLQREKLQREKDMLLAEAFSLKQ--QLEEKDMDIA-GFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1544
Cdd:PRK04778 306 KYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsyTLNESELESVrQLEKQLESLEKQYDEITERIAEQEIAYSELQEEL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1545 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQ---THSKEMESRD-----EEVEEARQSCQKKLKQMEVQLE 1616
Cdd:PRK04778 386 EEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNklhEIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELE 465
|
410 420
....*....|....*....|....*...
gi 42794779 1617 EEYEDKQKVLREKRELEGKLATLSDQVN 1644
Cdd:PRK04778 466 EKPINMEAVNRLLEEATEDVETLEEETE 493
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1394-1825 |
1.44e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKkkcqRLTAelqdTKLHLEGQQVRNHELEKKQRR---FDSELSQA 1470
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFS----RFIG----SHLAVAFEADPEAELRQLNRRrveLERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1471 HEEAQREKLQREKLQREKDML--LAEAFSLkqqleekdMDIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLrdle 1548
Cdd:PRK04863 857 ESQEQQQRSQLEQAKEGLSALnrLLPRLNL--------LADETLADRVEEIREQLD----EAEEAKRFVQQHGNAL---- 920
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1549 akvkdqeEELDEQAGTIQMLEQaklrlemEMERMRQthskemesrdeEVEEARQScQKKLKQ--------MEVQLEEEYE 1620
Cdd:PRK04863 921 -------AQLEPIVSVLQSDPE-------QFEQLKQ-----------DYQQAQQT-QRDAKQqafaltevVQRRAHFSYE 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1621 DKQKVLREKRELEGKLatlsdQVNRRDFESEK-RLRKDLKRTKALLADAQLMLDHLKNSAPSKREI-AQLKNQLEesEFT 1698
Cdd:PRK04863 975 DAAEMLAKNSDLNEKL-----RQRLEQAEQERtRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMlQELKQELQ--DLG 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1699 CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA--QASRDLAQI 1776
Cdd:PRK04863 1048 VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKD 1127
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1777 NDLQAQL---EEANKEKQEL-------QEKLQALQSQVEFLEQSMVDKSLVSRQEAKIR 1825
Cdd:PRK04863 1128 NGVERRLhrrELAYLSADELrsmsdkaLGALRLAVADNEHLRDVLRLSEDPKRPERKVQ 1186
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1512-1579 |
1.46e-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: 47.62 E-value: 1.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1512 FTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML--EQAKLRLEMEM 1579
Cdd:pfam08614 76 LAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLqdELVALQLQLNM 145
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1404-1828 |
1.48e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.03 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQAD-------SEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVrnhelEKKQRRFDSELSQ------- 1469
Cdd:pfam05701 37 RKLVELELEKVQEEipeykkqSEAAEAAKAQVLEELESTKRLIEELKLNLERAQT-----EEAQAKQDSELAKlrveeme 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1470 ---AHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEkdmdiagfTQKVVSLEAELQDISSQESKDEASLAK-VKKQLR 1545
Cdd:pfam05701 112 qgiADEASVAAKAQLEVAKARHAAAVAELKSVKEELES--------LRKEYASLVSERDIAIKRAEEAVSASKeIEKTVE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1546 DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKlKQMEVQLEEEYEdkqKV 1625
Cdd:pfam05701 184 ELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLNWEKELKQAEEELQRLNQQLLSA-KDLKSKLETASA---LL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1626 LREKREL----EGKLATLSDQvNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQLEEsEFTCA 1700
Cdd:pfam05701 260 LDLKAELaaymESKLKEEADG-EGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaSLRSELEK-EKAEL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1701 AAVKARKAMEveiedlhlqiddiAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKhkaaVAQASRDLAQINDL- 1779
Cdd:pfam05701 338 ASLRQREGMA-------------SIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQ----LQQAAQEAEEAKSLa 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 42794779 1780 QAQLEEANKEKQElQEKLQALQSQVEfleqsmvdkslvSRQEAKIRELE 1828
Cdd:pfam05701 401 QAAREELRKAKEE-AEQAKAAASTVE------------SRLEAVLKEIE 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1602-1773 |
1.65e-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: 48.38 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1602 QSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrDFESE-KRLRKDLKRTKALLADAQLMLDHLKNSap 1680
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE--DLEKEiKRLELEIEEVEARIKKYEEQLGNVRNN-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1681 skREIAQLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQEDMN 1756
Cdd:COG1579 89 --KEYEALQKEIESLK-------RRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 42794779 1757 ELMKKHKAAVAQASRDL 1773
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1745-1938 |
1.70e-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: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1745 QNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvDKSLVSRQEAKI 1824
Cdd:pfam12795 8 AKLDEAAKKKLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAE-------AAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1825 RELETRLEFERTQvkrLESLASRLKENMEKLTEERD------QRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1898
Cdd:pfam12795 81 EELEQRLLQTSAQ---LQELQNQLAQLNSQLIELQTrperaqQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 42794779 1899 RKKHELEMDLESLEAANQSLQADL-----KLAFKRIGDLQAAIED 1938
Cdd:pfam12795 158 LAALKAQIDMLEQELLSNNNRQDLlkarrDLLTLRIQRLEQQLQA 202
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1394-1603 |
1.85e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEE 1473
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1474 AQREKLQREKLqrekDMLL-AEAFS--------LKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL 1544
Cdd:COG3883 95 LYRSGGSVSYL----DVLLgSESFSdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1545 RDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQS 1603
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1539-1887 |
2.17e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 49.45 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1539 KVKKQLRDLEAKVKDQEEELDeqagtiQMLEqaklrlemEMERMRQTHSKEMesrdEEVEearqscqkklkqmevQLEEE 1618
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIE------QILE--------ELQELLESEEKNR----EEVE---------------QLKDL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1619 YEDKQKVLREKR--------ELEGKLATLSDQVNRRDFESEK-----------RLRKDLKRTKALLADAQLMLDHLKNSA 1679
Cdd:PRK04778 149 YRELRKSLLANRfsfgpaldELEKQLENLEEEFSQFVELTESgdyveareildQLEEELAALEQIMEEIPELLKELQTEL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1680 PSkrEIAQLKN---QLEESEFtcaaaVKARKAMEVEIEDLHLQIDDiakaktaLEEQLSRLQREKNEIQNR-LEEDQEDM 1755
Cdd:PRK04778 229 PD--QLQELKAgyrELVEEGY-----HLDHLDIEKEIQDLKEQIDE-------NLALLEELDLDEAEEKNEeIQERIDQL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1756 NELMKKHKAAVAQASRDLAQINDLQAQLEEANKE-KQELQ-------------EKLQALQSQVEFLE-QSMVDKSLVSRQ 1820
Cdd:PRK04778 295 YDILEREVKARKYVEKNSDTLPDFLEHAKEQNKElKEEIDrvkqsytlneselESVRQLEKQLESLEkQYDEITERIAEQ 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1821 EAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEErdqriaaENREKEQNKRLQRQLRDTKEEM 1887
Cdd:PRK04778 375 EIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLRKD-------ELEAREKLERYRNKLHEIKRYL 434
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1688-1922 |
2.21e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1688 LKNQLEESEFTCAAAVKARKAMEVEIEDlhlQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVA 1767
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREK---EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSR--QEAKIRELETRLEFERTQVK 1839
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELermkerAKKAGAQRkeEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1840 RL--------------ESLASRLKENMEKLTeerdQRIAAENREKEQNKRLQRQLRDTKEEmgelarkeAEASRKKHE-L 1904
Cdd:pfam07888 189 SLskefqelrnslaqrDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQER--------LNASERKVEgL 256
|
250
....*....|....*...
gi 42794779 1905 EMDLESLEAANQSLQADL 1922
Cdd:pfam07888 257 GEELSSMAAQRDRTQAEL 274
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1701-1892 |
2.42e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.51 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1701 AAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQLSRLQRekneIQNRLEEDQEDMNELMKKHKAAVAQASRDLA------ 1774
Cdd:COG1842 20 KAEDPEKMLDQAIRDME---EDLVEARQALAQVIANQKR----LERQLEELEAEAEKWEEKARLALEKGREDLArealer 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1775 ------QINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslvsRQEAKIRELETRLEFERTQVKRLESLAS-R 1847
Cdd:COG1842 93 kaeleaQAEALEAQLAQLEEQVEKLKEALRQLESKLE-------------ELKAKKDTLKARAKAAKAQEKVNEALSGiD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1848 LKENMEKLT--EERDQRIAAEN---REKEQNKRLQRQLRDTKEEMG---ELAR 1892
Cdd:COG1842 160 SDDATSALErmEEKIEEMEARAeaaAELAAGDSLDDELAELEADSEvedELAA 212
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1469-1695 |
2.52e-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: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1469 QAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKdmdiagfTQKVVSLEAELQDIssqeskdEASLAKVKKQLRDLE 1548
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEEL-------NEEYNELQAELEAL-------QAEIDKLQAEIAEAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1549 AKVKDQEEELDEQA----------GTIQMLEQAKL------RLEMeMERMRQTHSKEMesrdEEVEEARQSCQKKLKQME 1612
Cdd:COG3883 79 AEIEERREELGERAralyrsggsvSYLDVLLGSESfsdfldRLSA-LSKIADADADLL----EELKADKAELEAKKAELE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1613 VQLEEEYEDKQKVLREKRELEGKLATLSDQVNrrdfesekRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQL 1692
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLA--------QLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
...
gi 42794779 1693 EES 1695
Cdd:COG3883 226 AAA 228
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1649-1922 |
2.70e-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: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1649 ESEKRLRKDLKRTKALLADAQlmlDHLKNSAPSKREIAQLKNQL-EESEFTCAAAVKARKAMEVEIEDLHLQIDdiaKAK 1727
Cdd:pfam09311 16 EQEAETRDQVKKLQEMLRQAN---DQLEKTMKDKKELEDKMNQLsEETSNQVSTLAKRNQKSETLLDELQQAFS---QAK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1728 TALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVaqaSRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL 1807
Cdd:pfam09311 90 RNFQDQLAVLMDSREQVSDELVRLQKDNESLQGKHSLHV---SLQQAEKFDMPDTVQELQELVLKYREELIEVRTAADHM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMVDKSLVSR-----QEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQrIAAENREKeqnkrlQRQLRD 1882
Cdd:pfam09311 167 EEKLKAEILFLKeqiqaEQCLKENLEETLQAEIENCKEEIASISSLKVELERIKAEKEQ-LENGLTEK------IRQLED 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 42794779 1883 TKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADL 1922
Cdd:pfam09311 240 LQTTKGSLETQLKKETNEKAAVEQLVFEEKNKAQRLQTEL 279
|
|
| PDZ2_DLG5-like |
cd06765 |
PDZ domain 2 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
270-308 |
3.07e-05 |
|
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: 43.87 E-value: 3.07e-05
10 20 30
....*....|....*....|....*....|....*....
gi 42794779 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06765 35 LTVGDRIIAINGIALDNKSLSECEALLRSCRDSLSLSLM 73
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1388-1568 |
3.18e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.86 E-value: 3.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1388 RLQQEFEDKLEVEQQNKRQLER---RLGDLQADSEESQRALQQLKKKCQRLTAELQ----DTKLHLEG-------QQVrn 1453
Cdd:PHA02562 217 RKQNKYDELVEEAKTIKAEIEEltdELLNLVMDIEDPSAALNKLNTAAAKIKSKIEqfqkVIKMYEKGgvcptctQQI-- 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1454 HELEKKQRRFDSELSQAHEEAQREKLQREKLQREKDMLLA---EAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQE 1530
Cdd:PHA02562 295 SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEqskKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEF 374
|
170 180 190
....*....|....*....|....*....|....*...
gi 42794779 1531 SKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQML 1568
Cdd:PHA02562 375 VDNAEELAKLQDELDKIVKTKSELVKEKYHRGIVTDLL 412
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1595-1865 |
3.36e-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: 48.80 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1595 EEVEEARQSCQKKLKQMEvQLEEEYED--------KQKVLREKRE----LEGKLATLSDQVNR-----RDFESEKRLRKD 1657
Cdd:COG5185 232 EEALKGFQDPESELEDLA-QTSDKLEKlveqntdlRLEKLGENAEsskrLNENANNLIKQFENtkekiAEYTKSIDIKKA 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1658 LKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKtALEEQLSRL 1737
Cdd:COG5185 311 TESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELD-SFKDTIEST 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1738 QREKNEIQNRLEEDQEDMNELMKKHKAAVAQasrdlaQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLV 1817
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADR------QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQS 463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1818 SRQEAK---IRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA 1865
Cdd:COG5185 464 RLEEAYdeiNRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
|
| PDZ1_harmonin |
cd06737 |
PDZ domain 1 of harmonin isoforms a, b, and c, and related domains; PDZ (PSD-95 (Postsynaptic ... |
217-310 |
3.56e-05 |
|
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: 44.17 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 217 TLRELELQRRPTGDFGFSLRrttmldrGPEGQACRRVVHFAEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMI 296
Cdd:cd06737 1 KLRLVRLDRRGPESLGFSVR-------GGLEHGCGLFVSHVSPG-SQADNK-GLRVGDEIVRINGYSISQCTHEEVINLI 71
|
90
....*....|....
gi 42794779 297 RQSgDSVRLKVQPI 310
Cdd:cd06737 72 KTK-KTVSLKVRHV 84
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1249-1615 |
3.77e-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: 48.75 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1249 VQLSEEQIRNKDEEIQQlrsklekAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRA-EKEMK 1327
Cdd:pfam15964 341 VQMTEEANFEKTKALIQ-------CEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQMEVMEMEVMEARLIRAAEingEVDDDDAGGEWR-------LKYERAVREVDFTKKRLQQEfedkLEVE 1400
Cdd:pfam15964 414 QLEAQVEKVTREKNSLVSQLEEAQKQLASQ---EMDVTKVCGEMRyqlnqtkMKKDEAEKEHREYRTKTGRQ----LEIK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1401 QQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDT--KLHLEGQqvrnhELEKKQRRFDSEL-SQAHEEAQRE 1477
Cdd:pfam15964 487 DQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESehQLHLTRL-----EKESIQQSFSNEAkAQALQAQQRE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1478 K----------LQREKLQREKDMLLAEAFSLKQQLEEKdmdiagftqkVVSLEAELQDISSQESKDEASLAKVKKQLRDL 1547
Cdd:pfam15964 562 QeltqkmqqmeAQHDKTVNEQYSLLTSQNTFIAKLKEE----------CCTLAKKLEEITQKSRSEVEQLSQEKEYLQDR 631
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1548 EAKVKDQEEELDEQAgtIQ---MLEQAKLRLEmEMERMRQTHSK---EMESRDEEVEEARQSCQKKLKQMEVQL 1615
Cdd:pfam15964 632 LEKLQKRNEELEEQC--VQhgrMHERMKQRLR-QLDKHCQATAQqlvQLLSKQNQLFKERQNLTEEVQSLRSQV 702
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1712-1966 |
3.81e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1712 EIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQ 1791
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1792 ELQEKLQALQSQVEFLEQSmvdkslvsrqeakireletrlefertqvkrleslASRLKENMEKLTEERDQRIAAENREKE 1871
Cdd:COG4372 112 ELQEELEELQKERQDLEQQ----------------------------------RKQLEAQIAELQSEIAEREEELKELEE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1872 QNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINS 1951
Cdd:COG4372 158 QLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237
|
250
....*....|....*
gi 42794779 1952 EGDSDVDSELEDRVD 1966
Cdd:COG4372 238 LLDALELEEDKEELL 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1500-1799 |
3.87e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1500 QQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKdqeeELDEQAgtiqmleqaklrlemem 1579
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK----ELREEA----------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1580 ermrQTHSKEMESRDEEVEEARQSCQKKLKQMEvQLEEEYEDKQKVLREKRELEGKLATLSDQVNR---------RDFES 1650
Cdd:COG1340 60 ----QELREKRDELNEKVKELKEERDELNEKLN-ELREELDELRKELAELNKAGGSIDKLRKEIERlewrqqtevLSPEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1651 EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL 1730
Cdd:COG1340 135 EKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1731 EEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLaqindLQAQLEEANKEKQELQEKLQA 1799
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-----REKEKEELEEKAEEIFEKLKK 278
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1387-1889 |
4.07e-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: 48.75 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1387 KRLQQEFEDKLEVeqqnkrqLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhleGQQVRNHELEKKQRrfDSE 1466
Cdd:pfam15964 223 EKLKLLYEAKTEV-------LESQVKSLRKDLAESQKTCEDLKERLKHKESLVAAST----SSRVGGLCLKCAQH--EAV 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1467 LSQAHEEAQREKLQRekLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSleaelqdisSQESKDEASLAKVKK--QL 1544
Cdd:pfam15964 290 LAQTHTNVHMQTIER--LTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQ---------AVQMTEEANFEKTKAliQC 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1545 RDLEAKVKDQEEELDEQAGTiqmlEQAKLRLEMEMERmrqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEeeyedkqK 1624
Cdd:pfam15964 359 EQLKSELERQKERLEKELAS----QQEKRAQEKEALR------KEMKKEREELGATMLALSQNVAQLEAQVE-------K 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1625 VLREKRELEGKLATLSDQVNRRDFESEK---RLRKDLKRTKALLADAQLmlDHLKNSAPSKREIaQLKNQleeseftcaa 1701
Cdd:pfam15964 422 VTREKNSLVSQLEEAQKQLASQEMDVTKvcgEMRYQLNQTKMKKDEAEK--EHREYRTKTGRQL-EIKDQ---------- 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1702 avkarkamevEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNeLMKKHKAAVAQASRDLAQINDLQA 1781
Cdd:pfam15964 489 ----------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLH-LTRLEKESIQQSFSNEAKAQALQA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1782 QLEEankekQELQEKLQALQSQvefleqsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQ 1861
Cdd:pfam15964 558 QQRE-----QELTQKMQQMEAQ----------------HDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRS 616
|
490 500
....*....|....*....|....*...
gi 42794779 1862 RIAAENREKEQNKRLQRQLRDTKEEMGE 1889
Cdd:pfam15964 617 EVEQLSQEKEYLQDRLEKLQKRNEELEE 644
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1682-1913 |
4.27e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1761
Cdd:COG1340 21 REEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 HKAAVaQASRDLAQINDLQAQLEEA--------NKEKQ------ELQEKLQALQSQVEfleqsmvdkslvsrQEAKIREL 1827
Cdd:COG1340 101 LAELN-KAGGSIDKLRKEIERLEWRqqtevlspEEEKElvekikELEKELEKAKKALE--------------KNEKLKEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1828 ETRLEFERTQ-------VKRLESLASRLKENMEKLTEERDQ--------------RIAAENREKEQNKRLQRQLRDTKEE 1886
Cdd:COG1340 166 RAELKELRKEaeeihkkIKELAEEAQELHEEMIELYKEADElrkeadelhkeiveAQEKADELHEEIIELQKELRELRKE 245
|
250 260
....*....|....*....|....*..
gi 42794779 1887 MGELARKEAEASRKKHELEMDLESLEA 1913
Cdd:COG1340 246 LKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1588-1803 |
4.63e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1588 KEMESRDEEVEEARQSCQKKLKQMEVQLE---EEYEDKQKVLREKRE----LEGKLATLSDQVNRRDFESEKRLRkDLKR 1660
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEelnEEYNELQAELEALQAeidkLQAEIAEAEAEIEERREELGERAR-ALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1661 TKALLADAQLML------DHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQL 1734
Cdd:COG3883 98 SGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1735 SRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1803
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1459-1862 |
4.91e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 48.74 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1459 KQRRFDSElsqaheEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMD-IAGFTQKVVSLEAELQDISSQesKDEASL 1537
Cdd:PLN02939 38 RRRGFSSQ------QKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHNRASMQ--RDEAIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1538 AKVKKQLRdleaKVKDQEEELDEQAGT-IQMLEQAklrlEMEMERMRQTHSKEMESRDEEVEEaRQSCQKKLKQMEVQLE 1616
Cdd:PLN02939 110 AIDNEQQT----NSKDGEQLSDFQLEDlVGMIQNA----EKNILLLNQARLQALEDLEKILTE-KEALQGKINILEMRLS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1617 EEYEDKQKVLREKRELEgklaTLSDQVNRRDFESEKRLRKDLKRTKALLadaqLMLDHLKNSAPS-KREIAQLKNQL--- 1692
Cdd:PLN02939 181 ETDARIKLAAQEKIHVE----ILEEQLEKLRNELLIRGATEGLCVHSLS----KELDVLKEENMLlKDDIQFLKAELiev 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1693 EESEFTCAAAVKARKAMEVEIEDLHLQI----DDIAKAKT----ALEEQLSRLQREKNEIQNRLEedqedmnelmkkHKA 1764
Cdd:PLN02939 253 AETEERVFKLEKERSLLDASLRELESKFivaqEDVSKLSPlqydCWWEKVENLQDLLDRATNQVE------------KAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1765 AVAQASRDLA-QINDLQAQLEEANKEKQELqEKLQALQSQVefleqsmvdKSLVSRQEAKIRELETrlefertQVKRLES 1843
Cdd:PLN02939 321 LVLDQNQDLRdKVDKLEASLKEANVSKFSS-YKVELLQQKL---------KLLEERLQASDHEIHS-------YIQLYQE 383
|
410
....*....|....*....
gi 42794779 1844 LASRLKENMEKLTEERDQR 1862
Cdd:PLN02939 384 SIKEFQDTLSKLKEESKKR 402
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1417-1896 |
4.92e-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: 48.15 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1417 DSEESQRALQQLKKKCQRL---TAELQDTKLHLegqQVRNHELEKKQRRFDSELSQA--------HEEAQREKLQREKLQ 1485
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELdqqVSLLQEEKNSL---QQENKKLQERLDQLESGDDSGtpggkkylLLQKQLEQLQEENFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1486 RE--KDMLLAEAFSLKQQLEE---KDMDIAGFTQKVVSLEAE---LQDISSQESKDEASLAKVKKQLRDLEakvkdqeeE 1557
Cdd:pfam05622 78 LEtaRDDYRIKCEELEKEVLElqhRNEELTSLAEEAQALKDEmdiLRESSDKVKKLEATVETYKKKLEDLG--------D 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQagtIQMLEqaklrlEMEMERMRQTHSKEMESRDEEVEEAR-QSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKL 1636
Cdd:pfam05622 150 LRRQ---VKLLE------ERNAEYMQRTLQLEEELKKANALRGQlETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1637 ATLSDQVNRRDFEsekrlRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLeeseftcaaavkARKAMEVEIEdl 1716
Cdd:pfam05622 221 EALQKEKERLIIE-----RDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNL------------AAEIMPAEIR-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1717 hlqiddiakaktaleEQLSRLQREkneiqnrleedqedmNELMKkhkaaVAQASRDLAQINDLQAQLEEANKEKQELQEK 1796
Cdd:pfam05622 282 ---------------EKLIRLQHE---------------NKMLR-----LGQEGSYRERLTELQQLLEDANRRKNELETQ 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1797 LQALQSQVEFLEQsmvdkslvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAA-ENREKEQNKR 1875
Cdd:pfam05622 327 NRLANQRILELQQ-------------QVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKkEQIEELEPKQ 393
|
490 500
....*....|....*....|.
gi 42794779 1876 LQRQLRDTKEEMGELARKEAE 1896
Cdd:pfam05622 394 DSNLAQKIDELQEALRKKDED 414
|
|
| PDZ_6 |
pfam17820 |
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins. |
269-308 |
6.21e-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: 42.52 E-value: 6.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 42794779 269 GLVPGDRLVEINGHNVESKsrDEIVEMIRQSGDS-VRLKVQ 308
Cdd:pfam17820 15 GLRVGDVILAVNGKPVRSL--EDVARLLQGSAGEsVTLTVR 53
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1524-1776 |
6.38e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1524 QDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELD---EQAGTIQMLEQAKLRLEmEMERMRQTHSkEMESRDEEVEEA 1600
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrQKNGLVDLSEEAKLLLQ-QLSELESQLA-EARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1601 RQSCQKKLKQMEVQLEEEYEDK--QKVLREKRELEGKLATLSdqvnrrdfeseKRLRKDLKRTKALladaqlmldhlkns 1678
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELS-----------ARYTPNHPDVIAL-------------- 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1679 apsKREIAQLKNQLEEseftcaAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRL---QREKNEIQNRLEEDQEDM 1755
Cdd:COG3206 297 ---RAQIAALRAQLQQ------EAQRILASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELY 367
|
250 260
....*....|....*....|.
gi 42794779 1756 NELMKKHKAAVAQASRDLAQI 1776
Cdd:COG3206 368 ESLLQRLEEARLAEALTVGNV 388
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1757-1932 |
6.82e-05 |
|
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: 46.05 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1757 ELMKKHKAAVAQA--------SRDLAQINDLQAQLEEANK--------------EKQELQEKLQALQSQVEFLEQSMV-- 1812
Cdd:pfam13851 1 ELMKNHEKAFNEIknyynditRNNLELIKSLKEEIAELKKkeerneklmseiqqENKRLTEPLQKAQEEVEELRKQLEny 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1813 --DKSLVSRQEAKIRELEtrleferTQVKRLESLASRLKENMEKLTEERD---QRIAAENREKEQNKRLQRQLRDTK-EE 1886
Cdd:pfam13851 81 ekDKQSLKNLKARLKVLE-------KELKDLKWEHEVLEQRFEKVERERDelyDKFEAAIQDVQQKTGLKNLLLEKKlQA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42794779 1887 MGE-LARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDL 1932
Cdd:pfam13851 154 LGEtLEKKEAQLNEVLAAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
|
|
| PDZ_MPP-like |
cd06726 |
PDZ domain of membrane palmitoylated proteins (MPPs), and related domains; PDZ (PSD-95 ... |
273-309 |
7.31e-05 |
|
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: 43.02 E-value: 7.31e-05
10 20 30
....*....|....*....|....*....|....*..
gi 42794779 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06726 44 GDEILEINGIPVSGKTVDELQKLLSSLSGSVTFKLIP 80
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1573-1923 |
7.47e-05 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 47.93 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1573 LRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQmevQLEEEYEDKQKVLrekrELEGKLATLSDQVNRRDFESEK 1652
Cdd:PLN03229 432 RELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKK---EIDLEYTEAVIAM----GLQERLENLREEFSKANSQDQL 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1653 RLRkdlkrtkALLADAQLMLDHLKNSAPSKREIAQLKNQLEeseftcaaavkarkameveiedlhlQIDDIAKAKTALEE 1732
Cdd:PLN03229 505 MHP-------VLMEKIEKLKDEFNKRLSRAPNYLSLKYKLD-------------------------MLNEFSRAKALSEK 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1733 QlSRLQREKNEIQNRLEE--DQEDMNELMKKHKAAVAQ--ASRDLAQINDLQAQLEEANKEKQ-ELQEKLQALQSQVEFL 1807
Cdd:PLN03229 553 K-SKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASsgASSGDELDDDLKEKVEKMKKEIElELAGVLKSMGLEVIGV 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMVDKSLVSRQE---AKIREL--ETRLEFERT-QVKRLESLASRLKENMEKLTEERDQriaaenREKEQNKRLQRQLR 1881
Cdd:PLN03229 632 TKKNKDTAEQTPPPnlqEKIESLneEINKKIERViRSSDLKSKIELLKLEVAKASKTPDV------TEKEKIEALEQQIK 705
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 42794779 1882 DTKEEmgelARKEAEASRKKHELEMDLESLEAANQSLQADLK 1923
Cdd:PLN03229 706 QKIAE----ALNSSELKEKFEELEAELAAARETAAESNGSLK 743
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1419-1633 |
7.67e-05 |
|
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: 46.19 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1419 EESQRALQQLKK----KCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQaHEeaqreklqreklqREKDMLLAE 1494
Cdd:pfam15665 10 DEHEAEIQALKEaheeEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQ-HE-------------RMKRQALTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1495 AFSLKQQLEEKDM-DIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQL-RDLEAKVKDQEEELDEQAGTIQMLEQAK 1572
Cdd:pfam15665 76 FEQYKRRVEERELkAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFeQEKRKALEELRAKHRQEIQELLTTQRAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1573 LRLEM-EMERMRQTHSKEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDK---QKVLREkRELE 1633
Cdd:pfam15665 156 SASSLaEQEKLEELHKAELESLRKEVED--------LRKEKKKLAEEYEQKlskAQAFYE-RELE 211
|
|
| CtpA |
COG0793 |
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ... |
269-309 |
9.65e-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: 46.79 E-value: 9.65e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIR-QSGDSVRLKVQP 309
Cdd:COG0793 88 GIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLTIKR 129
|
|
| DUF4455 |
pfam14643 |
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, ... |
1253-1628 |
1.04e-04 |
|
Domain of unknown function (DUF4455); This domain family is found in bacteria and eukaryotes, and is approximately 480 amino acids in length. There are two completely conserved residues (W and P) that may be functionally important.
Pssm-ID: 464231 [Multi-domain] Cd Length: 469 Bit Score: 47.27 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1253 EEQIRNKDEEIQQLRSKLEKAEKERnelrlnSDRLESRISELTSELTDerntgesASQLLDAETAERLRAE-----KEMK 1327
Cdd:pfam14643 77 AQHSLLRKSWIKELDETLEKLEKER------ADKLKSVLKKYVEILED-------IAHLLPPDVYRLIDKEameinQALL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQmevmemevmearlIRAAEINGEVDD----DDAGGEWR-LKYERAVRE--VDFTKKRLQQEFEDKLEVE 1400
Cdd:pfam14643 144 ENRRAYAKLFAN-------------LMEAELKQELSFrlrwQDRVDRWKaLKTEHLIQEfkEFIASEEIQNPPERKKELE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1401 QQNKRQ---LERRLGDLQADSEESQRALQqlKKKCQRLTAELQD-------------TKLHLEGQQVRNHELEKKQRRFD 1464
Cdd:pfam14643 211 EMLKEQkklQQKRLELLQKISDLLPPAYS--KSKVEEWWASLEAlneqldqyhdqcmTKLRAEYEEVWQECLARVQKLKQ 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1465 S-ELSQAHEEAQREKLQRE-------KLQR--EKDMLLAEAF--SLKQQLEEKDMDIAGFTQKVVSLEAELQdissqesk 1532
Cdd:pfam14643 289 ElLDYKVCSEEEAEALVNEeflplvgKLQRdaEDELEKLDKFleELAKQTEAQSEDLFKFFREAAQLWDVHQ-------- 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1533 deaslAKVKKQLRDLEAKVKDQEEELDEQagtIQMLEQAklrLEMEMERMRQthskemESRDEEVEEARQSCQKKLKQME 1612
Cdd:pfam14643 361 -----TELAKQELELEKKLEQCRQKHDQE---NQAKEAA---LDKKLDQLRQ------ASTEEKLKECLDKALKFLDDIE 423
|
410
....*....|....*.
gi 42794779 1613 VQLEEEYEDKQKVLRE 1628
Cdd:pfam14643 424 KEYEDFHDKLTAIVKE 439
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1699-1896 |
1.05e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1699 CAAAVKARKAMEVEIEDLHLQIDDI-----AKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDL 1773
Cdd:PRK12704 19 VIGYFVRKKIAEAKIKEAEEEAKRIleeakKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 AQindlqaQLEEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsrQEAKIRELETRlefertQVKRLESLASrlkenme 1853
Cdd:PRK12704 99 DR------KLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEE------QLQELERISG------- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 42794779 1854 kLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAE 1896
Cdd:PRK12704 150 -LTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAK 191
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1551-1888 |
1.06e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 46.98 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1551 VKDQEEELDEQAGTIQMLEQAKLRL---------EMEMER-----MRQTHSKEMESRDEEVEEARQSCQKKL--KQMEVQ 1614
Cdd:pfam15742 1 VSSGEKLKYQQQEEVQQLRQNLQRLqilctsaekELRYERgknldLKQHNSLLQEENIKIKAELKQAQQKLLdsTKMCSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1615 LEEEYED-KQKVlrekRELEGKLATLSDQVnrrdfESEKRLRKDLKRTKALLADAQLMldhlknsapskreIAQLKNQLE 1693
Cdd:pfam15742 81 LTAEWKHcQQKI----RELELEVLKQAQSI-----KSQNSLQEKLAQEKSRVADAEEK-------------ILELQQKLE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1694 ESEFTCAAAVKA--RKAMEVEIEDLhlqIDDIAKAKTAL-EEQLSR--LQREKNEIQ-----NRLEEDQEDMNELMKKHK 1763
Cdd:pfam15742 139 HAHKVCLTDTCIleKKQLEERIKEA---SENEAKLKQQYqEEQQKRklLDQNVNELQqqvrsLQDKEAQLEMTNSQQQLR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1764 aaVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSL----------VSRQEAKIRELETRL 1831
Cdd:pfam15742 216 --IQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALqeELQQVLKQLdvhvrkynekHHHHKAKLRRAKDRL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1832 EFERTQ----VKRLESLASRLKENMEKLTEERDQrIAAENREKEQNKR-LQRQLRDtKEEMG 1888
Cdd:pfam15742 294 VHEVEQrderIKQLENEIGILQQQSEKEKAFQKQ-VTAQNEILLLEKRkLLEQLTE-QEELI 353
|
|
| PDZ5_DrPTPN13-like |
cd23060 |
PDZ domain 5 of Danio rerio tyrosine-protein phosphatase non-receptor type 13 (Ptpn13) and ... |
220-307 |
1.08e-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: 42.34 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 220 ELELQRRPTGDFGFSLRRttmldrGPEGQACRrvVHFAEPGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd23060 1 QIELEKPANGGLGFSLVG------GEGGSGIF--VKSISPG-GVADRDGRLQVGDRLLQVNGESVIGLSHSKAVNILRKA 71
|
....*...
gi 42794779 300 GDSVRLKV 307
Cdd:cd23060 72 KGTVQLTV 79
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1699-1953 |
1.26e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 47.27 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1699 CAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQIND 1778
Cdd:TIGR00618 154 FAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1779 LQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFER------------TQV-KRLESLA 1845
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARkaaplaahikavTQIeQQAQRIH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1846 SRLKENMEKLTEERDQR--IAAENREKEQNKRLQRQLRDTKEEMGELARKEA---EASRKKHELEMDLESLEAANQSLQA 1920
Cdd:TIGR00618 314 TELQSKMRSRAKLLMKRaaHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATsirEISCQQHTLTQHIHTLQQQKTTLTQ 393
|
250 260 270
....*....|....*....|....*....|....*...
gi 42794779 1921 DLKLAFKRIGDL-----QAAIEDEMESDENEDLINSEG 1953
Cdd:TIGR00618 394 KLQSLCKELDILqreqaTIDTRTSAFRDLQGQLAHAKK 431
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1705-1915 |
1.35e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 45.76 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQ-REKNEIQNRLEE-DQEDMNELMKKHKAAVAQASRDLAQIND---- 1778
Cdd:pfam12795 31 KIDASKQRAAAYQKALDDAPAELRELRQELAALQaKAEAAPKEILASlSLEELEQRLLQTSAQLQELQNQLAQLNSqlie 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1779 LQAQLEEANKEKQELQEKLQALQSQvefLEQSMVDKSLVSrqEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEE 1858
Cdd:pfam12795 111 LQTRPERAQQQLSEARQRLQQIRNR---LNGPAPPGEPLS--EAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLKAR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1859 RDQRiaaenreKEQNKRLQRQLRDTKEEMGELARKEAEASRKkhELEMDLESLEAAN 1915
Cdd:pfam12795 186 RDLL-------TLRIQRLEQQLQALQELLNEKRLQEAEQAVA--QTEQLAEEAAGDH 233
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1539-1694 |
1.40e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1539 KVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAKLRLEMEMERMRQTHSKEMESRDEEVEEArqscQKKLKQMEVQLEEE 1618
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEIHKLRNEFEKELRERRNELQKL----EKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1619 YEDKQKVLREKRELEGKLATLSDQVNRRDFESEK---RLRKDLKRTKALLAD--AQLMLDHLKNSApsKREIAQLKNQLE 1693
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEElieEQLQELERISGLTAEeaKEILLEKVEEEA--RHEAAVLIKEIE 179
|
.
gi 42794779 1694 E 1694
Cdd:PRK12704 180 E 180
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1555-1925 |
1.53e-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: 47.05 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1555 EEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEE--ARQSCQKKLKQMEVQLEEEYEDKQKVLREKREL 1632
Cdd:pfam07111 22 ERRLDTQRPTVTMWEQDVSGDGQGPGRRGRSLELEGSQALSQQAEliSRQLQELRRLEEEVRLLRETSLQQKMRLEAQAM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1633 EGKLATLSDQVNRRDFESekrlrkdlkrTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTcAAAVKARKAMEVE 1712
Cdd:pfam07111 102 ELDALAVAEKAGQAEAEG----------LRAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLT-QAHEEALSSLTSK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMN---ELMKKHKAAVAQASRDLAQINDLQAQLEEANKE 1789
Cdd:pfam07111 171 AEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEaqvTLVESLRKYVGEQVPPEVHSQTWELERQELLDT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1790 KQELQEKLQALQSQVEFLE---QSMVdKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEerdQRIAAE 1866
Cdd:pfam07111 251 MQHLQEDRADLQATVELLQvrvQSLT-HMLALQEEELTRKIQPSDSLEPEFPKKCRSLLNRWREKVFALMV---QLKAQD 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1867 NREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1925
Cdd:pfam07111 327 LEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRA 385
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1728-1886 |
1.57e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1728 TALEEQLSRLQREKN----EIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQ 1803
Cdd:pfam09787 43 TALTLELEELRQERDllreEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1804 VEFLEQSMVdKSLVSRQEaKIRELETRLEFERTQV--KRLES-----LASRLKENMEKLTEERDQrIAAENREKE----Q 1872
Cdd:pfam09787 123 LRYLEEELR-RSKATLQS-RIKDREAEIEKLRNQLtsKSQSSssqseLENRLHQLTETLIQKQTM-LEALSTEKNslvlQ 199
|
170
....*....|....
gi 42794779 1873 NKRLQRQLRDTKEE 1886
Cdd:pfam09787 200 LERMEQQIKELQGE 213
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1784-1899 |
1.59e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1784 EEANKEKQELQEKLQALQSQVEFLEqsmvdkslvsrqeAKIRELETRLEFERTQVKRLESLASRLKENMEKltEERDQRi 1863
Cdd:COG2433 402 EHEERELTEEEEEIRRLEEQVERLE-------------AEVEELEAELEEKDERIERLERELSEARSEERR--EIRKDR- 465
|
90 100 110
....*....|....*....|....*....|....*.
gi 42794779 1864 AAENREKEqNKRLQRQLRDTKEEMGELARKEAEASR 1899
Cdd:COG2433 466 EISRLDRE-IERLERELEEERERIEELKRKLERLKE 500
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1682-1900 |
1.94e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 46.22 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIddiakakTALEEQLSRLQREKNEiQNRLEEDQEDMNELMKK 1761
Cdd:PRK11637 67 QQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQI-------DELNASIAKLEQQQAA-QERLLAAQLDAAFRQGE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1762 HKA--------AVAQASRDLA-----------QINDLQAQLEEANKEKQELQEKlqalQSQvefleqsmvDKSLVSRQEA 1822
Cdd:PRK11637 139 HTGlqlilsgeESQRGERILAyfgylnqarqeTIAELKQTREELAAQKAELEEK----QSQ---------QKTLLYEQQA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1823 KIRELE-TRLEFERTqvkrLESLASRLKENMEKLTEERDQRIAAENR----EKEQNKRLQRQLRdtkeEMGELARKEAEA 1897
Cdd:PRK11637 206 QQQKLEqARNERKKT----LTGLESSLQKDQQQLSELRANESRLRDSiaraEREAKARAEREAR----EAARVRDKQKQA 277
|
...
gi 42794779 1898 SRK 1900
Cdd:PRK11637 278 KRK 280
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1258-1583 |
2.02e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 45.68 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1258 NKDEEIQQLRSKLEK-AEKERnELRLNSDRLESRISELTSELTDERN--------TGESASQLLDAETAERLRAEKEMKE 1328
Cdd:pfam00038 1 NEKEQLQELNDRLASyIDKVR-FLEQQNKLLETKISELRQKKGAEPSrlyslyekEIEDLRRQLDTLTVERARLQLELDN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1329 LQTQYDALKKQMEVMEMEVMEARliraAEINGEVDDDDAGGEWRLKYERAVR----EVDFTKKRLQQEfedkleveqqnk 1404
Cdd:pfam00038 80 LRLAAEDFRQKYEDELNLRTSAE----NDLVGLRKDLDEATLARVDLEAKIEslkeELAFLKKNHEEE------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 rqlerrLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRN-HELEKKQRRFDSELSQA----HEEAQREKL 1479
Cdd:pfam00038 144 ------VRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNrEEAEEWYQSKLEELQQAaarnGDALRSAKE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1480 QREKLQREKDMLLAEAFSLKQQLEekdmdiagftqkvvSLEAELQDIssqESKDEASLAKVKKQLRDLEAKVKDQEEELD 1559
Cdd:pfam00038 218 EITELRRTIQSLEIELQSLKKQKA--------------SLERQLAET---EERYELQLADYQELISELEAELQETRQEMA 280
|
330 340
....*....|....*....|....
gi 42794779 1560 EQAGTIQMLEQAKLRLEMEMERMR 1583
Cdd:pfam00038 281 RQLREYQELLNVKLALDIEIATYR 304
|
|
| PDZ2_Par3-like |
cd23058 |
PDZ domain 2 of partitioning defective 3 (Par3), and related domains; PDZ (PSD-95 ... |
260-307 |
2.10e-04 |
|
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: 42.24 E-value: 2.10e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 260 GAGTKDlalG-LVPGDRLVEINGHNVESKSRDEIVEMIRQS--GDSVRLKV 307
Cdd:cd23058 43 GAAIQD---GrLKAGDRLLEVNGVDVTGKTQEEVVSLLRSTklGGTVSLVV 90
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1649-1948 |
2.11e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1649 ESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMeveiedlhlqiddiAKAKT 1728
Cdd:pfam15905 60 ELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSL--------------SASVA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1729 ALEEQLSRLQREKNEIQNRLEED--QEDMN----ELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQS 1802
Cdd:pfam15905 126 SLEKQLLELTRVNELLKAKFSEDgtQKKMSslsmELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1803 QVEFLEQSMVD-KSLVSRQEAKIRELetrlefertqvkrleslaSRLKENMEKLTEERDQriaAENREKEQNKRLQRQLR 1881
Cdd:pfam15905 206 KLVSTEKEKIEeKSETEKLLEYITEL------------------SCVSEQVEKYKLDIAQ---LEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1882 DTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKlafKRIGDLQAAIedEMESDENEDL 1948
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLN---AELEELKEKL--TLEEQEHQKL 326
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1247-1566 |
2.15e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEM 1326
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1327 KELQTQYDALKKQMevmemevmearliraaeingevddddaggewrlkyeravrevdftkKRLQQEFEDKleveQQNKRQ 1406
Cdd:COG4372 104 ESLQEEAEELQEEL----------------------------------------------EELQKERQDL----EQQRKQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1407 LERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlegQQVRNHELEKKQRRFDSELSQAHEEAQREKLQREKLQR 1486
Cdd:COG4372 134 LEAQIAELQSEIAEREEELKELEEQLESLQEELAALE-----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1487 EKDMLLAEAfslKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ 1566
Cdd:COG4372 209 IESLPRELA---EELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALEL 285
|
|
| PDZ3_DLG5-like |
cd06767 |
PDZ domain 3 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
2.19e-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: 41.54 E-value: 2.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06767 42 GLEYGDQLLEVNGINLRNATEQQAALILRQCGDTITMLVQ 81
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1709-1947 |
2.24e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1709 MEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKkhkaaVAQASRDLAQIND---LQAQLEE 1785
Cdd:PRK05771 77 KKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEP-----WGNFDLDLSLLLGfkyVSVFVGT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1786 ANKEKQElQEKLQALQSQVEFLEQSMVDKSLV----SRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEerdq 1861
Cdd:PRK05771 152 VPEDKLE-ELKLESDVENVEYISTDKGYVYVVvvvlKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEE---- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1862 riaaenrekeqnkrLQRQLRDTKEEMGELARKEAEASRKKHE-LEMDLESLEAANQSLQADLKLAF------KRIGDLQA 1934
Cdd:PRK05771 227 --------------IEKERESLLEELKELAKKYLEELLALYEyLEIELERAEALSKFLKTDKTFAIegwvpeDRVKKLKE 292
|
250 260
....*....|....*....|..
gi 42794779 1935 AIED---------EMESDENED 1947
Cdd:PRK05771 293 LIDKatggsayveFVEPDEEEE 314
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1254-1617 |
2.70e-04 |
|
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: 45.79 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTG-----ESASQLLDAETAERLRAEKEMKE 1328
Cdd:pfam05701 70 EELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQGIADEASVAakaqlEVAKARHAAAVAELKSVKEELES 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1329 LQTQYDALKKQMEVMEMEVMEArLIRAAEINGEVDDddaggewrlkyerAVREVDFTKKRLQQEFEDKLEVE-------- 1400
Cdd:pfam05701 150 LRKEYASLVSERDIAIKRAEEA-VSASKEIEKTVEE-------------LTIELIATKESLESAHAAHLEAEehrigaal 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1401 --QQNKRQLERRLGDLQadsEESQRALQQ------LKKKCQRLTAELQDTKLHL----EGQQVRNHELEKKQRRFDSELS 1468
Cdd:pfam05701 216 arEQDKLNWEKELKQAE---EELQRLNQQllsakdLKSKLETASALLLDLKAELaaymESKLKEEADGEGNEKKTSTSIQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1469 QAHEEAQRE----KLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQK-------VVSLEAELQDISSQeskdeasL 1537
Cdd:pfam05701 293 AALASAKKEleevKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQRegmasiaVSSLEAELNRTKSE-------I 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1538 AKVKKQLRDLEAKVKDQEEELDEQAgtiQMLEQAKLRLEMEMERMRQTHskemesrdEEVEEARQSCQkklkQMEVQLEE 1617
Cdd:pfam05701 366 ALVQAKEKEAREKMVELPKQLQQAA---QEAEEAKSLAQAAREELRKAK--------EEAEQAKAAAS----TVESRLEA 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1244-1338 |
2.72e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1244 RPLIEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgesasqlldAETAERLRAE 1323
Cdd:COG2433 396 EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEAR-----------SEERREIRKD 464
|
90
....*....|....*
gi 42794779 1324 KEMKELQTQYDALKK 1338
Cdd:COG2433 465 REISRLDREIERLER 479
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1820-1928 |
2.83e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1820 QEAKIRELETRLEFERTQVKRLESLASRLKENMEklteERDQRIAaenREKEQNKRLQRQLRDTKEEMGELARKEAEASR 1899
Cdd:COG2433 404 EERELTEEEEEIRRLEEQVERLEAEVEELEAELE----EKDERIE---RLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|..
gi 42794779 1900 KKHELE---MDLESLEAANQSLQADLKLAFKR 1928
Cdd:COG2433 477 LERELEeerERIEELKRKLERLKELWKLEHSG 508
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1765-1898 |
2.85e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1765 AVAQASRDLAQINDLQAQLEEANKEKQ-ELQEKL--QALQSQVEFLEQsmvdkslVSRQEAKIRELEtrlefertqvKRL 1841
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALNKQKLlEAEDKLvqQDLEQTLALLDK-------IDRQKEETEQLK----------QQL 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1842 ESLASRLKENMEKLT--EERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEAS 1898
Cdd:PRK11281 90 AQAPAKLRQAQAELEalKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYN 148
|
|
| PDZ_syntrophin-like |
cd06801 |
PDZ domain of syntrophins, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), ... |
270-308 |
2.97e-04 |
|
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: 41.41 E-value: 2.97e-04
10 20 30
....*....|....*....|....*....|....*....
gi 42794779 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06801 44 LFVGDAILSVNGENLEDATHDEAVQALKNAGDEVTLTVK 82
|
|
| PDZ_rhophilin-like |
cd06712 |
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
219-307 |
3.22e-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: 41.03 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRpTGDFGFSLRrttmldrgpeGQACRRVvHFAEPGaGTKDLAlGLVPGDRLVEINGHNVESKSRDEIVEMIRQ 298
Cdd:cd06712 2 RTVHLTKE-EGGFGFTLR----------GDSPVQV-ASVDPG-SCAAEA-GLKEGDYIVSVGGVDCKWSKHSEVVKLLKS 67
|
90
....*....|
gi 42794779 299 SG-DSVRLKV 307
Cdd:cd06712 68 AGeEGLELQV 77
|
|
| PDZ1_L-delphilin-like |
cd06743 |
PDZ domain 1 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ... |
269-299 |
3.39e-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: 41.11 E-value: 3.39e-04
10 20 30
....*....|....*....|....*....|.
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQS 299
Cdd:cd06743 36 GLQPGDQILELDGQDVSSLSCEAIIALARRC 66
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1425-1653 |
3.47e-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: 45.90 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1425 LQQLKKKCQRLTAELQdTKLHLEGQQV-RNHELEKKQRRFDSELSQAHEeaqreklqrEKLQREKDMLLaeafSLKQQLE 1503
Cdd:pfam07111 483 LEQLREERNRLDAELQ-LSAHLIQQEVgRAREQGEAERQQLSEVAQQLE---------QELQRAQESLA----SVGQQLE 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1504 EKDMDIAGFTQKVVSLEAEL---QDISSQESKDEasLAKVKKQLRDLEAKVKDQ-EEELDEQAGTIQMLEQAKLRLEMEM 1579
Cdd:pfam07111 549 VARQGQQESTEEAASLRQELtqqQEIYGQALQEK--VAEVETRLREQLSDTKRRlNEARREQAKAVVSLRQIQHRATQEK 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1580 ERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEyedKQKVLREKRELEGKLATLSDQVNRRDFESEKR 1653
Cdd:pfam07111 627 ERNQELRRLQDEARKEEGQRLARRVQELERDKNLMLATL---QQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPR 697
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1730-1977 |
3.51e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.50 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1730 LEEQLSRLQREKNeiQNRLEEDQEdMNELMKKHKAAVAQASRDLAQINDLQAQLEeaNKEKQElQEKLQALQSQVEFLEQ 1809
Cdd:pfam05557 7 SKARLSQLQNEKK--QMELEHKRA-RIELEKKASALKRQLDRESDRNQELQKRIR--LLEKRE-AEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1810 SMVDKSLVSRqeaKIRELETRLEFERTQVKRLESLASRLKENMEKlteeRDQRIAAENREKEqnkRLQRQLRdtkeemgE 1889
Cdd:pfam05557 81 KKKYLEALNK---KLNEKESQLADAREVISCLKNELSELRRQIQR----AELELQSTNSELE---ELQERLD-------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1890 LARKEAEASRKKHELEMDLESLEAANQ---------SLQADLKLAFKRIGDLQAAIEdEMES------DENEDLINSEGD 1954
Cdd:pfam05557 144 LKAKASEAEQLRQNLEKQQSSLAEAEQrikelefeiQSQEQDSEIVKNSKSELARIP-ELEKelerlrEHNKHLNENIEN 222
|
250 260
....*....|....*....|...
gi 42794779 1955 SDVdseLEDRVDGVKSWLSKNKG 1977
Cdd:pfam05557 223 KLL---LKEEVEDLKRKLEREEK 242
|
|
| PDZ_MPP3-MPP4-MPP7-like |
cd06799 |
PDZ domain of membrane palmitoylated proteins 3 (MPP3), MPP4, and MPP7, and related domains; ... |
269-309 |
3.54e-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: 41.07 E-value: 3.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 42794779 269 GLV-PGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06799 40 GLIhVGDELREVNGISVEGKDPEEVIQILANSQGPITFKLIP 81
|
|
| Phage_HK97_TLTM |
pfam06120 |
Tail length tape measure protein; This family consists of the tail length tape measure protein ... |
1687-1902 |
3.69e-04 |
|
Tail length tape measure protein; This family consists of the tail length tape measure protein from bacteriophage HK97 and related sequences from Escherichia coli O157:H7.
Pssm-ID: 428779 [Multi-domain] Cd Length: 295 Bit Score: 44.84 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1687 QLKNQLEESEFTCAAAVKARKAmEVEIEDLHLQIDDIAKAKTALEEQ--LSRLQREKNE--------IQNRLEEDQEDMN 1756
Cdd:pfam06120 41 QKQEQARQSALEYAATIDQVRA-NLNKMTLPETADNSGKTKESLAAQnkLVDEQRQKVEglksaiagYQQMLASPGPSIN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1757 ELMKKHKAAVAQASRDLAQINDL----QAQLEEANKEKQELQEKLQALQSQVEFL--EQSMVDKSLvsRQEAKIRELETR 1830
Cdd:pfam06120 120 GYLINHLISQEDAVKSLAAAQDElsveQSRLNELSKKSEEIQSALKAVESQRDFLirQQSAAQNNM--RHSLLMVNAEHS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1831 lEFERTQ-------VKRLESLASRLKENMEKLTEERDQRIAAENREKEQN-----KRLQRQLRDTKEEMGELARKEAEAS 1898
Cdd:pfam06120 198 -EFNRIMsagnqilTNRLALVNSPMRIPAAPLSEKQQDFIQKSERDKELSaltgeARVIRQAEFAADDIGLLNKPEFADN 276
|
....
gi 42794779 1899 RKKH 1902
Cdd:pfam06120 277 RQKY 280
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
1730-1910 |
4.04e-04 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 44.82 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1730 LEEQLSRLQREKNEIQNRLEEDQE-DMNELMKKHKaavaqasRDLAQINDLQAQLEEANKEKQELQEKL-QALQSQVEFL 1807
Cdd:pfam09755 112 LSRKLTQLRQEKVELEQTLEQEQEyQVNKLMRKIE-------KLEAETLNKQTNLEQLRREKVELENTLeQEQEALVNRL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1808 EQSMvdkslvSRQEAKIRELETRLEFERT--------------------QVKRLESLASRLKENMEKLTEERDQRIAA-- 1865
Cdd:pfam09755 185 WKRM------DKLEAEKRLLQEKLDQPVSappsprdstsegdtaqnltaHIQYLRKEVERLRRQLATAQQEHTEKMAQya 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 42794779 1866 --ENREKEQNKRLQRQLRDTKEEMGELARKEAEAsrkKHELEMDLES 1910
Cdd:pfam09755 259 qeERHIREENLRLQRKLQLEMERREALCRHLSES---ESSLEMDEER 302
|
|
| PDZ1_PTPN13-like |
cd23072 |
PDZ domain 1 of protein tyrosine phosphatase non-receptor type 13 (PTPN13), and related ... |
259-309 |
4.04e-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: 41.32 E-value: 4.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 259 PGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV-QP 309
Cdd:cd23072 39 PG-GPADLDGRLKPGDRLISVNDVSLEGLSHDAAVEILQNAPEDVTLVVsQP 89
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1784-1906 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1784 EEANKEKQELQEKLQALQSQVEFLEQSMvdkslvSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKL------TE 1857
Cdd:pfam20492 2 EEAEREKQELEERLKQYEEETKKAQEEL------EESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLeesaemEA 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 42794779 1858 ERDQRIAAENREKEQNKRLQRQlrdtkeemgELARKEAEASRKKHELEM 1906
Cdd:pfam20492 76 EEKEQLEAELAEAQEEIARLEE---------EVERKEEEARRLQEELEE 115
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1520-1924 |
4.17e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.10 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1520 EAELQDISSQESKDEASLAKVKKQLR----DLEAKVKD----QEEELDEQAGTIQMLEQAKLRLEMEMERMRQthskEME 1591
Cdd:pfam03528 3 DEDLQQRVAELEKENAEFYRLKQQLEaefnQKRAKFKElylaKEEDLKRQNAVLQEAQVELDALQNQLALARA----EME 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1592 SRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREkrelegklatlsdqvNRRDFESEKRLRKDLKRTKalladaqlm 1671
Cdd:pfam03528 79 NIKAVATVSENTKQEAIDEVKSQWQEEVASLQAIMKE---------------TVREYEVQFHRRLEQERAQ--------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1672 LDHLKNSApsKREIAQLKNQLEESEFTCAAAVKARKAMEvEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQnrlEED 1751
Cdd:pfam03528 135 WNQYRESA--EREIADLRRRLSEGQEEENLEDEMKKAQE-DAEKLRSVVMPMEKEIAALKAKLTEAEDKIKELE---ASK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1752 QEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE-ANKEKQELQEKLQALQsqvefLEQSMVDKSLVSRQEAKIRELETR 1830
Cdd:pfam03528 209 MKELNHYLEAEKSCRTDLEMYVAVLNTQKSVLQEdAEKLRKELHEVCHLLE-----QERQQHNQLKHTWQKANDQFLESQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1831 LEFERtQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLES 1910
Cdd:pfam03528 284 RLLMR-DMQRMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINS 362
|
410
....*....|....
gi 42794779 1911 LEAANQSLQADLKL 1924
Cdd:pfam03528 363 AHGSVHSLDTDVVL 376
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1509-1753 |
4.19e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1509 IAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQaklrlememermrqthsk 1588
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1589 EMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKVLREKRELEGKlaTLSDQVNRRDF-----ESEKRLRKDLKRTKA 1663
Cdd:COG3883 66 EIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDVLLGSE--SFSDFLDRLSAlskiaDADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1664 LLADAQLMLDHLKNsapskrEIAQLKNQLEEseftcaaavkARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNE 1743
Cdd:COG3883 144 ELEAKKAELEAKLA------ELEALKAELEA----------AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250
....*....|
gi 42794779 1744 IQNRLEEDQE 1753
Cdd:COG3883 208 AEAAAAAAAA 217
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1386-1633 |
4.27e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 4.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1386 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEES--QRALQQLKKKCQRLTAELQDTKLHLEGQQVRnHELEKKQRRF 1463
Cdd:pfam13868 50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEReqKRQEEYEEKLQEREQMDEIVERIQEEDQAEA-EEKLEKQRQL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1464 DSELSQAHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMdiagftqkvvsleaelqdisSQESKDEASLAKVKKQ 1543
Cdd:pfam13868 129 REEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE--------------------AEREEIEEEKEREIAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELDEQagtiqmleQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK----KLKQMEVQLEEEY 1619
Cdd:pfam13868 189 LRAQQEKAQDEKAERDEL--------RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEqielKERRLAEEAEREE 260
|
250
....*....|....
gi 42794779 1620 EDKQKVLREKRELE 1633
Cdd:pfam13868 261 EEFERMLRKQAEDE 274
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1733-1922 |
4.40e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1733 QLSRLQREKNEIQNRLEEDQEDMNEL---MKKHKAAVAQASRdlaQINDLQAQLEEANKEKQELQEKLQALQSQvefleQ 1809
Cdd:PRK11637 48 QLKSIQQDIAAKEKSVRQQQQQRASLlaqLKKQEEAISQASR---KLRETQNTLNQLNKQIDELNASIAKLEQQ-----Q 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1810 SMVDKSLVSRQEAKIRE-----LETRLEFERTQVK-RLESLASRL----KENMEKLTEERDQrIAAENREKEQNKRLQRQ 1879
Cdd:PRK11637 120 AAQERLLAAQLDAAFRQgehtgLQLILSGEESQRGeRILAYFGYLnqarQETIAELKQTREE-LAAQKAELEEKQSQQKT 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 42794779 1880 LRDTKEEMgELARKEAEASRKKhelemDLESLEAANQSLQADL 1922
Cdd:PRK11637 199 LLYEQQAQ-QQKLEQARNERKK-----TLTGLESSLQKDQQQL 235
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1738-1917 |
4.42e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 45.33 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1738 QREKNEIQNRLEEDQEDMNELMKKHkaaVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEfleqsmvdkslv 1817
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREE---LELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAA------------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1818 sRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENR--EKEQNKRLQRQLRdtKEEMGELARKEA 1895
Cdd:pfam15709 418 -QERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRlmEMAEEERLEYQRQ--KQEAEEKARLEA 494
|
170 180
....*....|....*....|..
gi 42794779 1896 EASRKKHELEMDLESLEAANQS 1917
Cdd:pfam15709 495 EERRQKEEEAARLALEEAMKQA 516
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1248-1564 |
4.63e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 45.33 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRL----NSDRLESRISELTSELTDE-RNTGEsasQLLDAETAERLRA 1322
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLeklgENAESSKRLNENANNLIKQfENTKE---KIAEYTKSIDIKK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1323 EKEMKELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGE-WRLKYERAVREVDF----------------T 1385
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEaIKEEIENIVGEVELsksseeldsfkdtiesT 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1386 KKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKcqrlTAELQDTKLHLEgqqvrnHELEKKQRRFDS 1465
Cdd:COG5185 390 KESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSS----NEEVSKLLNELI------SELNKVMREADE 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEAQREKLQR-----EKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLE---AELQDISSQESKDEASL 1537
Cdd:COG5185 460 ESQSRLEEAYDEINRSvrskkEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLdqvAESLKDFMRARGYAHIL 539
|
330 340
....*....|....*....|....*..
gi 42794779 1538 AKVKKQlRDLEAKvKDQEEELDEQAGT 1564
Cdd:COG5185 540 ALENLI-PASELI-QASNAKTDGQAAN 564
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1260-1439 |
5.11e-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: 43.76 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1260 DEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQT--QYDALK 1337
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1338 KQmevmemEVMEARLIRAAeingevddddaggewrlkyERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQAD 1417
Cdd:COG1579 96 KE------IESLKRRISDL-------------------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|..
gi 42794779 1418 SEESQRALQQLKKKCQRLTAEL 1439
Cdd:COG1579 151 LAELEAELEELEAEREELAAKI 172
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1645-1941 |
5.13e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1645 RRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVE-----IEDLHLQ 1719
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEerkryRQELEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1720 IDDIAKAKtalEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQE-KLQ 1798
Cdd:pfam13868 82 IEEREQKR---QEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1799 ALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAENREKEQNKRLQR 1878
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQ 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1879 QLRDtKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEME 1941
Cdd:pfam13868 239 QARE-EQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1576-1902 |
5.18e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.86 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1576 EMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQMEVQLEEEyeDKQKVLREKRELEGKLAtLSDQVNRRDFESEKRLR 1655
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEE--DSELKPSGQGGLDEEEA-FLDRTAKREERRQKRLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1656 KDLKRTKALLADAqlmldhlknsAPSKREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLS 1735
Cdd:pfam02029 81 EALERQKEFDPTI----------ADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1736 RLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEA---NKEKQELQEKLQALQSQVEFLEQSMV 1812
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEVTKLKVTTKRRQGGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1813 DKSLVSRQEAKIR-ELETRLE-------------FERTQVKR------LESLASRLKENMEKLTEERDQRiaaENREKEQ 1872
Cdd:pfam02029 231 SQSQEREEEAEVFlEAEQKLEelrrrrqekeseeFEKLRQKQqeaeleLEELKKKREERRKLLEEEEQRR---KQEEAER 307
|
330 340 350
....*....|....*....|....*....|
gi 42794779 1873 NKRLQRQLRDTKEEMgELARKEAEASRKKH 1902
Cdd:pfam02029 308 KLREEEEKRRMKEEI-ERRRAEAAEKRQKL 336
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1760-1903 |
5.57e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1760 KKHKAAVAQASRDLAQIndlqaqLEEANKEKQELQeKLQALQSQVEFLE-QSMVDKSLVSRqEAKIRELETRLEFERTQV 1838
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI------LEEAKKEAEAIK-KEALLEAKEEIHKlRNEFEKELRER-RNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1839 -KRLESLASR------LKENMEKLTEERDQRIA-AENREKEQNKRLQRQLRDTKEEMGELARKEAEaSRKKHE 1903
Cdd:PRK12704 99 dRKLELLEKReeelekKEKELEQKQQELEKKEEeLEELIEEQLQELERISGLTAEEAKEILLEKVE-EEARHE 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1404-1621 |
5.66e-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: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1404 KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTK-----LHLEGQQvrnHELEKKQRRFDSELSQAHEEAQREK 1478
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRqknglVDLSEEA---KLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1479 LQREKLQREKDMLLAEAFSLKQqleekDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQ---- 1554
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEaqri 314
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1555 ----EEELDEQAGTIQMLEQAKLRLEMEMERMRQThSKEMESRDEEVEEARQ---SCQKKLKQMEVQLEEEYED 1621
Cdd:COG3206 315 laslEAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRLEREVEVARElyeSLLQRLEEARLAEALTVGN 387
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1456-1668 |
6.00e-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: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1456 LEKKQRRFDSELSQAheEAQREKLQREK----LQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQ--DISSQ 1529
Cdd:COG3206 180 LEEQLPELRKELEEA--EAALEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGsgPDALP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1530 ESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLK 1609
Cdd:COG3206 258 ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLA 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 42794779 1610 QMEVQLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfesEKRLRKDLKRTKALLADA 1668
Cdd:COG3206 338 QLEARLAELPELEAELRRLEREVEVARELYESLLQRLE---EARLAEALTVGNVRVIDP 393
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1775-1949 |
6.03e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.48 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1775 QINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSmvdkslvsrqeakIRELETrlEFERTQvKRLESLASRLKEnMEK 1854
Cdd:pfam00261 9 ELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRR-------------IQLLEE--ELERTE-ERLAEALEKLEE-AEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1855 LTEERDQ-RIAAENREKEQNKR---LQRQLRDTKEEMGELARKEAEASRKKHELEMDLE-------SLEAANQSLQADLK 1923
Cdd:pfam00261 72 AADESERgRKVLENRALKDEEKmeiLEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLEraeeraeLAESKIVELEEELK 151
|
170 180
....*....|....*....|....*..
gi 42794779 1924 LAFKRIGDLQAAIEDEMES-DENEDLI 1949
Cdd:pfam00261 152 VVGNNLKSLEASEEKASEReDKYEEQI 178
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1535-1862 |
6.27e-04 |
|
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: 44.30 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1535 ASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQMLEQAklrLEMEMERMRQtHSKEMESRDEEVEEARQSCQKKLKQMEVQ 1614
Cdd:pfam04108 3 SSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRG---LSVQLANLEK-VREGLEKVLNELKKDFKQLLKDLDAALER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1615 LEEEYE--DKQKVLREKRELEGKLATLSDQVNRRDFES---------------EKRLRKDLKRTKALLADAQLMLDHLKN 1677
Cdd:pfam04108 79 LEETLDklRNTPVEPALPPGEEKQKTLLDFIDEDSVEIlrdalkelidelqaaQESLDSDLKRFDDDLRDLQKELESLSS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1678 SAPSKREIAQLKNQLEESEftcaaavkarKAMEVEIEDLHLQIDDIAKAKTALE--------------EQLSRLQREKNE 1743
Cdd:pfam04108 159 PSESISLIPTLLKELESLE----------EEMASLLESLTNHYDQCVTAVKLTEggraemlevlendaRELDDVVPELQD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1744 IQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQL-----------EEANKEKQELQEKLQALQSQVEFLEQ--S 1810
Cdd:pfam04108 229 RLDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLpeylaalkefeERWEEEKETIEDYLSELEDLREFYEGfpS 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1811 MVDKSLVsrqeakirELETRLEFErtqvKRLESLASRLKENMEKLTEERDQR 1862
Cdd:pfam04108 309 AYGSLLL--------EVERRREWA----EKMKKILRKLAEELDRLQEEERKR 348
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1741-1923 |
6.45e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1741 KNEIQNRLEE--DQEDMNELMKKHKAAVAQASRDLAQI-------NDLQAQLEEANKEKQELQEKLQALQSQveflEQSM 1811
Cdd:PRK11281 38 EADVQAQLDAlnKQKLLEAEDKLVQQDLEQTLALLDKIdrqkeetEQLKQQLAQAPAKLRQAQAELEALKDD----NDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1812 VDKSLVSRQeakIRELETRLEfertqvKRLESLASRLKEnmekLTEERDQRIAAENR-EKEQN------KRLQ---RQLR 1881
Cdd:PRK11281 114 TRETLSTLS---LRQLESRLA------QTLDQLQNAQND----LAEYNSQLVSLQTQpERAQAalyansQRLQqirNLLK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 42794779 1882 DTKEEmgelaRKEAEASRKKhELEMDLESLEAANQSLQADLK 1923
Cdd:PRK11281 181 GGKVG-----GKALRPSQRV-LLQAEQALLNAQNDLQRKSLE 216
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1614-1920 |
6.63e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.96 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLE 1693
Cdd:TIGR00618 180 QLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1694 ESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKnEIQNRLEEDQEDMNELMKKhkaavaqasrdL 1773
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRIHTELQSKMRSRAKL-----------L 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1774 AQINDLQAQleeaNKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLASRLKENME 1853
Cdd:TIGR00618 328 MKRAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELD 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1854 KLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQA 1920
Cdd:TIGR00618 404 ILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
|
| PDZ5_MUPP1-like |
cd06669 |
PDZ domain 5 of multi-PDZ-domain protein 1 (MUPP1), PATJ (protein-associated tight junction) ... |
269-311 |
6.73e-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: 40.67 E-value: 6.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSG-DSVRLKV-QPIP 311
Cdd:cd06669 54 RLLPGDRLVFVNDVSLENASLDEAVQALKSAPpGTVRIGVaKPLP 98
|
|
| PDZ_SYNPO2-like |
cd10820 |
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ... |
269-308 |
7.29e-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: 39.98 E-value: 7.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd10820 39 GLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQLLIK 78
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1252-1470 |
7.55e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1252 SEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDerntgesasqlldaetaerlrAEKEMKELQT 1331
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA---------------------LQAEIDKLQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1332 QYDALKKQmeVMEMEVMEARLIRAAEINGEVDDDDA---GGE------WRLKYERAVREVDFTKKRLQQEFEDKLEVEQQ 1402
Cdd:COG3883 73 EIAEAEAE--IEERREELGERARALYRSGGSVSYLDvllGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 1403 NKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQA 1470
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAA 218
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1312-1578 |
7.90e-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: 44.29 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1312 LDAETAERLRAEKEMKELQTQYDALKK----------------------QMEVMEMEVMEARLIRAAEINGEVDDDDAGG 1369
Cdd:pfam05622 199 LSEESKKADKLEFEYKKLEEKLEALQKekerliierdtlretneelrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1370 EWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQ 1449
Cdd:pfam05622 279 EIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDS 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1450 QVRNHELEKKQRrfdsELSQAHEEAQREKLQREKLQREKDMLLAE-AFSLKQQLEEKDMDIAGFTQK-----------VV 1517
Cdd:pfam05622 359 SLLKQKLEEHLE----KLHEAQSELQKKKEQIEELEPKQDSNLAQkIDELQEALRKKDEDMKAMEERykkyvekaksvIK 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1518 SLEAELQDISSQEskdeasLAKVKKQLRDLEAKVKDQEEEldeqagtiqmLEQAKLRLEME 1578
Cdd:pfam05622 435 TLDPKQNPASPPE------IQALKNQLLEKDKKIEHLERD----------FEKSKLQREQE 479
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1683-1912 |
8.66e-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: 43.09 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1683 REIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKH 1762
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1763 KAAVAQASRDLAQINDLQAQL-------EEANKEKQELQEKLQALQSQVEFLEQSmvdkslVSRQEAKIRELETRLEFER 1835
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLkeakeiaEEADRKYEEVARKLVVVEGDLERAEER------AELAESKIVELEEELKVVG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42794779 1836 TQVKRLESLAsrlkenmekltEERDQRiaaENREKEQNKRLQRQLRDTKeemgelARKEaEASRKKHELEMDLESLE 1912
Cdd:pfam00261 155 NNLKSLEASE-----------EKASER---EDKYEEQIRFLTEKLKEAE------TRAE-FAERSVQKLEKEVDRLE 210
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1260-1494 |
9.37e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1260 DEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERL----------RAEKEMKE- 1328
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerfaaalgdAVERELREn 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1329 LQTQYDALKKQMEVMEMevmeaRLIRA---------AEINGEVDDDDAGGEWRLKYERaVREVDFtkKRLQQEFEDKLev 1399
Cdd:COG4913 771 LEERIDALRARLNRAEE-----ELERAmrafnrewpAETADLDADLESLPEYLALLDR-LEEDGL--PEYEERFKELL-- 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1400 eqqnKRQLERRLGDLQAD-SEESQRALQQLKkkcqRLTAELQ------DTKLHLEGQQVRNHELEKKQRRFD--SELSQA 1470
Cdd:COG4913 841 ----NENSIEFVADLLSKlRRAIREIKERID----PLNDSLKripfgpGRYLRLEARPRPDPEVREFRQELRavTSGASL 912
|
250 260
....*....|....*....|....
gi 42794779 1471 HEEAQREKlQREKLQREKDMLLAE 1494
Cdd:COG4913 913 FDEELSEA-RFAALKRLIERLRSE 935
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1689-1866 |
9.96e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1689 KNQLEESEFTCAAAVK-ARKAMEVEIEDLHLQI-DDIAKAKTALEEQLsrlqREKNEIQNRLEEDQEDMNELMKKHKAAV 1766
Cdd:PRK12704 30 EAKIKEAEEEAKRILEeAKKEAEAIKKEALLEAkEEIHKLRNEFEKEL----RERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1767 AQASRDLAQINDLQAQLEEANKEKQELQEKLQalQSQVEFLEQSMvdkSLvSRQEAK---IRELETRLEFERtqvkrles 1843
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELI--EEQLQELERIS---GL-TAEEAKeilLEKVEEEARHEA-------- 171
|
170 180 190
....*....|....*....|....*....|....
gi 42794779 1844 lASRLKENMEKLTEERD-----------QRIAAE 1866
Cdd:PRK12704 172 -AVLIKEIEEEAKEEADkkakeilaqaiQRCAAD 204
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1405-1584 |
1.04e-03 |
|
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: 43.21 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDtklhLEGQqvrnHELEKKQRRfdSELSQAHEEAQREKLQREKL 1484
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE----LEAQ----QQEEAESSR--EQLQELEEQLATERSARREA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1485 QREKDMLLAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQ-ESKDEASLAKvkkqlRDLEAKVKDQEEELDEQAG 1563
Cdd:pfam09787 113 EAELERLQEELRYLEEELRRSKATLQS---RIKDREAEIEKLRNQlTSKSQSSSSQ-----SELENRLHQLTETLIQKQT 184
|
170 180
....*....|....*....|.
gi 42794779 1564 TIQMLEQAKLRLEMEMERMRQ 1584
Cdd:pfam09787 185 MLEALSTEKNSLVLQLERMEQ 205
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
1725-1850 |
1.28e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 41.13 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1725 KAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQV 1804
Cdd:pfam10473 3 KKQLHVLEKLKESERKADSLKDKVENLERELEMSEENQELAILEAENSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEK 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42794779 1805 EFLEQSMVDKslvsrqEAKIRELETRLEFERTQVKRLESLASRLKE 1850
Cdd:pfam10473 83 ENLTKELQKK------QERVSELESLNSSLENLLEEKEQEKVQMKE 122
|
|
| PDZ2_MUPP1-like |
cd06667 |
PDZ domain 2 of multi-PDZ-domain protein 1 (MUPP1) and PATJ (protein-associated tight junction) ... |
259-307 |
1.34e-03 |
|
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: 39.57 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 42794779 259 PGaGTKDLALGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKV 307
Cdd:cd06667 31 PG-GVADRDGRLRSGDHILQIGDTNLRGMGSEQVAQVLRQCGSHVRLVV 78
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1682-1803 |
1.39e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAK----TALEEQLSRLQREKNEIQNRLEEDQEDMNE 1757
Cdd:smart00787 157 KEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDptelDRAKEKLKKLLQEIMIKVKKLEELEEELQE 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 42794779 1758 LMKKHKAAVAQASRDLAQINDLQAQLEEAN----KEKQELQEKLQALQSQ 1803
Cdd:smart00787 237 LESKIEDLTNKKSELNTEIAEAEKKLEQCRgftfKEIEKLKEQLKLLQSL 286
|
|
| 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 |
1.50e-03 |
|
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: 39.56 E-value: 1.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 258 EPGAGTKDLALGLvpGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06724 37 EGGAAQKDGRLQV--GDKLLAVNDVSLEEVTHEEAVAALKNTSDVVYLKVA 85
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1391-1526 |
1.53e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1391 QEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQdtklhlEGQQVrnheLEKKQRRFDSELSQA 1470
Cdd:pfam02841 179 QEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQK------EEEQM----MEAQERSYQEHVKQL 248
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1471 HEEAQREklqREKLQREKDMLLAeafslKQQLEEKDMDIAGFTQKVVSLEAELQDI 1526
Cdd:pfam02841 249 IEKMEAE---REQLLAEQERMLE-----HKLQEQEELLKEGFKTEAESLQKEIQDL 296
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1254-1871 |
1.80e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1254 EQIRNKDEEIQQLRSKLEKAEKER------NELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAeRLRAEKEMK 1327
Cdd:PTZ00440 1190 EEIESYKKDIDQVKKNMSKERNDHlttfeyNAYYDKATASYENIEELTTEAKGLKGEANRSTNVDELKEI-KLQVFSYLQ 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALKKQMEVMEMEVMEARLIRAAEINGEVDDDDAGGEwrlKYER-AVREVDFTKkRLQQEFEDKLEVEQQNKRQ 1406
Cdd:PTZ00440 1269 QVIKENNKMENALHEIKNMYEFLISIDSEKILKEILNSTKKAE---EFSNdAKKELEKTD-NLIKQVEAKIEQAKEHKNK 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1407 LERRLGDLQADSEesqraLQQLKKKCQRLTAELQDTKLHLEgqqvrnhELEKKQRRFDSELSQAH------------EEA 1474
Cdd:PTZ00440 1345 IYGSLEDKQIDDE-----IKKIEQIKEEISNKRKEINKYLS-------NIKSNKEKCDLHVRNASrgkdkidflnkhEAI 1412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1475 QREKLQREKLQREKDML------LAEAFSLKQQLEEKDMDIAGFTQKVVSLeaeLQD--ISSQESKDEaslaKVKKQLRD 1546
Cdd:PTZ00440 1413 EPSNSKEVNIIKITDNInkckqySNEAMETENKADENNDSIIKYEKEITNI---LNNssILGKKTKLE----KKKKEATN 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1547 LEAKVKDQEEELDEQAGTIQmleqaklrlememERMRQTHSKEMESRDEEV------EEARQSCQKKLKQMEVQLEEEYE 1620
Cdd:PTZ00440 1486 IMDDINGEHSIIKTKLTKSS-------------EKLNQLNEQPNIKREGDVlnndksTIAYETIQYNLGRVKHNLLNILN 1552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1621 DKQK---VLREKRELEGKLATLSDQVNRRDFES-EKRLRKDLKRTKALLADAQLMLDHLKNSAPSKREIAQLKNQLEES- 1695
Cdd:PTZ00440 1553 IKDEietILNKAQDLMRDISKISKIVENKNLENlNDKEADYVKYLDNILKEKQLMEAEYKKLNEIYSDVDNIEKELKKHk 1632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1696 --------EFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTAL-------EEQLSRLQREKNEIQNRLEEDQEDMNELMK 1760
Cdd:PTZ00440 1633 knyeigllEKVIEINKNIKLYMDSTKESLNSLVNNFSSLFNNFylnkyniNENLEKYKKKLNEIYNEFMESYNIIQEKMK 1712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1761 KhkaavaqASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQsMVDKSLVSRQEAKIRELETRLEFERTQVKR 1840
Cdd:PTZ00440 1713 E-------VSNDDVDYNEAKTLREEAQKEEVNLNNKEEEAKKYLNDIKK-QESFRFILYMKEKLDELSKMCKQQYNIVDE 1784
|
650 660 670
....*....|....*....|....*....|....
gi 42794779 1841 LESLASRLKENMEKLTEER---DQRIAAENREKE 1871
Cdd:PTZ00440 1785 GYNYIKKKIEYIKTLNDENnlsDSLNQAEDKNKE 1818
|
|
| PDZ4_DLG5-like |
cd06766 |
PDZ domain 4 of Discs Large 5 (Dlg5) and related domains; PDZ (PSD-95 (Postsynaptic density ... |
254-308 |
2.08e-03 |
|
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: 38.91 E-value: 2.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 254 VHFAEPGAGTKDLAlGLVPGDRLVEINGHNVESKSRDEI-VEMIRQSgDSVRLKVQ 308
Cdd:cd06766 28 VEDVEDDSPAKGPD-GLVPGDLILEYNSVDMRNKTAEEAyLEMLKPA-ETVTLKVQ 81
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1477-1628 |
2.15e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.43 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1477 EKLQREKLQREKDMLLAEAFSLKQQLEEKdmdIAGFTQKVVSLEAELQdissQESKDEASLAKVKKQLRDLEAKVKDQEE 1556
Cdd:pfam13851 34 EIAELKKKEERNEKLMSEIQQENKRLTEP---LQKAQEEVEELRKQLE----NYEKDKQSLKNLKARLKVLEKELKDLKW 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1557 ELDeqagtiqMLEQAKLRLEMEMErmrqthskEMESRDEE-VEEARQSCQKK---LKQMEVQLEEEYEDKQKVLRE 1628
Cdd:pfam13851 107 EHE-------VLEQRFEKVERERD--------ELYDKFEAaIQDVQQKTGLKnllLEKKLQALGETLEKKEAQLNE 167
|
|
| RseP |
COG0750 |
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ... |
269-308 |
2.33e-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: 42.38 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 42794779 269 GLVPGDRLVEINGHNVEskSRDEIVEMIRQS-GDSVRLKVQ 308
Cdd:COG0750 145 GLQPGDRIVAINGQPVT--SWDDLVDIIRASpGKPLTLTVE 183
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
1714-1807 |
2.39e-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: 41.92 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1714 EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEEANKekqEL 1793
Cdd:pfam14932 70 EALEESLEEIREATEDLEAELQELQKTKQLKINRLNKLQAQASSLSQGLRALVAEEEEAAKQLEELQEELAALNA---KT 146
|
90
....*....|....
gi 42794779 1794 QEKLQALQSQVEFL 1807
Cdd:pfam14932 147 NNVLQSLQSEVKEL 160
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1412-1556 |
2.44e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1412 GDLQADSEESQRALQQLKKKCQRLTAELQDTKlhlEGQQVRNHELEKKQRRFDSELSQAhEEAQREKLQREKLQREKDML 1491
Cdd:PRK09510 65 NRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQ---AAEQERLKQLEKERLAAQEQKKQA-EEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42794779 1492 LAEAFSLKQQLEEKDMDIAGftqKVVSLEAELQDISSQESKDEaslAKVKKQLrDLEAKVKDQEE 1556
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAA---KKAAAEAKKKAEAEAAKKAA---AEAKKKA-EAEAAAKAAAE 198
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1598-1763 |
2.51e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 42.72 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1598 EEARQSCQKKLKQMEVQLEEEYEDKQKvLREKRELegklatLSDQVNR--RDFESEKRLRKDL-KRTKALLADAQlmlDH 1674
Cdd:pfam10168 553 DLAREEIQKRVKLLKLQKEQQLQELQS-LEEERKS------LSERAEKlaEKYEEIKDKQEKLmRRCKKVLQRLN---SQ 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1675 LKNSAPSKREIAQLKNQLEESEFTCAAAVK-ARKAMEVeiedlhlQIDDIAKAKTALEE---QLSRLQREKneIQNRLEE 1750
Cdd:pfam10168 623 LPVLSDAEREMKKELETINEQLKHLANAIKqAKKKMNY-------QRYQIAKSQSIRKKsslSLSEKQRKT--IKEILKQ 693
|
170
....*....|...
gi 42794779 1751 DQEDMNELMKKHK 1763
Cdd:pfam10168 694 LGSEIDELIKQVK 706
|
|
| 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 |
2.82e-03 |
|
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: 38.69 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQS--GDSVRLKVQ 308
Cdd:cd06732 39 GLQEGDLIVEINGQNVQNLSHAQVVDVLKECpkGSEVTLLVQ 80
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1682-1827 |
2.85e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1682 KREIAQLKNQLEEsefTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEedqEDMNELMKK 1761
Cdd:PRK00409 508 KKLIGEDKEKLNE---LIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAE---KEAQQAIKE 581
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1762 HKAAVAQASRDLAQindLQAQLEEANKEkQELQEKLQALQSQVEFLE-----QSMVDKSLVSRQEAKIREL 1827
Cdd:PRK00409 582 AKKEADEIIKELRQ---LQKGGYASVKA-HELIEARKRLNKANEKKEkkkkkQKEKQEELKVGDEVKYLSL 648
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1456-1618 |
3.24e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1456 LEKKQRRFDSELSQAHEEAQREKlqREKLQREKDmllaEAFSLKQQLEekdmdiagftQKVVSLEAELQDISSQESKDEA 1535
Cdd:PRK12704 33 IKEAEEEAKRILEEAKKEAEAIK--KEALLEAKE----EIHKLRNEFE----------KELRERRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 SLakvKKQLRDLEAKvkdqEEELDEQAGTIQMLEQAKLRLEMEMERMRQTHSKEME-----SRDE-------EVE-EARQ 1602
Cdd:PRK12704 97 NL---DRKLELLEKR----EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELErisglTAEEakeilleKVEeEARH 169
|
170
....*....|....*.
gi 42794779 1603 SCQKKLKQMEVQLEEE 1618
Cdd:PRK12704 170 EAAVLIKEIEEEAKEE 185
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1701-1905 |
3.30e-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: 41.20 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1701 AAVKARKAMEVEIEDLHlqiDDIAKAKTALEEQLSRlqreKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLA-----Q 1775
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQ---SELVKARQALAQTIAR----QKQLERRLEQQTEQAKKLEEKAQAALTKGNEELArealaE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1776 INDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKslvsrqEAKIRELETRLEFERTQVKRLESLAS-RLKENMEK 1854
Cdd:pfam04012 92 KKSLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQL------KAKKNLLKARLKAAKAQEAVQTSLGSlSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 42794779 1855 LtEERDQRIAaenrEKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELE 1905
Cdd:pfam04012 166 F-ERIEEKIE----EREARADAAAELASAVDLDAKLEQAGIQMEVSEDVLA 211
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1247-1486 |
3.32e-03 |
|
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: 41.98 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1247 IEVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSD-------RLESRISELTSELTDERNTGESASQLLDAETAER 1319
Cdd:pfam19220 146 EEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEeqaaelaELTRRLAELETQLDATRARLRALEGQLAAEQAER 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1320 LRAEKEMKELQTQYdALKKQMEVMEMEVMEARLIRAAEINGEVDDddaggewrlkyerAVREvdftKKRLQQEFEDKLEV 1399
Cdd:pfam19220 226 ERAEAQLEEAVEAH-RAERASLRMKLEALTARAAATEQLLAEARN-------------QLRD----RDEAIRAAERRLKE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1400 EQQNKRQLERRLGDLQADSE-------ESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKK----QRRFDSELS 1468
Cdd:pfam19220 288 ASIERDTLERRLAGLEADLErrtqqfqEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRiaelTKRFEVERA 367
|
250 260
....*....|....*....|
gi 42794779 1469 QAHEEAQR--EKLQREKLQR 1486
Cdd:pfam19220 368 ALEQANRRlkEELQRERAER 387
|
|
| Uso1_p115_C |
pfam04871 |
Uso1 / p115 like vesicle tethering protein, C terminal region; Also known as General vesicular ... |
1822-1947 |
3.44e-03 |
|
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: 39.30 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1822 AKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIAAEnrekEQNKRLQRQLRDTKEEMGELARKEAEASRKK 1901
Cdd:pfam04871 1 AKKSELESEASSLKNENTELKAELQELSKQYNSLEQKESQAKELE----AEVKKLEEALKKLKAELSEEKQKEKEKQSEL 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 42794779 1902 HELEMDLESLEAANQSLQADLKlafKRIGDLQAAIEDEMESDENED 1947
Cdd:pfam04871 77 DDLLLLLGDLEEKVEKYKARLK---ELGEEVLSDDEDDDEDDEEDD 119
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1248-1477 |
3.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1248 EVQLSEEQIRNKDEEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERntgesasqlldAETAERLRAEKEMK 1327
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR-----------EELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1328 ELQTQYDALkkqmevmEMEVMEARLIRAAEINGEVDDDDAggewrlkyeRAVREVDFTKKRL---QQEFEDKLEVEQQNK 1404
Cdd:COG3883 100 GSVSYLDVL-------LGSESFSDFLDRLSALSKIADADA---------DLLEELKADKAELeakKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSELSQAHEEAQRE 1477
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PDZ_RGS12-like |
cd06710 |
PDZ domain of regulator of G-protein signaling 12 (RGS12), and related domains; PDZ (PSD-95 ... |
219-308 |
3.65e-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: 38.00 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 219 RELELQRRPTGdFGFSLRrttmldrgpeGQA-CrrVVHFAEPGAGTKDLalGLVPGDRLVEINGHNVESKSRDEIVEMIR 297
Cdd:cd06710 1 RTVEIARGRAG-YGFTIS----------GQApC--VLSCVVRGSPADVA--GLKAGDQILAVNGINVSKASHEDVVKLIG 65
|
90
....*....|.
gi 42794779 298 QSGDSVRLKVQ 308
Cdd:cd06710 66 KCTGVLRLVIA 76
|
|
| PDZ5_GRIP1-2-like |
cd06682 |
PDZ domain 5 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
3.72e-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: 38.48 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|....*....
gi 42794779 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06682 46 LEPGDKLLAIDNIRLDNCSMEDAAQILQQAEDIVKLKIR 84
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1261-1872 |
4.00e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.48 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1261 EEIQQLRSKLEKAEKERNELRLNSDRLESRISELTSELTDERNTGESASQLLDAETAERLRAEKEMKELQ-TQYDALKKQ 1339
Cdd:PRK10246 191 EQHKSARTELEKLQAQASGVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASrRQQALQQAL 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1340 MEVMEMEVMEARLIRAAEINGEVDDDDAGGEWRLKYERAVREVDFTKKRLQQEFEDKLEVEQQNKRQLERRLGDLQ---- 1415
Cdd:PRK10246 271 AAEEKAQPQLAALSLAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQslnt 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1416 -------------------ADSEESQRALQQLKKKCQRLTAELQ------DTKLHLEGQQVRNH-ELEKKQRRFDSELSQ 1469
Cdd:PRK10246 351 wlaehdrfrqwnnelagwrAQFSQQTSDREQLRQWQQQLTHAEQklnalpAITLTLTADEVAAAlAQHAEQRPLRQRLVA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1470 AHEEAQREKLQREKLQREKDMLLAEAFSLKQQLEEKDMDIAGFTQKVVSL------EAELQDISSQESKDEA-------- 1535
Cdd:PRK10246 431 LHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVkticeqEARIKDLEAQRAQLQAgqpcplcg 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1536 -----------SLAKVKKQLR--DLEAKVKDQEEELDEQAGTIQMLEQAKLRLEMEMERMRQthskEMESRDEEVEEARQ 1602
Cdd:PRK10246 511 stshpaveayqALEPGVNQSRldALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQ----EEQALTQQWQAVCA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1603 SCQKKLKQME-----VQLEEEYEDKQKVLREKRELEGKLATLSDQVnrrdfeseKRLRKDLKRTKALLADAqlmLDHLKN 1677
Cdd:PRK10246 587 SLNITLQPQDdiqpwLDAQEEHERQLRLLSQRHELQGQIAAHNQQI--------IQYQQQIEQRQQQLLTA---LAGYAL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1678 SAP---------SKREIAQLKNQLEESEFT--------CAAAVKARKAM-EVEIEDLHLQIDDIAKAKT---ALEEQLSR 1736
Cdd:PRK10246 656 TLPqedeeaswlATRQQEAQSWQQRQNELTalqnriqqLTPLLETLPQSdDLPHSEETVALDNWRQVHEqclSLHSQLQT 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1737 LQREKNEIQNRLEEDQEdmnelmkkHKAAVAQASRDLAQINDLQAQLEEAN-----KEKQELQEKLQALQSQVEFLEQsm 1811
Cdd:PRK10246 736 LQQQDVLEAQRLQKAQA--------QFDTALQASVFDDQQAFLAALLDEETltqleQLKQNLENQRQQAQTLVTQTAQ-- 805
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42794779 1812 vdkSLVSRQEAKIRELETRLEFERTQVkRLESLASRLKENMEKLTEERDQ-RIAAENREKEQ 1872
Cdd:PRK10246 806 ---ALAQHQQHRPDGLDLTVTVEQIQQ-ELAQLAQQLRENTTRQGEIRQQlKQDADNRQQQQ 863
|
|
| PDZ_PDLIM-like |
cd06753 |
PDZ domain of PDZ-LIM family proteins, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
269-308 |
4.02e-03 |
|
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: 37.89 E-value: 4.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 42794779 269 GLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06753 39 NLRPGDVILAINGESTEGMTHLEAQNKIKAATGSLSLTLE 78
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1549-1799 |
4.11e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.24 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1549 AKVKDQEEElDEQAgtiqmlEQAKLRLEMEMERMRqthsKEMESRDEEVEEARQSCQKKLKQMEVQLEEEYEDKQKvlRE 1628
Cdd:PRK05035 436 AEIRAIEQE-KKKA------EEAKARFEARQARLE----REKAAREARHKKAAEARAAKDKDAVAAALARVKAKKA--AA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1629 KRELEGKLATLSDQvnrRDFESEKRLRKDLKRTKALLADAQlmldhlKNSAPSKREIAqlknqleeseftcaAAV---KA 1705
Cdd:PRK05035 503 TQPIVIKAGARPDN---SAVIAAREARKAQARARQAEKQAA------AAADPKKAAVA--------------AAIaraKA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1706 RKAMEVEIEDLHLQIDDIAKAKTALEeqLSRLQREKNEiQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLEE 1785
Cdd:PRK05035 560 KKAAQQAANAEAEEEVDPKKAAVAAA--IARAKAKKAA-QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE 636
|
250
....*....|....
gi 42794779 1786 ANKEKQELQEKLQA 1799
Cdd:PRK05035 637 PEEPVDPRKAAVAA 650
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1705-1809 |
4.44e-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: 39.09 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQINDLQAQLE 1784
Cdd:pfam13863 11 VQLALDAKREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|....*
gi 42794779 1785 EANKEKQELQEKLQALQSQVEFLEQ 1809
Cdd:pfam13863 91 ELKSEISKLEEKLEEYKPYEDFLEK 115
|
|
| PDZ2_APBA1_3-like |
cd06793 |
PDZ domain 2 of amyloid-beta A4 precursor protein-binding family A member 1 (APBA1), APBA2, ... |
273-309 |
4.50e-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: 37.77 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|....*..
gi 42794779 273 GDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQP 309
Cdd:cd06793 42 GHRIIEINGQSVVATPHEKIVQLLSNSVGEIHMKTMP 78
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1784-1923 |
4.54e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1784 EEANKEKQELQEKLQALQSQVEFLEQsmvdkslvsRQEAKIRELETRLefertqvKRLESLASRLKENMEKLTEERDQRI 1863
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELER---------ELEQKAEEAEALL-------KEAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1864 AaenrekEQNKRLQRQLRDTKEEMGELAR------KEAEASRKKHELEMDLESLEAANQSLQADLK 1923
Cdd:PRK00409 569 E------EAEKEAQQAIKEAKKEADEIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKK 628
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1405-1645 |
4.65e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1405 RQLERRLGDLQADSEESQRALQQLKKKCQRLT-AELQdtklhlEGQQVrnhELEKKQRRfdseLSQAheeaqrEKLqREK 1483
Cdd:COG0497 168 RALKKELEELRADEAERARELDLLRFQLEELEaAALQ------PGEEE---ELEEERRR----LSNA------EKL-REA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1484 LQREKDML----------LAEAFSLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESK-------DEASLAKVKK---Q 1543
Cdd:COG0497 228 LQEALEALsggeggaldlLGQALRALERLAEYDPSLAELAERLESALIELEEAASELRRyldslefDPERLEEVEErlaL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1544 LRDLEAKVKDQEEELdeqagtIQMLEQAKLRLEmemermrqthskEMESRDEEVEEarqscqkkLKQMEVQLEEEYEDKQ 1623
Cdd:COG0497 308 LRRLARKYGVTVEEL------LAYAEELRAELA------------ELENSDERLEE--------LEAELAEAEAELLEAA 361
|
250 260
....*....|....*....|...
gi 42794779 1624 KVLREKRElegKLA-TLSDQVNR 1645
Cdd:COG0497 362 EKLSAARK---KAAkKLEKAVTA 381
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1688-1833 |
4.83e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1688 LKNQLEESEFTCAAAVKARKAMEVEIEDLHLQIDDIakaKTALEEQLSRLQREKNEIQNRleeDQEDMNELMKKHKAAVA 1767
Cdd:smart00787 145 LKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDR---KDALEEELRQLKQLEDELEDC---DPTELDRAKEKLKKLLQ 218
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1768 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQSMVDKSLVSRQEakIRELETRLEF 1833
Cdd:smart00787 219 EIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKE--IEKLKEQLKL 282
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
1713-1951 |
4.87e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 41.07 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLHLQIDDIAKAKTALEEQLsrlqrekNEIQNRLEEDQEDMNELMKKHKAAVAQA-SRDLAQ-----INDLQAQLEEA 1786
Cdd:pfam13949 19 IERLEKSLDDLPKLKQRNREIL-------DEAEKLLDEEESEDEQLRAKYGTRWTRPpSSELTAtlraeIRKYREILEQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1787 NKEKQELQEKLQALQSQVEFLEQSMVD--KSLVSRQEAKIRELETRlefertQVKRLESLASRLkenmEKLTEERDQRIa 1864
Cdd:pfam13949 92 SESDSQVRSKFREHEEDLELLSGPDEDleAFLPSSRRAKNSPSVEE------QVAKLRELLNKL----NELKREREQLL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1865 AENREKEQNKRLQRQLRDTKEEMGELARKEA---EASRKKHELEMDLESLEAANQSLQADLKLAFKRIgdLQAAIEDEME 1941
Cdd:pfam13949 161 KDLKEKARNDDISPKLLLEKARLIAPNQEEQlfeEELEKYDPLQNRLEQNLHKQEELLKEITEANNEF--LQDKRVDSEK 238
|
250
....*....|
gi 42794779 1942 SDENEDLINS 1951
Cdd:pfam13949 239 QRQREEALQK 248
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1683-1873 |
4.90e-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: 40.51 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1683 REIAQLKNQLEESEFTCAAAVKARKAMEVEI-----EDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNE 1757
Cdd:cd00176 7 RDADELEAWLSEKEELLSSTDYGDDLESVEAllkkhEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1758 LMKKHKAAVAQASRDLAQINDLQAQLEEANKEKQELQEKLQALQSQvefleQSMVDKSLVSRQEAKIRELETRLEFERTQ 1837
Cdd:cd00176 87 RWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE-----DLGKDLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 42794779 1838 VKRLESLASRLKENMEKLTEERDQRIAAENREKEQN 1873
Cdd:cd00176 162 LKSLNELAEELLEEGHPDADEEIEEKLEELNERWEE 197
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1389-1550 |
5.05e-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: 40.27 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1389 LQQEFEDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQD---TKLHLEGQQVRNHELEKKQRrfds 1465
Cdd:pfam13851 27 LIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENyekDKQSLKNLKARLKVLEKELK---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1466 ELSQAHEEaqreKLQR-EKLQREKDmllaeafSLKQQLEEKDMDI---AGF-----TQKVVSL-------EAELQDISSQ 1529
Cdd:pfam13851 103 DLKWEHEV----LEQRfEKVERERD-------ELYDKFEAAIQDVqqkTGLknlllEKKLQALgetlekkEAQLNEVLAA 171
|
170 180
....*....|....*....|..
gi 42794779 1530 ESKDEASLAKVKKQLRD-LEAK 1550
Cdd:pfam13851 172 ANLDPDALQAVTEKLEDvLESK 193
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1543-1797 |
5.12e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1543 QLRDLeaKVKDQEEELDEQAGTIQMLEQA--KLRLEMEMERMRQthSKEMESRDEEVEEARQSCQKKLKQmevqLEEEYE 1620
Cdd:PRK05771 32 HIEDL--KEELSNERLRKLRSLLTKLSEAldKLRSYLPKLNPLR--EEKKKVSVKSLEELIKDVEEELEK----IEKEIK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1621 DKQKVLR----EKRELEGKLATLSdqvNRRDFESEKRLRKDLKRTKALLADAQlmldhlKNSAPSKREIAQLKNQLEESE 1696
Cdd:PRK05771 104 ELEEEISelenEIKELEQEIERLE---PWGNFDLDLSLLLGFKYVSVFVGTVP------EDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1697 F----TCAAAVKARKAMEV--EIEDLHLQIDDIAKAKTALEEqLSRLQREKNEIQNRLEEDQEDMNELMKKHKaavaqas 1770
Cdd:PRK05771 175 DkgyvYVVVVVLKELSDEVeeELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYL------- 246
|
250 260
....*....|....*....|....*....
gi 42794779 1771 rdlaqiNDLQAQLE--EANKEKQELQEKL 1797
Cdd:PRK05771 247 ------EELLALYEylEIELERAEALSKF 269
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1705-1804 |
5.18e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEV-----EIEDLHLQIDDIAKAKTALE--------EQLSRLQREKNEiqnrLEEDQEDMNELMKKHKAAVAQASR 1771
Cdd:COG0542 400 ARVRMEIdskpeELDELERRLEQLEIEKEALKkeqdeasfERLAELRDELAE----LEEELEALKARWEAEKELIEEIQE 475
|
90 100 110
....*....|....*....|....*....|...
gi 42794779 1772 DLAQINDLQAQLEEANKEKQELQEKLQALQSQV 1804
Cdd:COG0542 476 LKEELEQRYGKIPELEKELAELEEELAELAPLL 508
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1754-1858 |
5.67e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.82 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1754 DMNELMKKHKAAVAQASRDLAQINDLQAQLEeanKEKQELQEKLQALQSQVEFLEQSMVDKslvsrQEAKIRELETrlEF 1833
Cdd:COG2825 30 DVQRILQESPEGKAAQKKLEKEFKKRQAELQ---KLEKELQALQEKLQKEAATLSEEERQK-----KERELQKKQQ--EL 99
|
90 100
....*....|....*....|....*
gi 42794779 1834 ERTQVKRLESLASRLKENMEKLTEE 1858
Cdd:COG2825 100 QRKQQEAQQDLQKRQQELLQPILEK 124
|
|
| PDZ2_GRIP1-2-like |
cd06681 |
PDZ domain 2 of glutamate receptor-interacting protein 1 (GRIP1) and GRIP2, and related ... |
270-308 |
6.04e-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: 37.98 E-value: 6.04e-03
10 20 30
....*....|....*....|....*....|....*....
gi 42794779 270 LVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVRLKVQ 308
Cdd:cd06681 49 IKPGDRLLSVDGISLHGATHAEAMSILKQCGQEATLLIE 87
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1725-2018 |
6.13e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 41.96 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1725 KAKTALEEQLSRLQ--REKNEIQNRLEEDQedmnelmkkhkaavAQASRDLAQINDLQAQLEEANKEKQELQEKLqaLQS 1802
Cdd:PTZ00108 1031 AKKKDLVKELKKLGyvRFKDIIKKKSEKIT--------------AEEEEGAEEDDEADDEDDEEELGAAVSYDYL--LSM 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1803 QVEFLEQSMVDKsLVSRQEAKIRELEtrlEFERTQVKR--LESLAsRLKENMEKLTEERDQRIAAENREKEQNKRLQRQL 1880
Cdd:PTZ00108 1095 PIWSLTKEKVEK-LNAELEKKEKELE---KLKNTTPKDmwLEDLD-KFEEALEEQEEVEEKEIAKEQRLKSKTKGKASKL 1169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1881 RDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLAFKRIGDLQAAIEDEMESDENEDLINSEGDSDVDSE 1960
Cdd:PTZ00108 1170 RKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNN 1249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 42794779 1961 LEDRVDGVKSWLSKNKGPSKAASDDgsLKSSSPTSYWKSLAPDRSDDEHDPLDNTSRP 2018
Cdd:PTZ00108 1250 SSKSSEDNDEFSSDDLSKEGKPKNA--PKRVSAVQYSPPPPSKRPDGESNGGSKPSSP 1305
|
|
| PDZ_ARHGEF11-12-like |
cd23069 |
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density ... |
253-308 |
6.63e-03 |
|
PDZ domain of ARHGEF11, ARHGEF12, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of ARHGEF11, ARHGEF12, and related domains. This subfamily includes the GEFs (guanine exchange factors) ARHGEF11 (Rho guanine nucleotide exchange factor 11, known as PDZ-RhoGEF) and ARHGEF12 (Rho guanine nucleotide exchange factor 12, also known as leukemia-associated RhoGEF). GEFs activate Rho GTPases by promoting GTP binding. ARHGEF11/12 are regulators of G protein signaling (RGS) domain-containing GEFs; the RGS domain mediates their binding to and activation of Galpha (and Gq also in the case of ARHGEF12), in response to G-protein coupled receptor activation. ARHGEF11 and 12 are involved in serum-signaling, and regulate Yes-Associated Protein (YAP1)-dependent transcription. The ARHGEF12 PDZ domain binds plexin-B1 and the receptor tyrosine kinase insulin-like growth factor receptor (IGF-R1) beta-subunit. ARHGEF12 also interacts with glutamate receptor delta-1(GluD1), a postsynaptic organizer of inhibitory synapses in cortical pyramidal neurons. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This ARHGEF11-12-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: 467282 [Multi-domain] Cd Length: 76 Bit Score: 37.37 E-value: 6.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 253 VVHFAEPGAGTKdlaLGLVPGDRLVEINGHNVESKSRDEIVEMIRqSGDSVRLKVQ 308
Cdd:cd23069 25 VQSVKEGGAAYR---AGVQEGDRIIKVNGTLVTHSNHLEVVKLIK-SGSYVALTLL 76
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1394-1761 |
6.63e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEQQNKRQLERRLGDLQADSEESQRALQQLKKKCQRLT-------------------------AELQDTKLHLEG 1448
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNrllprlnlladetladrveeireqlDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1449 QQVRNHELEKKQRRFDSELSQaHEEAQREKLQREKLQREKDM---LLAE--------AFSLKQQLEEKDMDIA-GFTQKV 1516
Cdd:PRK04863 916 HGNALAQLEPIVSVLQSDPEQ-FEQLKQDYQQAQQTQRDAKQqafALTEvvqrrahfSYEDAAEMLAKNSDLNeKLRQRL 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1517 VSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQ---------MLEQAKLRLEMEMERMRQThs 1587
Cdd:PRK04863 995 EQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvpadsgAEERARARRDELHARLSAN-- 1072
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1588 kemESRDEEVEEARQSC--------------QKKLKQMEVQLEEEYEDKQKVLR-------EKRELEGKLATLSDQvnrr 1646
Cdd:PRK04863 1073 ---RSRRNQLEKQLTFCeaemdnltkklrklERDYHEMREQVVNAKAGWCAVLRlvkdngvERRLHRRELAYLSAD---- 1145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1647 dfESEKRLRKDLKRTKALLADAQLMLDHLKNSAPSKReiAQLKNQleeseFTCAAAVKARKAMEVEIedlhLQIDDIAKA 1726
Cdd:PRK04863 1146 --ELRSMSDKALGALRLAVADNEHLRDVLRLSEDPKR--PERKVQ-----FYIAVYQHLRERIRQDI----IRTDDPVEA 1212
|
410 420 430
....*....|....*....|....*....|....*
gi 42794779 1727 KTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKK 1761
Cdd:PRK04863 1213 IEQMEIELSRLTEELTSREQKLAISSESVANIIRK 1247
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1383-1606 |
6.65e-03 |
|
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: 40.95 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1383 DFTKKRLQ------QEFEDKLEVEQQN----KRQLERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEgqqvr 1452
Cdd:pfam15905 148 DGTQKKMSslsmelMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETE----- 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1453 nhelekKQRRFDSELSQAHEEAQREKLqreklqrekdmllaEAFSLKQQLEEKDMDIagftqkvVSLEAELQdissqESK 1532
Cdd:pfam15905 223 ------KLLEYITELSCVSEQVEKYKL--------------DIAQLEELLKEKNDEI-------ESLKQSLE-----EKE 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42794779 1533 DEaslakvkkqlrdLEAKVKDQEEELdeqagtiQMLEQAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQK 1606
Cdd:pfam15905 271 QE------------LSKQIKDLNEKC-------KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQK 325
|
|
| PDZ_MAST1 |
cd23073 |
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ... |
225-314 |
6.71e-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: 38.08 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 225 RRPTGDFGFSLRRTTMLDRGPEGQACRRVVHFAEPGAGTKDLalGLVPGDRLVEINGHNVESKSRDEIVEMIRQSGDSVR 304
Cdd:cd23073 8 QRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEA--GLCAGDLITHVNGEPVHGMVHPEVVELILKSGNKVA 85
|
90
....*....|
gi 42794779 305 LKVQPIPELS 314
Cdd:cd23073 86 VTTTPFENTS 95
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
1715-1804 |
6.89e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 40.87 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1715 DLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLaqiNDLQAQLEEANKEKQELQ 1794
Cdd:TIGR04320 262 KLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNL---ATAQAALANAEARLAKAK 338
|
90
....*....|
gi 42794779 1795 EKLQALQSQV 1804
Cdd:TIGR04320 339 EALANLNADL 348
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1614-1929 |
6.92e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1614 QLEEEYEDKQKVLREKRELEGKLATLSDQVNRRDfESEKRLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQL 1692
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLE-EELEQARSELEQLEEELEELNEQLQAAQAElAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1693 EESEFTCAAAVKARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQRE----KNEIQNRLEEDQE-DMNELMKKHKAAVA 1767
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQleslQEELAALEQELQAlSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1768 QASRDLAQINDLQAQLEEANKEKQELQEKLQALQ--SQVEFLEQSMVDKSLVSRQEAKIRELETRLEFERTQVKRLESLA 1845
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKdsLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1846 SRLKENMEKLTEERDQRIAAENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKKHELEMDLESLEAANQSLQADLKLA 1925
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
....
gi 42794779 1926 FKRI 1929
Cdd:COG4372 351 LDND 354
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1730-1919 |
7.28e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.20 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1730 LEEQLSRLQREKNEIQNRLEEDQEDMNELMKKHKAAVAQASRDLAQIND----LQAQLEEANKEKQELQEKLQAlqsQVE 1805
Cdd:pfam15070 34 LSEQVRTLREEKERSVSQVQELETSLAELKNQAAVPPAEEEQPPAGPSEeeqrLQEEAEQLQKELEALAGQLQA---QVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1806 FLEQSmvdKSLVSRQEAKIRELETRLEFERTQVKRLEslasRLKENME--KLTeerDQRIAAENRE-KEQNKRLQRQ-LR 1881
Cdd:pfam15070 111 DNEQL---SRLNQEQEQRLLELERAAERWGEQAEDRK----QILEDMQsdRAT---ISRALSQNRElKEQLAELQNGfVK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 42794779 1882 DTKEEM-------------GELARKEAEASRKKHEL--EMDLESLEAanQSLQ 1919
Cdd:pfam15070 181 LTNENMeltsalqseqhvkKELAKKLGQLQEELGELkeTLELKSQEA--QSLQ 231
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1657-1913 |
7.33e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.43 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1657 DLKRTKALLADAQLMLDHLKNSAPSKREIA-QLKNQLEESEftcaaavKARKAMEVEIEDLHLQIDDIAKAKTALEEQLS 1735
Cdd:pfam15964 348 NFEKTKALIQCEQLKSELERQKERLEKELAsQQEKRAQEKE-------ALRKEMKKEREELGATMLALSQNVAQLEAQVE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1736 RLQREKNEIQNRLEEDQEDmnelMKKHKAAVAQASRDLA-QINDLQAQLEEANKEKQELQEKlqaLQSQVEFLEQsmvdk 1814
Cdd:pfam15964 421 KVTREKNSLVSQLEEAQKQ----LASQEMDVTKVCGEMRyQLNQTKMKKDEAEKEHREYRTK---TGRQLEIKDQ----- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1815 slvsrqeaKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDqriaaenrEKEQNKRLQRQLRDTKEE-MGELARK 1893
Cdd:pfam15964 489 --------EIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLG--------ESEHQLHLTRLEKESIQQsFSNEAKA 552
|
250 260
....*....|....*....|.
gi 42794779 1894 EA-EASRKKHELEMDLESLEA 1913
Cdd:pfam15964 553 QAlQAQQREQELTQKMQQMEA 573
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1558-1802 |
7.62e-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: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1558 LDEQAGTIQMLEQAklrlemeMERMRQTHSKEMESRDEEVEEARQScQKKLKQMEVQLEEEYEDKQKVLREKRElegKLA 1637
Cdd:pfam04012 17 LDKAEDPEKMLEQA-------IRDMQSELVKARQALAQTIARQKQL-ERRLEQQTEQAKKLEEKAQAALTKGNE---ELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1638 tlsdqvnRRDFESEKRLRKDLKRTKALLADAQLMLDHLKNS-APSKREIAQLKNQLEeseftcaaAVKARKAMeveiedl 1716
Cdd:pfam04012 86 -------REALAEKKSLEKQAEALETQLAQQRSAVEQLRKQlAALETKIQQLKAKKN--------LLKARLKA------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1717 hlqiddiAKAKTALEEQLSRLQREKNEIQ-NRLEEDQEDMnelmkkhkAAVAQASRDLAQINDLQAQLEEANKEKQELQE 1795
Cdd:pfam04012 144 -------AKAQEAVQTSLGSLSTSSATDSfERIEEKIEER--------EARADAAAELASAVDLDAKLEQAGIQMEVSED 208
|
....*..
gi 42794779 1796 KLQALQS 1802
Cdd:pfam04012 209 VLARLKA 215
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1458-1610 |
7.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.23 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1458 KKQRRFDSELSQAHEEAQRE--KLQREKLQREKDMLLAEAFSLKQQL----EEKDMDIAGFTQKVVSLEAELQDISSQES 1531
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEaeEKLEAALLEAKELLLRERNQQRQEArrerEELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1532 KDEASLAKVKKQLRDLEAKVKDQEEELDEQAGTIQmlEQAK----LRLEMEMERMRQTHSKEMESRDEevEEARQSCQKK 1607
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRVAGLTP--EQARklllKLLDAELEEEKAQRVKKIEEEAD--LEAERKAQNI 181
|
...
gi 42794779 1608 LKQ 1610
Cdd:PRK12705 182 LAQ 184
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1626-1960 |
8.30e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1626 LREKRELEGKLATLSDQVNRRDFESEKRLRKD-LKRTKALLADaqlmLDHLKNSAPSKREIAQLKNQLEESEFTCAAAVK 1704
Cdd:COG5185 66 VLDGLNYQNDVKKSESSVKARKFLKEKKLDTKiLQEYVNSLIK----LPNYEWSADILISLLYLYKSEIVALKDELIKVE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1705 ARKAMEVEIEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNRLEEDQEDMNELmkkHKAAVAQASRDLAQINDLQAQLE 1784
Cdd:COG5185 142 KLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1785 EANKEKQElqeklqalqsqvefleqsmvdkslvsrQEAKIRELETRLEFERTQVKRLESLASRLKENMEKLTEERDQRIA 1864
Cdd:COG5185 219 STLLEKAK---------------------------EIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1865 AEN----REKEQNKRLQRQLRDTKEEMGELArKEAEASRKKHELEMDLESLEaANQSLQADLKLAFKRIGDLQAAIEDEM 1940
Cdd:COG5185 272 ENAesskRLNENANNLIKQFENTKEKIAEYT-KSIDIKKATESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQ 349
|
330 340
....*....|....*....|.
gi 42794779 1941 ES-DENEDLINSEGDSDVDSE 1960
Cdd:COG5185 350 ESlTENLEAIKEEIENIVGEV 370
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1788-1901 |
8.41e-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: 40.64 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1788 KEKQELQEKLQALQSQVEFLEQSmvDKSLvSRQEAKIRELETRLEFERTQVKRLESLASRL-----------KENMEKLT 1856
Cdd:cd16269 167 KAEEVLQEFLQSKEAEAEAILQA--DQAL-TEKEKEIEAERAKAEAAEQERKLLEEQQRELeqkledqersyEEHLRQLK 243
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 42794779 1857 EERDQRIaaENREKEQNKRLQRQLRDTKEEMGELARKEAEASRKK 1901
Cdd:cd16269 244 EKMEEER--ENLLKEQERALESKLKEQEALLEEGFKEQAELLQEE 286
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1713-1880 |
8.51e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.11 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1713 IEDLHLQIDDIAKAKTALEEQLSRLQREKNEIQNR----------LEEDQEDMNELMKKHKAAVaqasRDLA-QINDLQA 1781
Cdd:pfam17078 5 IESLHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKeskflenlasLKHENDNLSSMLNRKERRL----KDLEdQLSELKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1782 QLEEANKEKQELQEKLQALQSQVEFLEQSM------VDKSLVSRQEAK------IRELETRLE-FERTQVKRLESLASRL 1848
Cdd:pfam17078 81 SYEELTESNKQLKKRLENSSASETTLEAELerlqiqYDALVDSQNEYKdhyqqeINTLQESLEdLKLENEKQLENYQQRI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 42794779 1849 KENM----EKLTEERDQRIAAENREKEQNKRLQRQL 1880
Cdd:pfam17078 161 SSNDkdidTKLDSYNNKFKNLDNIYVNKNNKLLTKL 196
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1408-1563 |
8.78e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1408 ERRLGDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSElsqaheeaQREKLQREklqRE 1487
Cdd:COG2433 398 EREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE--------ERREIRKD---RE 466
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42794779 1488 KDMLLAEAFSLKQQLEEKDMDIAGFTQKVvsleAELQDISSQESKDEASLAKVKKQLRdleakvKDQEEELDEQAG 1563
Cdd:COG2433 467 ISRLDREIERLERELEEERERIEELKRKL----ERLKELWKLEHSGELVPVKVVEKFT------KEAIRRLEEEYG 532
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1256-1610 |
9.06e-03 |
|
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: 40.67 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1256 IRNKDEEIQQLRSKLEKAE--KERNELRLNSDRLESRISELTSELTDERNTgesasQLLDAETAERLRAEKEMKELQTQY 1333
Cdd:pfam13868 1 LRENSDELRELNSKLLAAKcnKERDAQIAEKKRIKAEEKEEERRLDEMMEE-----ERERALEEEEEKEEERKEERKRYR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1334 DALKKQMEVMEMEVMEARLIRAAEingevddddagGEWRLKYERAVREVDFTKKRLQQEFEDKL--EVEQQNKRQLERRL 1411
Cdd:pfam13868 76 QELEEQIEEREQKRQEEYEEKLQE-----------REQMDEIVERIQEEDQAEAEEKLEKQRQLreEIDEFNEEQAEWKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1412 GDLQADSEESQRALQQLKKKCQRLTAELQDTKLHLEGQQVRNHELEKKQRRFDSElsQAHEEAQREKLQREKLQREKDML 1491
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDE--KAERDELRAKLYQEEQERKERQK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1492 LAEAfsLKQQLEEKDMDIAGFTQKVVSLEAELQDISSQESKDEASLAKVKKQLRDLEAKVKDQEEELDEQ--AGTIQMLE 1569
Cdd:pfam13868 223 EREE--AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEhrRELEKQIE 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 42794779 1570 QAKLRLEMEMERMRQTHSKEMESRDEEVEEARQSCQKKLKQ 1610
Cdd:pfam13868 301 EREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1394-1599 |
9.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 9.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1394 EDKLEVEqqnkrqlerrlgDLQADSEESQRALQQLKKKCQRLTAELQdtKLHLEGQQvrnhELEKKQRRFDSELSQAHEE 1473
Cdd:PRK00409 513 EDKEKLN------------ELIASLEELERELEQKAEEAEALLKEAE--KLKEELEE----KKEKLQEEEDKLLEEAEKE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1474 AQrEKLqrEKLQREKDMLLAEafsLKQQLEEKDMDIAgftqkvvslEAELQDIssqeskdeasLAKVKKQLRDLEAKVKD 1553
Cdd:PRK00409 575 AQ-QAI--KEAKKEADEIIKE---LRQLQKGGYASVK---------AHELIEA----------RKRLNKANEKKEKKKKK 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1554 QEEELDE-------------QAGTI-QMLEQAKLRLEMEMERMRqTHSKEMESRDEEVEE 1599
Cdd:PRK00409 630 QKEKQEElkvgdevkylslgQKGEVlSIPDDKEAIVQAGIMKMK-VPLSDLEKIQKPKKK 688
|
|
| IQ |
smart00015 |
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ... |
1187-1209 |
9.83e-03 |
|
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.
Pssm-ID: 197470 [Multi-domain] Cd Length: 23 Bit Score: 35.38 E-value: 9.83e-03
|
| GimC |
COG1382 |
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones]; |
1773-1858 |
9.98e-03 |
|
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440992 [Multi-domain] Cd Length: 121 Bit Score: 37.95 E-value: 9.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42794779 1773 LAQINDLQAQLEEANKEKQELQEKLQALQSQVEFLEQ----SMVDKS----LVSRQEAK-IRELETRLEFERTQVKRLES 1843
Cdd:COG1382 13 LAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKlpddAEVYKSvgnlLVKTDKEEvIKELEEKKETLELRLKTLEK 92
|
90
....*....|....*
gi 42794779 1844 LASRLKENMEKLTEE 1858
Cdd:COG1382 93 QEERLQKQLEELQEK 107
|
|
| |
